Summary
The distribution of connectin (titin), nebulin and α-actinin in the areas of myotendinous junctions of chicken pectoralis muscles was examined by immunocytochemical methods. Staining with antibodies against connectin (4C9, SM1 and P1200) and nebulin formed ‘doublets’ flanking nonterminal Z-bands; near the end of muscle fibres ‘singlets’ were seen within the terminal sarcomere on the side adjacent to the terminal Z-bands. The apical regions of muscle processes, where no myosin filaments are present although actin filaments exist, were reactive with anti-nebulin but not with anti-connection. Antibodies against pectoralis (skeletal muscle type) α-actinin stained non terminal Z-bands and that against gizzard (smooth muscle type) the sarcolemma. Terminal Z-bands were unreactive with both of these antibodies. These findings indicate that, although terminal and nonterminal Z-bands differ in their molecular composition, connectin and nebulin filaments appear to link myosin and actin filaments, respectively, to both Z-band types.
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ENDO, T. & MASAKI, T. (1984) Differential expression and distribution of chicken skeletal- and smooth-muscle-type α-actinins during myogenesis in culture. J. Cell Biol. 99, 2322–32.
FÜRST, 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.
KIMURA, S., MATSUURA, T., OHTSUKA, S., NAKAUCHI, Y., MATSUNO, A. & MARUYAMA, K. (1992) Characterization and localization of α-connectin (titin 1): an elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell Motil. 13, 39–47.
ISHIKAWA, H., SAWADA, H. & YAMADA, E. (1983) Surface and internal morphology of skeletal muscle. In: Handbook of Physiology (edited by PEACHEY, L. D, ADRIAN, R. H. & GEIGER, S. R.), vol. 10, pp. 1–21. Bethesda: American Physiological Society.
ITOH, Y., SUZUKI, T., KIMURA, S., OHASHI, K., HIGUCHI, H., SAWADA, H., SHIMIZU, T., SHIBATA, M. & MARUYAMA, K. (1988) Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104, 504–8.
MARUYAMA, K. (1986) Connectin, an elastic filamentous protein of striated muscle. Int. Rev. Cytol. 104, 81–114.
MARUYAMA, K. & SHIMADA, Y. (1978) Fine structure of the myotendinous junction of lathyritic rat muscle with special reference to connectin, a muscle elastic protein. Tissue Cell 10, 741–8.
MARUYAMA, K., YOSHIOKA, T., HIGUCHI, H., OHASHI, K., KIMURA, 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.
MARUYAMA, K., MATSUNO, A., HIGUCHI, H., SHIMAOKA, S., KIMURA, S. & SHIMIZU, T. (1989) Behaviour of connectin (titin) and nebulin in skinned muscle fibres released after extreme stretch as revealed by immunoelectron microscopy. J. Muscle Res. Cell Motil. 10, 350–9.
MATSUNO, A., TAKANO-OHMURO, H., ITOH, Y., MATSUURA, T., SHIBATA, M., NAKANE, H., KAMINUMA, T. & MARUYAMA, K. (1989) Anti-connectin monoclonal antibodies that react with the unc-22 gene product bind dense bodies of Caenorhabditis (nematode) bodywall muscle cells. Tissue Cell 21, 495–505.
MATSUURA, T., KIMURA, S., OHTSUKA, S. & MARUYAMA, K. (1991) Isolation and characterization of 1,200 kDa peptide of α-connectin. J. Biochem. 110, 474–8.
SAITO, H. & IKENOYA, T. (1988) Three-dimensional ultrastructure of the proximal portion of the transverse muscle of the mouse tongue: reconstructed from transmission electron micrographs. J. Electron Microsc. 37, 8–16.
SHIMADA, Y., ATSUTA, F., SONODA, M., SHIOZAKI, M. & MARUYAMA, K. (1993) Distribution of connectin (titin) and transverse tubules at myotendinous junctions. Scanning Microsc. 7, 157–63.
SUZUKI, T., SAWADA, H. & MARUYAMA, K. (1987) Localization of connectin and nebulin in chicken breast muscle by immunoelectron microscopy. Biomed. Res. 8, 285–7.
TIDBALL, J. G. (1987) Alpha-actinin is absent from the terminal segments of myofibrils and from subsarcolemmal densities in frog skeletal muscle. Exp. Cell Res. 170, 469–82.
TIDBALL, J. G. & LIN, C. (1989) Structural changes at the myogenic cell surface during the formation of myotendinous junctions. Cell Tissue Res. 257, 77–84.
TROTTER, J. A., SAMORA, A. & BACA, J. (1985) Three-dimensional structure of the murine muscle-tendon junction. Anat. Rec. 213, 16–25.
WANG, K. & WRIGHT, J. (1988) Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 107, 2199–212.
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Atsuta, F., Sato, K., Maruyama, K. et al. Distribution of connectin (titin), nebulin and α-actinin at myotendinous junctions of chicken pectoralis muscles: an immunofluorescence and immunoelectron microscopic study. J Muscle Res Cell Motil 14, 511–517 (1993). https://doi.org/10.1007/BF00297213
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DOI: https://doi.org/10.1007/BF00297213