UNSPECIFIED (1999) Activation of protein kinase C by oxytocin inhibits the biological activity of the human myometrial corticotropin-releasing hormone receptor at term. ENDOCRINOLOGY, 140 (2). pp. 585-594.

Full text not available from this repository, contact author.

Request Changes to record.

Abstract

The role of placental CRH in human pregnancy is currently unknown. The myometrium expresses CRH receptors that during pregnancy become coupled to adenylate cyclase. Oxytocin (OT) is one of the main regulators of uterine activity, acting via activation of the inositol triphosphate pathway. In view of the possible cross-talk between the CRH and OT signal transduction pathways we have sought to examine in more detail the second messenger mechanisms involved.

CRH receptor binding affinity for CRH and activation of adenylate cyclase were reduced in the presence of OT in pregnant (at term, but not preterm) human myometrium. OT action was mediated via pertussis toxin-sensitive G proteins, which directly inhibit adenylate cyclase and, via activation of protein kinase C, phosphorylate the CRH receptor, leading to desensitization. Activation of protein kinase C by OT could be partially inhibited in human pregnant myometrial cells by OT antagonists (F327 and CAP476; 1 mu M) or phospholipase C inhibitors (U73122; 10 mu M).

These results suggest that in term myometrium, CRH receptor function is modulated by OT, leading to reduced biological activity, lower cAMP levels, and a subsequent shift, in favor of contractility rather than relaxation.

Item Type:	Journal Article
Subjects:	R Medicine > RC Internal medicine
Journal or Publication Title:	ENDOCRINOLOGY
Publisher:	ENDOCRINE SOC
ISSN:	0013-7227
Official Date:	February 1999
Dates:	Date Event February 1999 UNSPECIFIED
Volume:	140
Number:	2
Number of Pages:	10
Page Range:	pp. 585-594
Publication Status:	Published

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item