Journal: The Journal of Neuroscience

Article Title: Blockade of Astrocytic Calcineurin/NFAT Signaling Helps to Normalize Hippocampal Synaptic Function and Plasticity in a Rat Model of Traumatic Brain Injury

doi: 10.1523/jneurosci.1930-15.2016

Figure Lengend Snippet: Figure7. AAV-Gfa2-VIVITdoesnotalterGFAPorIba1levels,butcausesanincreaseinhevin levels.RepresentativeWesternblots(A,C)andmean SD.GFAPandIba1proteinlevels(B,D) in the contralateral and ipsilateral hippocampus of AAV-treated rats at 7 d after CCI. Note that both glial markers showed a significant increase in the hippocampus of the ipsilateral hemi- sphere, but were not significantly altered by pretreatment with AAV-Gfa2-VIVIT. #p 0.001 ipsilateralversuscontralateral,Fisher’sPLSD.n5–6rats,group.E–H,RepresentativeWest- ern blots (E, G) and mean SD SPARC and hevin protein levels (F, H) in the contralateral and ipsilateralhippocampusofAAV-treatedratsat7dafterCCI.Novirusorinjury-dependenteffects wereobservedforSPARC.Incontrast,hevinwassensitivetobothinjuryandAAVtreatment.In bothAAVgroups,hevinwaselevatedintheipsilateralrelativetothecontralateralhemisphere. OverallhevinlevelsweregreaterintheVIVIT-treatedgroupregardlessofhemisphere,butwere highest in the injured hemisphere. *p 0.05; #p 0.001 ipsilateral versus contralateral, Fisher’s LSD, n 5–6 rats.

Article Snippet: Westerns were performed with the following primary antibodies: GFAP (Cell Signaling Technology, catalog #3670S), Iba1 (Wako, catalog #019-19741), PSD-95 (Cell Signaling Technology, catalog #3450S), synapsin-1 (Cell Signaling Technology, catalog #6710S), GluR1 (Millipore, catalog #AB1504), NR2A (Millipore 07-632), NR2B (Millipore, catalog #05-920), CNA (Millipore, catalog #07-1492), GAPDH (Abcam, catalog #ab9484), hevin (R&D Systems, catalog #MAB2836), and SPARC (R&D Systems, catalog #MAB942).

Techniques:

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 1. Quantification of TSP-1, TSP-2, TNC, and SPARC mRNA expression in human fetal and adult adrenal glands. A, qRT-PCR was performed on RNA isolated from human fetal (14–23 wk, n 7) and adult adrenals (n 4). TSP-1 (open circle), TSP-2 (black triangle), TNC (X), and SPARC (black square) mRNA expression normalized to GUS, an endogenous control. The human adult brain serves as a positive control for expression of the matricellular proteins (values are shown on log scale). B, SPARC mRNA levels in fetal and adult adrenals. *, P 0.005. C, Western blot analysis of SPARC protein in human fetal and adult adrenals. Immunoblot was performed using tissue lysate of a 20-wk human fetal adrenal and human adult adrenal tissue lysate from a commercial source (Pierce). Protein (10 g/lane) was loaded in right two lanes. Human SPARC protein (10 ng) was used as a positive control (PC). Equal loading of protein was confirmed by probing for actin. Densitometric analysis showed 2.8-fold higher expression of SPARC protein in the fetal adrenal than the adult. The blot shown is representative of two experiments with similar results.

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Expressing, Quantitative RT-PCR, Isolation, Control, Positive Control, Western Blot

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 4. Effects of forskolin and 8-Br-cAMP on SPARC mRNA levels. FZ cells isolated from human fetal adrenals were exposed to forskolin (F; 1 M) or 8-Br-cAMP (Br; 1 mM) for 48 h. GUS-normalized data (mean SE) are from four independent experiments using different fetal adrenals. *, P 0.05, **, P 0.01 vs. unstimulated, time- matched controls (Co).

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Isolation

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 3. A, Dose-dependent effect of ACTH on SPARC and P450c17 mRNA levels. Isolated human fetal adrenal cortical cells (FZ cells) were treated with various concentrations of ACTH for 48 h. Total RNA was extracted and analyzed by qRT-PCR. Constitutively expressed GUS mRNA levels served as normalization controls. Data shown are mean SE of three independent experiments on cells derived from different fetuses. SPARC and P450c17 mRNA levels were increased after exposure to ACTH for 48 h in a dose-dependent manner (P 0.05 and P 0.01, respectively, based on Friedman’s ANOVA). B, Time- dependent effect of ACTH on SPARC mRNA levels. Isolated FZ cells (left panel) or DZ cells (right panel) were treated with ACTH (1 nM) for 24 or 48 h. Each bar represents mean SE of four independent experiments using different fetal adrenals. Black and white bars indicate ACTH-treated and time-matched, unstimulated control cells, respectively. *, P 0.05 vs. control (without ACTH treatment).

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Isolation, Quantitative RT-PCR, Derivative Assay, Control

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 2. SPARC protein expression in the human fetal adrenal gland. A, Immunofluorescence of a 22-wk gestation human fetal adrenal gland showing SPARC staining restricted to the FZ. Note the lack of staining in the narrow band corresponding to the DZ. B, Labeling for SPARC (red) and CD56 (green), a DZ cell marker, in a 21-wk human fetal adrenal gland, illustrating the lack of SPARC immunoreactivity in the DZ. C and D, Labeling for SPARC and LDL-R, a FZ cell marker, on an 18-wk human fetal adrenal gland, illustrating FZ-specific lo- calization of SPARC. Note costaining for LDL-R on the membrane (red) and SPARC protein (green) in the cytoplasm in FZ cells. Original magnification, 100 (A and C) and 200 (B and D).

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Expressing, Immunofluorescence, Staining, Labeling, Marker, Membrane

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 6. Zonal expression of mRNAs encoding SPARC, ACTH-R, LDL-R, and P450c17. Outer, DZ and inner, FZ cells in the midges- tation HFA (18–22 wk) were collected using laser capture microdis- section. Total RNA was extracted from cells of the respective zones and analyzed by qRT-PCR as described in Materials and Methods. GUS-normalized data are shown. SPARC, ACTH-R, LDL-R, and P450c17 mRNA levels were observed primarily in the FZ (black bars), compared with those of the DZ (white bars).

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Expressing, Quantitative RT-PCR

Journal: The Journal of clinical endocrinology and metabolism

Article Title: Differential zonal expression and adrenocorticotropin regulation of secreted protein acidic and rich in cysteine (SPARC), a matricellular protein, in the midgestation human fetal adrenal gland: implications for adrenal development.

doi: 10.1210/jc.2005-2514

Figure Lengend Snippet: FIG. 5. Western blot analysis of SPARC protein in cultured human fetal adrenal cortical cells (FZ cells) and conditioned medium. A, The cells were incubated with basal media or in the presence of different concentrations of ACTH (0.001–10 nM) for 48 h. Total cell protein was analyzed by immunoblot. Fifty micrograms of protein were loaded per lane. Data (mean SE) are the densitometric units of SPARC relative to actin from three experiments using different fetal adrenals. The relative ratio of unstimulated cells (control) is arbitrarily presented as 1. SPARC protein levels in cell lysates were increased after expo- sure to ACTH for 48 h in a dose-dependent manner (P 0.05, based on Kruskal-Wallis ANOVA). A representative blot from a 21-wk-old human fetal adrenal is shown above. B, Exposure to 8-Br-cAMP (Br; 1 mM) for 48 h increased abundance of SPARC protein in cell lysates (50 g protein/lane), mimicking the effects of ACTH (Ac; 1 nM). The summary of densitometric evaluation of three independent experi- ments is shown below. Data (mean SE) are the densitometric units of SPARC relative to actin, and the relative ratio of the control (Co; unstimulated cells) is arbitrarily presented as 1. A representative blot from a 19-wk-old human fetal adrenal is shown above. C, Exposure to 8-Br-cAMP (Br; 1 mM) for 48 h increased SPARC secretion into the conditioned medium, mimicking the effects of ACTH (Ac; 1 nM). Total protein (150 g protein) was loaded in each lane, and equal loading was confirmed by the Ponceau S staining. Densitometry is shown for three experiments using different fetal adrenals, with a representa- tive blot from a 22-wk-old human fetal adrenal. The relative ratio of the control (Co; unstimulated cells) is arbitrarily presented as 1. *, P 0.05, **, P 0.01, based on Mann-Whitney U test in comparison with respective control (unstimulated cells).

