Pathways Used by Relaxin to Regulate Myometrial Phospholipase C

: 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 (...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2005-05, Vol.1041 (1), p.300-304
Main Authors: ZHONG, MIAO, KU, CHUN-YING, SANBORN, BARBARA M.
Format: Article
Language:English
Subjects:
Activation
Amino Acid Sequence
Animals
cAMP
Cell Line
Female
Humans
Isoenzymes - chemistry
Isoenzymes - metabolism
Kinases
Mathematical models
Models, Biological
Molecular Sequence Data
myometrium
Myometrium - drug effects
Myometrium - enzymology
Myometrium - metabolism
Pathways
Phospholipase
Phospholipase C beta
Phosphorylation
Phosphorylation - drug effects
PLCβ3
Proteins
Receptors
relaxin
Relaxin - pharmacology
Sequence Alignment
Signal Transduction - drug effects
Type C Phospholipases - chemistry
Type C Phospholipases - metabolism
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Summary:: 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)‐β3 and inhibit Gαq‐stimulated PLC activity. Therefore, PLCβ3 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 PLCβ3 in PHM1 cells.
ISSN:0077-8923
1749-6632
DOI:10.1196/annals.1282.045