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PMID: 7706272 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Adenylate kinase-catalyzed phosphoryl transfer couples ATP utilization with its generation by glycolysis in intact muscle.

The Journal of biological chemistry ·Vol. 270 ·No. 13 ·1995-03-31 ·Pages 7311-9

Zeleznikar RJ, Dzeja PP, Goldberg ND

Abstract

We previously suggested that an importance of adenylate kinase (AdK) in skeletal muscle is to function as a high energy phosphoryl transfer system regulating ATP generation in correspondence with its consumption by specific cellular processes. The present experiments are intended to define the ATP-generating system coupled to and regulated by AdK-catalyzed phosphotransfer in skeletal muscle and also to examine the relationship between AdK- and creatine kinase (CK)-catalyzed phosphotransfer. Rates of phosphoryl transfer catalyzed by AdK were assessed in intact, isolated rat diaphragm by determining rates of AMP phosphorylation with endogenously generated [gamma-18O]ATP under conditions of altered anaerobic and aerobic ATP production. AdK-catalyzed phosphoryl transfer rates accelerated incrementally up to 12-fold in direct proportion to stimulated contractile frequency in parallel with equivalent increases in rates of ATP generation by lactate producing glycolysis. Stoichiometric equivalent increases of AdK-catalyzed phosphotransfer and anaerobic ATP production also occurred up to more than 20-fold when oxidative phosphorylation was impaired by either O2 deprivation or treatment with KCN or p-(trifluoromethoxy)-phenylhydrazone. These enhanced rates of AMP phosphorylation were balanced by virtually identically increased rates of AdK-catalyzed generation of AMP. This AMP was traced to arise from AdK-catalyzed phosphotransfer involving ADP generated by a muscle ATPase. Increased AdK-catalyzed phosphotransfer paired with the apparent compensatory increase in ATP generation by anaerobic glycolysis in oxygen-deprived muscle occurred coincident with diminished rates of CK-catalyzed phosphoryl transfer indicative of a pairing between oxidatively produced ATP and CK-catalyzed phosphotransfer. A metabolic model consistent with these results and conforming to the Mitchell general principle of vectorial ligand conduction is suggested.

MeSH Terms
Adenosine Diphosphate/metabolism Adenosine Monophosphate/metabolism Adenosine Triphosphate/metabolism Adenylate Kinase/metabolism Anaerobiosis Animals Creatine Kinase/metabolism Diaphragm/metabolism Glycolysis In Vitro Techniques Kinetics Lactates/analysis Male Models, Biological Muscle Contraction Muscle, Skeletal/metabolism,physiology Oxygen Isotopes Phosphotransferases/metabolism Rats Rats, Sprague-Dawley
Chemicals
Lactates Oxygen Isotopes Adenosine Monophosphate Adenosine Diphosphate Adenosine Triphosphate Phosphotransferases Creatine Kinase Adenylate Kinase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Zeleznikar R J
Department of Biochemistry, University of Minnesota, Medical School, Minneapolis 55455, USA.
Dzeja P P
Goldberg N D
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1995-03-31
Pages
7311-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM28818 · United States
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