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The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1986 Feb;77(2):340–347. doi: 10.1172/JCI112310

Distribution of cardiac myosin isozymes in human conduction system. Immunohistochemical study using monoclonal antibodies.

M Kuro-o, H Tsuchimochi, S Ueda, F Takaku, Y Yazaki
PMCID: PMC423352  PMID: 3511096

Abstract

To determine the presence and distribution of cardiac myosin isozymes in the human conduction system, we performed an immunohistochemical study using monoclonal antibodies CMA19 and HMC14, which are specific for myosin heavy chains of human atrial type (alpha-type) and ventricular type (beta-type), respectively. Serial frozen sections of human hearts were obtained from autopsy samples and examined by indirect immunofluorescence. Alpha-type was found in all myofibers of sinus node and atrio-ventricular node, and in 55.2 +/- 10.2% (mean +/- SD, n = 5) of the myofibers of ventricular conduction tissue, which consists of the bundle of His, bundle branches, and the Purkinje network. In contrast, beta-type was found in all myofibers of the atrio-ventricular node and ventricular conduction tissue, whereas almost all myofibers of the sinus node were unlabeled by HMC14. Although the number of ventricular myofibers labeled by CMA19 was small, the labeled myofibers were more numerous in the subepicardial region than in the subendocardial region. These findings show that the gene coding for alpha-type is expressed predominantly in specialized myocardium compared with the adjacent ordinary working myocardium.

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Selected References

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  1. Alpert N. R., Mulieri L. A. Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. A characterization of heat liberation in normal and hypertrophied right ventricular papillary muscles. Circ Res. 1982 Apr;50(4):491–500. doi: 10.1161/01.res.50.4.491. [DOI] [PubMed] [Google Scholar]
  2. Banerjee S. K., Wiener J. Effects of aging on atrial and ventricular human myosin. Basic Res Cardiol. 1983 Nov-Dec;78(6):685–694. doi: 10.1007/BF01907216. [DOI] [PubMed] [Google Scholar]
  3. Chizzonite R. A., Everett A. W., Clark W. A., Jakovcic S., Rabinowitz M., Zak R. Isolation and characterization of two molecular variants of myosin heavy chain from rabbit ventricle. Change in their content during normal growth and after treatment with thyroid hormone. J Biol Chem. 1982 Feb 25;257(4):2056–2065. [PubMed] [Google Scholar]
  4. Ebrecht G., Rupp H., Jacob R. Alterations of mechanical parameters in chemically skinned preparations of rat myocardium as a function of isoenzyme pattern of myosin. Basic Res Cardiol. 1982 Mar-Apr;77(2):220–234. doi: 10.1007/BF01908175. [DOI] [PubMed] [Google Scholar]
  5. González-Sánchez A., Bader D. Characterization of a myosin heavy chain in the conductive system of the adult and developing chicken heart. J Cell Biol. 1985 Jan;100(1):270–275. doi: 10.1083/jcb.100.1.270. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gorza L., Mercadier J. J., Schwartz K., Thornell L. E., Sartore S., Schiaffino S. Myosin types in the human heart. An immunofluorescence study of normal and hypertrophied atrial and ventricular myocardium. Circ Res. 1984 Jun;54(6):694–702. doi: 10.1161/01.res.54.6.694. [DOI] [PubMed] [Google Scholar]
  7. Gorza L., Pauletto P., Pessina A. C., Sartore S., Schiaffino S. Isomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study. Circ Res. 1981 Oct;49(4):1003–1009. doi: 10.1161/01.res.49.4.1003. [DOI] [PubMed] [Google Scholar]
  8. Gorza L., Sartore S., Schiaffino S. Myosin types and fiber types in cardiac muscle. II. Atrial myocardium. J Cell Biol. 1982 Dec;95(3):838–845. doi: 10.1083/jcb.95.3.838. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Guesdon J. L., Ternynck T., Avrameas S. The use of avidin-biotin interaction in immunoenzymatic techniques. J Histochem Cytochem. 1979 Aug;27(8):1131–1139. doi: 10.1177/27.8.90074. [DOI] [PubMed] [Google Scholar]
  10. Hoh J. F., McGrath P. A., Hale P. T. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol. 1978 Nov;10(11):1053–1076. doi: 10.1016/0022-2828(78)90401-7. [DOI] [PubMed] [Google Scholar]
  11. Köhler G., Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975 Aug 7;256(5517):495–497. doi: 10.1038/256495a0. [DOI] [PubMed] [Google Scholar]
  12. Lompre A. M., Schwartz K., d'Albis A., Lacombe G., Van Thiem N., Swynghedauw B. Myosin isoenzyme redistribution in chronic heart overload. Nature. 1979 Nov 1;282(5734):105–107. doi: 10.1038/282105a0. [DOI] [PubMed] [Google Scholar]
  13. Mahdavi V., Chambers A. P., Nadal-Ginard B. Cardiac alpha- and beta-myosin heavy chain genes are organized in tandem. Proc Natl Acad Sci U S A. 1984 May;81(9):2626–2630. doi: 10.1073/pnas.81.9.2626. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Saito K., Tamura Y., Saito M., Matsumura K., Niki T., Mori H. Comparison of the subunit compositions and ATPase activities of myosin in the myocardium and conduction system. J Mol Cell Cardiol. 1981 Mar;13(3):311–322. doi: 10.1016/0022-2828(81)90319-9. [DOI] [PubMed] [Google Scholar]
  15. Sartore S., Gorza L., Pierobon Bormioli S., Dalla Libera L., Schiaffino S. Myosin types and fiber types in cardiac muscle. I. Ventricular myocardium. J Cell Biol. 1981 Jan;88(1):226–233. doi: 10.1083/jcb.88.1.226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Sartore S., Pierobon-Bormioli S., Schiaffino S. Immunohistochemical evidence for myosin polymorphism in the chicken heart. Nature. 1978 Jul 6;274(5666):82–83. doi: 10.1038/274082a0. [DOI] [PubMed] [Google Scholar]
  17. Tamura Y., Nishimoto T., Miyakami S., Sako H., Saito K., Mori H. Characteristics of ATPase activity and the subunit composition of myosin in the conduction system of bovine heart. FEBS Lett. 1984 Dec 10;178(2):209–212. doi: 10.1016/0014-5793(84)80602-x. [DOI] [PubMed] [Google Scholar]
  18. Thornell L. E., Eriksson A., Stigbrand T., Sjöström M. Structural proteins in cow Purkinje and ordinary ventricular fibres-a marked difference. J Mol Cell Cardiol. 1978 Jul;10(7):605–616. doi: 10.1016/s0022-2828(78)80002-9. [DOI] [PubMed] [Google Scholar]
  19. Tsuchimochi H., Sugi M., Kuro-o M., Ueda S., Takaku F., Furuta S., Shirai T., Yazaki Y. Isozymic changes in myosin of human atrial myocardium induced by overload. Immunohistochemical study using monoclonal antibodies. J Clin Invest. 1984 Aug;74(2):662–665. doi: 10.1172/JCI111466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yazaki Y., Mochinaga S., Raben M. S. Fractionation of the light chains from rat and rabbit cardiac myosin. Biochim Biophys Acta. 1973 Dec 6;328(2):464–469. doi: 10.1016/0005-2795(73)90281-x. [DOI] [PubMed] [Google Scholar]
  21. Yazaki Y., Raben M. S. Cardiac myosin adenosinetriphosphatase of rat and mouse. Distinctive enzymatic properties compared with rabbit and dog cardiac myosin. Circ Res. 1974 Jul;35(1):15–23. doi: 10.1161/01.res.35.1.15. [DOI] [PubMed] [Google Scholar]
  22. Yazaki Y., Raben M. S. Effect of the thyroid state on the enzymatic characteristics of cardiac myosin. A difference in behavior of rat and rabbit cardiac myosin. Circ Res. 1975 Jan;36(1):208–215. doi: 10.1161/01.res.36.1.208. [DOI] [PubMed] [Google Scholar]
  23. Yazaki Y., Tsuchimochi H., Kuro-o M., Kurabayashi M., Isobe M., Ueda S., Nagai R., Takaku F. Distribution of myosin isozymes in human atrial and ventricular myocardium: comparison in normal and overloaded heart. Eur Heart J. 1984 Dec;5 (Suppl F):103–110. doi: 10.1093/eurheartj/5.suppl_f.103. [DOI] [PubMed] [Google Scholar]
  24. Yazaki Y., Ueda S., Nagai R., Shimada K. Cardiac atrial myosin adenosine triphosphatase of animals and humans: distinctive enzymatic properties compared with cardiac ventricular myosin. Circ Res. 1979 Oct;45(4):522–527. doi: 10.1161/01.res.45.4.522. [DOI] [PubMed] [Google Scholar]

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