Summary
The location of cardiac titin epitopes in the sarcomere of rabbit cardiac, atrial and ventricular muscle was studied by using polyclonal antibodies against skeletal muscle titin. The results show that incubation with the antibody leads to the appearance of four electron-dense stripes in the A band of both atrial and ventricular cardiac muscle. The location and intensity of these stripes were identical to those observed in skeletal muscle. In conclusion we demonstrate that titins from skeletal and cardiac muscles share some common antigenic determinants.
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Furst, D. O., Osborn, M., Nave, R. &Weber, K. (1988) The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten non-repetitive epitopes starting at the Z-line extends close to the M-line.J. Cell Biol. 106, 1563–72.
Hill, C. &Weber, K. (1986) Monoclonal antibodies distinguish titins from heart and skeletal muscle.J. Cell Biol. 102, 1099–1108.
Horowits, R. &Podolsky, R. J. (1987) The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments.J. Cell Biol. 105, 2217–23.
Hu, D. H., Kumura, S. &Maruyama, K. (1986) Sodium dodecyl sulphate gel electrophoresis studies of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles.J. Biochem. 99, 1485–92.
Kurzban, G. P. &Wang, K. (1988) Giant polypeptides of skeletal muscle titin: sedimentation equilibrium in guanidine hydrochloride.Biochem. Biophys. Res. Comm. 150, 1155–61.
Locker, R. H. &Wild, D. J. C. (1986) A comparative study of high molecular weight proteins in various types of muscle across the animal kingdom.J. Biochem. (Tokyo)99, 1473–84.
Maruyama, K., Kimura, S., Ohashi, K. &Kuwano, Y. (1981) Connectin, an elastic protein of muscle. Identification of ‘titin’ with connectin.J. Biochem. (Tokyo)89, 701–9.
Maruyama, K. (1986) Connectin, an elastic filamentous protein of striated muscle.Int. Rev. Cytol. 104, 81–114.
Maruyama, K., Yoshioka, T., Higuchi, H., Ohashi K., Kumura, S. &Natori, R. (1985) Connectin filaments link thick filaments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy.J. Cell Biol. 101, 2167–72.
Pierobon-Bormioli, S., Betto, R. &Salviati, G. (1989) The organization of titin (connectin) and nebulin in the sarcomeres: an immunocytolocalization study.J. Muscle Res. Cell Motil. 10, 446–56.
Salviati, G., Betto, R., Ceoldo, S. &Pierobon-Bormioli, S. (1990) Morphological and functional characterization of the endosarcomeric elastic filament.Am. J. Physiol 259, C144-C149.
Schultheiss, T., Zhongxiang, L., Lu, M. H., Murray, J., Fischman, D. A., Weber, K, Masaki, T., Imamura, M. &Holtzer, H. (1990) Differential distribution of subsets of myofibrillar proteins in cardiac non-striated and striated myofibrils.J. Cell Biol. 110, 1159–72.
Tokuyasu, K. T. (1989) Immunocytochemical studies of cardiac myofibrillogenesis in early chick embryos. III Generation of fasciae adherentes and costameres.J. Cell Biol. 108, 43–53.
Towbin, H., Staehelin, T. &Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications.Proc. Natl. Acad. Sci. (USA)76, 4350–4.
Wang, K., McLure, J. &Tu, A. (1979) Titin: major myofibrillar components of striated muscle.Proc. Natl. Acad. Sci. (USA)76, 3698–702.
Wang, K. (1982) Purification of titin and nebulin.Methods Enzymol. 85b, 264–74.
Wang, K. (1985) Sarcomere-associated cytoskeletal lattices in striated muscle, review and hypothesis. InCell and Muscle Motility. (edited byShay, J. W.) Vol. 6, pp. 315–69. New York, London: Plenum Press.
Wang, S. M. &Greaser, M. L. (1985) Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils.J. Muscle Res. Cell Motil,6, 293–312.
Wang, S. M., Greaser, M. L., Schultz, E., Bulinski, J. C., Lin, J. J-C. &Lessard, J. L. (1988) Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin and myosin.J. Cell Biol. 107, 1075–83.
Whiting, A., Wardale, J. &Trinick, J. (1989) Does titin regulate the length of muscle thick filaments?J. Mol. Biol. 205, 263–8.
Winegrad, S. (1986) Membrane control of force generation. InThe Heart and Cardiovascular System. (edited byFozzard, H. A., Haber, E., Jennings, R. B., Katz, A. M. &Morgan, H. E.) Scientific Foundation Vol. 1, pp. 703–73. New York: Raven Press.
Wood, D. S., Zollmann, J. &Reuben, J. P. (1978) Human skeletal muscle. Properties of the ‘chemically skinned’ fibres.Science 187, 1075–6.
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Pierobon-Bormioli, S., Biral, D., Betto, R. et al. Immunoelectron microscopic epitope locations of titin in rabbit heart muscle. J Muscle Res Cell Motil 13, 35–38 (1992). https://doi.org/10.1007/BF01738425
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DOI: https://doi.org/10.1007/BF01738425