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 journalArticle

Abstract

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
Volume268
Issue number6 37-6
StatePublished - 1995
Externally publishedYes

Fingerprint

3-methyl-2-oxobutanoate dehydrogenase (lipoamide)
3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
Muscle
Rats
Muscles
muscles
Messenger RNA
rats
skeletal muscle
Skeletal Muscle
RNA
Branched Chain Amino Acids
Malate Dehydrogenase
reticulocytes
Proteolysis
Glyceraldehyde-3-Phosphate Dehydrogenases
branched chain amino acids
glyceraldehyde-3-phosphate dehydrogenase
Muscle Proteins
amino acid metabolism

Keywords

  • 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)

Cite this

England, B. K., Greiber, S., Mitch, W. E., Bowers, B. A., Herring, W. J., McKean, M., ... Danner, D. J. (1995). Rat muscle branched-chain ketoacid dehydrogenase activity and mRNAs increase with extracellular acidemia. American Journal of Physiology - Cell Physiology, 268(6 37-6).

Rat muscle branched-chain ketoacid dehydrogenase activity and mRNAs increase with extracellular acidemia. / England, B. K.; Greiber, S.; Mitch, W. E.; Bowers, B. A.; Herring, W. J.; McKean, M.; Ebb, R. G.; Price, S. R.; Danner, D. J.

In: American Journal of Physiology - Cell Physiology, Vol. 268, No. 6 37-6, 1995.

Research output: Contribution to journalArticle

England, BK, Greiber, S, Mitch, WE, Bowers, BA, Herring, WJ, McKean, M, Ebb, RG, Price, SR & Danner, DJ 1995, 'Rat muscle branched-chain ketoacid dehydrogenase activity and mRNAs increase with extracellular acidemia', American Journal of Physiology - Cell Physiology, vol. 268, no. 6 37-6.
England, B. K. ; Greiber, S. ; Mitch, W. E. ; Bowers, B. A. ; Herring, W. J. ; McKean, M. ; Ebb, R. G. ; Price, S. R. ; Danner, D. J. / Rat muscle branched-chain ketoacid dehydrogenase activity and mRNAs increase with extracellular acidemia. In: American Journal of Physiology - Cell Physiology. 1995 ; Vol. 268, No. 6 37-6.
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