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Pericyte‐specific expression of Rgs5: implications for PDGF and EDG receptor signaling during vascular maturation
Author(s) -
Cho Hyeseon,
Kozasa Tohru,
Bondjers Cecilia,
Betsholtz Christer,
Kehrl John H.
Publication year - 2003
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.02-0340fje
Subject(s) - heterotrimeric g protein , platelet derived growth factor receptor , microbiology and biotechnology , platelet derived growth factor , signal transduction , biology , g protein , pericyte , growth factor , g protein coupled receptor , s1pr1 , phosphorylation , gq alpha subunit , growth factor receptor , receptor , cancer research , vascular endothelial growth factor , vascular endothelial growth factor a , biochemistry , endothelial stem cell , in vitro , vegf receptors
RGS proteins finely tune heterotrimeric G‐protein signaling. Implying the need for such fine‐tuning in the developing vascular system, in situ hybridization revealed a striking and extensive expression pattern of Rgs5 in the arterial walls of E12.5–E17.5 mouse embryos. The distribution and location of the Rgs5 ‐positive cells typified that of pericytes and strikingly overlapped the known expression pattern of platelet‐derived growth factor receptor (PDGFR)‐β. Both E14.5 PDGFR‐β‐ and platelet‐derived growth factor (PDGF)‐B‐deficient mice exhibited markedly reduced levels of Rgs5 in their vascular plexa and small arteries. This likely reflects the loss of pericytes in the mutant mice. RGS5 acts as a potent GTPase activating protein for Giα and Gqα and it attenuated angiotensin II‐, endothelin‐1‐, sphingosine‐1‐phosphate‐, and PDGF‐induced ERK‐2 phosphorylation. Together these results indicate that RGS5 exerts control over PDGFR‐β and GPCR‐mediated signaling pathways active during fetal vascular maturation.