Basic Research in Cardiology

, Volume 76, Issue 1, pp 79–88 | Cite as

The adaptive changes in the isoenzyme pattern of myosin from hypertrophied rat myocardium as a result of pressure overload and physical training

Original Contributions

Summary

The distribution of cardiac myosin isoenzymes is altered as a result of pressure overload and physical training. Using polyacrylamide gel electrophoresis in sodium pyrophosphate, it was found that myosin fromlleft ventricles of adult rats exists in three polymorphic form, V1, V2 and V3. Cardiac hypertrophy due to renal hypertension (Goldblatt II) led to a shift of the isoenzymes towards V3, whereas swimming training resulted in an opposite redistribution. The isoenzyme V1 predominated, only traces of V2 and V3 were detectable. The changes in the isoenzyme distribution were reflected in al altered ATPase activity of myofibrils. in a representative sample of the Goldblatt rats, the activity was reduced by 11% and the swimming training led to an increase by 10%. Changes in myofibrillar ATPase can, therefore, be traced to alterations in the isoenzyme pattern of myosin. The polymorphism of myosin has a two-faced aspect as regards cardiac performance. For example, a shift towards V3 is expected to increase the economy for tension development during isovolumetric contraction at the expense of a reduced maximum speed of ventricular contraction.

Key words

myosin hypertrophy pressure overload physical training 

Zusammenfassung

Das Isoenzymmuster von Myosin aus dem linken Ventrikel kann durch eine Druckhypertrophie und ein körperliches Training verändert werden. Mit Hilfe der Polyacrylamid-Gel-elektrophorese in Natriumpyrophosphat konnte gezeigt werden, daß Myosin aus den linken Ventrikeln von erwachsenen Ratten in drei polymorphen Formen, V1, V2 und V3, vorkommt. Eine Herzhypertrophie als Folge eines renalen Hochdruckes (Goldblatt II) führte zu einer Verschiebung der Isoenzyme in Richtung von V3, während ein Schwimmtraining zu einer entgegengesetzten Umverteilung führte. Das Isoenzym V1 dominierte, von V2 und V3 waren nur Spuren erkennbar. Die Verschiebungen im Isoenzymmuster führen zu einer verän derten myofibrillären ATPase-Aktivität. Bei einem repräsentativen Beispiel der Goldblatt-Ratten war die Aktivität um 11% erniedrigt, während sie nach einem Schwimmtraining um 10% erhöht war. Eine Veränderung in der myofibrillären ATPase-Aktivität muß daher auf eine Umverteilung im Isoenzymmuster des Myosins zurückgeführt werden. Der Polymorphismus von Myosin hat doppelwertige Auswirkungen auf die Herzfunktion. So führt zum Beispiel eine Verschiebung in Richtung von V3 zu einer höheren Ökonomie der Spannungsentwicklung bei der isovolumetrischen Anspannungsphase auf Kosten einer verringerten maximalen Kontraktionsgeschwindigkeit der Ventrikel.

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Copyright information

© Dr. Dietrich Steinkopff Verlag 1981

Authors and Affiliations

  • H. Rupp
    • 1
  1. 1.Physiol. Institut, Lehrstuhl IIUniversität TübingenTübingen

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