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. 1973 Mar;132(3):527–535. doi: 10.1042/bj1320527

The effects of calcium ions on the activities of trehalase, hexokinase, phosphofructokinase, fructose diphosphatase and pyruvate kinase from various muscles

H Vaughan 1, S D Thornton 1, E A Newsholme 1
PMCID: PMC1177617  PMID: 4353381

Abstract

1. The effects of Ca2+ on the activities and regulatory properties of trehalase, hexokinase, phosphofructokinase, fructose diphosphatase and pyruvate kinase from vertebrate red and white muscle and insect fibrillar and non-fibrillar muscle have been investigated. These muscles were selected because of the possible difference in the role of glycolysis in energy production in the vertebrate muscles, and the possible difference in the role of Ca2+ in the control of contraction in the two types of insect muscle. An increase in Ca2+ concentration from 0.001μm to 10μm did not modify the activities nor did it modify the regulatory properties of these enzymes from these various muscles. 2. Concentrations of Ca2+ above 0.1mm inhibited the activities of hexokinase and phosphofructokinase from the different muscles. It has been suggested that this inhibition may provide the basis for a theory of regulation of glycolysis (Margreth et al., 1967). If phosphofructokinase is located within the sarcoplasmic reticulum, its activity will be inhibited when the muscle is at rest, but the release of Ca2+ from the reticulum during contraction will lead to a stimulation of its activity and hence an increase in glycolytic flux. The distribution of hexokinase and phosphofructokinase in the various cell fractions of these muscles was very variable. In particular, both enzymes were present almost exclusively in the 100000g supernatant fraction in the extracts of insect flight muscles. Thus there is no correlation between the properties of the enzymes and their distribution in muscle. 3. It is concluded that Ca2+ does not control the activities of the important regulatory enzymes of glycolysis in muscle. It is suggested that in some muscles the sensitivity of the control mechanism at the level of phosphofructokinase to changes in the concentration of AMP may be increased by a process known as `substrate-cycling'.

