Influence of the thyroid state on myocardial myosin in the adult pig heart

Wiegand, V.; Henniges, H.; Oberschmidt, R.; Kreuzer, H

doi:10.1016/s0022-2828(84)80553-2

Cited by 2 publications

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“…In several experimental models of myocardial hypertrophy and insufficiency, heavy chain transitions have been found in the rodent heart as the basis of altered myofibrillar ATPase a c t i v i t i e~.~-~.~ No comparable isomyosin shift concomitant with changes in myocardial contractility exists in the myocardium of higher mammals. [33][34][35] In accordance, no isomyosin transition based on a heavy chain polymorphism seems to take place in human dilated cardiomyopathy . Concomitantly, myofibrillar and myosin ATPase activities of the cardiomyopathic myocardium were unchanged in the present study.…”

Section: Discussionmentioning

confidence: 70%

Structure and function of contractile proteins in human dilated cardiomyopathy

Wiegand

Ebecke

Figulla

et al. 1989

Clinical Cardiology

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Summary: The pathogenesis of reduced systolic left ventricular function in dilated cardiomyopathy is yet unclear. To analyze a possible involvement of contractile protein, function and structure of left ventricular myofibrils were examined in hearts of patients with advanced cardiomyopathy undergoing heart transplantation and in normal control hearts (from renal transplant donors). Myosin and actin content of the left ventricular myocardium was slightly reduced in cardiomyopathic hearts. Myofibrillar polypeptide composition was determined using twodimensional electrophoresis and immunoblotting . No differences in constituting polypeptides were apparent, including Z-line proteins and proteins of the endosarcomeric lattice. M-line-bound creatine kinase was identical in both groups. Further, basal and maximal myofibrillar adenosine triphosphatase (ATPase) activities were unaltered in dilated cardiomyopathy. The structure of purified myosin was identical in both groups by the following criteria: electrophoretic mobility of native myosin, identical pattern of light chains after isoelectric focusing, identical cleavage peptides of myosin's heavy chain, and identical patterns after immunoblotting of heavy chain cleavage peptides using polyclonal antibodies generated against myosin from normal and cardiomyopathic ventricles. Ca2+-activated, K'-EDTA-activated and actin-activated myosin ATPase activities were identical in control and cardiomyopathic hearts. A structural alteration or functional defect of myofibrils does not seem to be primarily involved in the pathogenesis of reduced myocardial contractility in dilated cardiomyopathy .

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Section: Discussionmentioning

confidence: 70%

Structure and function of contractile proteins in human dilated cardiomyopathy

Wiegand

Ebecke

Figulla

et al. 1989

Clinical Cardiology

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“…With the increased differentiation from the primitive cardiac tube in the second month of the gestation up to the completely developed heart, a change in the myosin gene expression probably occurs. The alteration of this gene expression, coupled with changed mechanical properties, is discussed as a consequence of thyroidal (1,3,34) and neural (13,21) influences. Besides the isoenzyme which is typical for the ventricle, pyrophosphate gel electrophoresis reveals a fetal isomyosin type with a slower electrophoretic mobility, indicating subtle structural differences between human fetal and adult ventricular heavy chains.…”

Section: Discussionmentioning

confidence: 99%

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

Hoffmann

Siegert

1987

Basic Res Cardiol

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Two distinct types of native isomyosins, referred to as human fetal HF and human ventricular myosin HV-3, have been identified in the human fetal heart during two different periods of gestation and in the neonatal state, whose relative parts change with development. In the adult ventricle, only HV-3 was found. Two myosin isoforms designated as HA-3 and HA-1 occur in the atrial myocardium of the normal human heart, which are electrophoretically distinct from the fetal isoenzymes. In fetal tissue, the myosin light chain complement is composed of atrial and ventricular light chains. In support of recent results, we also found identical spots from the atrial ALC-1 and the fetal light chain FLC, suggesting a homology between them. Apart from the light chains typical for this tissue, the atrial myocardium also contains ventricular light chains. Therefore we hypothesize that atrial myosin consists of two atrial isoenzymes and presumably of a ventricular type, too. Differences between atrial and ventricular myosin from human hearts were demonstrated by measuring the temperature dependence of the Ca2+-ATPase.

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Influence of the thyroid state on myocardial myosin in the adult pig heart

Cited by 2 publications

References 0 publications

Structure and function of contractile proteins in human dilated cardiomyopathy

Structure and function of contractile proteins in human dilated cardiomyopathy

Atrial and ventricular myosins from human hearts. I. Isoenzyme distribution during development and in the adult

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