Linked Life Data

11781141

Source:http://linkedlifedata.com/resource/pubmed/id/11781141

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-1-8
pubmed:abstractText
The Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is thought to be activated during the cholinergic stimulation of gastric acid secretion. The carbachol-induced acid production of cultured rabbit parietal cells was dose-dependently inhibited by the CaMKII inhibitor KN-62 as measured by accumulation of the weak base [(14)C]aminopyrine ([(14)C]-AP). Inhibition by KN-62 was most efficient at concentrations of carbachol >10(-6) M. After carbachol stimulation, we observed an activation of CaMKII activity, and its translocation to the apical membrane of gastric mucosal cells. We found a doubling of the abundance of CaMKII to the stimulus-associated apical membrane (SA vesicles) compared to the apical membrane from the resting state after carbachol induction. This was shown by both an anti-CaMKII serum and the 1.8-fold increase of the CaMKII phosphotransferase activity in vitro. The SA vesicles exhibited a strong increase of autoactivated CaMKII probed with an anti-autoactivated CaMKII antibody. Additionally, we observed a colocalization of both CaMKII and the H(+)-K(+)-ATPase of SA vesicles similar to the colocalization of both enzymes to the tubulovesicles suggesting them as at least one pool for the SA vesicular CaMKII. Our data indicate that the activation of CaMKII and the carbachol-dependent redistribution of CaMKII to the SA vesicles are distinct processes that occur in parallel to regulate the activity and localization of CaMKII. These findings contribute to the model implicating an involvement for CaMKII in the intracellular dynamics of the acid secretion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0898-6568
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11781141-1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine, pubmed-meshheading:11781141-Aminopyrine, pubmed-meshheading:11781141-Animals, pubmed-meshheading:11781141-Calcium-Calmodulin-Dependent Protein Kinase Type 2, pubmed-meshheading:11781141-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:11781141-Carbachol, pubmed-meshheading:11781141-Cell Membrane, pubmed-meshheading:11781141-Cell Polarity, pubmed-meshheading:11781141-Cells, Cultured, pubmed-meshheading:11781141-Cholinergic Agonists, pubmed-meshheading:11781141-Dose-Response Relationship, Drug, pubmed-meshheading:11781141-Enzyme Activation, pubmed-meshheading:11781141-Gastric Acid, pubmed-meshheading:11781141-H(+)-K(+)-Exchanging ATPase, pubmed-meshheading:11781141-Male, pubmed-meshheading:11781141-Parietal Cells, Gastric, pubmed-meshheading:11781141-Protein Transport, pubmed-meshheading:11781141-Rabbits, pubmed-meshheading:11781141-Rats, pubmed-meshheading:11781141-Rats, Wistar, pubmed-meshheading:11781141-Secretory Vesicles
pubmed:year
2002
pubmed:articleTitle
CaMKII is activated and translocated to the secretory apical membrane during cholinergically conveyed gastric acid secretion.
pubmed:affiliation
Institut für Zoophysiologie der Westfälischen Wilhelms-Universität Münster, Hindenburgplatz 55, D-48143 Münster, Germany. fahrman@uni-muenster.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't