Linked Life Data

15956722

Source:http://linkedlifedata.com/resource/pubmed/id/15956722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-6-15
pubmed:abstractText
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)-beta3 and inhibit Galpha(q)-stimulated PLC activity. Therefore, PLCbeta3 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 PLCbeta3 in PHM1 cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
1041
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
300-4
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Pathways used by relaxin to regulate myometrial phospholipase C.
pubmed:affiliation
Department of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural