| Nutritional and hormonal regulation of the activity state of hepatic branched-chain alpha-keto acid dehydrogenase complex. | |
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MedLine Citation:
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PMID: 2634349 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The hepatic branched-chain alpha-keto acid dehydrogenase complex plays an important role in regulating branched-chain amino acid levels. These compounds are essential for protein synthesis but are toxic if present in excess. When dietary protein is deficient, the hepatic enzyme is present in the inactive, phosphorylated state to allow conservation of branched-chain amino acids for protein synthesis. When dietary protein is excessive, the enzyme is in the active, dephosphorylated state to commit the excess branched-chain amino acids to degradation. Inhibition of protein synthesis by cycloheximide, even when the animal is starving for protein, results in activation of the hepatic branched-chain alpha-keto acid dehydrogenase complex to prevent accumulation of branched-chain amino acids. Likewise, the increase in branched-chain amino acids caused by body wasting during starvation and uncontrolled diabetes is blunted by activation of the hepatic branched-chain alpha-keto acid dehydrogenase complex. The activity state of the hepatic branched-chain alpha-keto acid dehydrogenase complex is regulated in the short term by the concentration of branched-chain alpha-keto acids (inhibitors of branched-chain alpha-keto acid dehydrogenase kinase) and in the long term by alteration in the total branched chain alpha-keto acid dehydrogenase kinase activity. |
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Authors:
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R A Harris; G W Goodwin; R Paxton; P Dexter; S M Powell; B Zhang; A Han; Y Shimomura; R Gibson |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Annals of the New York Academy of Sciences Volume: 573 ISSN: 0077-8923 ISO Abbreviation: Ann. N. Y. Acad. Sci. Publication Date: 1989 |
Date Detail:
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Created Date: 1990-05-31 Completed Date: 1990-05-31 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 7506858 Medline TA: Ann N Y Acad Sci Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 306-13 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, Indiana University School of Medicine, Indianapolis 46223. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) Animals Cells, Cultured Cycloheximide / pharmacology Diabetes Mellitus, Experimental / enzymology* Dietary Proteins / pharmacology Ketone Oxidoreductases / metabolism* Liver / drug effects, enzymology* Male Models, Biological Multienzyme Complexes / metabolism* Nutritional Physiological Phenomena* Rats Rats, Inbred Strains Reference Values Starvation |
| Grant Support | |
ID/Acronym/Agency:
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DK19259/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Dietary Proteins; 0/Multienzyme Complexes; 66-81-9/Cycloheximide; EC 1.2.-/Ketone Oxidoreductases; EC 1.2.4.4/3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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