These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Studies of the mechanisms of action of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP) in the ovine anterior pituitary: evidence that CRF and AVP stimulate protein phosphorylation and dephosphorylation. Author: Liu JP. Journal: Mol Cell Endocrinol; 1994 Dec; 106(1-2):57-66. PubMed ID: 7895915. Abstract: This study was undertaken to determine the roles of corticotropin-releasing factor (CRF) and arginine vasopressin (AVP) in the regulation of adrenocorticotropin (ACTH) secretion in perfused ovine anterior pituitary (AP) cells and their ability to cause protein phosphorylation and dephosphorylation in these cells. Freshly dispersed ovine AP cells were maintained in a miniperifusion chamber and ACTH secretion was monitored every 20 s. When cells were perfused with CRF (1 nM, 5 min) or AVP (1 nM, 5 min), ACTH release was increased 20-fold and 12-fold, respectively. When an ovine AP cell membrane fraction was incubated with either CRF or AVP, CRF stimulated the phosphorylation of at least 11 proteins and the dephosphorylation of at least 5 phosphoproteins, whereas AVP caused the phosphorylation of at least 15 proteins and the dephosphorylation of 5 proteins. A comparison of the proteins phosphorylated by CRF or AVP with those phosphorylated by cAMP or protein kinase C activators suggested that the hormone-stimulated phosphorylation may also involve unidentified protein kinases. Additionally, at least eight proteins appeared to be phosphorylated by both CRF and AVP. Furthermore, in the case of four particular proteins both CRF and AVP stimulated phosphorylation at low concentrations of Ca2+ (0.1-1 microM), but at high concentrations of Ca2+ (10-100 microM) CRF or AVP triggered dephosphorylation of these proteins.(ABSTRACT TRUNCATED AT 250 WORDS)[Abstract] [Full Text] [Related] [New Search]