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Santa Cruz Biotechnology pp2ac sirna
Pp2ac Sirna, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/pp2ac sirna/product/Santa Cruz Biotechnology
Average 90 stars, based on 1 article reviews

pp2ac sirna - by Bioz Stars, 2026-04

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PP2Ac expression in BMDM cells infected with M. bovis . ( A – C ) BMDM cells were infected with M. bovis (multiplicity of infection (MOI) 5, 10, 20 and 40) for 24 h. ( A , B ) Cell lysates were used for PP2Ac protein expression by Western blot (WB) assay. ( C ) Total RNA was extracted and the expression of PP2Acα at mRNA level was determined by quantitative real-time polymerase chain reaction (qRT-PCR). ( D , F ) BMDM cells were infected with M. bovis (MOI 1:10) for indicated time periods. ( D , E ) Cell lysates were used for the expression of PP2Ac protein level by WB. β-actin was used as loading control. ( F ) mRNA level of PP2Acα was determined by qRT-PCR. Data represent the mean ± standard deviation (SD) from three independent experiments. (hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: PP2Ac expression in BMDM cells infected with M. bovis . ( A – C ) BMDM cells were infected with M. bovis (multiplicity of infection (MOI) 5, 10, 20 and 40) for 24 h. ( A , B ) Cell lysates were used for PP2Ac protein expression by Western blot (WB) assay. ( C ) Total RNA was extracted and the expression of PP2Acα at mRNA level was determined by quantitative real-time polymerase chain reaction (qRT-PCR). ( D , F ) BMDM cells were infected with M. bovis (MOI 1:10) for indicated time periods. ( D , E ) Cell lysates were used for the expression of PP2Ac protein level by WB. β-actin was used as loading control. ( F ) mRNA level of PP2Acα was determined by qRT-PCR. Data represent the mean ± standard deviation (SD) from three independent experiments. (hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Expressing, Infection, Western Blot, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Control, Standard Deviation

PP2Ac expression in RAW264.7 cells infected with M. bovis . ( A – C ) RAW264.7 cells were infected with M. bovis (MOI 5, 10, 20 and 40) for 24 h. ( A , B ) Cell lysates were used for PP2Ac protein expression by WB assay. ( C ) Total RNA was extracted and the expression PP2Acα at mRNA level was determined by qRT-PCR. ( D , F ) RAW264.7 cells were infected with M. bovis (MOI 1:10) for indicated time period. ( D , E ) Cell lysates were used for the expression of PP2Ac protein by WB. β-actin was used as loading control. ( F ) The mRNA level of PP2Acα was determined by qRT-PCR. Data represent the mean ± SD from three independent experiments. (MOI stands for multiplicity of infection, hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: PP2Ac expression in RAW264.7 cells infected with M. bovis . ( A – C ) RAW264.7 cells were infected with M. bovis (MOI 5, 10, 20 and 40) for 24 h. ( A , B ) Cell lysates were used for PP2Ac protein expression by WB assay. ( C ) Total RNA was extracted and the expression PP2Acα at mRNA level was determined by qRT-PCR. ( D , F ) RAW264.7 cells were infected with M. bovis (MOI 1:10) for indicated time period. ( D , E ) Cell lysates were used for the expression of PP2Ac protein by WB. β-actin was used as loading control. ( F ) The mRNA level of PP2Acα was determined by qRT-PCR. Data represent the mean ± SD from three independent experiments. (MOI stands for multiplicity of infection, hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Expressing, Infection, Quantitative RT-PCR, Control

Targeting PP2Ac via tyrosine kinase inhibitor (TKI)-nilotinib in M. bovis infected macrophages. ( A – E ) BMDM cells were pretreated with TKI-nilotinib (0 µM or 10 µM) (DMSO 0.1% used as sample diluent control) for 2 h and then infected with M. bovis (MOI 1:10) for indicated time periods. The expression level of ( B ) PP2Ac, ( C ) p -AMPK and ( D ) p -ULK1 were evaluated by using WB and normalized to β-actin. ( E ) The relative expression of PP2Acα at mRNA level was determined by using qRT-PCR. ( F – J ) RAW264.7 cells were treated with TKI-nilotinib (0 µM and 10 µM) followed by M. bovis (MOI 1:10) infection for indicated time periods. The expression levels of ( F ) PP2Ac, ( G ) p -AMPK and ( H ) p -ULK1 cells lysates were determined by WB and normalized to β-actin. ( J ) The relative expression of PP2Acα at mRNA level was determined by using qRT-PCR. Data represent the mean ± SD from three independent experiments. (hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: Targeting PP2Ac via tyrosine kinase inhibitor (TKI)-nilotinib in M. bovis infected macrophages. ( A – E ) BMDM cells were pretreated with TKI-nilotinib (0 µM or 10 µM) (DMSO 0.1% used as sample diluent control) for 2 h and then infected with M. bovis (MOI 1:10) for indicated time periods. The expression level of ( B ) PP2Ac, ( C ) p -AMPK and ( D ) p -ULK1 were evaluated by using WB and normalized to β-actin. ( E ) The relative expression of PP2Acα at mRNA level was determined by using qRT-PCR. ( F – J ) RAW264.7 cells were treated with TKI-nilotinib (0 µM and 10 µM) followed by M. bovis (MOI 1:10) infection for indicated time periods. The expression levels of ( F ) PP2Ac, ( G ) p -AMPK and ( H ) p -ULK1 cells lysates were determined by WB and normalized to β-actin. ( J ) The relative expression of PP2Acα at mRNA level was determined by using qRT-PCR. Data represent the mean ± SD from three independent experiments. (hpi stands for hours post infection) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Infection, Control, Expressing, Quantitative RT-PCR

Upregulation of PP2Ac abrogates autophagy via modulating AMP-activated protein kinase (AMPK) activation during M. bovis infection. ( A ) BMDM cells were pretreated with okadaic acid (10 nM), TKI-nilotinib (10 µM) alone or okadaic acid + nilotinib followed by M. bovis (MOI 1:10) 24 h (DMSO 0.1% used as solvent control). The expression levels of ( B ) PP2Ac, ( C ) p -AMPK, ( D ) LC3-II, and ( E ) P62 were determined by WB and normalized against β-actin. Data represents the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments ) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: Upregulation of PP2Ac abrogates autophagy via modulating AMP-activated protein kinase (AMPK) activation during M. bovis infection. ( A ) BMDM cells were pretreated with okadaic acid (10 nM), TKI-nilotinib (10 µM) alone or okadaic acid + nilotinib followed by M. bovis (MOI 1:10) 24 h (DMSO 0.1% used as solvent control). The expression levels of ( B ) PP2Ac, ( C ) p -AMPK, ( D ) LC3-II, and ( E ) P62 were determined by WB and normalized against β-actin. Data represents the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments ) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Activation Assay, Infection, Solvent, Control, Expressing

Down-regulation of PP2Ac promotes autophagy via mediating AMPK activation during M. bovis infection. ( A ) BMDM cells were pretreated with forskolin (10 µM), TKI-nilotinib (10 µM) alone or forskolin + nilotinib followed by infection with M. bovis (MOI 1:10) 24 h (DMSO 0.1% used as solvent control). The expression levels of ( B ) PP2Ac, ( C ) p -AMPK, ( D ) LC3-II, and ( E ) P62 were determined by WB and normalized against β-actin. Data represents the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: Down-regulation of PP2Ac promotes autophagy via mediating AMPK activation during M. bovis infection. ( A ) BMDM cells were pretreated with forskolin (10 µM), TKI-nilotinib (10 µM) alone or forskolin + nilotinib followed by infection with M. bovis (MOI 1:10) 24 h (DMSO 0.1% used as solvent control). The expression levels of ( B ) PP2Ac, ( C ) p -AMPK, ( D ) LC3-II, and ( E ) P62 were determined by WB and normalized against β-actin. Data represents the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Activation Assay, Infection, Solvent, Control, Expressing

