Linked Life Data

11078445

Source:http://linkedlifedata.com/resource/pubmed/id/11078445

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2000-11-15
pubmed:abstractText
The stress-activated p38 mitogen-activated protein kinase (MAPK) was recently shown to be activated by insulin in muscle and adipose cells in culture. Here, we explore whether such stimulation is observed in rat skeletal muscle and whether muscle contraction can also affect the enzyme. Insulin injection (2 U over 3.5 min) resulted in increases in p38 MAPK phosphorylation measured in soleus (3.2-fold) and quadriceps (2.2-fold) muscles. Increased phosphorylation (3.5-fold) of an endogenous substrate of p38 MAPK, cAMP response element binder (CREB), was also observed. After in vivo insulin treatment, p38 MAPKalpha and p38 MAPKbeta isoforms were found to be activated (2.1- and 2.4-fold, respectively), using an in vitro kinase assay, in immunoprecipitates from quadriceps muscle extracts. In vitro insulin treatment (1 nmol/l over 4 min) and electrically-induced contraction of isolated extensor digitorum longus (EDL) muscle also doubled the kinase activity of p38 MAPKalpha and p38 MAPKbeta. The activity of both isoforms was inhibited in vitro by 10 micromol/l SB203580 in all muscles. To explore the possible participation of p38 MAPK in the stimulation of glucose uptake, EDL and soleus muscles were exposed to increasing doses of SB203580 before and during stimulation by insulin or contraction. SB203580 caused a significant reduction in the insulin- or contraction-stimulated 2-deoxyglucose uptake. Maximal inhibition (50-60%) occurred with 10 micromol/l SB203580. These results show that p38 MAPKalpha and -beta isoforms are activated by insulin and contraction in skeletal muscle. The data further suggest that activation of p38 MAPK may participate in the stimulation of glucose uptake by both stimuli in rat skeletal muscle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1794-800
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11078445-Animals, pubmed-meshheading:11078445-Cyclic AMP Response Element-Binding Protein, pubmed-meshheading:11078445-Deoxyglucose, pubmed-meshheading:11078445-Electric Stimulation, pubmed-meshheading:11078445-Enzyme Activation, pubmed-meshheading:11078445-Enzyme Inhibitors, pubmed-meshheading:11078445-Imidazoles, pubmed-meshheading:11078445-Immunosorbent Techniques, pubmed-meshheading:11078445-Insulin, pubmed-meshheading:11078445-Isoenzymes, pubmed-meshheading:11078445-Male, pubmed-meshheading:11078445-Mitogen-Activated Protein Kinases, pubmed-meshheading:11078445-Muscle, Skeletal, pubmed-meshheading:11078445-Muscle Contraction, pubmed-meshheading:11078445-Phosphorylation, pubmed-meshheading:11078445-Pyridines, pubmed-meshheading:11078445-Rats, pubmed-meshheading:11078445-Rats, Wistar, pubmed-meshheading:11078445-p38 Mitogen-Activated Protein Kinases
pubmed:year
2000
pubmed:articleTitle
Activation of p38 mitogen-activated protein kinase alpha and beta by insulin and contraction in rat skeletal muscle: potential role in the stimulation of glucose transport.
pubmed:affiliation
Programme in Cell Biology, Hospital for Sick Children, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't