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Avanti Polar vpc32183 inhibitor

Inhibition of PA-stimulated myoblast proliferation and Akt and ERK1/2 phosphorylation by the lysoPA (LPA) receptor antagonist <t>VPC32183.</t> Myoblasts were serum-starved in DMEM supplemented with 0.1% BSA for 24 h. ( A ) The cells were preincubated for 30 min with 5 μM VPC32183 and were then challenged with 15 μM PA or 15 μM LPA for 16 h, as indicated. [ 3 H]Thymidine incorporation was measured as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed in triplicate. (* p < 0.05, control versus PA or LPA-treated cells, # p < 0.05; PA or LPA-treated cells versus PA or LPA-treated cells in the presence of VPC32183). ( B ) Cells were treated as in panel A. Cell proliferation was determined by staining the myoblasts with crystal violet as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed. Control versus PA-treated cells; ** p < 0.01, control versus LPA-treated cells; # p < 0.05; PA- or LPA-treated cells versus PA- or LPA-treated cells in the presence of VPC32183). ( C ) Cells were preincubated with 5 μM VPC32183 for 30 min and then treated with 15 μM PA for 5 min. Cell lysates were analyzed by western blotting as described in the Materials and Methods section. Phosphorylation of Akt and ERK1/2 was determined using specific antibodies against phospho-Akt (P-Akt) or phospho-ERK1/2 (P-ERK1/2). Equal loading of protein was monitored using specific antibodies to total Akt and total ERK1/2. Panel C shows a representative blot of three independent experiments. ( D , E ) Results of scanning densitometry of the exposed films. Data are expressed as arbitrary units of intensity relative to the control siRNA values in the absence of agonist or inhibitor (Ctrl) and are the mean ± SEM of 3 replicate experiments. (* p < 0.05; ** p < 0.01; control versus PA-treated cells, # p < 0.05, ### p < 0.001; PA-treated cells versus PA-treated cells in the presence of VPC32183, as indicated).

Vpc32183 Inhibitor, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 92/100, based on 55 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 92 stars, based on 55 article reviews

vpc32183 inhibitor - by Bioz Stars, 2026-03

92/100 stars

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1) Product Images from "Phosphatidic Acid Stimulates Myoblast Proliferation through Interaction with LPA1 and LPA2 Receptors"

Article Title: Phosphatidic Acid Stimulates Myoblast Proliferation through Interaction with LPA1 and LPA2 Receptors

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms22031452

Inhibition of PA-stimulated myoblast proliferation and Akt and ERK1/2 phosphorylation by the lysoPA (LPA) receptor antagonist VPC32183. Myoblasts were serum-starved in DMEM supplemented with 0.1% BSA for 24 h. ( A ) The cells were preincubated for 30 min with 5 μM VPC32183 and were then challenged with 15 μM PA or 15 μM LPA for 16 h, as indicated. [ 3 H]Thymidine incorporation was measured as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed in triplicate. (* p < 0.05, control versus PA or LPA-treated cells, # p < 0.05; PA or LPA-treated cells versus PA or LPA-treated cells in the presence of VPC32183). ( B ) Cells were treated as in panel A. Cell proliferation was determined by staining the myoblasts with crystal violet as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed. Control versus PA-treated cells; ** p < 0.01, control versus LPA-treated cells; # p < 0.05; PA- or LPA-treated cells versus PA- or LPA-treated cells in the presence of VPC32183). ( C ) Cells were preincubated with 5 μM VPC32183 for 30 min and then treated with 15 μM PA for 5 min. Cell lysates were analyzed by western blotting as described in the Materials and Methods section. Phosphorylation of Akt and ERK1/2 was determined using specific antibodies against phospho-Akt (P-Akt) or phospho-ERK1/2 (P-ERK1/2). Equal loading of protein was monitored using specific antibodies to total Akt and total ERK1/2. Panel C shows a representative blot of three independent experiments. ( D , E ) Results of scanning densitometry of the exposed films. Data are expressed as arbitrary units of intensity relative to the control siRNA values in the absence of agonist or inhibitor (Ctrl) and are the mean ± SEM of 3 replicate experiments. (* p < 0.05; ** p < 0.01; control versus PA-treated cells, # p < 0.05, ### p < 0.001; PA-treated cells versus PA-treated cells in the presence of VPC32183, as indicated).

