Source:http://linkedlifedata.com/resource/pubmed/id/12832424
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2003-9-12
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pubmed:abstractText |
The effect of diabetes and exercise on skeletal muscle (SkM) AMP-activated protein kinase (AMPK)alpha1 and -alpha2 activities and site-specific phosphorylation of acetyl-CoA carboxylase was examined in the same six dogs before alloxan (35 mg/kg)-induced diabetes (C) and after 4-5 wk of suboptimally controlled hyperglycemic and hypoinsulinemic diabetes (DHG) in the presence and absence of 300-min phlorizin (50 microg.kg-1.min-1)-induced "normoglycemia" (DNG). In each study, the dog underwent a 150-min [3-3H]glucose infusion period, followed by a 30-min treadmill exercise test (60-70% maximal oxygen capacity) to measure the rate of glucose disposal into peripheral tissues (Rdtissue). SkM biopsies were taken from the thigh (vastus lateralis) before and immediately after exercise. In the C and DHG states, the rise in plasma free fatty acids (FFA) with exercise ( approximately 40%) was similar. In the DNG group, preexercise FFA were significantly higher, but the absolute rise in FFA with exercise was similar. However, the exercise-induced increment in Rdtissue was significantly blunted (by approximately 40-50%) in the DNG group compared with the other states. In SkM, preexercise AMPKalpha1 and -alpha2 activities were significantly elevated (by approximately 60-125%) in both diabetic states, but unlike the C group these activities did not rise further with exercise. Additionally, preexercise acetyl-CoA carboxylase phosphorylation in both diabetic states was elevated by approximately 70-80%, but the increases with exercise were similar to the C group. Preexercise AMPKalpha1 and -alpha2 activities were negatively correlated with Rdtissue during exercise for the combined groups (both P < 0.02). In conclusion, the elevated preexercise SkM AMPKalpha1 and -alpha2 activities contribute to the ongoing basal supply of glucose and fatty acid metabolism in suboptimally controlled hypoinsulinemic diabetic dogs; but whether they also play a permissive role in the metabolic stress response to exercise remains uncertain.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyl-CoA Carboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
8750-7587
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
95
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1523-30
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12832424-AMP-Activated Protein Kinases,
pubmed-meshheading:12832424-Acetyl-CoA Carboxylase,
pubmed-meshheading:12832424-Animals,
pubmed-meshheading:12832424-Diabetes Mellitus, Experimental,
pubmed-meshheading:12832424-Dogs,
pubmed-meshheading:12832424-Isoenzymes,
pubmed-meshheading:12832424-Male,
pubmed-meshheading:12832424-Motor Activity,
pubmed-meshheading:12832424-Multienzyme Complexes,
pubmed-meshheading:12832424-Muscle, Skeletal,
pubmed-meshheading:12832424-Phosphorylation,
pubmed-meshheading:12832424-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12832424-Time Factors,
pubmed-meshheading:12832424-Tissue Distribution
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pubmed:year |
2003
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pubmed:articleTitle |
Skeletal muscle basal AMP-activated protein kinase activity is chronically elevated in alloxan-diabetic dogs: impact of exercise.
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pubmed:affiliation |
Dept. of Endocrinology and Diabetes, St. Vincent's Hospital Melbourne, 35 Victoria Parade, Fitzroy 3065, Victoria, Australia. christm@svhm.org.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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