Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1985 Jan 1;100(1):270–275. doi: 10.1083/jcb.100.1.270

Characterization of a myosin heavy chain in the conductive system of the adult and developing chicken heart

PMCID: PMC2113473  PMID: 3880754

Abstract

A monoclonal antibody (anterior latissimus dorsi 58 [ALD58]; antimyosin heavy chain, MHC) directed against myosin from slow tonic muscle was found to react specifically with the striated muscle cells of the conductive system in the adult chicken heart. This monoclonal antibody was used to study the expression of myosin in the conductive system of the adult and developing heart. Using immunofluorescence microscopy with ALD58, muscle cells of the conductive system were demonstrated in both the atria and ventricles of the adult heart as previously shown by Sartore et al. (Sartore, S., S. Pierobon-Bormioli, and S. Schiafinno, 1978, Nature (Lond.), 274: 82-83). Radioactive myosin from adult atria and ventricles was precipitated with ALD58 and subjected to limited proteolysis and subsequent peptide mapping. Peptide maps of ALD58 reactive myosin from atria and ventricles were very similar, if not identical, but differed from peptide maps of ordinary atrial and ventricular myosin. The same antibody was used to study cardiac myogenesis in the chick embryo. When ALD58 was reacted with myosin isolated from atria and ventricles at selected stages of development in radioimmunoassays, reactivity was not observed until the last week of embryonic life (greater than 15 d of egg incubation). Thereafter concomitant and progressively increased reactivity was observed in atrial and ventricular preparations. Also, no ALD58 positive cells were observed in immunofluorescence studies of embryonic hearts until 17 d of egg incubation. Primary cell cultures of embryonic hearts also proved to be negative for this antibody. This study demonstrates that an epitope recognized by ALD58 associated with an antimyosin heavy chain of striated muscle cells of the adult heart conductive system is absent or present in only small amounts in the early embryonic heart.