Figure Legend Snippet: Inhibition of PA-stimulated myoblast proliferation and Akt and ERK1/2 phosphorylation by the lysoPA (LPA) receptor antagonist VPC32183. Myoblasts were serum-starved in DMEM supplemented with 0.1% BSA for 24 h. ( A ) The cells were preincubated for 30 min with 5 μM VPC32183 and were then challenged with 15 μM PA or 15 μM LPA for 16 h, as indicated. [ 3 H]Thymidine incorporation was measured as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed in triplicate. (* p < 0.05, control versus PA or LPA-treated cells, # p < 0.05; PA or LPA-treated cells versus PA or LPA-treated cells in the presence of VPC32183). ( B ) Cells were treated as in panel A. Cell proliferation was determined by staining the myoblasts with crystal violet as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed. Control versus PA-treated cells; ** p < 0.01, control versus LPA-treated cells; # p < 0.05; PA- or LPA-treated cells versus PA- or LPA-treated cells in the presence of VPC32183). ( C ) Cells were preincubated with 5 μM VPC32183 for 30 min and then treated with 15 μM PA for 5 min. Cell lysates were analyzed by western blotting as described in the Materials and Methods section. Phosphorylation of Akt and ERK1/2 was determined using specific antibodies against phospho-Akt (P-Akt) or phospho-ERK1/2 (P-ERK1/2). Equal loading of protein was monitored using specific antibodies to total Akt and total ERK1/2. Panel C shows a representative blot of three independent experiments. ( D , E ) Results of scanning densitometry of the exposed films. Data are expressed as arbitrary units of intensity relative to the control siRNA values in the absence of agonist or inhibitor (Ctrl) and are the mean ± SEM of 3 replicate experiments. (* p < 0.05; ** p < 0.01; control versus PA-treated cells, # p < 0.05, ### p < 0.001; PA-treated cells versus PA-treated cells in the presence of VPC32183, as indicated).

Techniques Used: Inhibition, Staining, Western Blot

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Journal: International Journal of Molecular Sciences

Article Title: Phosphatidic Acid Stimulates Myoblast Proliferation through Interaction with LPA1 and LPA2 Receptors

doi: 10.3390/ijms22031452

Figure Lengend Snippet: Inhibition of PA-stimulated myoblast proliferation and Akt and ERK1/2 phosphorylation by the lysoPA (LPA) receptor antagonist VPC32183. Myoblasts were serum-starved in DMEM supplemented with 0.1% BSA for 24 h. ( A ) The cells were preincubated for 30 min with 5 μM VPC32183 and were then challenged with 15 μM PA or 15 μM LPA for 16 h, as indicated. [ 3 H]Thymidine incorporation was measured as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed in triplicate. (* p < 0.05, control versus PA or LPA-treated cells, # p < 0.05; PA or LPA-treated cells versus PA or LPA-treated cells in the presence of VPC32183). ( B ) Cells were treated as in panel A. Cell proliferation was determined by staining the myoblasts with crystal violet as described in the Materials and Methods section. Results are expressed relative to the control value without agonist and are the mean ± SEM of 3 independent experiments performed. Control versus PA-treated cells; ** p < 0.01, control versus LPA-treated cells; # p < 0.05; PA- or LPA-treated cells versus PA- or LPA-treated cells in the presence of VPC32183). ( C ) Cells were preincubated with 5 μM VPC32183 for 30 min and then treated with 15 μM PA for 5 min. Cell lysates were analyzed by western blotting as described in the Materials and Methods section. Phosphorylation of Akt and ERK1/2 was determined using specific antibodies against phospho-Akt (P-Akt) or phospho-ERK1/2 (P-ERK1/2). Equal loading of protein was monitored using specific antibodies to total Akt and total ERK1/2. Panel C shows a representative blot of three independent experiments. ( D , E ) Results of scanning densitometry of the exposed films. Data are expressed as arbitrary units of intensity relative to the control siRNA values in the absence of agonist or inhibitor (Ctrl) and are the mean ± SEM of 3 replicate experiments. (* p < 0.05; ** p < 0.01; control versus PA-treated cells, # p < 0.05, ### p < 0.001; PA-treated cells versus PA-treated cells in the presence of VPC32183, as indicated).

Article Snippet: Sphingosine-1-phosphate, N-palmitoyl-ceramide-1-phosphate (C1P), 1,2-dipalmitoyl- sn -glycerol-3-phosphate (16:0-PA), 1-palmitoyl-2-oleoyl- sn -glycerol-3-phosphate (16:0-18:1-PA) and the VPC32183 inhibitor were supplied by Avanti Polar Lipids (Alabaster, AL, USA).

Techniques: Inhibition, Staining, Western Blot

Inhibition of PA-stimulated adenocarcinoma cell migration by the LPA1 receptor antagonists AM966, Ki16425, and VPC32183. A549 cells were seeded in Boyden chambers and incubated in serum-free RPMI 1640 culture medium supplemented with 0.2% BSA. The cells were preincubated for 90 min with or without the LPA1 receptor antagonists AM966 (1 µM) ( A ), Ki16425 (10 µM) ( B ), or VPC32183 (5 µM) ( C ) as indicated, before stimulation with PA (10 µM). Cell migration was measured as indicated in Materials and Methods. Data are expressed relative to the control value without agonist and are given as the mean ± SD of 3 independent experiments carried out in duplicate. (* p < 0.05, control versus PA-treated cells; # p < 0.05, PA-treated cells versus PA-treated cells in the presence of VPC32183; ## p < 0.01, PA-treated cells versus PA-treated cells in the presence of AM966 or Ki16425). AM = AM966, Ki = Ki16425 and VPC = VPC232183. Cell viability was monitored by staining the cells with crystal violet after 24 h treatment with the inhibitors as indicated in Materials and Methods. Concentrations of AM966 (0–10 µM), Ki16425 (0–10 µM), and VPC32183 (5–10 µM) were not toxic for A549 cells ( D – F ). Data are expressed relative to the value without the inhibitor (0 µM) and are given as the mean ± SD of 3 independent experiments carried out in triplicate.

Journal: Biomedicines

Article Title: Phosphatidic Acid Stimulates Lung Cancer Cell Migration through Interaction with the LPA1 Receptor and Subsequent Activation of MAP Kinases and STAT3

doi: 10.3390/biomedicines11071804

Figure Lengend Snippet: Inhibition of PA-stimulated adenocarcinoma cell migration by the LPA1 receptor antagonists AM966, Ki16425, and VPC32183. A549 cells were seeded in Boyden chambers and incubated in serum-free RPMI 1640 culture medium supplemented with 0.2% BSA. The cells were preincubated for 90 min with or without the LPA1 receptor antagonists AM966 (1 µM) ( A ), Ki16425 (10 µM) ( B ), or VPC32183 (5 µM) ( C ) as indicated, before stimulation with PA (10 µM). Cell migration was measured as indicated in Materials and Methods. Data are expressed relative to the control value without agonist and are given as the mean ± SD of 3 independent experiments carried out in duplicate. (* p < 0.05, control versus PA-treated cells; # p < 0.05, PA-treated cells versus PA-treated cells in the presence of VPC32183; ## p < 0.01, PA-treated cells versus PA-treated cells in the presence of AM966 or Ki16425). AM = AM966, Ki = Ki16425 and VPC = VPC232183. Cell viability was monitored by staining the cells with crystal violet after 24 h treatment with the inhibitors as indicated in Materials and Methods. Concentrations of AM966 (0–10 µM), Ki16425 (0–10 µM), and VPC32183 (5–10 µM) were not toxic for A549 cells ( D – F ). Data are expressed relative to the value without the inhibitor (0 µM) and are given as the mean ± SD of 3 independent experiments carried out in triplicate.

Article Snippet: Phosphatidic acid (from egg yolk lecithin), 1,2-dipalmitoyl-sn-glycero-3-phosphate (16:0 PA), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate (16:0-18:1 PA), 1-Oleoyl-sn-glycerol 3-phosphate (Oleoyl-L-α-lysophosphatidic acid), and VPC32183 were from Avanti Polar lipids (Birmingham, AL, USA).

Techniques: Inhibition, Migration, Incubation, Control, Staining

Mitochondrial membrane potential during Taxol treatment is protected by LPA receptor-dependent signaling. Mitochondria from SKOV3 cells treated with Taxol or Taxol in combination with 5 uM VPC32183 for 24 h were imaged by TEM. Images are representative of 20 or more slices containing multiple mitochondria.

Journal: Redox Biology

Article Title: Blocking LPA-dependent signaling increases ovarian cancer cell death in response to chemotherapy

doi: 10.1016/j.redox.2018.01.002

Figure Lengend Snippet: Mitochondrial membrane potential during Taxol treatment is protected by LPA receptor-dependent signaling. Mitochondria from SKOV3 cells treated with Taxol or Taxol in combination with 5 uM VPC32183 for 24 h were imaged by TEM. Images are representative of 20 or more slices containing multiple mitochondria.

Article Snippet: VPC32183 and alkyl-linked 18:1 lysophosphatidic acid (LPA) [1-(9Z-octadecenyl)-2-hydroxy- sn -glycero-3-phosphate (ammonium salt)] was from Avanti Polar Lipids, Inc.

Techniques:

Blocking LPA-dependent signaling increases the death response to both Taxol and cisplatin. SKOV3 cells were incubated with LPA or VPC32183 at indicated concentrations for 24 h before harvesting and immunoblotting for caspase cleavage. The data shown are representative of Western blots from three independent experiments.