Altered distribution of myosin isoenzymes in the cardiomyopathic Syrian hamster (BIO 8.262)

Wiegand, V.; Stroh, Eileen; Henniges, A.; Lossnitzer, K; Kreuzer, H

doi:10.1007/bf01907213

Cited by 17 publications

(3 citation statements)

References 19 publications

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“…However, the amount of mRNA expressed at 2 days after birth is far less than at 20 days after birth, which in turn, is less than at 7 months. This pattern corresponds very closely to the ventricular myosin protein pattern seen during maturation of both rat and hamster heart (28,41); these data suggest that the mRNA represented by pVHC1 is coding for the a ventricular myosin heavy chain.…”

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confidence: 74%

“…Some strains of this animal exhibit an autosomal recessive defect, a cardiomyopathy, which appears 30-45 days after birth (25)(26)(27). It has been reported that development of the cardiomyopathy is associated with an altered distribution of the three myosin isozymes (28,29); there is a shift from the V1 form of the ventricular myosin isozymes (which contains a higher ATPase activity than the V3 form) to the V3 form. It has been speculated that this shift in the myosin isozymes to the V3 form and to a lower ATPase activity is a compensatory process that may lead to a more economical working of the myocardial cell (29).…”

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confidence: 99%

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Construction and characterization of the alpha form of a cardiac myosin heavy chain cDNA clone and its developmental expression in the Syrian hamster.

Liew¹,

Jandreski²

1986

Proc. Natl. Acad. Sci. U.S.A.

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A cDNA clone, pVHCl, was isolated from a Syrian hamster heart cDNA library and was compared to the rat a (pCMHC21) and ,8 (pCMHC5) ventricular myosin heavy chain cDNA clones. The DNA sequence and amino acid sequence deduced from the DNA show more homology with pCMHC21 than pCMHC5. This indicates that pVHCl is an a ventricular myosin heavy chain cDNA clone. However, even though pVHC1 shows a high degree of nucleotide and amino acid conservation with the rat myosin heavy chain sequences, the carboxyl-terminal peptide and the 3'-untranslated region are highly divergent and specific for this cDNA clone. There appears to be an amino acid deletion in the 3' end of the hamster a myosin heavy chain as compared to the rat a myosin heavy chain. S1 nuclease mapping experiments have shown that the mRNA represented by this cDNA clone is scarcely expressed in neonatal development, but its expression increases with age and reaches maximal levels in adult life. This cDNA clone provides a useful tool to follow the myosin heavy chain mRNA changes during development and during the genesis of a cardiomyopathy, an autosomal recessive defect carried by the Syrian hamster.The Syrian hamster has several features that can be used to study myocardial cells during normal growth and during the development of heart disease. Some strains of this animal exhibit an autosomal recessive defect, a cardiomyopathy, which appears 30-45 days after birth (25-27). It has been reported that development of the cardiomyopathy is associated with an altered distribution of the three myosin isozymes (28,29); there is a shift from the V1 form of the ventricular myosin isozymes (which contains a higher ATPase activity than the V3 form) to the V3 form. It has been speculated that this shift in the myosin isozymes to the V3 form and to a lower ATPase activity is a compensatory process that may lead to a more economical working of the myocardial cell (29).This report deals with the construction of a myocardial cDNA library from Syrian hamster ventricular tissue and the characterization of the a form of a ventricular myosin heavy chain cDNA clone. This specific cDNA clone, through the use of the S1 nuclease mapping technique, provides a feasible means of examining the expression of hamster ventricular myosin isoforms during growth and the course of developing cardiomyopathy.Considerable evidence indicates that several muscle-specific contractile proteins, including the myosin heavy chain, are constituted by multigene families. Differential expression of myosin light and heavy chains have been demonstrated in muscle and nonmuscle cell types as well as in invertebrate and avian muscle tissues by peptide mapping, immunological cross-reactivity, and DNA analysis (1-5). The myosin isozymes in cardiac tissue present a particularly intriguing challenge for the examination of differential expression during development.The isoforms of ventricular myosin, which are expressed as either homodimers of the a myosin heavy chain (V1 form) or the 13 myosin heavy chain (V3 ...

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confidence: 74%

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confidence: 99%

Construction and characterization of the alpha form of a cardiac myosin heavy chain cDNA clone and its developmental expression in the Syrian hamster.

Liew¹,

Jandreski²

1986

Proc. Natl. Acad. Sci. U.S.A.

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“…The isomyocin pattern was not different in CMH and F1B before 220 days. Thus the shift from V1 to V3 seems to occur later than in other cardiomyopathic hamster strains (Wiegand et al , 1983; Malhotra et al , 1985; Lambert et al , 1995). Moreover, no difference in myosin isoform Ca 2+ ‐activted ATPase activity was observed between F1B and CMH at this stage.…”

Section: Discussionmentioning

confidence: 80%

Effect of trimetazidine and verapamil on the cardiomyopathic hamster myosin phenotype

D'hahan

Taouil

Janmot

et al. 1998

British J Pharmacology

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1 In this study we investigated whether long-term trimetazidine (anti-ischaemic drug) therapy alters the ventricular myosin heavy chain (MHC) isoform composition in a model of cardiomyopathy. 2 MHC isoforms were analysed in the native state by electrophoresis in a pyrophosphate buer. Myosin isoform patterns were studied in cardiac muscle from cardiomyopathic hamsters (CMH) of the BIO 14 : 6 strain during the time course of the disease and compared with those of healthy golden hamsters (F1B). The correlation between myosin pro®le and Ca 2+ -activated ATPase activity was determined from 220 days. 3 At the stage of insuciency (350 days), CMH presented the most abnormal phenotype with 53% V1-24% V3 compared to 79% V1-7% V3 (P50.001), in F1B. Trimetazidine was administered to cardiomyopathic hamsters from the early stage of active disease (30 days) to the congestive stages (220 ± 350 days). Within 65 days, trimetazidine treatment, in CMH and F1B, reduced V1 to a low level (53% and 62%, respectively), which remained constant throughout the treatment. This level was similar to that in 220 and 350 days-old untreated-CMH. In sharp contrast, a standard calcium blocker, verapamil, administered to CMH in the same conditions resulted in a higher V1 (about 70%) and higher global myosin ATPase activity from 220 days. 4 Previous results in terms of hypertrophy and survival, compared to these results, suggest that verapamil and trimetazidine treatments reveal a disssociation between ventricular hypertrophy and isomyosin distribution. In addition, the shift in favour of V3 may not necessarily be an aggravating factor of the disease but an adaptative compensatory event.

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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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Altered distribution of myosin isoenzymes in the cardiomyopathic Syrian hamster (BIO 8.262)

Cited by 17 publications

References 19 publications

Construction and characterization of the alpha form of a cardiac myosin heavy chain cDNA clone and its developmental expression in the Syrian hamster.

Construction and characterization of the alpha form of a cardiac myosin heavy chain cDNA clone and its developmental expression in the Syrian hamster.

Effect of trimetazidine and verapamil on the cardiomyopathic hamster myosin phenotype

Structure and function of contractile proteins in human dilated cardiomyopathy

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