sirna shrna Search Results


96
OriGene mer shrnas against rat cdc2
Figure 1. Spinal cord injury induces upregulation of expression of E2F1 and its downstream targets. Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A. 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and <t>CDK1.</t> GAPDH signal served as a loading control. B– C. The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E. Cyclin A expression was increased at all time points. F. Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H. Quantification of respective western blots in panel D. N = 4 rats/time point. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g001
Mer Shrnas Against Rat Cdc2, supplied by OriGene, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
OriGene pi3kc2α sirna pool
FCHSD2 Is Not Directly Recruited to CCPs by <t>PI3KC2α</t> or Its Kinase Activity, Related to <xref ref-type=Figure 2 (A) Top: Transferrin uptake assay by flow cytometry comparing wild-type and FCHSD2 KO cells silenced for PI3KC2α. Uptake of Alexa488 labeled transferrin normalized by the amount of surface transferrin receptor for each condition and against uptake for the wild-type cells in each experiment. Each value represents median fluorescence from at least 5000 cells (n = 12, mean ± SD). ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. Bottom: Immunoblots showing PI3KC2α knockdown in wild-type and FCHSD2 KO cells. (B) Kymographs of HeLa FCHSD2-Venus stables silenced for PI3KC2α and control cells. Cells were transfected with mCherry-ClathrinLC 24 hs before imaging. Kymographs generated from 120 s movies at 1Hz. Note the elongated CCP lifetimes in PI3KC2α knockdown cells as described in Posor et al. (2013) . (C) Autoinhibition of FCHSD2. Representative images of a center slice from cells expressing different FCHSD2 truncation constructs and co-stained with phalloidin (Actin). The bar graph (upper right) shows the quantification of cellular protrusions/μm for each construct. The non-inhibited BAR domain produces many protrusions. Numbers inside bars represent number of cells measured. The line graph (bottom right) shows the fluorescence profile of sum intensity projections for cells expressing each construct. Due to the natural thinning of cells from their centers to the edge, a gradually decaying line indicates that the fluorescent protein is primarily cytosolic while a flat line with an abrupt fall on the cell edge indicates that the fluorescent protein is primarily bound to the membrane. While the presence of SH3-1 significantly reduces the generation of cellular protrusions generated by the FCHSD2 F-BAR, a significant fraction of the protein remains bound to the membrane (green line). Only the combined presence of SH3-1 and SH3-2 is capable to avoid promiscuous binding of the BAR domain to the membrane. Data is shown as mean ± SD in bar graph and as ± SEM in fluorescence profiles. ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. (D) Immunoblots for intersectin knockdown in FCHSD2-Venus HeLa cells. " width="250" height="auto" />
Pi3kc2α Sirna Pool, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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91
OriGene scramble sirna
Figure <t>3.</t> <t>ACSL1</t> <t>siRNA</t> transfection reduced TNFα-mediated MMP-9 production. We transfected THP-1 monocytic cells with siRNA targeting human ACSL1 gene expression or scrambled siRNA (a control siRNA). (A,B) After 36 h, we performed real-time PCR to measure ACSL1 gene expression or western blotting for protein to test the knocking down efficiency. (C) We then incubated ACSL1-deficient cells with TNFα for 24 h. We determined mRNA expression of MMP-9 by real-time PCR. (D) We determined MMP-9 protein in culture media using ELISA. (E) The effect of siRNA transfection in combination with TNFα on cell viability was evaluated by measuring cell metabolic activity (MTT assay). The cell viability is expressed as the percentage of cells compared to the condition of vehicle control. Three independent experiments were performed with similar results. All data are expressed as mean ± SEM (n ≥ 3). t test or onene way ANOVA (Dunnett’s Test) for comparing treatments vs control) were used). **p < 0.01, ***p < 0.001.
Scramble Sirna, supplied by OriGene, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriGene hmgb1 small interfering rna sirna target rat hmgb1
The expression of <t>HMGB1,</t> TLR4, and RAGE proteins and mRNA in the spinal dorsal horn. (a) Diagram of the timeline of this experiment. (b-d) Images showing HMGB1 expression in the spinal dorsal horn of naïve rats (b) and rats receiving intrathecal (i.t.) injection of saline (c) and i.t. injection of morphine (d). (e-g) Images showing TLR4 expression in the spinal dorsal horn of naïve rats (e) and rats receiving i.t. injection of saline (f) and i.t. injection of morphine (g). (gh-j) The images showing RAGE expressed in spinal dorsal horn in rats of naïve rats (h) and rats receiving i.t. injection of saline (i) and i.t. injection of morphine (j). (k) Repeated intrathecal (i.t.) injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE proteins in the spinal dorsal horn. * P < 0.05, ** P < 0.01 vs. control group (i.t. injection of saline daily for 6 days). (l) Repeated i.t. injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE mRNA in the spinal dorsal horn. * P < 0.05, ** P < 0.01, *** P < 0.001 vs. saline group (i.t. injection of saline daily for 6 days). (m) Repeated subcutaneous (s.c.) injections of morphine caused increased expression of HMGB1 mRNA in the spinal dorsal horn of mice. * P < 0.05; ** P < 0.01 vs. control (s.c. saline daily for 9 days). Data are presented as the mean ± SEM and were analyzed with one-way ANOVA. Images in b-j, scale bar = 200 μm. Sa: saline
Hmgb1 Small Interfering Rna Sirna Target Rat Hmgb1, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriGene sirna against sclerostin
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Sirna Against Sclerostin, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriGene slc7a11 mouse sirna oligo duplexes
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Slc7a11 Mouse Sirna Oligo Duplexes, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
OriGene ahr sirna
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Ahr Sirna, supplied by OriGene, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriGene sequences targeting wnk3
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Sequences Targeting Wnk3, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
OriGene trpv4 specific mouse sirna duplexes
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Trpv4 Specific Mouse Sirna Duplexes, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
OriGene unique 27mer sirna duplex targeting rab18
Figure 1. Breast cancer–derived <t>sclerostin</t> inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control <t>siRNA</t> (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.
Unique 27mer Sirna Duplex Targeting Rab18, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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OriGene sr305039

Sr305039, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
OriGene 27mer sirna duplex

27mer Sirna Duplex, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Figure 1. Spinal cord injury induces upregulation of expression of E2F1 and its downstream targets. Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A. 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B– C. The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E. Cyclin A expression was increased at all time points. F. Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H. Quantification of respective western blots in panel D. N = 4 rats/time point. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g001

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 1. Spinal cord injury induces upregulation of expression of E2F1 and its downstream targets. Analysis of expression of E2F1 and its transcriptional target genes in intact and injured spinal cord were performed by western blotting. A. 5-mm-long segment centered at the injury epicenter was dissected and homogenized in RIPA buffer. Equal amounts of protein were electrophoretically separated on NuPAGE Novex Bis-Tris gradient gels, transferred to nitrocellulose membranes, and blotted with antibodies to E2F1 and CDK1. GAPDH signal served as a loading control. B– C. The signal quantifications for E2F1 (B) and CDK1 (C) using Gel-Pro Analyzer software are displayed. E2F1 and CDK1 expression level was upregulated as early as 15 min and sustained until 3 days after injury. D–E. Cyclin A expression was increased at all time points. F. Bim and c-Myb, downstream targets of E2F1 were upregulated as early as 5 h post-injury and sustained until day 3 after SCI. G–H. Quantification of respective western blots in panel D. N = 4 rats/time point. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g001

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Expressing, Western Blot, Control, Software

Figure 2. CDK1 activity is increased after spinal cord injury. Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A. Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D. Quantification of respective western blots in panel A. n = 4 rats/time point. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g002

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 2. CDK1 activity is increased after spinal cord injury. Western blotting analysis of common CDK substrates, CDK1 co-activator cyclin B1 and phosphorylations of specific CDK1 substrate (Ser54)-n-myc was performed in homogenates obtained from intact and injured spinal cord. A. Cyclin B1 expression was upregulated at all time points tested. Phosphorylation (Ser54) of n-myc and phospho-CDK substrate motif signal levels were increased from 5 h to day 7. B–D. Quantification of respective western blots in panel A. n = 4 rats/time point. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g002

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Activity Assay, Western Blot, Expressing, Phospho-proteomics

Figure 3. The temporal profile and cell specificity of E2F1 and CDK1 expression after SCI. A–B. Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1+ cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1+ cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1+ oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1+ oligodendrocytes. CDK1+ cells also appeared in the lesion area. H–I. CDK1 was expressed by CC1+ oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J. Only a small subset of CDK1+ cells in the lesion area were positive for OX42 at 24 h after SCI. K. Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 mm for A–B, F–G. Scale bar = 100 mm for C–E, H–J, K–L. doi:10.1371/journal.pone.0042129.g003

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 3. The temporal profile and cell specificity of E2F1 and CDK1 expression after SCI. A–B. Coronal section in intact spinal cord (A) showed that E2F1 is relatively weak and detected mainly in neurons of the gray matter. At 24 h after SCI, E2F1 immunoreactivity was upregulated not only in gray matter but also in lesion area (B). C. E2F1+ cells were also co-labelled with NeuN in the dorsal horn of the gray matter at 1 day after SCI. D–E. Only a small subset of E2F1+ cells in the lesion area were positive for OX42 at 24 h (D) and 7 d (E) after SCI. F–G. In the intact spinal cord (F), CDK1 immunoreactivity is relatively weak and detected mainly in motor neurons in the ventral horn and CC1+ oligodendrocytes. At 24 h after SCI (G), CDK1 immunoreactivity was upregulated not only in the ventral horn but also in the spared white matter, colocalized with CC1+ oligodendrocytes. CDK1+ cells also appeared in the lesion area. H–I. CDK1 was expressed by CC1+ oligodendrocytes in the white matter in the intact spinal cord (H) and at 1 day after SCI. J. Only a small subset of CDK1+ cells in the lesion area were positive for OX42 at 24 h after SCI. K. Coronal section in intact spinal cord (a) shows that E2F1 was expressed in the motor neurons in the ventral horn. Immunoreactivity of E2F1 (b–d) was increased at 5 h, and 1–3 days post injury, and highly expressed by motor neurons. L. In intact spinal cord (a), CDK1/NeuN was detected in the motor neurons in the ventral horn. At 5 h after injury, immunoreactivity of CDK1 (b) was increased and sustained until 3 days post injury (c–d), and highly expressed by motor neurons. All images were taken at 2 mm rostral to epicenter. Scale bar = 500 mm for A–B, F–G. Scale bar = 100 mm for C–E, H–J, K–L. doi:10.1371/journal.pone.0042129.g003

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Expressing

Figure 4. E2F1 gene silencing down-regulates endogenous CDK1 expression in vitro. A. 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B. Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g004

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 4. E2F1 gene silencing down-regulates endogenous CDK1 expression in vitro. A. 27 mer siRNA duplexes for human E2F1 or trilencer-27 universal scrambled negative control siRNA duplex was transfected in the human neuroblastoma SH-SY5Y cells. Two days after transfection, the cells were harvested and subjected to western blotting using mouse monoclonal antibodies to E2F1 and CDK1. Transfection with shRNA against E2F1 resulted in reduction of E2F1 expression (58% to 66% of control), accompanied by 50% of reduction of CDK1 expression. B. Primary rat cerebral cortical neurons were transfected with shRNA against rat E2F1. E2F1 protein expression was robust reduced to 47% or 59% for shRNAs 1 and 2 respectively, and E2F1 knockdown resulted in reduction of CDK1 expression from 47% to 64% for shRNAs 1 and 2 respectively. N = 4 dishes from 3 independent culture. *P,0.05 vs sham group. doi:10.1371/journal.pone.0042129.g004

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Expressing, In Vitro, Negative Control, Transfection, Western Blot, Bioprocessing, shRNA, Control, Knockdown

Figure 5. Colocalization of E2F1/CDK1 upregulation with neuronal apoptosis in injured spinal cord. A–C. Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of a-fodrin after SCI. N = 4 rats/time points. *p,0.05 vs sham group. D. E2F1+ cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 mm. E. Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 mm for D(a–h) and 500 mm for D(i–l). doi:10.1371/journal.pone.0042129.g005

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 5. Colocalization of E2F1/CDK1 upregulation with neuronal apoptosis in injured spinal cord. A–C. Western blot analysis shows a significant increase in biochemical markers of apoptosis, active caspase-3 signal, as well as 145/150 kDa cleavage product of a-fodrin after SCI. N = 4 rats/time points. *p,0.05 vs sham group. D. E2F1+ cells were co-label with cleaved caspase 3 (yellow, arrow heads) in the gray matter at 2 mm rostral to the epicenter at 1 day after SCI. Scale bar = 100 mm. E. Coronal section in intact spinal cord (top panel) shows that CDK1 was expressed in the motor neurons in the ventral horn (VH). At 1 day after injury, immunoreactivity of CDK1 (middle panel, green) was increased, and highly expressed by apoptotic motor neurons (red), as shown at 2 mm rostral to epicenter. CDK1 was rarely expressed by inter-neurons in the dorsal horn (DH) after SCI (bottom panel). Scale bar = 100 mm for D(a–h) and 500 mm for D(i–l). doi:10.1371/journal.pone.0042129.g005

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Western Blot

Figure 6. E2F1/CDK1 expression is necessary for trophic deprivation-induced neuronal apoptosis. Rat cortical neurons were co- transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß- galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A. Neurons transfected with E2F1 vector (0.6 mg DNA/0.56106 neurons) increased basal apoptosis as compared to empty vector. B. Neurons transfected with CDK1 (0.8 mg DNA/0.56106

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 6. E2F1/CDK1 expression is necessary for trophic deprivation-induced neuronal apoptosis. Rat cortical neurons were co- transfected with expression plasmids for ß-galactosidase with, either empty vector or vector expressing E2F1 or CDK1 (A and B). Similarly, ß- galactosidase plasmid was co-transfected along with scrambled, E2F1 or CDK1 shRNAs (C, D and E) and the extent of apoptosis was examined 48 h after transfection, or after an additional 24 h of trophic deprivation (TD) induction post 48 h transfection. A. Neurons transfected with E2F1 vector (0.6 mg DNA/0.56106 neurons) increased basal apoptosis as compared to empty vector. B. Neurons transfected with CDK1 (0.8 mg DNA/0.56106

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Expressing, Transfection, Plasmid Preparation

Figure 7. Pharmacological inhibition of CDK1 blocks neuronal apoptosis. Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A. Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B. A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 mM; *p,0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 mM (***p,0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C. Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 mM; *p,0.001, vs. vehicle) and CR8 at concentrations as low as 1 mM (***p,0.001, vs. vehicle). doi:10.1371/journal.pone.0042129.g007

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 7. Pharmacological inhibition of CDK1 blocks neuronal apoptosis. Cortical neurons were pre-treated with Roscovitine or CR8 (CDK1 inhibitors) or vehicle and then exposed to TD-or campthotecin induced apoptosis. A. Representative photomicrographs of control and trophic deprived neurons treated with the indicated concentrations Roscovitine and CR8 are shown. Upper row presents phase contrast images (Healthy neurons are indicated by larger cell bodies and abundant processes; Apoptotic neurons display shrunken cell bodies and sparse or lost processes). Lower row shows chromatin staining with Hoechst 33258. Arrows and arrowheads indicate surviving and apoptotic neurons, respectively suggesting an attenuation of TD-induced neuronal death in neurons pre-treated with Roscovinine or CR8. B. A quantitative assessment of the percentage of nuclei featuring chromatin condensation demonstrates a significant attenuation of TD-induced apoptosis in neurons pre-treated with Roscovitine (10 mM; *p,0.05, vs. TD vehicle) whereas CR8 at concentrations as low as 1 mM (***p,0.001, vs. TD vehicle) almost completely blocked development of apoptotic features in neuronal nuclei. C. Significant attenuation of campthotecin-induced apoptosis in neurons pre-treated with Roscovitine (50 mM; *p,0.001, vs. vehicle) and CR8 at concentrations as low as 1 mM (***p,0.001, vs. vehicle). doi:10.1371/journal.pone.0042129.g007

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Inhibition, Control, Staining

Figure 8. CR8 administration reduces SCI-induced activation of the E2F1/CDK1 signaling pathway. Samples were obtained from rats exposed to spinal cord injury and CR8 treatment (1 mg/kg intraperitoneal administration) and analyzed by western blotting. Equal protein loading is demonstrated by consistent GAPDH levels. A. CR8 attenuated SCI mediated increase in E2F1 and its target cyclin A expression. B–C. Quantification of respective western blots in panel A. D. CR8 reduced SCI induced increase in phospho-(Ser54)-n-myc, phosphorylated CDK substrates and expression of cyclin B1. E–G. Quantification of respective western blots in panel E. H–J. Administration of CR8 significantly reduced Bim and c-Myb expression at 24 h after SCI. H shows representative Western blots for Bim, c-Myb, and the loading control, GAPDH. I and J show quantitative analysis of Bim and c- Myb expression. N = 4. *p,0.05 vs. vehicle group. doi:10.1371/journal.pone.0042129.g008

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 8. CR8 administration reduces SCI-induced activation of the E2F1/CDK1 signaling pathway. Samples were obtained from rats exposed to spinal cord injury and CR8 treatment (1 mg/kg intraperitoneal administration) and analyzed by western blotting. Equal protein loading is demonstrated by consistent GAPDH levels. A. CR8 attenuated SCI mediated increase in E2F1 and its target cyclin A expression. B–C. Quantification of respective western blots in panel A. D. CR8 reduced SCI induced increase in phospho-(Ser54)-n-myc, phosphorylated CDK substrates and expression of cyclin B1. E–G. Quantification of respective western blots in panel E. H–J. Administration of CR8 significantly reduced Bim and c-Myb expression at 24 h after SCI. H shows representative Western blots for Bim, c-Myb, and the loading control, GAPDH. I and J show quantitative analysis of Bim and c- Myb expression. N = 4. *p,0.05 vs. vehicle group. doi:10.1371/journal.pone.0042129.g008

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques: Activation Assay, Western Blot, Expressing, Control

Figure 9. SCI-induced immunoreactivity of E2F1 and CDK1 was attenuated by CR8 treatment. A. Coronal section in intact spinal cord (a– c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B. In intact spinal cord (a–c), CDK1/ NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 mm for C–F. doi:10.1371/journal.pone.0042129.g009

Journal: PloS one

Article Title: Inhibition of E2F1/CDK1 pathway attenuates neuronal apoptosis in vitro and confers neuroprotection after spinal cord injury in vivo.

doi: 10.1371/journal.pone.0042129

Figure Lengend Snippet: Figure 9. SCI-induced immunoreactivity of E2F1 and CDK1 was attenuated by CR8 treatment. A. Coronal section in intact spinal cord (a– c) shows that E2F1 was expressed in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of E2F1 (d–f) was increased, and highly expressed by motor neurons. The upregulation of E2F1 was clearly attenuated by CR8 treatment (g–i). B. In intact spinal cord (a–c), CDK1/ NeuN was detected in the motor neurons in the ventral horn. At 1 day after injury, immunoreactivity of CDK1 (d–f) was increased, and highly expressed by motor neurons. CDK1 upregulation was attenuated by CR8 treatment (g–i). All images were taken at 2 mm rostral to epicenter. Scale bar = 100 mm for C–F. doi:10.1371/journal.pone.0042129.g009

Article Snippet: 27 mer siRNA duplexes for human E2F1 (ID 1869), trilencer-27 universal scrambled negative control siRNA duplex (SR30004), constructs expressing 29 mer shRNAs against Rat Cdc2 and E2F1 in pGFPV-RS vectors were obtained from Origene Technologies Inc. Rat Neuron NucleofectorH Kit (VPG-1003) was purchased from Lonza.

Techniques:

FCHSD2 Is Not Directly Recruited to CCPs by PI3KC2α or Its Kinase Activity, Related to <xref ref-type=Figure 2 (A) Top: Transferrin uptake assay by flow cytometry comparing wild-type and FCHSD2 KO cells silenced for PI3KC2α. Uptake of Alexa488 labeled transferrin normalized by the amount of surface transferrin receptor for each condition and against uptake for the wild-type cells in each experiment. Each value represents median fluorescence from at least 5000 cells (n = 12, mean ± SD). ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. Bottom: Immunoblots showing PI3KC2α knockdown in wild-type and FCHSD2 KO cells. (B) Kymographs of HeLa FCHSD2-Venus stables silenced for PI3KC2α and control cells. Cells were transfected with mCherry-ClathrinLC 24 hs before imaging. Kymographs generated from 120 s movies at 1Hz. Note the elongated CCP lifetimes in PI3KC2α knockdown cells as described in Posor et al. (2013) . (C) Autoinhibition of FCHSD2. Representative images of a center slice from cells expressing different FCHSD2 truncation constructs and co-stained with phalloidin (Actin). The bar graph (upper right) shows the quantification of cellular protrusions/μm for each construct. The non-inhibited BAR domain produces many protrusions. Numbers inside bars represent number of cells measured. The line graph (bottom right) shows the fluorescence profile of sum intensity projections for cells expressing each construct. Due to the natural thinning of cells from their centers to the edge, a gradually decaying line indicates that the fluorescent protein is primarily cytosolic while a flat line with an abrupt fall on the cell edge indicates that the fluorescent protein is primarily bound to the membrane. While the presence of SH3-1 significantly reduces the generation of cellular protrusions generated by the FCHSD2 F-BAR, a significant fraction of the protein remains bound to the membrane (green line). Only the combined presence of SH3-1 and SH3-2 is capable to avoid promiscuous binding of the BAR domain to the membrane. Data is shown as mean ± SD in bar graph and as ± SEM in fluorescence profiles. ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. (D) Immunoblots for intersectin knockdown in FCHSD2-Venus HeLa cells. " width="100%" height="100%">

Journal: Cell

Article Title: A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-Coated Pits

doi: 10.1016/j.cell.2018.05.020

Figure Lengend Snippet: FCHSD2 Is Not Directly Recruited to CCPs by PI3KC2α or Its Kinase Activity, Related to Figure 2 (A) Top: Transferrin uptake assay by flow cytometry comparing wild-type and FCHSD2 KO cells silenced for PI3KC2α. Uptake of Alexa488 labeled transferrin normalized by the amount of surface transferrin receptor for each condition and against uptake for the wild-type cells in each experiment. Each value represents median fluorescence from at least 5000 cells (n = 12, mean ± SD). ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. Bottom: Immunoblots showing PI3KC2α knockdown in wild-type and FCHSD2 KO cells. (B) Kymographs of HeLa FCHSD2-Venus stables silenced for PI3KC2α and control cells. Cells were transfected with mCherry-ClathrinLC 24 hs before imaging. Kymographs generated from 120 s movies at 1Hz. Note the elongated CCP lifetimes in PI3KC2α knockdown cells as described in Posor et al. (2013) . (C) Autoinhibition of FCHSD2. Representative images of a center slice from cells expressing different FCHSD2 truncation constructs and co-stained with phalloidin (Actin). The bar graph (upper right) shows the quantification of cellular protrusions/μm for each construct. The non-inhibited BAR domain produces many protrusions. Numbers inside bars represent number of cells measured. The line graph (bottom right) shows the fluorescence profile of sum intensity projections for cells expressing each construct. Due to the natural thinning of cells from their centers to the edge, a gradually decaying line indicates that the fluorescent protein is primarily cytosolic while a flat line with an abrupt fall on the cell edge indicates that the fluorescent protein is primarily bound to the membrane. While the presence of SH3-1 significantly reduces the generation of cellular protrusions generated by the FCHSD2 F-BAR, a significant fraction of the protein remains bound to the membrane (green line). Only the combined presence of SH3-1 and SH3-2 is capable to avoid promiscuous binding of the BAR domain to the membrane. Data is shown as mean ± SD in bar graph and as ± SEM in fluorescence profiles. ∗∗∗ p > 0.001, ns = non-significant. One-way ANOVA with Tukey’s post hoc analysis. (D) Immunoblots for intersectin knockdown in FCHSD2-Venus HeLa cells.

Article Snippet: PI3KC2α siRNA pool , Origene , Cat# SR303516.

Techniques: Activity Assay, Flow Cytometry, Labeling, Fluorescence, Western Blot, Knockdown, Control, Transfection, Imaging, Generated, Expressing, Construct, Staining, Membrane, Binding Assay

Journal: Cell

Article Title: A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-Coated Pits

doi: 10.1016/j.cell.2018.05.020

Figure Lengend Snippet:

Article Snippet: PI3KC2α siRNA pool , Origene , Cat# SR303516.

Techniques: Virus, Recombinant, Labeling, Cloning, Stable Transfection, Expressing, esiRNA, Plasmid Preparation, Software

Figure 3. ACSL1 siRNA transfection reduced TNFα-mediated MMP-9 production. We transfected THP-1 monocytic cells with siRNA targeting human ACSL1 gene expression or scrambled siRNA (a control siRNA). (A,B) After 36 h, we performed real-time PCR to measure ACSL1 gene expression or western blotting for protein to test the knocking down efficiency. (C) We then incubated ACSL1-deficient cells with TNFα for 24 h. We determined mRNA expression of MMP-9 by real-time PCR. (D) We determined MMP-9 protein in culture media using ELISA. (E) The effect of siRNA transfection in combination with TNFα on cell viability was evaluated by measuring cell metabolic activity (MTT assay). The cell viability is expressed as the percentage of cells compared to the condition of vehicle control. Three independent experiments were performed with similar results. All data are expressed as mean ± SEM (n ≥ 3). t test or onene way ANOVA (Dunnett’s Test) for comparing treatments vs control) were used). **p < 0.01, ***p < 0.001.

Journal: Scientific reports

Article Title: TNFα induces matrix metalloproteinase-9 expression in monocytic cells through ACSL1/JNK/ERK/NF-kB signaling pathways.

doi: 10.1038/s41598-023-41514-6

Figure Lengend Snippet: Figure 3. ACSL1 siRNA transfection reduced TNFα-mediated MMP-9 production. We transfected THP-1 monocytic cells with siRNA targeting human ACSL1 gene expression or scrambled siRNA (a control siRNA). (A,B) After 36 h, we performed real-time PCR to measure ACSL1 gene expression or western blotting for protein to test the knocking down efficiency. (C) We then incubated ACSL1-deficient cells with TNFα for 24 h. We determined mRNA expression of MMP-9 by real-time PCR. (D) We determined MMP-9 protein in culture media using ELISA. (E) The effect of siRNA transfection in combination with TNFα on cell viability was evaluated by measuring cell metabolic activity (MTT assay). The cell viability is expressed as the percentage of cells compared to the condition of vehicle control. Three independent experiments were performed with similar results. All data are expressed as mean ± SEM (n ≥ 3). t test or onene way ANOVA (Dunnett’s Test) for comparing treatments vs control) were used). **p < 0.01, ***p < 0.001.

Article Snippet: We transfected the cells separately with siRNA against ACSL1 (30 nM; OriGene Technologies, Inc., Rockville, MD, USA), scramble siRNA (30 nM; OriGene Technologies, Inc., Rockville, MD, USA), and pmaxGFP (0.5 ug; Amaxa Nucleofector Kit V for THP-1cells, Lonza, Cologne, Germany).

Techniques: Transfection, Gene Expression, Control, Real-time Polymerase Chain Reaction, Western Blot, Incubation, Expressing, Enzyme-linked Immunosorbent Assay, Activity Assay, MTT Assay

The expression of HMGB1, TLR4, and RAGE proteins and mRNA in the spinal dorsal horn. (a) Diagram of the timeline of this experiment. (b-d) Images showing HMGB1 expression in the spinal dorsal horn of naïve rats (b) and rats receiving intrathecal (i.t.) injection of saline (c) and i.t. injection of morphine (d). (e-g) Images showing TLR4 expression in the spinal dorsal horn of naïve rats (e) and rats receiving i.t. injection of saline (f) and i.t. injection of morphine (g). (gh-j) The images showing RAGE expressed in spinal dorsal horn in rats of naïve rats (h) and rats receiving i.t. injection of saline (i) and i.t. injection of morphine (j). (k) Repeated intrathecal (i.t.) injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE proteins in the spinal dorsal horn. * P < 0.05, ** P < 0.01 vs. control group (i.t. injection of saline daily for 6 days). (l) Repeated i.t. injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE mRNA in the spinal dorsal horn. * P < 0.05, ** P < 0.01, *** P < 0.001 vs. saline group (i.t. injection of saline daily for 6 days). (m) Repeated subcutaneous (s.c.) injections of morphine caused increased expression of HMGB1 mRNA in the spinal dorsal horn of mice. * P < 0.05; ** P < 0.01 vs. control (s.c. saline daily for 9 days). Data are presented as the mean ± SEM and were analyzed with one-way ANOVA. Images in b-j, scale bar = 200 μm. Sa: saline

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The expression of HMGB1, TLR4, and RAGE proteins and mRNA in the spinal dorsal horn. (a) Diagram of the timeline of this experiment. (b-d) Images showing HMGB1 expression in the spinal dorsal horn of naïve rats (b) and rats receiving intrathecal (i.t.) injection of saline (c) and i.t. injection of morphine (d). (e-g) Images showing TLR4 expression in the spinal dorsal horn of naïve rats (e) and rats receiving i.t. injection of saline (f) and i.t. injection of morphine (g). (gh-j) The images showing RAGE expressed in spinal dorsal horn in rats of naïve rats (h) and rats receiving i.t. injection of saline (i) and i.t. injection of morphine (j). (k) Repeated intrathecal (i.t.) injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE proteins in the spinal dorsal horn. * P < 0.05, ** P < 0.01 vs. control group (i.t. injection of saline daily for 6 days). (l) Repeated i.t. injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE mRNA in the spinal dorsal horn. * P < 0.05, ** P < 0.01, *** P < 0.001 vs. saline group (i.t. injection of saline daily for 6 days). (m) Repeated subcutaneous (s.c.) injections of morphine caused increased expression of HMGB1 mRNA in the spinal dorsal horn of mice. * P < 0.05; ** P < 0.01 vs. control (s.c. saline daily for 9 days). Data are presented as the mean ± SEM and were analyzed with one-way ANOVA. Images in b-j, scale bar = 200 μm. Sa: saline

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Expressing, Injection, Saline, Control

The cell types that express HMGB1, TLR4, and RAGE in the rats spinal dorsal horn following repeated intrathecal (i.t.) injections of morphine. (a-c) Representative images showing that HMGB1 colocalized with the spinal neuronal marker NeuN (a), the astrocytic marker GFAP (b), and the microglial marker OX42 (c). (d-f) Representative images showing TLR4 colocalization with NeuN (d), GFAP (e), and OX42 (f). (g-i) Representative images showing RAGE colocalization with NeuN (g) and GFAP (h) but not with OX42 (i). Images in a-i, scale bar = 50 μm.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The cell types that express HMGB1, TLR4, and RAGE in the rats spinal dorsal horn following repeated intrathecal (i.t.) injections of morphine. (a-c) Representative images showing that HMGB1 colocalized with the spinal neuronal marker NeuN (a), the astrocytic marker GFAP (b), and the microglial marker OX42 (c). (d-f) Representative images showing TLR4 colocalization with NeuN (d), GFAP (e), and OX42 (f). (g-i) Representative images showing RAGE colocalization with NeuN (g) and GFAP (h) but not with OX42 (i). Images in a-i, scale bar = 50 μm.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Marker

Effects of morphine exposure on the expression and release of HMGB1 in primary cultured spinal neurons. (A) Diagram of the timeline of this experiment. (b-g) The cultured neuron purity was calculated by labeling neurons with the neuronal marker MAP2 and glial cells with GFAP (an astrocytic marker) and OX42 (a microglial marker). The images were merged in (d) and (g). Scale bar = 50 μm. (h-j) Representative images showing the colocalization of the neuronal marker NeuN (h) with the TLR4 protein (i) in cultured cells (j). (k-m) Images showing the neuronal marker NeuN (k) colocalized with TLR4 mRNA (i) in cultured cells (m). Images in h-m, scale bar = 50 μm. (n, o) Morphine exposure promoted the expression of HMGB1 in primary cultured spinal neurons in a dose- (neurons were cultured with different concentrations of morphine for 12 h) (n) and time- (neurons were cultured in medium containing 20 μM morphine for different amounts of time) (o) dependent manner. * P < 0.05; ** P < 0.0; *** P < 0.001 vs. control group. (p, q) Morphine challenge resulted in the increased release of HMGB1 from cultured neurons in a dose- (p) and time- (q) dependent manner. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. control group. Data are presented as the mean ± SEM and were analyzed with two-way ANOVA.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: Effects of morphine exposure on the expression and release of HMGB1 in primary cultured spinal neurons. (A) Diagram of the timeline of this experiment. (b-g) The cultured neuron purity was calculated by labeling neurons with the neuronal marker MAP2 and glial cells with GFAP (an astrocytic marker) and OX42 (a microglial marker). The images were merged in (d) and (g). Scale bar = 50 μm. (h-j) Representative images showing the colocalization of the neuronal marker NeuN (h) with the TLR4 protein (i) in cultured cells (j). (k-m) Images showing the neuronal marker NeuN (k) colocalized with TLR4 mRNA (i) in cultured cells (m). Images in h-m, scale bar = 50 μm. (n, o) Morphine exposure promoted the expression of HMGB1 in primary cultured spinal neurons in a dose- (neurons were cultured with different concentrations of morphine for 12 h) (n) and time- (neurons were cultured in medium containing 20 μM morphine for different amounts of time) (o) dependent manner. * P < 0.05; ** P < 0.0; *** P < 0.001 vs. control group. (p, q) Morphine challenge resulted in the increased release of HMGB1 from cultured neurons in a dose- (p) and time- (q) dependent manner. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. control group. Data are presented as the mean ± SEM and were analyzed with two-way ANOVA.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Expressing, Cell Culture, Labeling, Marker, Control

The role of the chronic i.t. morphine exposure-induced upregulation of HMGB1 in the spinal dorsal horn in the development of analgesic tolerance and hyperalgesia. (a) Diagram of the timeline of this experiment. (b) Repeated i.t. injections of morphine led to a significant reduction in morphine’s maximal possible analgesic effect (% MPAE). # P < 0.05; ## P < 0.01 vs. day one. Data are presented as the mean ± SEM and were analyzed by two-way ANOVA. Intrathecal coadministration of morphine (Mor) plus glycyrrhizin (GL), an inhibitor of HMGB1, dose-dependently prevented the decrease in the MPAE. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle (Veh) group (one-way ANOVA). (c, d) Chronic i.t. morphine exposure resulted in decreased paw withdrawal threshold (PWT) (c) and paw withdrawal latency (PWL) (d) in the left hind paw. ## P < 0.01 vs. baseline. Repeated intrathecal coinjections of morphine plus GL prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT and PWL were not changed by repeated i.t. injections of GL alone. (e) Repeated i.t. injections of morphine plus vehicle (Veh: transfection regent) or morphine plus scramble (sc) RNA resulted in significant reductions in the MPAE at day 5 and day 7. ## P < 0.01 vs. day one (two-way ANOVA). This effect was clearly prevented by the coadministration of morphine with HMGB1 siRNA intrathecally. ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle or morphine plus HMGB1 scRNA (one-way ANOVA). (f, g) Repeated i.t. injections of morphine plus vehicle or morphine plus HMGB1 scRNA led to significant decreases in PWT (f) and PWL (g) in the left hind paw, but these reductions were prevented by i.t. coinjections of morphine plus HMGB1 siRNA. # P < 0.05, ## P < 0.01 vs. baseline; * P < 0.05, ** P < 0.01 vs. morphine plus vehicle or morphine plus HMGB1 scRNA (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of HMGB1 siRNA or transfection regent alone. (h, i) Repeated i.t. coinjections of morphine plus vehicle or morphine plus HMGB1 scRNA led to significantly increased expression of the HMGB1 protein (h) and HMGB1 mRNA (i) in the spinal dorsal horn. These effects were inhibited by i.t. coadministration of morphine with HMGB1 siRNA. * P < 0.05, ** P < 0.01 vs. vehicle group; ### P < 0.001 vs. morphine plus vehicle or morphine plus scramble RNA (one-way ANOVA).

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The role of the chronic i.t. morphine exposure-induced upregulation of HMGB1 in the spinal dorsal horn in the development of analgesic tolerance and hyperalgesia. (a) Diagram of the timeline of this experiment. (b) Repeated i.t. injections of morphine led to a significant reduction in morphine’s maximal possible analgesic effect (% MPAE). # P < 0.05; ## P < 0.01 vs. day one. Data are presented as the mean ± SEM and were analyzed by two-way ANOVA. Intrathecal coadministration of morphine (Mor) plus glycyrrhizin (GL), an inhibitor of HMGB1, dose-dependently prevented the decrease in the MPAE. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle (Veh) group (one-way ANOVA). (c, d) Chronic i.t. morphine exposure resulted in decreased paw withdrawal threshold (PWT) (c) and paw withdrawal latency (PWL) (d) in the left hind paw. ## P < 0.01 vs. baseline. Repeated intrathecal coinjections of morphine plus GL prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT and PWL were not changed by repeated i.t. injections of GL alone. (e) Repeated i.t. injections of morphine plus vehicle (Veh: transfection regent) or morphine plus scramble (sc) RNA resulted in significant reductions in the MPAE at day 5 and day 7. ## P < 0.01 vs. day one (two-way ANOVA). This effect was clearly prevented by the coadministration of morphine with HMGB1 siRNA intrathecally. ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle or morphine plus HMGB1 scRNA (one-way ANOVA). (f, g) Repeated i.t. injections of morphine plus vehicle or morphine plus HMGB1 scRNA led to significant decreases in PWT (f) and PWL (g) in the left hind paw, but these reductions were prevented by i.t. coinjections of morphine plus HMGB1 siRNA. # P < 0.05, ## P < 0.01 vs. baseline; * P < 0.05, ** P < 0.01 vs. morphine plus vehicle or morphine plus HMGB1 scRNA (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of HMGB1 siRNA or transfection regent alone. (h, i) Repeated i.t. coinjections of morphine plus vehicle or morphine plus HMGB1 scRNA led to significantly increased expression of the HMGB1 protein (h) and HMGB1 mRNA (i) in the spinal dorsal horn. These effects were inhibited by i.t. coadministration of morphine with HMGB1 siRNA. * P < 0.05, ** P < 0.01 vs. vehicle group; ### P < 0.001 vs. morphine plus vehicle or morphine plus scramble RNA (one-way ANOVA).

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Tail Flick Test, Transfection, Expressing

The effects of repeated i.t. administration of glycyrrhizin (GL) and an HMGB1 neutralizing antibody on established morphine tolerance and hyperalgesia. (a) Diagram of the timeline of this experiment. (b-d) Repeated i.t. coinjections of morphine plus vehicle (saline) resulted in a significant decrease in the MPAE on day 7, day 9 and day 11. ### P < 0.001 vs. day one (two-way ANOVA) (b). This reduction was reversed by the i.t. coadministration of morphine with GL started at day 7. ** P < 0.01, *** P < 0.001 vs. morphine plus vehicle group (Student’s t-test). The morphine withdrawal-induced reductions in PWT (c) and PWL (d) in the left hind paw were also partially reversed in the morphine plus GL group. # P < 0.05, ### P < 0.001 vs. baseline. * P < 0.01, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of GL or saline alone. (e) The reduction in the MPAE induced by repeated i.t. injections of morphine were also partially reversed by the i.t. coinjection of morphine with an HMGB1 neutralizing antibody starting at day 7. * P < 0.05, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (f, g) Coadministration of morphine with an HMGB1 neutralizing antibody alleviated morphine withdrawal-induced mechanical allodynia (f) and thermal hyperalgesia (g). * P < 0.05 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of control IgG or ACSF alone. ACSF: artificial cerebrospinal fluid; Mor: morphine; Veh: vehicle.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The effects of repeated i.t. administration of glycyrrhizin (GL) and an HMGB1 neutralizing antibody on established morphine tolerance and hyperalgesia. (a) Diagram of the timeline of this experiment. (b-d) Repeated i.t. coinjections of morphine plus vehicle (saline) resulted in a significant decrease in the MPAE on day 7, day 9 and day 11. ### P < 0.001 vs. day one (two-way ANOVA) (b). This reduction was reversed by the i.t. coadministration of morphine with GL started at day 7. ** P < 0.01, *** P < 0.001 vs. morphine plus vehicle group (Student’s t-test). The morphine withdrawal-induced reductions in PWT (c) and PWL (d) in the left hind paw were also partially reversed in the morphine plus GL group. # P < 0.05, ### P < 0.001 vs. baseline. * P < 0.01, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of GL or saline alone. (e) The reduction in the MPAE induced by repeated i.t. injections of morphine were also partially reversed by the i.t. coinjection of morphine with an HMGB1 neutralizing antibody starting at day 7. * P < 0.05, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (f, g) Coadministration of morphine with an HMGB1 neutralizing antibody alleviated morphine withdrawal-induced mechanical allodynia (f) and thermal hyperalgesia (g). * P < 0.05 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT, and PWL were not changed by repeated i.t. injections of control IgG or ACSF alone. ACSF: artificial cerebrospinal fluid; Mor: morphine; Veh: vehicle.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Saline, Tail Flick Test, Control

The role of spinal HMGB1 in morphine tolerance and morphine withdrawal-induced hyperalgesia in female rats. (a) Repeated intrathecal (i.t.) injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE proteins in the spinal dorsal horn. * P < 0.05, ** P < 0.01 vs. control group (i.t. injection of saline daily for 6 days). (b) Intrathecal coadministration of morphine (Mor) plus glycyrrhizin (GL), an inhibitor of HMGB1, prevented the decrease in the MPAE. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle (Veh) group (one-way ANOVA). (c, d) Repeated intrathecal coinjections of morphine plus GL prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (e) The reduction in the MPAE induced by repeated i.t. injections of morphine were also partially reversed by the i.t. coinjection of morphine with an HMGB1 neutralizing antibody starting at day 7. * P < 0.05, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (f, g) Coadministration of morphine with an HMGB1 neutralizing antibody alleviated morphine withdrawal-induced mechanical allodynia (f) and thermal hyperalgesia (g). * P < 0.05 vs. morphine plus vehicle group (Student’s t-test). (h, i) All rats, male (h) and female (i) showed equivalent time in the pairing chambers prior to conditioning day. After rats received vehicle, clonidine, and GL i.t. injection, the times that spent in chambers between vehicle-, clonidine-, and GL-paired group were no reached statistical difference at testing day in male(h) and female rats (i).

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The role of spinal HMGB1 in morphine tolerance and morphine withdrawal-induced hyperalgesia in female rats. (a) Repeated intrathecal (i.t.) injections of morphine led to a significant increase in the expression of HMGB1, TLR4, and RAGE proteins in the spinal dorsal horn. * P < 0.05, ** P < 0.01 vs. control group (i.t. injection of saline daily for 6 days). (b) Intrathecal coadministration of morphine (Mor) plus glycyrrhizin (GL), an inhibitor of HMGB1, prevented the decrease in the MPAE. * P < 0.05; ** P < 0.01; *** P < 0.001 vs. morphine plus vehicle (Veh) group (one-way ANOVA). (c, d) Repeated intrathecal coinjections of morphine plus GL prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (e) The reduction in the MPAE induced by repeated i.t. injections of morphine were also partially reversed by the i.t. coinjection of morphine with an HMGB1 neutralizing antibody starting at day 7. * P < 0.05, ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). (f, g) Coadministration of morphine with an HMGB1 neutralizing antibody alleviated morphine withdrawal-induced mechanical allodynia (f) and thermal hyperalgesia (g). * P < 0.05 vs. morphine plus vehicle group (Student’s t-test). (h, i) All rats, male (h) and female (i) showed equivalent time in the pairing chambers prior to conditioning day. After rats received vehicle, clonidine, and GL i.t. injection, the times that spent in chambers between vehicle-, clonidine-, and GL-paired group were no reached statistical difference at testing day in male(h) and female rats (i).

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Expressing, Control, Injection, Saline

The signaling pathway involved in the morphine-mediated increase in the expression and release of HMGB1 in primary cultured spinal neurons. (a) Diagram of the timeline of this experiment. (b-e) The morphine plus vehicle-induced increased expression of HMGB1 in cultured spinal neurons was not blocked by the treatment of morphine plus CTOP (b) but was blocked by morphine plus TAK-242 (c), morphine plus naloxone (d), and morphine plus TLR4 siRNA (e). The concentration of morphine in the media was 20 μM, and the neurons were cultured for 12 hours. (f-i) The treatment of morphine plus CTOP in cultured spinal neurons did not reduce the morphine-stimulated increase in the release of HMGB1 (f). However, morphine plus TAK-242 (g), morphine plus naloxone (h), and morphine plus TLR4 siRNA (i) treatments resulted in significant reductions in the release of HMGB1 from cultured neurons. Compared to the normal control neurons (in which nothing was added to the media), the neurons treated with vehicle alone did not exhibit a change in the levels of HMGB1 released. * P < 0.05, ** P < 0.01 vs. control (Vehicle). # P < 0.05, ## P < 0.01 vs. morphine plus vehicle (Veh: b, c, d, f, g, and h: normal saline containing 10% DMSO; e and i: transfection regent). Data are presented as the mean ± SEM and were analyzed by one-way ANOVA. (j-m) Images showing the results of the cell death assay for cultured spinal neurons. (j) and (k) are the normal cultured neurons under different magnifications. (l) and (m) are the neurons treated with morphine and costained with Hoechst/propidium iodide (PI). Images in j scale bar = 100 μm; k-m scale bar = 50 μm.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: The signaling pathway involved in the morphine-mediated increase in the expression and release of HMGB1 in primary cultured spinal neurons. (a) Diagram of the timeline of this experiment. (b-e) The morphine plus vehicle-induced increased expression of HMGB1 in cultured spinal neurons was not blocked by the treatment of morphine plus CTOP (b) but was blocked by morphine plus TAK-242 (c), morphine plus naloxone (d), and morphine plus TLR4 siRNA (e). The concentration of morphine in the media was 20 μM, and the neurons were cultured for 12 hours. (f-i) The treatment of morphine plus CTOP in cultured spinal neurons did not reduce the morphine-stimulated increase in the release of HMGB1 (f). However, morphine plus TAK-242 (g), morphine plus naloxone (h), and morphine plus TLR4 siRNA (i) treatments resulted in significant reductions in the release of HMGB1 from cultured neurons. Compared to the normal control neurons (in which nothing was added to the media), the neurons treated with vehicle alone did not exhibit a change in the levels of HMGB1 released. * P < 0.05, ** P < 0.01 vs. control (Vehicle). # P < 0.05, ## P < 0.01 vs. morphine plus vehicle (Veh: b, c, d, f, g, and h: normal saline containing 10% DMSO; e and i: transfection regent). Data are presented as the mean ± SEM and were analyzed by one-way ANOVA. (j-m) Images showing the results of the cell death assay for cultured spinal neurons. (j) and (k) are the normal cultured neurons under different magnifications. (l) and (m) are the neurons treated with morphine and costained with Hoechst/propidium iodide (PI). Images in j scale bar = 100 μm; k-m scale bar = 50 μm.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Expressing, Cell Culture, Concentration Assay, Control, Saline, Transfection

Effects of TLR4/NF-κB signaling activation on the expression of HMGB1 in the spinal cord and the development of morphine tolerance and hyperalgesia. (a) Repeated i.t. coinjections of morphine with TAK-242 inhibited the phosphorylation of NF-κB p65 and reduced HMGB1 expression. (b) Repeated i.t. coinjections of morphine with PDTC reduced HMGB1 expression. Data shown in (a) and (b) are presented as the mean ± SEM and were analyzed by one-way ANOVA. * P < 0.05, ** P < 0.01 vs. control (i.t. saline containing 10% DMSO); # P < 0.05, ## P < 0.01 vs. morphine plus vehicle group. (c) Repeated i.t. coinjections of morphine plus TAK-242 dose-dependently prevented the decrease in morphine’s MPAE. ### P < 0.001 vs. day one (two-way ANOVA); * P < 0.05, ** P < 0.01, *** P < 0.001 vs. morphine plus vehicle group (one-way ANOVA). Repeated i.t. injections of saline or TAK-242 alone did not change the basal MPAE value. (d, e) Chronic i.t. morphine exposure resulted in decreased paw withdrawal threshold (PWT) (d) and paw withdrawal latency (PWL) (e) in the left hind paw. ## P < 0.01 vs. baseline. Repeated i.t. coinjections of morphine plus TAK-242 prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT and PWL were not changed by repeated i.t. injections of TAK-242 alone.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: Effects of TLR4/NF-κB signaling activation on the expression of HMGB1 in the spinal cord and the development of morphine tolerance and hyperalgesia. (a) Repeated i.t. coinjections of morphine with TAK-242 inhibited the phosphorylation of NF-κB p65 and reduced HMGB1 expression. (b) Repeated i.t. coinjections of morphine with PDTC reduced HMGB1 expression. Data shown in (a) and (b) are presented as the mean ± SEM and were analyzed by one-way ANOVA. * P < 0.05, ** P < 0.01 vs. control (i.t. saline containing 10% DMSO); # P < 0.05, ## P < 0.01 vs. morphine plus vehicle group. (c) Repeated i.t. coinjections of morphine plus TAK-242 dose-dependently prevented the decrease in morphine’s MPAE. ### P < 0.001 vs. day one (two-way ANOVA); * P < 0.05, ** P < 0.01, *** P < 0.001 vs. morphine plus vehicle group (one-way ANOVA). Repeated i.t. injections of saline or TAK-242 alone did not change the basal MPAE value. (d, e) Chronic i.t. morphine exposure resulted in decreased paw withdrawal threshold (PWT) (d) and paw withdrawal latency (PWL) (e) in the left hind paw. ## P < 0.01 vs. baseline. Repeated i.t. coinjections of morphine plus TAK-242 prevented the reduction in PWT and PWL after morphine withdrawal. * P < 0.05; ** P < 0.01 vs. morphine plus vehicle group (Student’s t-test). The basal tail-flick response, PWT and PWL were not changed by repeated i.t. injections of TAK-242 alone.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Activation Assay, Expressing, Phospho-proteomics, Control, Saline, Tail Flick Test

Signaling pathway of spinal HMGB1-mediated morphine tolerance and hyperalgesia. (a) Compared to morphine plus vehicle treatment, intrathecal administration of morphine with HMGB1 siRNA inhibited the increase in NF-κB p-p65 levels and the decrease in cytoplasmic IκB-α levels. However, p-p38 and p-JNK levels were not changed by this treatment. Data are presented as the mean ± SEM and were analyzed by one-way ANOVA. * P < 0.05, ** P < 0.01 vs. vehicle (Veh: transfection regent); # P < 0.05, ## P < 0.01 vs. morphine plus vehicle or morphine plus scramble (sc) RNA group. (b, c) A single i.t. injection of recombinant HMGB1 resulted in the increased expression of p-p65, TNF-α and IL-1β in the dorsal horn at 3 hours, which persisted to 6 hours after the injection (b). These effects were partially blocked by the coinjection of HMGB1 with TAK-242 (c). * P < 0.05, ** P < 0.01 vs. control (i.t. ACSF); # P < 0.05 vs. HMGB1 plus vehicle (Veh: ACSF). (d) A bolus i.t. coinjection of morphine with HMGB1 reduced the analgesic efficacy of morphine. * P < 0.05 vs. morphine plus ACSF group. (e-f) Bolus i.t. injection of HMGB1 led to a reduction in the paw withdrawal threshold (e) and paw withdrawal latency (f) in the left hind paw, which occurred at 3 hours and persisted to 6 hours after the injection. * P < 0.05 vs. baseline; # P < 0.05 vs. ACSF group. ACSF: artificial cerebrospinal fluid. Data of (d), (e), and (f) were analyzed by Student’s t-test.

Journal: Neurotherapeutics

Article Title: Chronic morphine-mediated upregulation of high mobility group box 1 in the spinal cord contributes to analgesic tolerance and hyperalgesia in rats

doi: 10.1007/s13311-019-00800-w

Figure Lengend Snippet: Signaling pathway of spinal HMGB1-mediated morphine tolerance and hyperalgesia. (a) Compared to morphine plus vehicle treatment, intrathecal administration of morphine with HMGB1 siRNA inhibited the increase in NF-κB p-p65 levels and the decrease in cytoplasmic IκB-α levels. However, p-p38 and p-JNK levels were not changed by this treatment. Data are presented as the mean ± SEM and were analyzed by one-way ANOVA. * P < 0.05, ** P < 0.01 vs. vehicle (Veh: transfection regent); # P < 0.05, ## P < 0.01 vs. morphine plus vehicle or morphine plus scramble (sc) RNA group. (b, c) A single i.t. injection of recombinant HMGB1 resulted in the increased expression of p-p65, TNF-α and IL-1β in the dorsal horn at 3 hours, which persisted to 6 hours after the injection (b). These effects were partially blocked by the coinjection of HMGB1 with TAK-242 (c). * P < 0.05, ** P < 0.01 vs. control (i.t. ACSF); # P < 0.05 vs. HMGB1 plus vehicle (Veh: ACSF). (d) A bolus i.t. coinjection of morphine with HMGB1 reduced the analgesic efficacy of morphine. * P < 0.05 vs. morphine plus ACSF group. (e-f) Bolus i.t. injection of HMGB1 led to a reduction in the paw withdrawal threshold (e) and paw withdrawal latency (f) in the left hind paw, which occurred at 3 hours and persisted to 6 hours after the injection. * P < 0.05 vs. baseline; # P < 0.05 vs. ACSF group. ACSF: artificial cerebrospinal fluid. Data of (d), (e), and (f) were analyzed by Student’s t-test.

Article Snippet: The HMGB1 small interfering RNA (siRNA) target rat hmgb1 was purchased from OriGene (OriGene Technologies, Rockville, SR506455).

Techniques: Transfection, Injection, Recombinant, Expressing, Control

Figure 1. Breast cancer–derived sclerostin inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control siRNA (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.

Journal: JCI insight

Article Title: Sclerostin inhibition alleviates breast cancer-induced bone metastases and muscle weakness.

doi: 10.1172/jci.insight.125543

Figure Lengend Snippet: Figure 1. Breast cancer–derived sclerostin inhibits Wnt signaling in osteoblasts. (A and B) Calvarial cells were differentiated into osteoblasts in the presence of control medium or cancer-conditioned medium (CM) collected from MDA-MB-231 metastatic breast cancer cells. Osteoblast differen- tiation was determined by quantification of Runx2 and osteocalcin (Ocn) gene expression (A) and by alizarin red S staining (B) (n = 4 independent experiments). (C) Calvarial osteoblasts were cultured in the presence of the indicated amount of MDA-MB-231–derived CM. Wnt signaling activity was determined by TOPflash reporter assay (n = 4 independent experiments). (D) Sclerostin mRNA expression was quantified in nonmetastatic MCF-7 and metastatic MDA-MB-231 breast cancer cells by qRT-PCR (n = 6 independent experiments). (E) SOST mRNA expression was analyzed in breast cancer tissue from 48 patients. Proportion of sclerostin-positive and sclerostin-negative tissue samples is shown for all patients and for triple-negative (ER–, PR–, HER–) and in hormone receptor–negative (ER–, PR–, HER+) patients. All, n = 48; ER–, PR–, HER-, n = 9; ER–, HER–, HER+, n = 7. (F) Wnt signaling activity in calvarial osteoblasts cultured with control medium or with CM from MDA-MB-231 cells transfected with scrambled control siRNA (si-Ctrl CM) or siRNA against sclerostin (si-Sclerostin CM) (n = 6 independent experiments). (G) Wnt signaling activity in calvarial osteoblasts isolated from mice heterozygous for the Lrp5 mutation G171V (Lrp5-G171V+/T) and from control littermates (Lrp5-G171V+/+) stimulated with control medium or cancer CM (n = 4 independent experiments). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (A and D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (C, F, and G); *P < 0.05, **P < 0.01, ***P < 0.001.

Article Snippet: MDA-MB-231 cells were transfected with scrambled control siRNA or siRNA against sclerostin (Origene) using Lipofectamine 3000 (Thermo Fisher Scientific) according to the manufacturer’s instructions.

Techniques: Derivative Assay, Control, Gene Expression, Staining, Cell Culture, Activity Assay, Reporter Assay, Expressing, Quantitative RT-PCR, Transfection, Isolation, Mutagenesis, Two Tailed Test

Figure 2. Pharmacological inhibition of sclerostin reduces bone metastatic burden in mice. MDA-MB-231 breast cancer cells stably expressing the lucifer- ase gene were injected into the left ventricle of 8-week-old female immune-compromised SCID mice. Micrometastases were detected 2 weeks after breast cancer cell injection by bioluminescence imaging (BLI). Mice were randomized and received either vehicle (n = 8) or anti-sclerostin antibody (Scl-Ab; n = 8) once a week for 4 weeks. (A and B) Tumor growth in bone was visualized after 4 weeks of treatment (A) and quantified (B) by BLI. Values are represented in a log10 scale. (C and D) Quantification of the metastasis area (C) in the tibia (D) of cancer-bearing mice treated with vehicle (n = 16 tibiae) or Scl-Ab (n = 16 tibiae) using histological sections. Scale bar: 1 mm. (E and F) Quantification of human leukocyte antigen (HLA) mRNA expression in the lung (E) and brain (F) by qRT-PCR (n = 8). (G) Kaplan-Meier survival curve of cancer-bearing mice treated with vehicle (n = 6) or Scl-Ab (n = 6). Data are presented as mean ± SEM. Two groups were compared using 2-tailed Student’s t test; *P < 0.05.

Journal: JCI insight

Article Title: Sclerostin inhibition alleviates breast cancer-induced bone metastases and muscle weakness.

doi: 10.1172/jci.insight.125543

Figure Lengend Snippet: Figure 2. Pharmacological inhibition of sclerostin reduces bone metastatic burden in mice. MDA-MB-231 breast cancer cells stably expressing the lucifer- ase gene were injected into the left ventricle of 8-week-old female immune-compromised SCID mice. Micrometastases were detected 2 weeks after breast cancer cell injection by bioluminescence imaging (BLI). Mice were randomized and received either vehicle (n = 8) or anti-sclerostin antibody (Scl-Ab; n = 8) once a week for 4 weeks. (A and B) Tumor growth in bone was visualized after 4 weeks of treatment (A) and quantified (B) by BLI. Values are represented in a log10 scale. (C and D) Quantification of the metastasis area (C) in the tibia (D) of cancer-bearing mice treated with vehicle (n = 16 tibiae) or Scl-Ab (n = 16 tibiae) using histological sections. Scale bar: 1 mm. (E and F) Quantification of human leukocyte antigen (HLA) mRNA expression in the lung (E) and brain (F) by qRT-PCR (n = 8). (G) Kaplan-Meier survival curve of cancer-bearing mice treated with vehicle (n = 6) or Scl-Ab (n = 6). Data are presented as mean ± SEM. Two groups were compared using 2-tailed Student’s t test; *P < 0.05.

Article Snippet: MDA-MB-231 cells were transfected with scrambled control siRNA or siRNA against sclerostin (Origene) using Lipofectamine 3000 (Thermo Fisher Scientific) according to the manufacturer’s instructions.

Techniques: Inhibition, Stable Transfection, Expressing, Injection, Imaging, Quantitative RT-PCR

Figure 4. Inhibition of sclerostin prevents breast cancer–induced loss of muscle function. (A) Specific force of the extensor digitorum longus (EDL) muscle from healthy mice without treatment (n = 5), or treated with vehicle (n = 10) or anti-sclerostin antibody (Scl-Ab, n = 10); and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). N, newtons. (B) Endurance of the EDL muscle of mice with bone metastases treated with vehicle (n = 8) or Scl-Ab (n = 8). max, maximum. (C) Succinate dehydroxygenase–stained (SDH-stained) tibialis anterior muscle sections from healthy mice without treatment or with vehicle or Scl-Ab treatment, as well as from mice with bone metastases treated with vehicle or Scl-Ab stained. Two representative muscles are shown per group. Scale bar: 50 μm. (D) Quantification of the cross-sectional area (CSA) of all muscle fibers, oxidative fibers, and nonoxida- tive fibers using SDH-stained muscle sections from healthy mice without treatment (n = 5), or with vehicle (n = 10) or Scl-Ab treatment (n = 10); and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). Data are presented as mean ± SEM. Three or more groups were compared using ANOVA followed by Tukey’s post hoc analysis; *P < 0.05, **P < 0.01, ***P < 0.001.

Journal: JCI insight

Article Title: Sclerostin inhibition alleviates breast cancer-induced bone metastases and muscle weakness.

doi: 10.1172/jci.insight.125543

Figure Lengend Snippet: Figure 4. Inhibition of sclerostin prevents breast cancer–induced loss of muscle function. (A) Specific force of the extensor digitorum longus (EDL) muscle from healthy mice without treatment (n = 5), or treated with vehicle (n = 10) or anti-sclerostin antibody (Scl-Ab, n = 10); and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). N, newtons. (B) Endurance of the EDL muscle of mice with bone metastases treated with vehicle (n = 8) or Scl-Ab (n = 8). max, maximum. (C) Succinate dehydroxygenase–stained (SDH-stained) tibialis anterior muscle sections from healthy mice without treatment or with vehicle or Scl-Ab treatment, as well as from mice with bone metastases treated with vehicle or Scl-Ab stained. Two representative muscles are shown per group. Scale bar: 50 μm. (D) Quantification of the cross-sectional area (CSA) of all muscle fibers, oxidative fibers, and nonoxida- tive fibers using SDH-stained muscle sections from healthy mice without treatment (n = 5), or with vehicle (n = 10) or Scl-Ab treatment (n = 10); and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). Data are presented as mean ± SEM. Three or more groups were compared using ANOVA followed by Tukey’s post hoc analysis; *P < 0.05, **P < 0.01, ***P < 0.001.

Article Snippet: MDA-MB-231 cells were transfected with scrambled control siRNA or siRNA against sclerostin (Origene) using Lipofectamine 3000 (Thermo Fisher Scientific) according to the manufacturer’s instructions.

Techniques: Inhibition, Staining, Muscles

Figure 5. Treatment with an anti-sclerostin antibody reverses breast cancer–induced activation of NF-κB signaling and increased number of Pax7-positive cells. (A) Immunoblot analysis of phosphorylated IKKα and IKKβ (p-IKKα and p-IKKβ), phosphorylated NF-κBp65 (p-NF-κBp65), phos- phorylated p38 (p-p38), and total p38 in the gastrocnemius (GAS) muscle of healthy nontreated mice (n = 5) and cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). Actin was used as loading control. Representative samples are shown. (B) Immunoblot analysis of phosphorylated NF-κBp65 (p-NF-κBp65), phosphorylated p38 (p-p38) and total p38 in C2C12 myoblasts stimulated with vehicle (veh) or TGF-β1. Actin was used as loading control. Representative image of 6 independent experiments is shown. (C) Immunoblot analysis of phosphorylated NF-κBp65, p-p38, and total p38 in C2C12 cells treated with a control peptide or an NF-κB blocking peptide (NPD) and stimulated with vehicle or TGF-β1. Actin was used as loading control. Representative image of 4 independent experiments is shown. (D) Myogenin and MyoD mRNA expression was quantified by qRT-PCR in C2C12 cells after 10 days of myogenic differentiation (n = 4). (E) Pai1 mRNA expression was quantified in the GAS muscle from healthy nontreat- ed mice (n = 5) and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). (F) Immunohistochemical staining of Pax7 in the tibialis anterior (TA) muscle from healthy nontreated mice and from mice with bone metastases treated with vehicle or Scl-Ab. Scale bar: 50 μm (top row) and 100 μm (bottom row). (G) Quantification of Pax7-positive cells in the TA muscle from healthy nontreated mice (n = 5) and from mice with bone metastases treated with vehicle (n = 8) or Scl-Ab (n = 8). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (E and G); *P < 0.05, ***P < 0.001.

Journal: JCI insight

Article Title: Sclerostin inhibition alleviates breast cancer-induced bone metastases and muscle weakness.

doi: 10.1172/jci.insight.125543

Figure Lengend Snippet: Figure 5. Treatment with an anti-sclerostin antibody reverses breast cancer–induced activation of NF-κB signaling and increased number of Pax7-positive cells. (A) Immunoblot analysis of phosphorylated IKKα and IKKβ (p-IKKα and p-IKKβ), phosphorylated NF-κBp65 (p-NF-κBp65), phos- phorylated p38 (p-p38), and total p38 in the gastrocnemius (GAS) muscle of healthy nontreated mice (n = 5) and cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). Actin was used as loading control. Representative samples are shown. (B) Immunoblot analysis of phosphorylated NF-κBp65 (p-NF-κBp65), phosphorylated p38 (p-p38) and total p38 in C2C12 myoblasts stimulated with vehicle (veh) or TGF-β1. Actin was used as loading control. Representative image of 6 independent experiments is shown. (C) Immunoblot analysis of phosphorylated NF-κBp65, p-p38, and total p38 in C2C12 cells treated with a control peptide or an NF-κB blocking peptide (NPD) and stimulated with vehicle or TGF-β1. Actin was used as loading control. Representative image of 4 independent experiments is shown. (D) Myogenin and MyoD mRNA expression was quantified by qRT-PCR in C2C12 cells after 10 days of myogenic differentiation (n = 4). (E) Pai1 mRNA expression was quantified in the GAS muscle from healthy nontreat- ed mice (n = 5) and from cancer-bearing mice treated with vehicle (n = 8) or Scl-Ab (n = 8). (F) Immunohistochemical staining of Pax7 in the tibialis anterior (TA) muscle from healthy nontreated mice and from mice with bone metastases treated with vehicle or Scl-Ab. Scale bar: 50 μm (top row) and 100 μm (bottom row). (G) Quantification of Pax7-positive cells in the TA muscle from healthy nontreated mice (n = 5) and from mice with bone metastases treated with vehicle (n = 8) or Scl-Ab (n = 8). Data are presented as mean ± SEM. Two-tailed Student’s t test was used to compare 2 groups (D), and ANOVA followed by Tukey’s post hoc analysis was used to compare 3 or more groups (E and G); *P < 0.05, ***P < 0.001.

Article Snippet: MDA-MB-231 cells were transfected with scrambled control siRNA or siRNA against sclerostin (Origene) using Lipofectamine 3000 (Thermo Fisher Scientific) according to the manufacturer’s instructions.

Techniques: Activation Assay, Western Blot, Control, Blocking Assay, Expressing, Quantitative RT-PCR, Immunohistochemical staining, Staining, Two Tailed Test

Journal: iScience

Article Title: Characterization and prognostic value of LXR splice variants in triple-negative breast cancer

doi: 10.1016/j.isci.2021.103212

Figure Lengend Snippet:

Article Snippet: siLXRβ , Origene , Cat. SR305039.

Techniques: Recombinant, Modification, Blocking Assay, Purification, Reverse Transcription, Control, Software, Sequencing, Plasmid Preparation