Article Snippet: Primary antibody incubation was performed with a 1:50 dilution of goat antihuman SPARC polyclonal antibody (R&D Systems, Minneapolis, MN), a combination of the anti-SPARC antibody and a 1:30 dilution of rabbit antihuman LDL-R (Research Diagnostics, Flanders, NJ), or a combination of the anti-SPARC antibody and 1:10 dilution of mouse anti-CD56 monoclonal antibody (Leu-19; BD Biosciences, San Jose, CA), for 1 h at room temperature.

Techniques: Western Blot, Cell Culture, Incubation, Control, Staining, MANN-WHITNEY, Comparison

Journal: Journal of cell science

Article Title: Autocrine control of glioma cells adhesion and migration through IRE1α-mediated cleavage of SPARC mRNA.

doi: 10.1242/jcs.099291

Figure Lengend Snippet: Fig. 7. IRE1a-mediated Sparc mRNA controls U87 architectural structure. (A) EV and DN_IRE1 cells were subjected to SPARC silencing by siRNA or non-target luciferase (GL2) silencing as a control. SPARC protein levels and FAK phosphorylation were evaluated by western blotting. Tubulin (Tub) was used as a loading control. (B,C). Relative quantification of SPARC protein levels and FAK phosphorylation. Values were normalized to tubulin levels. (D) EV and DN_IRE1 cells were subjected to SPARC silencing by siRNA or non-target luciferase (GL2) silencing as a control and were assessed for RhoA activation. (*P,0.05; **P,0.01).

Article Snippet: Antibodies against P-FAK and fibronectin were purchased from BD Transduction Laboratory (Oxford, UK), alpha-tubulin from Sigma (St Louis, MO, USA), RhoA from Santa Cruz Biotechnology (Santa Cruz, CA) and SPARC from Cell Signaling Technology (Danvers, MA).

Techniques: Luciferase, Control, Phospho-proteomics, Western Blot, Quantitative Proteomics, Activation Assay

Journal: Journal of cell science

Article Title: Autocrine control of glioma cells adhesion and migration through IRE1α-mediated cleavage of SPARC mRNA.

doi: 10.1242/jcs.099291

Figure Lengend Snippet: Fig. 9. Schematic representation of the mode of action of IRE1a signaling in gliomas leading to control of cell proliferation and migration. U87 wild-type cancer cells can still proliferate under challenging conditions through enhanced adaptability. In contrast, when IRE1a signaling is impaired, cell proliferation capacity is decreased, which is associated to the post- transcriptional derepression of Sparc mRNA expression (1 and 2). Secreted SPARC (3) will in turn, interact with the extracellular matrix (4) and consecutively enhanced cell migration, stress fiber formation and focal adhesion number through RhoA-dependent mechanisms (5). ECM, extracellular matrix; ER, endoplasmic reticulum; FA, focal adhesion.

Article Snippet: Antibodies against P-FAK and fibronectin were purchased from BD Transduction Laboratory (Oxford, UK), alpha-tubulin from Sigma (St Louis, MO, USA), RhoA from Santa Cruz Biotechnology (Santa Cruz, CA) and SPARC from Cell Signaling Technology (Danvers, MA).

