Document Detail

Effect of a high-fat-sucrose diet on in vivo insulin receptor kinase activation.
MedLine Citation:
PMID:  2164785     Owner:  NLM     Status:  MEDLINE    
Insulin-stimulated glucose uptake into muscle is depressed by high-fat-sucrose (HFS) feeding of rats. To investigate the mechanism of this insulin resistance, the in vivo activation of the insulin receptor kinase in liver and muscle of control and HFS-fed rats was determined. Rats were injected with glucose and insulin and killed 0, 5, 15, and 30 min after injection. Insulin binding was not changed in partially purified receptors from muscle of HFS rats. In control rats insulin receptor kinase activity was maximally stimulated threefold in liver at 5 min and fourfold in muscle at 15 min after insulin-glucose injection. The insulin-stimulated tyrosine kinase activity of receptors isolated from the liver of rats fed the HFS diet was decreased by 30% in comparison with the controls. In contrast, receptors isolated from muscle did not show any difference in basal or insulin-stimulated kinase activity between HFS-fed and control rats. Decreased in vivo activation of the insulin receptor kinase may be at least partially responsible for insulin resistance in liver. Because insulin binding and insulin stimulation of receptor kinase were normal in muscle of HFS-fed animals, it is concluded that the insulin resistance of glucose uptake into muscle is caused by a defect distal to the insulin receptor.
J J Boyd; I Contreras; M Kern; E B Tapscott; D L Downes; W R Frisell; G L Dohm
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  259     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1990 Jul 
Date Detail:
Created Date:  1990-08-23     Completed Date:  1990-08-23     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  E111-6     Citation Subset:  IM    
Department of Biochemistry, School of Medicine, East Carolina University, Greenville, North Carolina 27858.
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MeSH Terms
Blood Glucose / metabolism
Dietary Carbohydrates / pharmacology*
Enzyme Activation
Glycogen Synthase / metabolism
Insulin / blood
Liver / enzymology*
Muscles / enzymology*
Protein-Tyrosine Kinases / metabolism*
Pyruvate Dehydrogenase Complex / metabolism
Rats, Inbred Strains
Receptor, Insulin / metabolism
Reference Values
Sucrose / pharmacology*
Grant Support
Reg. No./Substance:
0/Blood Glucose; 0/Dietary Carbohydrates; 0/Pyruvate Dehydrogenase Complex; 11061-68-0/Insulin; 57-50-1/Sucrose; EC Synthase; EC Kinases; EC, Insulin

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