PP2Ac promotes intracellular survival of M. bovis in murine macrophages. ( A ) PP2Ac protein level was determined by WB from BMDMs transfected with 50 µM SiRNA negative control and SiRNA PP2Ac for 36 h. ( B ) BMDMs were transfected with 50 µM SiRNA negative control and SiRNA PP2Ac and treated or untreated with TKI-nilotinib (10 µM) followed by infection with M. bovis for 24 h. The expression levels of ( C ) p -AMPK, ( D ) LC3-II and ( E ) P62 were determined by WB and normalized against β-actin. ( F ) The colocalization of LC3 with M. bovis was determined by confocal microscopy. ( G ) The colocalization % of LC3 was calculated by image-J software. ( H ) BMDMs were transfected with 50 µM SiRNA negative control and SiRNA PP2Ac and treated or untreated with nilotinib (10 µM) followed by infection with M. bovis for 24 h. A colony-forming unit (CFU) assay was performed for enumeration of total viable M. bovis bacilli. Data represent the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments ) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Journal: International Journal of Molecular Sciences

Article Title: PP2Ac Modulates AMPK-Mediated Induction of Autophagy in Mycobacterium bovis -Infected Macrophages

doi: 10.3390/ijms20236030

Figure Lengend Snippet: PP2Ac promotes intracellular survival of M. bovis in murine macrophages. ( A ) PP2Ac protein level was determined by WB from BMDMs transfected with 50 µM SiRNA negative control and SiRNA PP2Ac for 36 h. ( B ) BMDMs were transfected with 50 µM SiRNA negative control and SiRNA PP2Ac and treated or untreated with TKI-nilotinib (10 µM) followed by infection with M. bovis for 24 h. The expression levels of ( C ) p -AMPK, ( D ) LC3-II and ( E ) P62 were determined by WB and normalized against β-actin. ( F ) The colocalization of LC3 with M. bovis was determined by confocal microscopy. ( G ) The colocalization % of LC3 was calculated by image-J software. ( H ) BMDMs were transfected with 50 µM SiRNA negative control and SiRNA PP2Ac and treated or untreated with nilotinib (10 µM) followed by infection with M. bovis for 24 h. A colony-forming unit (CFU) assay was performed for enumeration of total viable M. bovis bacilli. Data represent the mean ± SD from three independent experiments. (“−“refers the untreated group and “+” refers the treated group for the mentioned treatments ) (* p < 0.05, ** p < 0.01, *** p < 0.001).

Article Snippet: SiRNA-NC (SC-37007), and SiRNA PP2Ac (SC-36302) were purchased from Santa cruz biotechnology (Paso Robles, CA, USA).

Techniques: Transfection, Negative Control, Infection, Expressing, Confocal Microscopy, Software, Colony-forming Unit Assay

Journal: Frontiers in Pharmacology

Article Title: Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

doi: 10.3389/fphar.2018.00682

Figure Lengend Snippet: Primary antibodies used in this study.

Article Snippet: HEK-293T cells were transfected with human tau40 plasmid together with human PP2Ac siRNA (QIAGEN, Hilden, Germany).

Techniques: Methylation

Cornel iridoid glycoside inhibits GSK-3β through decreasing PP2Ac demethylation to suppress tau hyperphosphorylation. (A,B) The phosphorylation at different sits of tau protein in HEK-293T cells transfected with wild type GSK-3β plasmid together with human tau40 plasmid was detected by western blotting assay. CIG at different doses was incubated with transfected cells for 24 h. (C,D) The levels of GSK-3β and phosphorylated GSK-3β at Ser9 site in GSK-3β-transfected cells. (E,F) Quantitative analysis of AKT and phosphorylated AKT at Ser473 in the cells transfected with GSK-3β plasmid. (G,H) The levels of PP2A catalytic C subunit (PP2Ac) and demethylated PP2Ac (dm-PP2Ac) at Leu309 site in cells transfected with GSK-3β plasmid. (I,J) The levels of PP2Ac and dm-PP2Ac at Leu309 in the hippocampus of rats intraventricularly injected with wortmannin/GFX. (K,L) The levels of GSK-3β and phosphorylated GSK-3β at Ser9 in HEK-293T cells transfected with PP2Ac siRNA. GAPDH was used as an internal control, and the expression level of control group was set as 100%. We detected p-tau and PP2Ac in the same electrophoresis and on the same membrane using different antibodies, and used the same loading control GAPDH in (A,G) . Data are present as mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group. WTM, wortmannin; GFX, GF-109203X; MEM, memantine, 3 mg/kg.

