Isomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study.

Gorza, Luisa; Pauletto, Paolo; Pessina, Achille C.; Sartore, Saverio; Schiaffino, Stefano

doi:10.1161/01.res.49.4.1003

Cited by 110 publications

(61 citation statements)

References 16 publications

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“…Alterations of the myosin isoforms have been reported to be associated with development, hormonal stimulation, and pressure-overload in the rat and rabbit (6,7,(11)(12)(13)(14)(15). We selected the 28-day-old hamster heart for the purpose of isolating both the a and the / 3 forms of the ventricular myosin heavy chain mRNAs.…”

Section: Resultsmentioning

confidence: 99%

“…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 form) or as heterodimers of the a and the , myosin heavy chain (V2 form) in the course of myocardial cell development (6)(7)(8)(9)(10), are a striking example of specific gene expression; these three forms of ventricular myosin have been extensively studied in rat and rabbit (6,7,(11)(12)(13)(14)(15). The molecular basis for the expression of the ventricular myosin isoforms has been actively investigated in relation to hormone induction (11,(16)(17)(18), stimulation by cardiac pressure overload as well as in disease states (19)(20)(21).…”

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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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Section: Resultsmentioning

confidence: 99%

mentioning

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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“…It exists as isozymes or isoforms in skeletal (Hoh and Yeoh 1979) and cardiac muscle (Hoh et al 1978), which differ in their ATPase activity and in their mobility on non-dissociating (pyrophosphate) gel electrophoresis (Pope et al 1980). The distribution of these isoforms is influenced by the innervation (Pette and Vrbova 1985), functional demand (Gorza et al 1981), hormones (Hoh et al 1978) and development (Hoh and Yeoh 1979). The type of myosin determines some of the fundamental characteristics of contractility.…”

Section: Introductionmentioning

confidence: 99%

The Heavy-chain Stoichiometry of Smooth Muscle Myosin is a Characteristic of Smooth Muscle Tissues

Mohammad¹,

Sparrow²

1988

Aust. Jnl. Of Bio. Sci.

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The stoichiometry of the two heavy chains of myosin in smooth muscle was determined by electrophoresing extracts of native myosin and of dissociated myosin on sodium dodecyl sulfate (SDS) 4%-polyacrylamide gels. The slower migrating heavy chain was 3·6 times more abundant in toad stomach, 2·3 in rabbit myometrium, 2·0 in rat femoral artery, 1·3 in guinea pig ileum, 0·93 in pig trachea and 0·69 in human bronchus, than the more rapidly migrating chain. Both heavy chains were identified as smooth muscle myosin by immunoblotting using antibodies to smooth muscle and nonmuscle myosin. The unequal proportion of heavy chains suggested the possibility of native isoforms of myosin comprised of heavy-chain homodimers. To test this, native myosin extracts were electrophoresed on non-dissociating (pyrophosphate) gels. When each band was individually analysed on SDS-polyacrylamide gel the slowest was found to be filamin and the other bands were myosin in which the relative proportion of the heavy chains was unchanged from that found in the original tissue extracts. Since this is incompatible with either a heterodimeric or a homodimeric arrangement it suggests that pyrophosphate gel electrophoresis is incapable of separating putative isoforms of native myosin.

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“…Mammalian atria and ventricles grafted separately to subcutaneous sites of the host displayed different average frequencies of autonomous pulsation, indicating that physiological features characteristic for their site of origin could be retained for several months (3). On the other hand, plasticity of the mammalian heart with respect to the type of myosin expressed has been demonstrated during development and under a variety of pathological conditions (4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15).…”

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“…In the rat, the ,ptype chain is nearly absent from the atria of the newborn animal but is the dominant form of the ventricle, from which, however, it disappears around postnatal day 30. Subsequently a fraction of the ventricular myocytes returns to the synthesis of ptype chains (6,14). Environmental factors like cardiac mechanical overload and hypothyroidism can drastically shift the relative regional expression of a-and p-type myosin heavy chain genes (17).…”

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confidence: 99%

Long-term expression of isomyosins and myoendocrine functions in ectopic grafts of atrial tissue.

Jockusch¹,

Füchtbauer²,

Füchtbauer³

et al. 1986

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

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Tissue fragments of newborn rat atria were transplanted under the dorsal skin or into the bed of the anterior tibial muscle of nude mice. After 5-11 weeks, the grafts, which had reorganized into beating atrium-like structures, were analyzed and compared to ventricular tissue transplanted the same way. As revealed by monoclonal antibodies against a-and a-type myosin heavy chains, atrial grafts retained a typical pattern of myosin expression distinct from that of ventricular grafts. The majority of ectopic atrial myocytes contained specific atrial granules in which cardiodilatin-immunoreactive material has been localized. Specific granules and cardiodilatin immunoreactivity were not found in myocytes of ventricular grafts. We conclude that the long-term maintenance of isomyosin expression and of the myoendocrine function of atrial tissue is largely independent of the anatomical environment.

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Isomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study.

Cited by 110 publications

References 16 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.

The Heavy-chain Stoichiometry of Smooth Muscle Myosin is a Characteristic of Smooth Muscle Tissues

Long-term expression of isomyosins and myoendocrine functions in ectopic grafts of atrial tissue.

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