Intracellular regulation of heterotrimeric G-protein signaling modulates vascular smooth muscle cell contraction

2011 ◽  
Vol 510 (2) ◽  
pp. 182-189 ◽  
Author(s):  
Guillaume Bastin ◽  
Scott P. Heximer
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
G Protein ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Intracellular Regulation ◽  
Heterotrimeric G Protein Signaling

scholarly journals The G Protein-Coupled Estrogen Receptor 1 (GPER1/GPR30) Agonist G-1 Regulates Vascular Smooth Muscle Cell Ca2+Handling

2013 ◽  
Vol 50 (5) ◽  
pp. 421-429 ◽  
Author(s):  
Anders Holm ◽  
Per Hellstrand ◽  
Björn Olde ◽  
Daniel Svensson ◽  
L.M. Fredrik Leeb-Lundberg ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
G Protein ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
G Protein Coupled ◽  
Estrogen Receptor 1

scholarly journals Characterization of a G Protein-activated Phosphoinositide 3-Kinase in Vascular Smooth Muscle Cell Nuclei

2001 ◽  
Vol 276 (25) ◽  
pp. 22170-22176 ◽  
Author(s):  
Daniel Bacqueville ◽  
Paul Déléris ◽  
Christiane Mendre ◽  
Marie-Thérèse Pieraggi ◽  
Hugues Chap ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
G Protein ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
Cell Nuclei ◽  
Phosphoinositide 3 Kinase

G protein-coupled receptors control vascular smooth muscle cell proliferation via pp60c-src and p21ras

1997 ◽  
Vol 272 (6) ◽  
pp. C2019-C2030 ◽  
Author(s):  
B. Schieffer ◽  
H. Drexler ◽  
B. N. Ling ◽  
M. B. Marrero
Keyword(s):  
Cell Proliferation ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cell ◽  
G Protein ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
G Protein Coupled Receptors ◽  
Smooth Muscle Cell Proliferation ◽  
G Protein Coupled

The binding of vasoactive peptides to their respective G protein-coupled receptors has been implicated in the pathogenesis of vascular smooth muscle cell proliferation, leading to the development of hypertension, arteriosclerosis, and restenosis after vascular injury. We previously showed that the cytosolic tyrosine kinase pp60c-src is crucial for angiotensin II (ANG II)-induced activation of the protooncogene p21ras. Therefore, we investigated the role of pp60c-src and p21ras in rat aortic smooth muscle cell proliferation induced by several G protein-coupled receptors. ANG II, endothelin-1, or thrombin increased cell proliferation and DNA synthesis. Electroporation of anti-pp60c-src antibodies into cells abolished proliferation in response to these G protein-coupled receptor ligands but not in response to platelet-derived growth factor-BB (PDGF-BB). In contrast, electroporation of anti-p21ras antibody completely blocked DNA synthesis and cell proliferation in response to ANG II, endothelin-1, thrombin, and PDGF-BB. Our data indicate that the pp60c-src tyrosine kinase is necessary and specific for vascular smooth muscle cell proliferation and DNA synthesis in response to G protein-coupled receptors but not classic growth factor receptors.

Involvement of Cyclooxygenase- and Lipoxygenase-Mediated Conversion of Arachidonic Acid in Controlling Human Vascular Smooth Muscle Cell Proliferation

1990 ◽  
Vol 63 (02) ◽  
pp. 291-297 ◽  
Author(s):  
Herm-Jan M Brinkman ◽  
Marijke F van Buul-Worteiboer ◽  
Jan A van Mourik
Keyword(s):  
Cell Proliferation ◽  
Arachidonic Acid ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Vascular Smooth Muscle Cell ◽  
Muscle Cells ◽  
Smooth Muscle Cell Proliferation

SummaryWe observed that the growth of human umbilical arterysmooth muscle cells was inhibited by the phospholipase A2 inhibitors p-bromophenacylbromide and mepacrine. Thesefindings suggest that fatty acid metabolism might be integrated in the control mechanism of vascular smooth muscle cell proliferation. To identify eicosanoids possibly involved in this process, we studied both the metabolism of arachidonic acid of these cells in more detail and the effect of certain arachidonic acid metabolites on smooth muscle cells growth. We found no evidence for the conversion of arachidonic acid via the lipoxygenase pathway. In contrast, arachidonic acid was rapidly converted via the cyclooxy-genase pathway. The following metabolites were identified: prostaglandin E2 (PGE2), 6-keto-prostaglandin F1α (6-k-PGF1α), prostaglandin F2α (PGF2α), 12-hydroxyheptadecatrienoic acid (12-HHT) and 11-hydroxyeicosatetetraenoic acid (11-HETE). PGE2 was the major metabolite detected. Arachidonic acid metabolites were only found in the culture medium, not in the cell. After synthesis, 11-HETE was cleared from the culture medium. We have previously reported that PGE2 inhibits the serum-induced [3H]-thymidine incorporation of growth-arrested human umbilical artery smooth muscle cells. Here we show that also 11-HETEexerts this inhibitory property. Thus, our data suggeststhat human umbilical artery smooth muscle cells convert arachidonic acid only via the cyclooxygenase pathway. Certain metabolites produced by this pathway, including PGE2 and 11-HETE, may inhibit vascular smooth muscle cell proliferation.

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