Journal: Frontiers in Pharmacology

Article Title: Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

doi: 10.3389/fphar.2018.00682

Figure Lengend Snippet: Cornel iridoid glycoside inhibits GSK-3β through decreasing PP2Ac demethylation to suppress tau hyperphosphorylation. (A,B) The phosphorylation at different sits of tau protein in HEK-293T cells transfected with wild type GSK-3β plasmid together with human tau40 plasmid was detected by western blotting assay. CIG at different doses was incubated with transfected cells for 24 h. (C,D) The levels of GSK-3β and phosphorylated GSK-3β at Ser9 site in GSK-3β-transfected cells. (E,F) Quantitative analysis of AKT and phosphorylated AKT at Ser473 in the cells transfected with GSK-3β plasmid. (G,H) The levels of PP2A catalytic C subunit (PP2Ac) and demethylated PP2Ac (dm-PP2Ac) at Leu309 site in cells transfected with GSK-3β plasmid. (I,J) The levels of PP2Ac and dm-PP2Ac at Leu309 in the hippocampus of rats intraventricularly injected with wortmannin/GFX. (K,L) The levels of GSK-3β and phosphorylated GSK-3β at Ser9 in HEK-293T cells transfected with PP2Ac siRNA. GAPDH was used as an internal control, and the expression level of control group was set as 100%. We detected p-tau and PP2Ac in the same electrophoresis and on the same membrane using different antibodies, and used the same loading control GAPDH in (A,G) . Data are present as mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group. WTM, wortmannin; GFX, GF-109203X; MEM, memantine, 3 mg/kg.

Article Snippet: HEK-293T cells were transfected with human tau40 plasmid together with human PP2Ac siRNA (QIAGEN, Hilden, Germany).

Techniques: Transfection, Plasmid Preparation, Western Blot, Incubation, Injection, Expressing, Electrophoresis

Cornel iridoid glycoside enhances PP2A activity through inhibiting PP2Ac demethylation directly. (A) The morphological changes of human neuroblastoma SK-N-SH cells exposed to okadaic acid (OA) at the dose of 20 nM for 6 h were observed under contrast microscope (Scale bar = 50 μm). CIG at different doses was preincubated with cells for 24 h. (B,C) The phosphorylation of different sites of tau protein in OA-induced model cells was detected by western blotting assay. (D) The activity of PP2A was measured by a biochemical assay ( n = 6 each group). (E,F) The levels of PP2Ac and demethylated PP2Ac (dm-PP2Ac) at Leu309 site were detected by western blotting. (G,H) The level of PP2Ac in HEK-293 cells transfected with PP2Ac siRNA. CIG was incubated with transfected cells for 24 h. (I,J) The phosphorylation of tau protein in PP2Ac siRNAc-transfected cells. GAPDH was used as an internal control, and the expression level of control group was set as 100%. We detected p-tau and PP2Ac in the same electrophoresis and on the same membrane using different antibodies, and used the same loading control GAPDH in (B,E) . Data represent mean ± SD; n = 3–4 each group. #P < 0.05, ##P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group.

