Skip to main content
Log in

Identification and pattern of expression of a developmental isoform of troponin I in chicken and rat cardiac muscle

  • Papers
  • Published:
Journal of Muscle Research & Cell Motility Aims and scope Submit manuscript

Summary

A monoclonal antibody that reacts with all known isoforms of troponin I detected a single isoform of cardiac troponin I in both a trial and ventricular chambers of adult chicken and rat hearts in an immunoblotting analysis. Another isoform of troponin I in addition to the adult cardiac form, however, was present in all chambers of the heart during early development in both species. This developmental isoform appeared to have the same electrophoretic mobility on SDS tris glycine polyacrylamide gels as that observed for the adult slow skeletal muscle isoform. In the rat, only the developmental isoform of troponin I was present in the early foetal heart and small amounts of the adult cardiac isoform were not apparent until late in gestation, whereas the developmental and adult isoforms were expressed in approximately equal amounts throughout embryonic development in the chicken. The level of developmental isoform of troponin I in both the chicken and the rat hearts gradually decreased so that only small amounts of this variant were detectable two weeks after birth or post hatching.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Bader, D., Masaki, T. &Fischman, D. A. (1982) Immunochemical analysis of myosin heavy chain during embryonic myogenesisin vivo andin vitro.J. Cell Biol. 95, 763–70.

    PubMed  Google Scholar 

  • Bandman, E., Matsuda, R. &Strohman, R. C. (1982) Developmental appearance of myosin heavy and light chain isoformsin vivo andin vitro in chicken skeletal muscle.Dev. Biol. 93, 508–18.

    PubMed  Google Scholar 

  • Billeter, R., Heizmann, C. W., Howald, H. &Jenny, E. (1981) Analysis of myosin light and heavy chains in single human skeletal muscle fibres.Eur. J. Biochem. 116, 389–95.

    PubMed  Google Scholar 

  • Chizzonite, R. A. &Zak, R. (1984) Regulation of myosin isoenzyme composition in foetal and neonatal rat ventricle by endogenous thyroid hormones.J. Biol. Chem. 259, 12628–32.

    PubMed  Google Scholar 

  • Clark, W. A., Chizzonite, R. A., Everett, A. W., Rabinowitz, M. &Zak, R. (1982) Species correlation between cardiac isoenzymes.J. Biol. Chem. 257, 5449–54.

    PubMed  Google Scholar 

  • Cooper, T. A. &Ordahl, C. P. (1985) A single troponin T gene regulated by different programs in cardiac and skeletal muscle development.Science 226, 979–82.

    Google Scholar 

  • Cummins, P., Price, K. M. &Littler, W. A. (1980) Foetal myosin light chain in human ventricle.J. Musc. Res Cell Motility 1, 357–66.

    Google Scholar 

  • De Blas, A. L. &Cherwinski, H. M. (1983) Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies.Analyt. Biochem. 133, 214–19.

    PubMed  Google Scholar 

  • Dhoot, G. K., Gell, P. G. H. G. &Perry, S. V. (1978) The localisation of the different forms of troponin I in skeletal and cardiac muscle cells.Exp. Cell. Res. 117, 357–70.

    PubMed  Google Scholar 

  • Dhoot, G. K., Dransfield, I., Grand, R. J. &Perry, S. V. (1986) Distribution of isoforms of the myofibrillar proteins in myoid cells of thymus.J. Musc. Res. Cell Motility 7, 351–60.

    Google Scholar 

  • Evans, D., Miller, J. B. &Stockdale, F. E. (1988) Developmental patterns of expression and coexpresion of myosin heavy chains in atria and ventricles of the avian heart.Dev. Biol. 127, 376–83.

    PubMed  Google Scholar 

  • Hoh, J. F. Y., McGrath, P. A. &Hale, P. T. (1977) Electrophoretic analysis of multiple forms of cardiac myosin: Effect of hypophysectomy and thyroxine replacement.J. Mol. Cel. Cardiol. 10, 1053–76.

    Google Scholar 

  • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature 277, 680–5.

    Google Scholar 

  • Lompre, A. M., Mercadier, J. J., Wisnewsky, C., Bouveret, A. &Schwartz, K. (1981) Species and age dependent changes in the relative amounts of cardiac myosin isozymes in mammals.Dev. Biol. 84, 286–90.

    Google Scholar 

  • Lowey, S. (1985) Myosin isozymes in developing chicken muscles In:Gene expression in muscle. (edited byR. C. Strohman &S. Wolf), New York: Plenum Press, pp. 269–80.

    Google Scholar 

  • Lowey, S., Benfield, P. A., LeBlanc, D. D. &Waller, G. S. (1983) Myosin isozymes in avian skeletal muscle I. Sequential expression of myosin isozymes in developing chicken pectoralis muscle.J. Musc. Res. Cell Motility 4, 695–717.

    Google Scholar 

  • Perry, S. V. (1979). The regulation of contractile activity in muscle.Biochem. Soc. Trans. 7, 593–617.

    PubMed  Google Scholar 

  • Rushbrook, J. I. &Stracher, A. (1979) Comparison of adult, embryonic and dystrophic myosin heavy chains from chicken muscle by sodium dodecylsulfate/polyacrylamide gel electrophoresis and peptide mappingProc. natn. Acad. Sci. USA 76, 4331–4.

    Google Scholar 

  • Sabry, M. A. &Dhoot, G. K. (1988a) Identification of developmental isoforms of cardiac troponin T in the chicken heart.J. Musc. Res. Cell Motility. 9, 104.

    Google Scholar 

  • Sabry, M. A. &Dhoot, G. K. (1988b) Identification of and changes in the expression of troponin T isoforms in the developing avian and mammalian heart.J. Mol. Cell Cardiol. In the press.

  • Sabry, M. A. &Dhoot, G. K. (1988c) Evidence for heterogeneity of troponin I in developing cardiac muscle.J. Musc. Res. Cell Motility 9, 104.

    Google Scholar 

  • Sartore, S., Gorza, L., Pierbon-Bormioli, S., Dalla-Libera, L. &Schiaffino, S. (1981) Myosin types and fibre types in cardiac muscle. 1. Ventricular myocardium.J. Cell. Biol. 88, 226–33.

    PubMed  Google Scholar 

  • Sperelakis, N. &Vogel, S. (1982) Development of electrical activity in cardiac pacemaker cells. In:Cellular pacemakers, Volume (1) (edited by:D. O. Carpenter), New York, A. Wiley-Interscience Publications pp. 9–66.

    Google Scholar 

  • Sweeney, L. J., Zak, R. &Manasek, F. J. (1987) Transitions in cardiac isomyosin expression during differentiation of the embryonic chick heart.Circ. Res. 61, 287–95.

    PubMed  Google Scholar 

  • Swynghedauw, B. (1986) Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscle.Physiol. Rev. 66, 711–71.

    Google Scholar 

  • Syska, H., Perry, S. V. &Trayer, I. P. (1974) A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle.FEBS Lett. 40, 253–7.

    PubMed  Google Scholar 

  • Towbin, H., Staehelin, T. &Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proc. natn. Acad. Sci. 76, 4350–4.

    Google Scholar 

  • Whalen, R. G., Sell, S. M., Butler-Browne, G. S., Schwartz, K., Bouvert, P. &Pinset-Harstorm, I. (1981) Three myosin isozymes appear sequentially in rat muscle development.Nature 292, 805–9.

    PubMed  Google Scholar 

  • Wilkinson, J. M. &Grand, R. J. A. (1978) Comparison of amino acid sequence of troponin I from different striated muscles.Nature 271, 31–5.

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sabry, M.A., Dhoot, G.K. Identification and pattern of expression of a developmental isoform of troponin I in chicken and rat cardiac muscle. J Muscle Res Cell Motil 10, 85–91 (1989). https://doi.org/10.1007/BF01739858

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01739858

Keywords

Navigation