Dependence of Protein Synthesis on Aortic Pressure and Calcium Availability

  • Ellen E. Gordon
  • Yuji Kira
  • Howard E. Morgan
Part of the Advances in Myocardiology book series (ADMY)


Increased aortic pressure accelerated protein synthesis in control–beating and ar- rested–drained hearts supplied with either glucose or pyruvate. Elevation of perfusion pressure from 60 to 120 mm Hg increased oxygen consumption in control–beating but not in arrested–drained preparations. Energy availability, as assessed by adenylate energy charge or creatine phosphate/creatine ratio, or both, was increased in arrested–drained hearts supplied with glucose and perfused at 60 and 120 mm Hg aortic pressure. In control–beating or arrested–drained hearts supplied with pyruvate, energy availability was not improved by elevation of aortic pressure from 60 to 120 mm Hg. An increase of perfusate calcium concentration from 0.5 to 5.0 mM in control–beating Langendorff preparations supplied with glucose and perfused at an aortic pressure of 90 mm Hg doubled oxygen consumption and decreased energy availability, but had no effect on the rate of protein synthesis. In arrested–drained hearts supplied with either glucose or pyruvate and calcium concentrations ranging from 0.5 to 5.0 mM, the rates at 120 mm Hg aortic pressure were 11–25% higher than at 60 mm Hg. These findings provide no evidence to implicate increased oxidative metabolism, energy availability, or extracellular calcium concentration as important factors in the mechanism that accounts for the effect of increased aortic pressure on protein synthesis.