Journal: Frontiers in Pharmacology

Article Title: Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

doi: 10.3389/fphar.2018.00682

Figure Lengend Snippet: Cornel iridoid glycoside enhances PP2A activity through inhibiting PP2Ac demethylation directly. (A) The morphological changes of human neuroblastoma SK-N-SH cells exposed to okadaic acid (OA) at the dose of 20 nM for 6 h were observed under contrast microscope (Scale bar = 50 μm). CIG at different doses was preincubated with cells for 24 h. (B,C) The phosphorylation of different sites of tau protein in OA-induced model cells was detected by western blotting assay. (D) The activity of PP2A was measured by a biochemical assay ( n = 6 each group). (E,F) The levels of PP2Ac and demethylated PP2Ac (dm-PP2Ac) at Leu309 site were detected by western blotting. (G,H) The level of PP2Ac in HEK-293 cells transfected with PP2Ac siRNA. CIG was incubated with transfected cells for 24 h. (I,J) The phosphorylation of tau protein in PP2Ac siRNAc-transfected cells. GAPDH was used as an internal control, and the expression level of control group was set as 100%. We detected p-tau and PP2Ac in the same electrophoresis and on the same membrane using different antibodies, and used the same loading control GAPDH in (B,E) . Data represent mean ± SD; n = 3–4 each group. #P < 0.05, ##P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group.

Article Snippet: HEK-293T cells were transfected with human tau40 plasmid together with human PP2Ac siRNA (QIAGEN, Hilden, Germany).

Techniques: Activity Assay, Microscopy, Western Blot, Transfection, Incubation, Expressing, Electrophoresis

Cornel iridoid glycoside inhibits demethylation of PP2Ac via decreasing PME-1. (A,B) The expression of PME-1 and LCMT-1 in OA-treated SK-N-SH cells, and the ratio of PME-1/LCMT-1. (C,D) The expression of PME-1 in mouse neuroblastoma N2a cells transduced with PME-1 genetic materials delivered by recombined lentivirus vector. CIG was incubated with the transduced cells for 24 h. (E,F) The expression of LCMT-1 in N2a cells transduced with PME-1 genetic materials. (G,H) The expression of demethylated PP2Ac (dm-PP2Ac) and methylated PP2Ac (m-PP2Ac). (I) The activity of PP2A measured by a biochemical assay, n = 6 per group. (J,K) The phosphorylation of tau at Thr217 (pT217). GAPDH was used as an internal control, and the expression level of control group was set as 100%. Data are expressed as mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group.

Journal: Frontiers in Pharmacology

Article Title: Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

doi: 10.3389/fphar.2018.00682

Figure Lengend Snippet: Cornel iridoid glycoside inhibits demethylation of PP2Ac via decreasing PME-1. (A,B) The expression of PME-1 and LCMT-1 in OA-treated SK-N-SH cells, and the ratio of PME-1/LCMT-1. (C,D) The expression of PME-1 in mouse neuroblastoma N2a cells transduced with PME-1 genetic materials delivered by recombined lentivirus vector. CIG was incubated with the transduced cells for 24 h. (E,F) The expression of LCMT-1 in N2a cells transduced with PME-1 genetic materials. (G,H) The expression of demethylated PP2Ac (dm-PP2Ac) and methylated PP2Ac (m-PP2Ac). (I) The activity of PP2A measured by a biochemical assay, n = 6 per group. (J,K) The phosphorylation of tau at Thr217 (pT217). GAPDH was used as an internal control, and the expression level of control group was set as 100%. Data are expressed as mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model group.

Article Snippet: HEK-293T cells were transfected with human tau40 plasmid together with human PP2Ac siRNA (QIAGEN, Hilden, Germany).

Techniques: Expressing, Transduction, Plasmid Preparation, Incubation, Methylation, Activity Assay

Cornel iridoid glycoside inhibits demethylation of PP2Ac not entirely dependent on LCMT-1. (A,B) The expression of LCMT-1 in LCMT-1 siRNA-transfected HEK-293T cells detected by western blotting assay. CIG was incubated with the transfected cells for 24 h. (C,D) The expression of demethylated PP2Ac (dm-PP2Ac) and methylated PP2Ac (m-PP2Ac) in the transfected cells. (E) The activity of PP2A measured by a biochemical assay, n = 6 each group. (F,G) The phosphorylation of tau at Thr217 (pT217). GAPDH was used as an internal control, and the expression level of control group was set as 100%. Data represent mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model cells.

Journal: Frontiers in Pharmacology

Article Title: Cornel Iridoid Glycoside Inhibits Tau Hyperphosphorylation via Regulating Cross-Talk Between GSK-3β and PP2A Signaling

doi: 10.3389/fphar.2018.00682

Figure Lengend Snippet: Cornel iridoid glycoside inhibits demethylation of PP2Ac not entirely dependent on LCMT-1. (A,B) The expression of LCMT-1 in LCMT-1 siRNA-transfected HEK-293T cells detected by western blotting assay. CIG was incubated with the transfected cells for 24 h. (C,D) The expression of demethylated PP2Ac (dm-PP2Ac) and methylated PP2Ac (m-PP2Ac) in the transfected cells. (E) The activity of PP2A measured by a biochemical assay, n = 6 each group. (F,G) The phosphorylation of tau at Thr217 (pT217). GAPDH was used as an internal control, and the expression level of control group was set as 100%. Data represent mean ± SD; n = 3–4 each group. # P < 0.05, ## P < 0.01, the model group compared with the control group; ∗ P < 0.05, ∗∗ P < 0.01, drug groups compared with the model cells.

Article Snippet: HEK-293T cells were transfected with human tau40 plasmid together with human PP2Ac siRNA (QIAGEN, Hilden, Germany).

Techniques: Expressing, Transfection, Western Blot, Incubation, Methylation, Activity Assay

p38 targets distinct phosphorylation sites of TSC2 in different CRC cell lines. A. WT , TSC1 −/− or TSC2 −/− MEF cells were treated with 10 μM SB202190 for 2 h and analyzed for P-S6K1 and P-S6 by immunoblot. B. CRC cells were transfected with two different TSC1 or TSC2 siRNAs, and then treated with 10 μM SB202190 for 2 h. TSC1, TSC2 and P-S6K1(T389) were analyzed by immunoblot. C. CRC cells were transfected with two different TSC1 or TSC2 siRNAs, and then treated with 10 μM SB202190 for 48 h. Cell growth was measured by SRB assay and expressed as percentage of SB202190/control (DMSO). Data represent means ± s.d. from three independent triplicate experiments. *P < 0.01 versus NC. D. Drug-sensitive CACO2, SW480 and RKO cells, and drug-resistant HCT116, SW620 and SW1116 cells were treated with 10 μM SB202190 for 2 h and analyzed for phosphorylation of TSC2 at S664, S1254, T1462 and S1798 by immunoblot. Boxed area highlights the different effects of SB202190 on TSC2 phosphorylation in drug-sensitive versus -resistant CRC cells. SE, short exposure, LE, long exposure. E. HCT116 and SW620 cells were treated with 10 μM SB202190 with or without Mek inhibitors 30 μM PD98059 or 10 μM U0126 for 2 h, and then analyzed for phosphorylation of TSC2, ERK, RSK, S6K1 and S6 by immunoblot.

Journal: EBioMedicine

Article Title: PP2AC Level Determines Differential Programming of p38-TSC-mTOR Signaling and Therapeutic Response to p38-Targeted Therapy in Colorectal Cancer

doi: 10.1016/j.ebiom.2015.11.031

Figure Lengend Snippet: p38 targets distinct phosphorylation sites of TSC2 in different CRC cell lines. A. WT , TSC1 −/− or TSC2 −/− MEF cells were treated with 10 μM SB202190 for 2 h and analyzed for P-S6K1 and P-S6 by immunoblot. B. CRC cells were transfected with two different TSC1 or TSC2 siRNAs, and then treated with 10 μM SB202190 for 2 h. TSC1, TSC2 and P-S6K1(T389) were analyzed by immunoblot. C. CRC cells were transfected with two different TSC1 or TSC2 siRNAs, and then treated with 10 μM SB202190 for 48 h. Cell growth was measured by SRB assay and expressed as percentage of SB202190/control (DMSO). Data represent means ± s.d. from three independent triplicate experiments. *P < 0.01 versus NC. D. Drug-sensitive CACO2, SW480 and RKO cells, and drug-resistant HCT116, SW620 and SW1116 cells were treated with 10 μM SB202190 for 2 h and analyzed for phosphorylation of TSC2 at S664, S1254, T1462 and S1798 by immunoblot. Boxed area highlights the different effects of SB202190 on TSC2 phosphorylation in drug-sensitive versus -resistant CRC cells. SE, short exposure, LE, long exposure. E. HCT116 and SW620 cells were treated with 10 μM SB202190 with or without Mek inhibitors 30 μM PD98059 or 10 μM U0126 for 2 h, and then analyzed for phosphorylation of TSC2, ERK, RSK, S6K1 and S6 by immunoblot.

Article Snippet: siRNA for human PP2AC, TSC1 and TSC2 were designed and synthesized by OriGene Technologies (MD, USA).

Techniques: Phospho-proteomics, Western Blot, Transfection, Sulforhodamine B Assay, Control

PP2AC determines differential programming of p38-to-mTORC1 signaling. A. The protein level of PP2A-A, PP2A-B and PP2A-C in different CRC cells as analyzed by immunoblot. B. HCT116 cells were transfected with four different PP2AC siRNAs (1, 2, 3 and 4), and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, MK2, ERK and RSK was analyzed by immunoblot. C. SW620 cells were transfected with four different PP2AC siRNAs (1, 2, 3 and 4), and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, S6, MK2, ERK and RSK was analyzed by immunoblot. D. RKO and SW480 cells were transfected with PP2AC plasmid and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, S6, MK2, ERK and RSK was analyzed by immunoblot. E. Effect of p38i on ERK-PP2AC interaction in sensitive and resistant CRC cells. HCT116, SW620, SW480 and RKO cells were treated without or with 10 μM SB202190 for 2 h. Endogenous PP2AC was immunoprecipitated with a PP2AC-specific antibody and analyzed for binding to ERK by Western blot. F. Immunohistochemistry (IHC) staining of primary human CRC tissue microarray. Shown are staining of tumor tissue sections (400 ×) representative of high PP2AC, medium PP2AC and low PP2AC staining. G. PP2AC is differentially expressed in CRC. Scatter plot shows PP2AC staining level in individual tumor as H-score.

Journal: EBioMedicine

Article Title: PP2AC Level Determines Differential Programming of p38-TSC-mTOR Signaling and Therapeutic Response to p38-Targeted Therapy in Colorectal Cancer

doi: 10.1016/j.ebiom.2015.11.031

Figure Lengend Snippet: PP2AC determines differential programming of p38-to-mTORC1 signaling. A. The protein level of PP2A-A, PP2A-B and PP2A-C in different CRC cells as analyzed by immunoblot. B. HCT116 cells were transfected with four different PP2AC siRNAs (1, 2, 3 and 4), and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, MK2, ERK and RSK was analyzed by immunoblot. C. SW620 cells were transfected with four different PP2AC siRNAs (1, 2, 3 and 4), and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, S6, MK2, ERK and RSK was analyzed by immunoblot. D. RKO and SW480 cells were transfected with PP2AC plasmid and then treated with 10 μM SB202190 for 2 h. Phosphorylation of TSC2, S6K1, S6, MK2, ERK and RSK was analyzed by immunoblot. E. Effect of p38i on ERK-PP2AC interaction in sensitive and resistant CRC cells. HCT116, SW620, SW480 and RKO cells were treated without or with 10 μM SB202190 for 2 h. Endogenous PP2AC was immunoprecipitated with a PP2AC-specific antibody and analyzed for binding to ERK by Western blot. F. Immunohistochemistry (IHC) staining of primary human CRC tissue microarray. Shown are staining of tumor tissue sections (400 ×) representative of high PP2AC, medium PP2AC and low PP2AC staining. G. PP2AC is differentially expressed in CRC. Scatter plot shows PP2AC staining level in individual tumor as H-score.

Article Snippet: siRNA for human PP2AC, TSC1 and TSC2 were designed and synthesized by OriGene Technologies (MD, USA).

Techniques: Western Blot, Transfection, Phospho-proteomics, Plasmid Preparation, Immunoprecipitation, Binding Assay, Immunohistochemistry, Microarray, Staining

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