Full Text

The Full Text of this article is available as a PDF (1.5 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bader D., Masaki T., Fischman D. A. Immunochemical analysis of myosin heavy chain during avian myogenesis in vivo and in vitro. J Cell Biol. 1982 Dec;95(3):763–770. doi: 10.1083/jcb.95.3.763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bandman E., Matsuda R., Micou-Eastwood J., Strohman R. In vitro translation of RNA from embryonic and from adult chicken pectoralis muscle produces different myosin heavy chains. FEBS Lett. 1981 Dec 28;136(2):301–305. doi: 10.1016/0014-5793(81)80640-0. [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. Clark W. A., Jr, Chizzonite R. A., Everett A. W., Rabinowitz M., Zak R. Species correlations between cardiac isomyosins. A comparison of electrophoretic and immunological properties. J Biol Chem. 1982 May 25;257(10):5449–5454. [PubMed] [Google Scholar]
  5. DEHAAN R. L. Differentiation of the atrioventricular conducting system of the heart. Circulation. 1961 Aug;24:458–470. doi: 10.1161/01.cir.24.2.458. [DOI] [PubMed] [Google Scholar]
  6. DeHaan R. L. The potassium-sensitivity of isolated embryonic heart cells increases with development. Dev Biol. 1970 Oct;23(2):226–240. doi: 10.1016/0012-1606(70)90096-5. [DOI] [PubMed] [Google Scholar]
  7. Eriksson A., Thornell L. E. Intermediate (skeletin) filaments in heart Purkinje fibers. A correlative morphological and biochemical identification with evidence of a cytoskeletal function. J Cell Biol. 1979 Feb;80(2):231–247. doi: 10.1083/jcb.80.2.231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Flink I. L., Rader J. H., Morkin E. Thyroid hormone stimulates synthesis of a cardiac myosin isozyme. Comparison of the two-two-dimensional electrophoretic patterns of the cyanogen bromide peptides of cardiac myosin heavy chains from euthyroid and thyrotoxic rabbits. J Biol Chem. 1979 Apr 25;254(8):3105–3110. [PubMed] [Google Scholar]
  9. Forsgren S., Strehler E., Thornell L. E. Differentiation of Purkinje fibres and ordinary ventricular and atrial myocytes in the bovine heart: an immuno- and enzyme histochemical study. Histochem J. 1982 Nov;14(6):929–942. doi: 10.1007/BF01005234. [DOI] [PubMed] [Google Scholar]
  10. González-Sánchez A., Bader D. Immunochemical analysis of myosin heavy chains in the developing chicken heart. Dev Biol. 1984 May;103(1):151–158. doi: 10.1016/0012-1606(84)90016-2. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. 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]
  13. 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]
  14. Hoh J. F., Yeoh G. P., Thomas M. A., Higginbottom L. Structural differences in the heavy chains of rat ventricular myosin isoenzymes. FEBS Lett. 1979 Jan 15;97(2):330–334. doi: 10.1016/0014-5793(79)80115-5. [DOI] [PubMed] [Google Scholar]
  15. Huszar G. Developmental changes of the primary structure and histidine methylation in rabbit skeletal muscle myosin. Nat New Biol. 1972 Dec 27;240(104):260–264. doi: 10.1038/newbio240260a0. [DOI] [PubMed] [Google Scholar]
  16. James T. N. Cardiac conduction system: fetal and postnatal development. Am J Cardiol. 1970 Feb;25(2):213–226. doi: 10.1016/0002-9149(70)90581-3. [DOI] [PubMed] [Google Scholar]
  17. Kirby M. L., Stewart D. E. Neural crest origin of cardiac ganglion cells in the chick embryo: identification and extirpation. Dev Biol. 1983 Jun;97(2):433–443. doi: 10.1016/0012-1606(83)90100-8. [DOI] [PubMed] [Google Scholar]
  18. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  20. Libera L. D., Sartore S., Schiaffino S. Comparative analysis of chicken atrial and ventricular myosins. Biochim Biophys Acta. 1979 Dec 14;581(2):283–294. doi: 10.1016/0005-2795(79)90248-4. [DOI] [PubMed] [Google Scholar]
  21. Long L., Fabian F., Mason D. T., Wikman-Coffelt J. A new cardiac myosin characterized from the canine atria. Biochem Biophys Res Commun. 1977 Jun 6;76(3):626–635. doi: 10.1016/0006-291x(77)91547-9. [DOI] [PubMed] [Google Scholar]
  22. Mahdavi V., Periasamy M., Nadal-Ginard B. Molecular characterization of two myosin heavy chain genes expressed in the adult heart. Nature. 1982 Jun 24;297(5868):659–664. doi: 10.1038/297659a0. [DOI] [PubMed] [Google Scholar]
  23. Matsuda R., Bandman E., Strohman R. C. The two myosin isoenzymes of chicken anterior latissimus dorsi muscle contain different myosin heavy chains encoded by separate mRNAs. Differentiation. 1982;23(1):36–42. doi: 10.1111/j.1432-0436.1982.tb01265.x. [DOI] [PubMed] [Google Scholar]
  24. Oliphant L. W., Loewen R. D. Filament systems in purkinje cells of the sheep heart: possible alterations of myofibrillogenesis. J Mol Cell Cardiol. 1976 Sep;08(9):679–688. doi: 10.1016/0022-2828(76)90010-9. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. 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]
  27. 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]
  28. Schwartz K., Bouveret P., Bercovici J., Swynghedauw B. An immunochemical difference between myosins from normal and hypertrophied rat hearts. FEBS Lett. 1978 Sep 1;93(1):137–140. doi: 10.1016/0014-5793(78)80822-9. [DOI] [PubMed] [Google Scholar]
  29. Sinha A. M., Umeda P. K., Kavinsky C. J., Rajamanickam C., Hsu H. J., Jakovcic S., Rabinowitz M. Molecular cloning of mRNA sequences for cardiac alpha- and beta-form myosin heavy chains: expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5847–5851. doi: 10.1073/pnas.79.19.5847. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. 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]
  31. Toyota N., Shimada Y. Isoform variants of troponin in skeletal and cardiac muscle cells cultured with and without nerves. Cell. 1983 May;33(1):297–304. doi: 10.1016/0092-8674(83)90358-6. [DOI] [PubMed] [Google Scholar]
  32. Truex R. C., Smythe M. Q. Comparative morphology of the cardiac conduction tissue in animals. Ann N Y Acad Sci. 1965 Sep 8;127(1):19–33. doi: 10.1111/j.1749-6632.1965.tb49390.x. [DOI] [PubMed] [Google Scholar]
  33. Umeda P. K., Kavinsky C. J., Sinha A. M., Hsu H. J., Jakovcic S., Rabinowitz M. Cloned mRNA sequences for two types of embryonic myosin heavy chains from chick skeletal muscle. II. Expression during development using S1 nuclease mapping. J Biol Chem. 1983 Apr 25;258(8):5206–5214. [PubMed] [Google Scholar]
  34. Whalen R. G., Sell S. M., Eriksson A., Thornell L. E. Myosin subunit types in skeletal and cardiac tissues and their developmental distribution. Dev Biol. 1982 Jun;91(2):478–484. doi: 10.1016/0012-1606(82)90055-0. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES