Advertisement

Ventricular Myocardium as a Fast- or Slow-Type Muscle. The Influence of Stressors and the Preventive Action of Intense Exercise

  • H. Rupp
  • R. Jacob
Part of the Developments in Cardiovascular Medicine book series (DICM, volume 46)

Abstract

Increased sympathetic outflow to the heart is associated with high heart rates and fast fiber shortening. It might, therefore, be expected that chronic, intermittently, increased sympathetic drive of heart leads to adaptational reactions at the myofibrillar level with improved potential to cope with the imposed load. Past fiber shortening can in principal be achieved either by increased transmembrane Ca2+ fluxes, or via an increase in the rate of cross bridge cycling. Altered transmembrane Ca2+ fluxes are employed primarily for acute adjustment of heart performance to given demands. The set-point of this modulation of velocity-dependent parameters is given by the isoenzyme population of myosin (1). Alterations in the myosin isoenzyme population are achieved only on a longer-term basis as can be inferred from the 5.5 days half-life of myosin (2). Intermittently increased sympathetic drive of the heart is expected to be associated possibly with an adaptive response in terms of expression of genes coding for the fast myosin isoenzyme.

Keywords

Ventricular Myocardium Cardiac Myosin Functional Load Fast Fiber Sympathetic Drive 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Rupp H: The determinants of the calcium-dependent activation of myofibrils from rat heart as judged by myofibrillar adenosine triphosphatase and superprecipitation of natural actomyosin. Mol Physiol (3): 249–263, 1983.Google Scholar
  2. 2.
    Everett AW, Prior G, Zak R: Equilibration of leucine between the plasma compartment and leucyl-tRNA in the heart, and turnover of cardiac myosin heavy chain. Biochem J (194): 365–368, 1981.PubMedGoogle Scholar
  3. 3.
    Rupp H, Felbier H-R, Jacob R: Blood pressure and cardiac myosin heterogeneity in the rat as influenced by swimming and emotional excitation. In: Jacob R, Gülch RW, Kissling G (eds) Cardiac adaptation to hemodynamic overload, training and stress. Steinkopff Verlag, Darmstadt, 1983, PP 274–281.Google Scholar
  4. 4.
    Rupp H, Bukhari AR, Jacob R: Stress can prevent swimming-exercise-induced reduction of adrenal PNMT activity in the rat. In: Usdin E, Kvetnansky R, Axelrod J (eds) Stress: The role of catecholamines and other neurotransmitters. Gordon & Breach Publ, New York, in press.Google Scholar
  5. 5.
    Rupp H, Felbier H-R, Bukhari AR, Jacob R: Modulation of myosin isoenzyme populations and activities of monoamine oxidase and phenylethanolamine-N-methyltransferase in pressure loaded and normal rat heart by swimming exercise and stress arising from electrostimulation in pairs. Can J Physiol Pharmacol, in press.Google Scholar
  6. 6.
    Rupp H, Jacob R: Response of blood pressure and cardiac myosin polymorphism to swimming training in the spontaneously hypertensive rat. Can J Physiol Pharmacol (60): 1098–1103, 1982.PubMedCrossRefGoogle Scholar
  7. 7.
    Rupp H: The adaptive changes in the isoenzyme pattern of myosin from hypertrophied rat myocardium as a result of pressure overload and physical training. Basic Res Cardiol (76): 79–88, 1981.PubMedCrossRefGoogle Scholar
  8. 8.
    Rupp H: Polymorphic myosin as the common determinant of myofibrillar ATPase in different haemodynamic and thyroid states. Basic Res Cardiol (77): 34–46, 1982.PubMedCrossRefGoogle Scholar
  9. 9.