Techniques: Control, Migration, Expressing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Expression levels of SPARCL1 in several types of cancer. (A) University of ALabama at Birmingham CANcer data analysis Portal database was used to analyze the expression levels of SPARCL1 in several types of pan-cancer tissues and their corresponding normal tissues. (B) Expression of SPARCL1 was significantly downregulated in breast cancer tissues compared with normal tissues. (C) Expression of the SPARCL1 protein in breast cancer. (D) Expression levels of SPARCL1 in breast cancer tissues were significantly lower than those in normal tissues, as indicated by the Gene Expression Profiling Interactive Analysis database. (E) SPARCL1 immunohistochemical staining performed on breast cancer and adjacent normal breast tissues (n=3). The intensity of the expressed protein is indicated by the brown coloration. *P<0.05. SPARCL1, secreted protein acidic and cysteine-rich like 1; TCGA, The Cancer Genome Atlas; CPTAC, Clinical Proteomic Tumor Analysis Consortium; TPM, transcripts per million; BRCA, breast cancer.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing, Gene Expression, Immunohistochemical staining, Staining

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Association between SPARCL1 expression and clinical pathological parameters. Using bc-GenExMiner v5.0 software, box plots were generated to demonstrate the associations between SPARCL1 expression and several clinical and pathological markers: (A) ER, (B) PR, (C) HER2, (D) ER/PR, (E) basal-like status, (F) TNBC status and (G) basal-like/TNBC status. (H) Reverse transcription-quantitative PCR was used to detect SPARCL1 expression in several breast cancer cell lines. (I) Overexpression assay for detection of the growth phenotype change after SPACLE1 overexpression in BT-549 cells. *P<0.05; **P<0.01; ***P<0.001. SPARCL1, secreted protein acidic and cysteine-rich like 1; ER, estrogen receptor; PR, progesterone receptor; HER2, human epidermal growth factor receptor 2; TNBC, triple-negative breast cancer; IHC, immunohistochemistry; RNA-seq, RNA-sequencing; OD, optical density.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing, Software, Generated, Reverse Transcription, Real-time Polymerase Chain Reaction, Over Expression, Immunohistochemistry, RNA Sequencing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Receiver operating characteristic curve analysis was used to assess the role of SPARCL1 in breast cancer clinical prognosis. False-positive rates are represented on the x-axis and true-positive rates are represented on the y-axis. SPARCL1, secreted protein acidic and cysteine-rich like 1; AUC, area under the curve.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques:

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Univariate Cox analysis for overall survival of patients with breast cancer.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Multivariate Cox analysis for overall survival of patients with breast cancer.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Association between breast cancer survival prognosis and SPARCL1 gene expression. (A) With the OncoLnc tool, the relationship between SPARCL1 expression and the prognosis of patients with breast cancer was analyzed. (B) Kaplan-Meier Plotter database was used to analyze survival data. (C) SPARCL1 survival analysis in triple negative breast cancer using the Gene Expression Profiling Interactive Analysis 2 database. SPARCL1, secreted protein acidic and cysteine-rich like 1; HR, hazard ratio.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Gene Expression, Expressing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Correlation between the levels of immune cell infiltration in breast cancer and the expression of SPARCL1. (A) Correlation between SPARCL1 expression and the level of immune infiltration in breast tumors. (B) Association between somatic copy number variations of SPARCL1 and the extent of immunological infiltrates. *P<0.05; **P<0.01; ***P<0.001. SPARCL1, secreted protein acidic and cysteine-rich like 1; BRCA, breast cancer; TPM, transcripts per million.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing

Journal: Oncology Letters

Article Title: Profile and clinical significance of SPARCL1 and its prognostic significance in breast cancer

doi: 10.3892/ol.2025.14942

Figure Lengend Snippet: Co-expression and mutational characteristics of SPARCL1 in breast cancer. (A) Pan-cancer frequency variations attributed to the mutation type of SPARCL1. (B) Frequency and nature of SPARCL1 genetic alterations identified in different subtypes of breast cancer. (C) Analysis of SPARCL1 mutations in breast cancer. Heat maps identifying the genes that exhibit (D) positive and (E) negative associations with SPARCL1 in breast cancer. (F) Relationship between SPARCL1 and LHFP expression and (G) SPARCL1 and AURKB expression in breast cancer, analyzed using the LinkedOmics database. SPARCL1, secreted protein acidic and cysteine-rich like 1; LHFP, lipoma HMGIC fusion partner; AURKB, Aurora kinase B.

Article Snippet: Goat anti-human MAST9 (SPARCL1) polyclonal antibodies (cat. no. AF2728; R&D Systems, Inc.) was used at a dilution of 1:100.

Techniques: Expressing, Mutagenesis

Journal: Cells

Article Title: In Vivo Effects of Bay 11-7082 on Fibroid Growth and Gene Expression: A Preclinical Study.

doi: 10.3390/cells13131091

Figure Lengend Snippet: Figure 3. Relative mRNA expression levels of SPARC, TDO2, MYD88, TLR6, TLR3, IL6, IL8, TNFα, TNFRSF11A, IL1β, COL3A1, FN1, LOX, TGFB3, CCND1, E2F1, CKS2, PRL, ESR1, PGR, VEGFC, PDGFA and HTR1B in subcutaneously implanted xenografts in ovariectomized CB-17 SCID/Beige mice (n = 10) following 8 weeks of treatment with vehicle or Bay 11-7082 (20 mg/kg/daily). Data are presented as mean ± SEM, with p values indicated on respective lines. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: Primary antibodies targeting COL3A1, FN1, SPARC, TDO2, and cleaved caspase-3 were purchased from Proteintech Group, Inc. (Chicago, IL, USA).

Techniques: Expressing

Journal: Cells

Article Title: In Vivo Effects of Bay 11-7082 on Fibroid Growth and Gene Expression: A Preclinical Study.

doi: 10.3390/cells13131091

Figure Lengend Snippet: Figure 4. (A) Representative Western blot analysis of COL3A1, FN1, SPARC, TDO2, and cleaved caspase 3, with corresponding bar graphs (B) showing their relative band densities in the xenografts (n = 10). (C) Total collagen levels assessed by enzyme-linked immunosorbent assay in the 10 xenografts. Data are presented as mean ± SEM of independent experiments, with p values indicated on the respective line. * p < 0.05; ** p < 0.01.

Article Snippet: Primary antibodies targeting COL3A1, FN1, SPARC, TDO2, and cleaved caspase-3 were purchased from Proteintech Group, Inc. (Chicago, IL, USA).

Techniques: Western Blot, Enzyme-linked Immunosorbent Assay

Journal: Cells

Article Title: In Vivo Effects of Bay 11-7082 on Fibroid Growth and Gene Expression: A Preclinical Study.

doi: 10.3390/cells13131091

Figure Lengend Snippet: Figure 6. Relative expression of SPARC, TDO2, MYD88, TLR6, TLR3, IL6, IL8, TNFα, TNFRSF11A, IL1β, COL3A1, FN1, LOX, TGFB3, CCND1, E2F1, CKS2, PRL, ESR1, PGR, VEGFC, PDGFA and HTR1B mRNA in fibroid explants (n = 4) following 48 h of treatment with vehicle or Bay 11-7082 (5 µM). The results are presented as mean ± SEM with p values indicated by corresponding lines. * p < 0.05; ** p < 0.01.

Article Snippet: Primary antibodies targeting COL3A1, FN1, SPARC, TDO2, and cleaved caspase-3 were purchased from Proteintech Group, Inc. (Chicago, IL, USA).

Techniques: Expressing

Journal: Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

Article Title: SPARCL1, a Novel Prognostic Predictive Factor for GI Malignancies: a Meta-Analysis.

doi: 10.1159/000485584

Figure Lengend Snippet: Fig. 5. The pooled OR of the association be tween SPARCL1 and GI malig nancies’ lymph nodes metasta sis.

Article Snippet: Goat polyclonal anti-human SPARCL1 IgG antibody (R&D Systems, Minnesota.

Techniques:

Journal: Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology

Article Title: SPARCL1, a Novel Prognostic Predictive Factor for GI Malignancies: a Meta-Analysis.

doi: 10.1159/000485584

Figure Lengend Snippet: Fig. 6. The pooled OR of the association between SPARCL1 and GI malignancies’ differentiation.

Article Snippet: Goat polyclonal anti-human SPARCL1 IgG antibody (R&D Systems, Minnesota.

Techniques: