Abstract
The heart, like most types of tissues, can adapt to envirommental factors and, more specifically, to its load. Overloading a heart as well as changing its initial length may increase work by means of two successive adaptational processes: (1) immediately by bringing the muscle’s own mechanical properties into play and (2) at a later stage by changing muscle mass and structure.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Barany M (1967) ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol 50: 197–216
Delcayre C, Swynghedauw B (1975) A comparative study of heart myosin ATPase and light subunits from different species. Pfluegers Arch, 355: 39–47
Leger JJ, Berson G, Delcayre C, Schwartz K, Leger J, Stephens M, Swynghedauw B (1975) Heart contractile proteins. Biochimie 55: 1249–1273
Klotz C, Aumont MC, Leger J J, Swynghedauw B (1975) Human cardiac myosin ATPase and light subunits. A comparative study. Biochim Biophys Acta 386: 461–469
Schwartz K, Bouveret P, Sebag C, Swynghedauw B (1977) Immunochemical evidence for the species-specificity of mammalian cardiac myosin and HMM. Biochim Biophys Acta 425: 24–36
Buller AJ, Mommaerts WFHM, Seraydarian K (1969) Enzymatic properties of myosin in fast and slow twitch muscles of the cat following cross-innervation. J Physiol (London) 205: 581–597
Sreter FA, Elzinga M, Mabuchi K (1975) The N-methylhistidine content of myosin in stimulated and cross re-innervated skeletal muscles of the rabbit. FEBS Lett. 57: 107–111
Katagiri I, Stone Freedberg A, Morkin E (1975) The effect of N-ethyl-maleimide on the ATPase activities of cardiac myosin from thyrotoxic rabbit. Life Sci 16: 1079–1087
Swynghedauw B, Leger JJ, Schwartz K (1976) The myosin isozyme hypothesis in chronic heart overloading. J Mol Cell Cardiol 8: 915–924
Stephens M, Leger JJ, Preteseille M, Swynghedauw B (1979) The relationship of a decline in myofibrillar ATPase activity to the development of severe left ventricular hypertrophy in the rat. Pathol Biol (Paris) 27: 41–44
Leclercq JF, Swynghedauw B (1976) Myofibrillar ATPase and OHPro content of human hypertrophied heart. Eur J Clin Invest 6: 27–33
D’Albis A, Gratzer WB (1973) Electrophoretic examination of native myosin. FEBS Lett 48: 292–296
Lompre AM, Schwartz K, D’Albis A, Lacombe G, Thiem NV, Swynghedauw B (1979) Myosin isoenzyme redistribution in chronic heart over-loading. Nature 282: 105–107
Swynghedauw B, Klotz C, Leger JJ, Preteseille M (1973) Heart myosin ATPase and light subunits in experimental rabbit’s chronic aortic insuffi–ciency. J Mol Cell Cardiol 5: 501–514
Schwartz K, Bouveret P, Bercovici J, Swynghedauw B (1978) An immuno-chemical difference between myosins in normal and hypertrophied rat hearts. FEBS Lett 93: 137–140
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1981 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Swynghedauw, B., Schwartz, K., Lacombe, G., Leger, J.J., Thiem, N.V., Lompre, A.M. (1981). Cardiac Myosin in Heart Overloading. In: Strauer, B.E. (eds) The Heart in Hypertension. International Boehringer Mannheim Symposia. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67922-3_8
Download citation
DOI: https://doi.org/10.1007/978-3-642-67922-3_8
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-10496-4
Online ISBN: 978-3-642-67922-3
eBook Packages: Springer Book Archive