Linked Life Data

10871188

Source:http://linkedlifedata.com/resource/pubmed/id/10871188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-7-6
pubmed:abstractText
5'AMP-activated protein kinase (AMPK) can be activated in response to cellular fuel depletion and leads to switching off ATP-consuming pathways and switching on ATP-regenerating pathways in many cell types. We have hypothesized that AMPK is a central mediator of insulin-independent glucose transport, which enables fuel-depleted muscle cells to take up glucose for ATP regeneration under conditions of metabolic stress. To test this hypothesis, rat epitrochlearis muscles were isolated and incubated in vitro under several conditions that evoke metabolic stress accompanied by intracellular fuel depletion. Rates of glucose transport in the isolated muscles were increased by all of these conditions, including contraction (5-fold above basal), hypoxia (8-fold), 2,4-dinotrophenol (11-fold), rotenone (7-fold), and hyperosmolarity (8-fold). All of these stimuli simultaneously increased both alpha1 and alpha2 isoform-specific AMPK activity. There was close correlation between alpha1 (r2 = 0.72) and alpha2 (r2 = 0.67) AMPK activities and the rate of glucose transport, irrespective of the metabolic stress used, all of which compromised muscle fuel status as judged by ATP, phosphocreatine, and glycogen content. 5-Aminoimidazole-4-carboxamide ribonucleoside, a pharmacological AMPK activator that is metabolized to an AMP-mimetic ZMP, also increased both glucose transport and AMPK activity but did not change fuel status. Insulin stimulated glucose transport by 6.5-fold above basal but did not affect AMPK activity. These results suggest that the activation of AMPK may be a common mechanism leading to insulin-independent glucose transport in skeletal muscle under conditions of metabolic stress.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0012-1797
pubmed:author
pubmed:issnType
Print
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
527-31
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10871188-2,4-Dinitrophenol, pubmed-meshheading:10871188-Adenosine Monophosphate, pubmed-meshheading:10871188-Adenosine Triphosphate, pubmed-meshheading:10871188-Animals, pubmed-meshheading:10871188-Biological Transport, pubmed-meshheading:10871188-Creatine, pubmed-meshheading:10871188-Enzyme Activation, pubmed-meshheading:10871188-Glucose, pubmed-meshheading:10871188-Kinetics, pubmed-meshheading:10871188-Male, pubmed-meshheading:10871188-Muscle, Skeletal, pubmed-meshheading:10871188-Muscle Contraction, pubmed-meshheading:10871188-Osmolar Concentration, pubmed-meshheading:10871188-Phosphocreatine, pubmed-meshheading:10871188-Protein Kinases, pubmed-meshheading:10871188-Rats, pubmed-meshheading:10871188-Rats, Sprague-Dawley, pubmed-meshheading:10871188-Rotenone, pubmed-meshheading:10871188-Stress, Physiological, pubmed-meshheading:10871188-Uncoupling Agents
pubmed:year
2000
pubmed:articleTitle
Metabolic stress and altered glucose transport: activation of AMP-activated protein kinase as a unifying coupling mechanism.
pubmed:affiliation
Joslin Diabetes Center, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02215, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't