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Selected References

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

  1. Brostrom C. O., Hunkeler F. L., Krebs E. G. The regulation of skeletal muscle phosphorylase kinase by Ca2+. J Biol Chem. 1971 Apr 10;246(7):1961–1967. [PubMed] [Google Scholar]
  2. CHAPPELL J. B., PERRY S. V. Biochemical and osmotic properties of skeletal muscle mitochondria. Nature. 1954 Jun 5;173(4414):1094–1095. doi: 10.1038/1731094a0. [DOI] [PubMed] [Google Scholar]
  3. Crabtree B., Newsholme E. A. The activities of phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenases in muscles from vertebrates and invertebrates. Biochem J. 1972 Jan;126(1):49–58. doi: 10.1042/bj1260049. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Crabtree B., Newsholme E. A. The activities of proline dehydrogenase, glutamate dehydrogenase, aspartate-oxoglutarate aminotransferase and alanine-oxoglutarate aminotransferase in some insect flight muscles. Biochem J. 1970 May;117(5):1019–1021. doi: 10.1042/bj1171019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ebashi S., Endo M. Calcium ion and muscle contraction. Prog Biophys Mol Biol. 1968;18:123–183. doi: 10.1016/0079-6107(68)90023-0. [DOI] [PubMed] [Google Scholar]
  6. England P. J., Randle P. J. Effectors of rat-heart hexokinases and the control of rates of glucose phosphorylation in the perfused rat heart. Biochem J. 1967 Dec;105(3):907–920. doi: 10.1042/bj1050907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HASSELBACH W., MAKINOSE M. UBER DEN MECHANISMUS DES CALCIUMTRANSPORTES DURCH DIE MEMBRANEN DES SARKOPLASMATISCHEN RETICULUMS. Biochem Z. 1963 Oct 14;339:94–111. [PubMed] [Google Scholar]
  8. KARPATKIN S., HELMREICH E., CORI C. F. REGULATION OF GLYCOLYSIS IN MUSCLE. II. EFFECT OF STIMULATION AND EPINEPHRINE IN ISOLATED FROG SARTORIUS MUSCLE. J Biol Chem. 1964 Oct;239:3139–3145. [PubMed] [Google Scholar]
  9. Newsholme E. A., Crabtree B., Higgins S. J., Thornton S. D., Start C. The activities of fructose diphosphatase in flight muscles from the bumble-bee and the role of this enzyme in heat generation. Biochem J. 1972 Jun;128(1):89–97. doi: 10.1042/bj1280089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Newsholme E. A., Crabtree B. The role of fructose-1,6-diphosphatase in the regulation of glycolysis in skeletal muscle. FEBS Lett. 1970 Apr 2;7(2):195–198. doi: 10.1016/0014-5793(70)80155-7. [DOI] [PubMed] [Google Scholar]
  11. Newsholme E. A., Robinson J., Taylor K. A radiochemical enzymatic activity assay for glycerol kinase and hexokinase. Biochim Biophys Acta. 1967 Mar 15;132(2):338–346. doi: 10.1016/0005-2744(67)90153-2. [DOI] [PubMed] [Google Scholar]
  12. Opie L. H., Mansford K. R., Owen P. Effects of increased heart work on glycolysis and adenine nucleotides in the perfused heart of normal and diabetic rats. Biochem J. 1971 Sep;124(3):475–490. doi: 10.1042/bj1240475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Opie L. H., Newsholme E. A. The inhibition of skeletal-muscle fructose 1,6-diphosphatase by adenosine monophosphate. Biochem J. 1967 Aug;104(2):353–360. doi: 10.1042/bj1040353. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ozawa E., Hosoi K., Ebashi S. Reversible stimulation of muscle phosphorylase b kinase by low concentrations of calcium ions. J Biochem. 1967 Apr;61(4):531–533. doi: 10.1093/oxfordjournals.jbchem.a128582. [DOI] [PubMed] [Google Scholar]
  15. PASSONNEAU J. V., LOWRY O. H. Phosphofructokinase and the Pasteur effect. Biochem Biophys Res Commun. 1962 Feb 20;7:10–15. doi: 10.1016/0006-291x(62)90134-1. [DOI] [PubMed] [Google Scholar]
  16. PORTZEHL H., CALDWELL P. C., RUEEGG J. C. THE DEPENDENCE OF CONTRACTION AND RELAXATION OF MUSCLE FIBRES FROM THE CRAB MAIA SQUINADO ON THE INTERNAL CONCENTRATION OF FREE CALCIUM IONS. Biochim Biophys Acta. 1964 May 25;79:581–591. doi: 10.1016/0926-6577(64)90224-4. [DOI] [PubMed] [Google Scholar]
  17. Pringle J. W. The contractile mechanism of insect fibrillar muscle. Prog Biophys Mol Biol. 1967;17:1–60. doi: 10.1016/0079-6107(67)90003-x. [DOI] [PubMed] [Google Scholar]
  18. REGEN D. M., DAVIS W. W., MORGAN H. E., PARK C. R. THE REGULATION OF HEXOKINASE AND PHOSPHOFRUCTOKINASE ACTIVITY IN HEART MUSCLE. EFFECTS OF ALLOXAN DIABETES, GROWTH HORMONE, CORTISOL, AND ANOXIA. J Biol Chem. 1964 Jan;239:43–49. [PubMed] [Google Scholar]
  19. Sacktor B., Hurlbut E. C. Regulation of metabolism in working muscle in vivo. II. Concentrations of adenine nucleotides, arginine phosphate, and inorganic phosphate in insect flight muscle during flight. J Biol Chem. 1966 Feb 10;241(3):632–634. [PubMed] [Google Scholar]
  20. Sacktor B., Wormser-Shavit E. Regulation of metabolism in working muscle in vivo. I. Concentrations of some glycolytic, tricarboxylic acid cycle, and amino acid intermediates in insect flight muscle during flight. J Biol Chem. 1966 Feb 10;241(3):624–631. [PubMed] [Google Scholar]
  21. Tanaka T., Harano Y., Sue F., Morimura H. Crystallization, characterization and metabolic regulation of two types of pyruvate kinase isolated from rat tissues. J Biochem. 1967 Jul;62(1):71–91. doi: 10.1093/oxfordjournals.jbchem.a128639. [DOI] [PubMed] [Google Scholar]

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