Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
1998-11-12
pubmed:abstractText
A high fat diet causes resistance of skeletal muscle glucose transport to insulin and contractions. We tested the hypothesis that fat feeding causes a change in plasma membrane composition that interferes with functioning of glucose transporters and/or insulin receptors. Epitrochlearis muscles of rats fed a high (50% of calories) fat diet for 8 weeks showed approximately 50% decreases in insulin- and contraction-stimulated 3-O-methylglucose transport. Similar decreases in stimulated glucose transport activity occurred in muscles of wild-type mice with 4 weeks of fat feeding. In contrast, GLUT1 overexpressing muscles of transgenic mice fed a high fat diet showed no decreases in their high rates of glucose transport, providing evidence against impaired glucose transporter function. Insulin-stimulated system A amino acid transport, insulin receptor (IR) tyrosine kinase activity, and insulin-stimulated IR and IRS-1 tyrosine phosphorylation were all normal in muscles of rats fed the high fat diet for 8 weeks. However, after 30 weeks on the high fat diet, there was a significant reduction in insulin-stimulated tyrosine phosphorylation in muscle. The increases in GLUT4 at the cell surface induced by insulin or muscle contractions, measured with the 3H-labeled 2-N-4-(1-azi-2,2, 2-trifluoroethyl)-benzoyl-1,3-bis-(D-mannose-4-yloxy)-2-propyla min e photolabel, were 26-36% smaller in muscles of the 8-week high fat-fed rats as compared with control rats. Our findings provide evidence that (a) impairment of muscle glucose transport by 8 weeks of high fat feeding is not due to plasma membrane composition-related reductions in glucose transporter or insulin receptor function, (b) a defect in insulin receptor signaling is a late event, not a primary cause, of the muscle insulin resistance induced by fat feeding, and (c) impaired GLUT4 translocation to the cell surface plays a major role in the decrease in stimulated glucose transport.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3-O-Methylglucose, http://linkedlifedata.com/resource/pubmed/chemical/Amino Acid Transport Systems, http://linkedlifedata.com/resource/pubmed/chemical/Blood Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Dietary Fats, http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 1, http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Slc2a1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Slc2a1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, rat
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26157-63
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:9748297-3-O-Methylglucose, pubmed-meshheading:9748297-Amino Acid Transport Systems, pubmed-meshheading:9748297-Animals, pubmed-meshheading:9748297-Biological Transport, pubmed-meshheading:9748297-Blood Glucose, pubmed-meshheading:9748297-Body Weight, pubmed-meshheading:9748297-Carrier Proteins, pubmed-meshheading:9748297-Dietary Fats, pubmed-meshheading:9748297-Glucose Transporter Type 1, pubmed-meshheading:9748297-Glucose Transporter Type 4, pubmed-meshheading:9748297-Insulin, pubmed-meshheading:9748297-Male, pubmed-meshheading:9748297-Mice, pubmed-meshheading:9748297-Mice, Transgenic, pubmed-meshheading:9748297-Monosaccharide Transport Proteins, pubmed-meshheading:9748297-Muscle, Skeletal, pubmed-meshheading:9748297-Muscle Contraction, pubmed-meshheading:9748297-Muscle Proteins, pubmed-meshheading:9748297-Protein-Tyrosine Kinases, pubmed-meshheading:9748297-Rats, pubmed-meshheading:9748297-Rats, Wistar, pubmed-meshheading:9748297-Receptor, Insulin
pubmed:year
1998
pubmed:articleTitle
A high fat diet impairs stimulation of glucose transport in muscle. Functional evaluation of potential mechanisms.
pubmed:affiliation
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA. phansen@imgate.wustl.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't