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Pathways Used by Relaxin to Regulate Myometrial Phospholipase C
Author(s) -
ZHONG MIAO,
KU CHUNYING,
SANBORN BARBARA M.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1282.045
Subject(s) - relaxin , phosphorylation , phospholipase c , signal transduction , microbiology and biotechnology , myometrium , protein kinase a , kinase , gq alpha subunit , receptor , biology , chemistry , endocrinology , medicine , g protein coupled receptor , hormone , biochemistry , uterus
A bstract : Relaxin exhibits pleiotropic effects on reproductive and nonreproductive tissues; the signaling mechanisms underlying these functions are still not well understood. Activation of protein kinase A and several other signal‐regulated protein kinases results in the phosphorylation of phospholipase C (PLC)‐β 3 and inhibit Gα q ‐stimulated PLC activity. Therefore, PLCβ 3 may be targeted by both contractant and relaxant signaling pathways in myometrium and play a critical role in the balance between them. PHM1 cells express mRNA for relaxin receptor LGR7, and relaxin inhibits oxytocin‐stimulated PLC activity in these cells. Thus, this model system may be useful in delineating signaling pathways used by relaxin. Here, we present evidence that relaxin stimulates phosphorylation of PLCβ 3 in PHM1 cells.