| Bimodal activation of acetyl-CoA carboxylase by glutamate. | |
| | |
MedLine Citation:
|
PMID: 10753875 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Acetyl-CoA carboxylase (ACC) catalyzes the formation of malonyl-CoA, an essential substrate for fatty acid biosynthesis and a potent inhibitor of fatty acid oxidation. Here, we provide evidence that glutamate may be a physiologically relevant activator of ACC. Glutamate induced the activation of both major isoforms of ACC, prepared from rat liver, heart, or white adipose tissue. In agreement with previous studies, a type 2A protein phosphatase contributed to the effects of glutamate on ACC. However, the protein phosphatase inhibitor microcystin LR did not abolish the effects of glutamate on ACC activity. Moreover, glutamate directly activated purified preparations of ACC when protein phosphatase activity was excluded. Phosphatase-independent ACC activation by glutamate was also reflected by polymerization of the enzyme as judged by size-exclusion chromatography. The sensitivity of ACC to direct activation by glutamate was diminished by treatment in vitro with AMP-activated protein kinase or cAMP-dependent protein kinase or by beta-adrenergic stimulation of intact adipose tissue. We conclude that glutamate, an abundant intracellular amino acid, induces ACC activation through complementary actions as a phosphatase activator and as a direct allosteric ligand for dephosphorylated ACC. This study supports the general hypothesis that amino acids fulfill important roles as signal molecules as well as intermediates in carbon and nitrogen metabolism. |
| | |
Authors:
|
A N Boone; A Chan; J E Kulpa; R W Brownsey |
Related Documents
:
|
22840055 - Carboxyalkylation of chitosan in the gel state. 741065 - Utilization of pyruvate, alanine and glutamate by isolated fat cells and their effects ... 17497675 - Among the branched-chain amino acids, only valine metabolism is up-regulated in astrocy... 6751975 - The stimulus-secretion coupling of amino acid-induced insulin release. xi. kinetics of ... 7561895 - Mechanistic evaluation of new plant-derived compounds that inhibit hiv-1 reverse transc... 23258535 - Glycosyltransferases from oat (avena) implicated in the acylation of avenacins. |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: The Journal of biological chemistry Volume: 275 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2000 Apr |
Date Detail:
|
Created Date: 2000-05-05 Completed Date: 2000-05-05 Revised Date: 2007-11-15 |
Medline Journal Info:
|
Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: UNITED STATES |
Other Details:
|
Languages: eng Pagination: 10819-25 Citation Subset: IM |
Affiliation:
|
Department of Biochemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Acetyl-CoA Carboxylase
/
drug effects*,
metabolism Adipose Tissue / enzymology Animals Cyclic AMP-Dependent Protein Kinases / pharmacology Enzyme Activation Glutamic Acid / pharmacology* Isoenzymes / drug effects Liver / enzymology Male Myocardium / enzymology Phosphoprotein Phosphatases / physiology Phosphorylation Polymers / metabolism Rats Rats, Wistar |
| Chemical | |
Reg. No./Substance:
|
0/Isoenzymes; 0/Polymers; 56-86-0/Glutamic Acid; EC 2.7.11.11/Cyclic AMP-Dependent Protein Kinases; EC 3.1.3.16/Phosphoprotein Phosphatases; EC 6.4.1.2/Acetyl-CoA Carboxylase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Nitric oxide reaction with lipid peroxyl radicals spares alpha-tocopherol during lipid peroxidation....
Next Document: Reactive nitrogen and oxygen species attenuate interleukin- 8-induced neutrophil chemotactic activit...