Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-11-30
pubmed:abstractText
The sodium-proton exchanger is activated by various agonists, including insulin, even in human red blood cell. MAPKinase, a family of ubiquitous serine/threonine kinases, plays an important role in the signal transduction pathways which lead to sodium-proton exchanger activation. The aim of our study was to establish the existence of MAPKinase in human red blood cell and to investigate the effects of its activation by insulin and okadaic acid on the sodium-proton exchanger. Immunoblot with antiMAPK antibody revealed the presence of two isoforms, p44(ERK1) and p42(ERK2). Insulin stimulated MAPKinase activity and increased the phosphorylation of MAPK tyrosine residues, with a peak time between 3 and 5 min. Okadaic acid, an inhibitor of serine/threonine phosphatases, stimulated MAPKinase activity. In the presence of PD98059, an inhibitor of MEK, the upstream activator of MAPKinase, insulin and okadaic acid failed to stimulate MAPKinase. Insulin and okadaic acid increased the activity of the sodium-proton exchanger and this effect was abolished by PD98059. In conclusion, we first describe the presence and activity of MAPKinase in human red blood cell. Furthermore, we demonstrate that in human red blood cell, insulin modulates the sodium-proton exchanger through MAPKinase activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
1421
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
140-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
MAPKinase and regulation of the sodium-proton exchanger in human red blood cell.
pubmed:affiliation
Department of Clinical and Experimental Medicine, University of Padua Medical School, Padua, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't