    Pope B, Hoh JFY, Weeds A: The ATPase activities of rat cardiac myosin isoenzymes. FEBS Lett (118): 205–208, 1980.PubMedCrossRefGoogle Scholar
  10. 10.
    Ebrecht G, Rupp H, Jacob R: Alterations of mechanical parameters in chemically skinned preparations of rat myocardium as a function of isoenzyme pattern of myosin. Basic Res Cardiol (77): 220–234, 1982.PubMedCrossRefGoogle Scholar
  11. 11.
    Clark AJ: Comparative Physiology of the Heart. University Press, Cambridge, 1927.Google Scholar
  12. 12.
    Zak R: Contractile function as a determinant of muscle growth. In: Dowben RM, Shay JW (eds) Cell and muscle motility, Vol 1. Plenum Publishing Corporation, New York, 1981, pp 1–33.Google Scholar
  13. 13.
    Takeda N, Rupp H, Fenchel G, Hoffmeister H-E, Jacob R: Myofibrillar ATPase activity of human biopsy material as related to hemodynamic parameters. Eur Heart J (5 Suppl 1): 1004, 1984.Google Scholar
  14. 14.
    Mercadier J-J, Bouveret P, Gorza L, Schiaffino S, Clark WA, Zak R, Swynghedauw B, Schwartz K: Myosin isoenzymes in normal and hypertrophied human ventricular myocardium. Circ Res (53): 52–62, 1983.PubMedGoogle Scholar
  15. 15.
    Hoh JEY, McGrath PA, Hale PT: Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol (10): 1053–1076, 1978.PubMedCrossRefGoogle Scholar
  16. 16.
    Banerjee SK: Comparative studies of atrial and ventricular myosin from normal, thyrotoxic, and thyroidectomized rabbits. Circ Res (52): 131–136, 1983.PubMedGoogle Scholar
  17. 17.
    Bukhari AR, Rupp H: Differential effect of thyroid hormones on catecholamine enzymes and myosin isoenzymes in ventricles and atria of the rat heart. In: Jacob R, Gülch RW, Kissling G (eds) Cardiac adaptation to hemodynamic overload, training and stress. Steinkopff Verlag, Darmstadt, 1983, PP 59–64.Google Scholar
  18. 18.
    Clark WA Jr, Chizzonite RA, Everett AW, Rabinowitz M, Zak R: Species correlations between cardiac isomyosins. A comparison of electrophoretic and immunological properties. J Biol Chem (257): 5449–5454, 1982.PubMedGoogle Scholar
  19. 19.
    Alpert NR, Mulieri LA, Litten RZ: Isoenzyme contribution to economy of contraction and relaxation in normal and hypertrophied hearts. In: Jacob R, Gülch RW, Kissling G (eds) Cardiac adaptation to hemodynamic overload, training and stress. Steinkopff Verlag, Darmstadt, 1983, PP 147–157.Google Scholar
  20. 20.
    Kissling G, Rupp H, Malloy L, Jacob R: Alterations in cardiac oxygen consumption under chronic pressure overload. Significance of the isoenzyme pattern of myosin. Basic Res Cardiol (77): 255–269, 1982.PubMedCrossRefGoogle Scholar
  21. 21.
    Kissling G, Malloy L, Rupp H: Energetics of the rat heart in chronic pressure overload. In: Jacob R, Gülch RW, Kissling G (eds) Cardiac adaptation to hemodynamic overload, training and stress. Steinkopff Verlag, Darmstadt, 1983, pp 167–173.Google Scholar
  22. 22.
    Hoh JPY, Yeoh GPS, Thomas MAW, Higginbottom L: Structural differences in the heavy chains of rat ventricular myosin isoenzymes. EEBS Lett (97): 330–334, 1979.Google Scholar
  23. 23.
    Rupp H, Bukhari AR, Jacob R: Regulation of cardiac myosin isoenzymes — the interrelationship with catecholamine metabolism. J Mol Cell Cardiol (15 Suppl 1): 317, 1983.Google Scholar
  24. 24.
    Jacob R, Kissling G, Ebrecht G, Holubarsch C, Medugorac I, Rupp H: Adaptive and pathological alterations in experimental cardiac hypertrophy. Advan Myocardiol (4): 55–77, 1983.Google Scholar

Copyright information

© Martinus Nijhoff Publishing, Boston 1985

Authors and Affiliations

  • H. Rupp
  • R. Jacob

There are no affiliations available

Personalised recommendations