Protein Synthesis Creatine Phosphate Aortic Pressure Extracellular Calcium Energy Availability 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Schreiber, S. S., Oratz, M., and Rothschild, M. A. 1966. Protein synthesis in the overloaded mammalian heart. Am. J. Physiol. 211:314–318.PubMedGoogle Scholar
  2. 2.
    Hjalmarson, A., and Isaksson, O. 1972. In vitro work load and rat heart metabolism. I. Effect on protein synthesis. Acta Physiol. Scand. 86:126–144.PubMedCrossRefGoogle Scholar
  3. 3.
    Morgan, H. E., Chua, B. H. L., Fuller, E. O., and Siehl, D. 1980. Regulation of protein synthesis and degradation during in vitro cardiac work. Am. J. Physiol. 238:E431-E442.Google Scholar
  4. 4.
    Kira, Y., Kochel, P. J., Gordon, E. E., and Morgan, H. E. 1984. Aortic perfusion pressure as a determinant of cardiac protein synthesis. Am. J. Physiol. 246:C247-C258, 1984.Google Scholar
  5. 5.
    Hjalmarson, A., and Isaksson, O. 1972. In Vitro work load and rat heart metabolism. III. Effect on ribosomal aggregation. Acta Physiol. Scand. 86:342–352.PubMedCrossRefGoogle Scholar
  6. 6.
    Schreiber, S. S., Rothschild, M. A., Evans, C., Reff, F., and Oratz, M. 1975. The effect of pressure or flow stress on right ventricular protein synthesis in the face of constant and restricted coronary perfusion. J. Clin. Invest. 55:1–11.PubMedCrossRefGoogle Scholar
  7. 7.
    Jefferson, L. S., Wolpert, E. B., Giger, K. E., and Morgan, H. E. 1971. Regulation of protein synthesis in heart muscle. III. Effect of anoxia on protein synthesis. J. Biol. Chem. 246:2171–2178.PubMedGoogle Scholar
  8. 8.
    Takala, T. 1981. Protein synthesis in the isolated perfused rat heart: Effects of mechanical work load, diastolic ventricular pressure and coronary flow on amino acid incorporation and its transmural distribution into left ventricular protein. Basic Res. Cardiol. 76:44–61.PubMedCrossRefGoogle Scholar
  9. 9.
    Schreiber, S. S., Hearse, D. J., Oratz, M., and Rothschild, M. A. 1977. Protein synthesis in prolonged cardiac arrest. J. Mol. Cell. Cardiol. 9:87–100.PubMedCrossRefGoogle Scholar
  10. 10.
    Opie, L. H. 1965. Coronary flow rate and perfusion pressure as determinants of mechanical function and oxidative metabolism of isolated perfused rat heart. J. Physiol. 180:529–543.PubMedGoogle Scholar
  11. 11.
    Neely, J. R., Liebermeister, H., Battersby, E. J., and Morgan, H. E. 1967. Effect of pressure development on oxygen consumption by isolated rat heart. Am. J. Physiol. 212:804–814.PubMedGoogle Scholar
  12. 12.
    Arnold, G. F., Kosche, E., Miessner, E., Neitzert, A., and Lochner, W. 1968. The importance of the perfusion pressure in the coronary arteries for the contractility and the oxygen consumption. Pfluegers Arch. 299:339–356.CrossRefGoogle Scholar
  13. 13.
    Vogel, W. M., Apstein, C. S., Briggs, L. L., Gaasch, W. H., and Ahn, J. 1982. Acute alterations in left ventricular diastolic chamber stiffness: Role of the “erectile” effect of coronary arterial pressure and flow in normal and damaged hearts. Circ. Res. 51:465–478.PubMedCrossRefGoogle Scholar
  14. 14.
    Peterson, M., and Lesch, M. 1972. Protein synthesis and amino acid transport in the isolated rabbit right ventricular papillary muscle. Circ. Res. 31:317–327.PubMedCrossRefGoogle Scholar
  15. 15.
    Flaim, K. E., Kochel, P. J., Kira, Y., Kobayashi, E. T., Fossel, E. T., Jefferson, L. S., and Morgan, H. E. 1983. Insulin effects on protein synthesis are independent of glucose and energy metabolism. Am. J. Physiol. 245(Cell Physiol. 14):C133–C143.Google Scholar
  16. 16.
    McKee, E. E., Cheung, J. Y., Rannels, D. E., and Morgan, H. E. 1978. Measurement of the rate of protein synthesis and compartmentation of heart phenylalanine. J. Biol. Chem. 253:1030–1040.PubMedGoogle Scholar
  17. 17.
    Kira, Y., Kochel, P., and Morgan, H. E. 1983. Aortic pressure and protein synthesis. In: J. J. Spitzer (ed.), Myocardial Injury. pp. 317–325, Plenum Press, New York.CrossRefGoogle Scholar
  18. 18.
    Morgenstern, C., Höljes, U., Arnold, G., and Lochner, W. 1973. The influence of coronary pressure and coronary flow on intracoronary blood volume and geometry of the left ventricle. Pfluegers Arch. 340:101–111.CrossRefGoogle Scholar
  19. 19.
    Poche, R., Arnold, G., and Gahlen, D. 1971. The influence of coronary perfusion pressure on metabolism and ultrastructure of the arrested aerobically perfused isolated guinea pig heart. Virchows Arch. B 8:252–266.Google Scholar
  20. 20.
    Walton, G. M., and Gill, G. N. 1976. Regulation of ternary (met-tRNAf-GTP-eukaryotic initiation factor 2) protein synthesis initiation complex formation by the adenylate energy charge. Biochem. Biophys. Acta 418:195–203.PubMedCrossRefGoogle Scholar
  21. 21.
    Schreiber, S. S., Oratz, M., Rothschild, M. A., and Smith, D. 1977. Increased cardiac contractility in high calcium perfusion and protein synthesis. J. Mol. Cell. Cardiol. 9:661–669.PubMedCrossRefGoogle Scholar
  22. 22.
    Dietrich, J. W., and Duffield, R. 1979. Effects of the calcium antagonist verapamil on in vitro synthesis of skeletal collagen and noncollagen protein. Endocrinology 105:1168–1171.PubMedCrossRefGoogle Scholar
  23. 23.
    Kameyama, T., and Etlinger, J. D. 1979. Calcium-dependent regulation of protein synthesis and degradation in muscle. Nature (London) 279:344–346.CrossRefGoogle Scholar
  24. 24.
    Lewis, S. E. M., Anderson, P., and Goldspink, D. F. 1982. The effects of calcium on protein turnover in skeletal muscles of the rat. Biochem. J. 204:257–264.PubMedGoogle Scholar
  25. 25.
    Sugden, P. H. 1980. The effects of calcium ions, ionophore A23187 and inhibition of energy metabolism on protein degradation in the rat diaphragm and epitrochlearis muscles in vitro. Biochem. J. 190:593–603.PubMedGoogle Scholar
  26. 26.
    Safer, B. 1983. 2B or not 2B: Regulation of the catalytic utilization of eIF-2. Cell 33:7–8.PubMedCrossRefGoogle Scholar
  27. 27.
    Ochoa, S. 1983. Regulation of protein synthesis initiation in eukaryotes. Arch. Biochem. Biophys. 223:325–349.PubMedCrossRefGoogle Scholar
  28. 28.
    Panniers, R., and Henshaw, E. C. 1983. A GDP/GTP exchange factor essential for eukaryotic initiation factor 2 cycling in Ehrlich ascites tumor cells and its regulation by eukaryotic initiation factor 2 phosphorylation. J. Biol. Chem. 258:7928–7934.PubMedGoogle Scholar
  29. 29.
    Proud, C. G., and Pain, V. M. 1982. Purification and phosphorylation of initiation factor eIF-2 from rabbit skeletal muscle. FEBS Lett. 143:55–59.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1985

Authors and Affiliations

  • Ellen E. Gordon
    • 1
  • Yuji Kira
    • 1
  • Howard E. Morgan
    • 1
  1. 1.Department of Physiology, The Milton S. Hershey Medical CenterThe Pennsylvania State UniversityHersheyUSA

Personalised recommendations