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Pathways Used by Relaxin to Regulate Myometrial Phospholipase C
Department of Biomedical Sciences, Colorado State University, Fort Collins, Colorado 80523, USA
Address correspondence to: Barbara M. Sanborn, Ph.D., Department of Biomedical Sciences, 102 Physiology, Campus Delivery 1680, Colorado State University, Fort Collins, CO 80523. Voice: 970-491-4263; fax: 970-491-7569. barbara.sanborn{at}colostate.edu
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)-ß3 and inhibit G
 q-stimulated PLC activity. Therefore, PLCß3 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 PLCß3 in PHM1 cells.
Key Words: relaxin • myometrium • PLCß3 • cAMP This article has been cited by other articles:
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