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

Hoffmann, Uwe; Siegert, E.

doi:10.1007/bf01907022

Cited by 9 publications

(5 citation statements)

References 35 publications

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“…Historically, myosin protein expression in the human heart has been studied electrophoretically with pyrophosphate gels (10,11,18,27). Myosin migrates as the intact hexameric enzyme under the nondenaturing conditions of pyrophosphate gels either as the V1 isoenzyme (which contains two molecules of MHC-␣), the V3 isoenzyme (which contains two molecules of MHC-␤), or the V2 isoenzyme (which contains one molecule of MHC-␣ and one of MHC-␤) (12).…”

mentioning

confidence: 99%

Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles

Reiser

Portman

Xue

et al. 2001

American Journal of Physiology-Heart and Circulatory Physiology

298

251

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The goal of this study was to test the hypothesis that the relative amounts of the cardiac myosin heavy chain (MHC) isoforms MHC-alpha and MHC-beta change during development and transition to heart failure in the human myocardium. The relative amounts of MHC-alpha and MHC-beta in ventricular and atrial samples from fetal (gestational days 47--110) and nonfailing and failing adult hearts were determined. The majority of the fetal right and left ventricular samples contained small relative amounts of MHC-alpha (mean < 5% of total MHC). There was a small significant decrease in the level of MHC-alpha in the ventricles between 7 and 12 wk of gestation. Fetal atria expressed predominantly MHC-alpha (mean > 95%), with MHC-beta being detected in most samples. The majority of adult nonfailing right and left ventricular samples had detectable levels of MHC-alpha ranging from 1 to 10%. Failing right and left ventricles expressed a significantly lower level of MHC-alpha. MHC-alpha comprised approximately 90% of the total MHC in adult nonfailing left atria, whereas the relative amount of MHC-alpha in the left atria of individuals with dilated or ischemic cardiomyopathy was approximately 50%. The differences in MHC isoform composition between fetal and nonfailing adult atria and between fetal and nonfailing adult ventricles were not statistically significant. We concluded that the MHC isoform compositions of fetal human atria are the same as those of nonfailing adult atria and that the ventricular MHC isoform composition is different between adult nonfailing and failing hearts. Furthermore, the marked alteration in atrial MHC isoform composition, associated with cardiomyopathy, does not represent a regression to a pattern that is uniquely characteristic of the fetal stage.

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confidence: 99%

Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles

Reiser

Portman

Xue

et al. 2001

American Journal of Physiology-Heart and Circulatory Physiology

298

251

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“…Changes in the relative amounts of these isoforms have been described during development Cummins and Lambert, 1986;Everett, 1986;Hoffmann and Siegert, 1987;Bouvagnet et al, 1987), as a result of altering hormonal conditions (Morkin, 1979;Effron et al, 1987), as a result of physical exercise (Belcastro et al, 19881, after dietary manipulations (Morris et al, 1987), and under several pathological conditions (Gorza et al, 1984;Bouvagnet et al, 1985;Hoffmann and Siegert, 1987;Buttrick et al, 1986).…”

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confidence: 99%

Spatial distribution of “Tissue‐Specific” antigens in the developing human heart and skeletal muscle. II. An immunohistochemical analysis of myosin heavy chain isoform expression patterns in the embryonic heart

Wessels

Vermeulen

Virágh³

et al. 1991

Anat. Rec.

113

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The spatial distribution of alpha- and beta-myosin heavy chain isoforms (MHCs) was investigated immunohistochemically in the embryonic human heart between the 4th and the 8th week of development. The development of the overall MHC isoform expression pattern can be outlined as follows: (1) In all stages examined, beta-MHC is the predominant isoform in the ventricles and outflow tract (OFT), while alpha-MHC is the main isoform in the atria. In addition, alpha-MHC is also expressed in the ventricles at stage 14 and in the OFT from stage 14 to stage 19. This expression pattern is very reminiscent of that found in chicken and rat. (2) In the early embryonic stages the entire atrioventricular canal (AVC) wall expresses alpha-MHC whereas only the lower part expresses beta-MHC. The separation of atria and ventricles by the fibrous annulus takes place at the ventricular margin of the AVC wall. Hence, the beta-MHC expressing part of the AVC wall, including the right atrioventricular ring bundle, is eventually incorporated in the atria. (3) In the late embryonic stages (approx. 8 weeks of development) areas of alpha-MHC reappear in the ventricular myocardium, in particular in the subendocardial region at the top of the interventricular septum. These coexpressing cells are topographically related to the developing ventricular conduction system. (4) In the sinoatrial junction of all hearts examined alpha- and beta-MHC coexpressing cells are observed. In the older stages these cells are characteristically localized at the periphery of the SA node.

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“…The clinical data of the adult patients who, as judged after autopsy, did not suffer from an evident heart disease, are listed in Part I, Table 1 (17). Their heart tissues were "normal".…”

Section: Tissue Sourcesmentioning

confidence: 99%

“…The gel electrophoretic techniques were described in Part I (17). Two-dimensional gel electrophoresis was carried out by the method of O'Farrell, gels were stained by a silver method (13).…”

Section: Gel Electrophoresismentioning

confidence: 99%

Atrial and ventricular myosins from human hearts II. Isoenzyme distribution after myocardial infarction

1987

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Human atrial and ventricular myosins were prepared from autopsy specimens from subjects with coronary heart disease. Cardiac myosin light chain isotypes were resolved using two-dimensional gel electrophoresis, whereas myosin isozymes were detected by pyrophosphate gel electrophoresis. Myocardial infarction and associated work overload cause a transition in the light chain complements of the myosins. Thus ventricular myosin light chains were found in pressure overloaded atria and atrial light chains have also been identified in the infarct ventricle of the human heart. Two molecular isoenzymes of the human atrial myosin, the relative proportions of which are changed after infarction, were separated under non-dissociating conditions by gel electrophoresis. A decrease in HA-3 and a corresponding increase in HA-1 were observed. Ventricular hypertrophy in patients with coronary insufficiency induces a second ventricle isomyosin, called HV-1, with the same electrophoretic mobility as HA-1. The relative part of this myosin type amounts to 20%. Comparative peptide mapping studies were carried out on myosin subfragment-1 preparations from normal and infarct ventricles. In the primary structures, the chymotrypsic digestions produced slight differences. These data demonstrate the heterogeneity of human atrial and ventricular myosins in patients with coronary heart disease.

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

Cited by 9 publications

References 35 publications

Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles

Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles

Spatial distribution of “Tissue‐Specific” antigens in the developing human heart and skeletal muscle. II. An immunohistochemical analysis of myosin heavy chain isoform expression patterns in the embryonic heart

Atrial and ventricular myosins from human hearts II. Isoenzyme distribution after myocardial infarction

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