Rat muscle branched-chain ketoacid dehydrogenase activity and mRNAs increase with extracellular acidemia

B. K. England, S. Greiber, W. E. Mitch, B. A. Bowers, W. J. Herring, M. McKean, R. G. Ebb, S. R. Price, D. J. Danner

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


The rate-limiting enzyme in branched-chain amino acid catabolism is branched-chain ketoacid dehydrogenase (BCKAD). In rats fed NH4Cl to induce acidemia, we find increased basal BCKAD activity as well as maximal activity in skeletal muscle. Concurrently, there is a > 10-fold increase in mRNAs of BCKAD subunits in skeletal muscle plus an increase in cardiac muscle but not in liver or kidney. There was no increase in mRNA for malate dehydrogenase or for cytosolic glyceraldehyde-3-phosphate dehydrogenase. Evaluation of the translation capacity of BCKAD mRNAs in muscle of acidemic rats yielded more immunoreactive BCKAD whether the proteins were synthesized from muscle RNA using rabbit reticulocyte lysate or directly using postmitochondrial homogenates. Although the RNA from muscle of acidemic rats yielded twice as much BCKAD protein, we found no net increase in mitochondrial BCKAD protein in muscle by Western blotting. Because there is increased proteolysis in muscle of rats with acidemia, the increase in mRNA might be a mechanism to augment BCKAD synthesis and activity in muscle.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Issue number6 37-6
StatePublished - 1995
Externally publishedYes


  • acidosis
  • branched-chain amino acids
  • gene expression
  • ketone-oxidoreductase
  • messenger ribonucleic acid translation

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Physiology
  • Agricultural and Biological Sciences(all)


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