Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1977 Jun 15;164(3):693–697. doi: 10.1042/bj1640693

Pyruvate dehydrogenase activity in hamster small intestine during development.

C M Schiller
PMCID: PMC1164848  PMID: 883960

Abstract

Total pyruvate dehydrogenase activities in hamster intestine increase from 40 nmol/min (munits) per g of intestine in the foetal animals to 460 munits/g in the adult, whereas the fraction of the enzyme in the active form increases from 34 to 42% of the total activity over the same period. However, a complete conversion of the enzyme into the active form is observed in the neonatal animal immediately after birth. Results from experiments in vitro suggested that the activation of pyruvate dehydrogenase is controlled, in part, by the [NAD+]/[NADH] ratio. This proposal was tested in vivo by examining the proportion of the enzyme in the active form during conditions when the [NAD+]/[NADH] ratio was markedly altered, and the data show a direct relationship between the mitochondrial redox state and activity of the active form.

Full text

PDF
693

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ballard F. J. Regulation of gluconeogenesis during exposure of young rats to hypoxic conditions. Biochem J. 1971 Jan;121(2):169–178. doi: 10.1042/bj1210169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ballard F. J. The development of gluconeogenesis in rat liver. Controlling factors in the newborn. Biochem J. 1971 Sep;124(2):265–274. doi: 10.1042/bj1240265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cooper R. H., Randle P. J., Denton R. M. Stimulation of phosphorylation and inactivation of pyruvate dehydrogenase by physiological inhibitors of the pyruvate dehydrogenase reaction. Nature. 1975 Oct 30;257(5529):808–809. doi: 10.1038/257808a0. [DOI] [PubMed] [Google Scholar]
  4. Denton R. M., Halperin M. L. The control of fatty acid and triglyceride synthesis in rat epididymal adipose tissue. Roles of coenzyme A derivatives, citrate and L-glycerol 3-phosphate. Biochem J. 1968 Nov;110(1):27–38. doi: 10.1042/bj1100027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Denton R. M., Randle P. J., Martin B. R. Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase. Biochem J. 1972 Jun;128(1):161–163. doi: 10.1042/bj1280161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hucho F., Randall D. D., Roche T. E., Burgett M. W., Pelley J. W., Reed L. J. -Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart. Arch Biochem Biophys. 1972 Jul;151(1):328–340. doi: 10.1016/0003-9861(72)90504-8. [DOI] [PubMed] [Google Scholar]
  7. Knowles S. E., Ballard F. J. Pyruvate dehydrogenase activity in rat liver during development. Biol Neonate. 1974;24(1):41–48. doi: 10.1159/000240630. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Linn T. C., Pettit F. H., Hucho F., Reed L. J. Alpha-keto acid dehydrogenase complexes. XI. Comparative studies of regulatory properties of the pyruvate dehydrogenase complexes from kidney, heart, and liver mitochondria. Proc Natl Acad Sci U S A. 1969 Sep;64(1):227–234. doi: 10.1073/pnas.64.1.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Linn T. C., Pettit F. H., Reed L. J. Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc Natl Acad Sci U S A. 1969 Jan;62(1):234–241. doi: 10.1073/pnas.62.1.234. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pettit F. H., Pelley J. W., Reed L. J. Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios. Biochem Biophys Res Commun. 1975 Jul 22;65(2):575–582. doi: 10.1016/s0006-291x(75)80185-9. [DOI] [PubMed] [Google Scholar]
  12. Pettit F. H., Roche T. E., Reed L. J. Function of calcium ions in pyruvate dehydrogenase phosphatase activity. Biochem Biophys Res Commun. 1972 Oct 17;49(2):563–571. doi: 10.1016/0006-291x(72)90448-2. [DOI] [PubMed] [Google Scholar]
  13. Roche T. E., Reed L. J. Monovalent cation requirement for ADP inhibition of pyruvate dehydrogenase kinase. Biochem Biophys Res Commun. 1974 Aug 19;59(4):1341–1348. doi: 10.1016/0006-291x(74)90461-6. [DOI] [PubMed] [Google Scholar]
  14. Schiller C. M., Taylor W. M., Halperin M. L. Control of fatty acid synthesis in white adipose tissue by insulin: coordination between the mitochondrial citrate transporter and pyruvate dehydrogenase. Can J Biochem. 1974 Oct;52(10):814–821. [PubMed] [Google Scholar]
  15. Siess E. A., Wieland O. H. Purification and characterization of pyruvate-dehydrogenase phosphatase from pig-heart muscle. Eur J Biochem. 1972 Mar 15;26(1):96–105. doi: 10.1111/j.1432-1033.1972.tb01744.x. [DOI] [PubMed] [Google Scholar]
  16. Taylor S. I., Mukherjee C., Jungas R. L. Studies on the mechanism of activation of adipose tissue pyruvate dehydrogenase by insulin. J Biol Chem. 1973 Jan 10;248(1):73–81. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES