Linked Life Data

2846075

Source:http://linkedlifedata.com/resource/pubmed/id/2846075

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-12-1
pubmed:abstractText
Activation of H+ secretion by the gastric parietal cell involves major changes in morphology, metabolic activity and ion pathways of the secretory membrane. These changes are elicited by histamine binding to the H2 receptor, raising cAMP levels and presumably activating cAMP-dependent protein kinase. Concomitantly, the intracellular free Ca2+ concentration, [Ca2+]i, increases. Studies were performed to determine whether cAMP-mediated protein phosphorylation accompanies histamine activation of H+ secretion and to catalogue the major protein species serving as substrates for cAMP-dependent protein kinase in the parietal cell. 80% pure rabbit parietal cells, prepared by Nycodenz bouyant density centrifugation, were used. To investigate only cAMP-mediated effects, histamine-dependent changes in [Ca2+]i in these cells were abolished by depleting intracellular Ca2+ stores and performing experiments under Ca2+-free conditions. Acid secretion and steady-state levels of protein phosphorylation were then measured in unstimulated (cimetidine-treated) and histamine-stimulated cells. In intact parietal cells, concommitant with histamine stimulation of H+ secretion, increases in the level of protein phosphorylation were observed. Significantly changing phosphoproteins found in supernatant fractions showed apparent subunit sizes of approx. 148, 130, 47 and 43 kDa, and in microsomal fractions included those at approx. 130, 51 and 47 kDa. In parietal cell homogenates, using [gamma-32P]ATP, cAMP elicited significant phosphorylation of eight supernatant proteins and twelve microsomal proteins, which included the histamine-dependent phosphoproteins found in the intact parietal cell, except for the 51 kDa microsomal protein. As a working hypothesis, these proteins are involved in stimulus-secretion coupling in the parietal cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
972
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-109
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Gastric H+ secretion: histamine (cAMP-mediated) activation of protein phosphorylation.
pubmed:affiliation
Department of Physiology and Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0576.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.