Summary
The anisotropic band of skeletal muscle is a complex structural assembly of the protein myosin and associated nonmyosin components. To study the relationships among these proteins, aggregates of thick myofilaments held together at the M line (A segments) have been prepared from fresh and glycerol extracted chicken pectoralis and rabbit psoas muscles and from fresh frog sartorius muscle. The structure of the A segments included several thick filaments, an M line, and a bare zone or pseudo-H zone, lateral to the M line. Most of the A segments exhibited a pattern of eleven periodic stripes in each half lateral to the bare zone. The A segments from fresh muscle displayed these stripes more consistently than did the A segments from glycerinated muscle. Some of the major stripes appeared to be double, and there were two subdivisions between the stripes nearest the bare zone. The more lateral of the major A band stripes, however, had one subdivision between them. The M line consisted of three prominent medial stripes and two fainter lateral stripes. In the M lines of rabbit A segments the lateral stripes were located well into the bare zone whereas the lateral stripes of M lines in chicken A segments were closer to the three medial M line stripes. Our results on the preparation and properties of A segments are compared with those of other investigators.
Similar content being viewed by others
References
Chowrashi PK, Pepe FA (1977) Light meromyosin paracrystal formation. J Cell Biol 74:136–152
Corsi A, Perry SV (1958) Some observations on the localization of myosin, actin and tropomyosin in the rabbit myofibril. Biochem J 68:12–17
Craig R (1977) Structure of A-segments from frog and rabbit skeletal muscle. J Mol Biol 109:69–81
Craig R, Offer G (1976) The location of C-protein in rabbit skeletal muscle. Proc R Soc Lond (Biol) 192:451–461
Ebashi S, Ohtsuki I, Mihashi K (1973) Regulatory proteins of muscle with special reference to troponin. Cold Spring Harb Symp Quant Biol 37:215–223
Endo M, Nonomura Y, Masaki T, Ohtsuki I, Ebashi S (1966) Localization of native tropomyosin in relation to striation patterns. J Biochem 60:605–608
Hanson J, Huxley HE (1955) The structural basis of contraction in striated muscle. Symp Soc Exp Biol 9:228–264
Hanson J, Lowy J (1963) The structure of F-actin and actin filaments isolated from muscle. J Mol Biol 6:46–60
Hanson J, O'Brien EJ, Bennett PM (1971) Structure of the myosin-containing filament assembly (A-segment) separated from frog skeletal muscle. J Mol Biol 58:865–871
Huxley HE (1963) Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol Biol 7:281–308
Huxley HE (1966) The fine structure of striated muscle and its functional significance. Harvey Lect 60:85–118
Huxley H, Hanson J (1954) Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature, London 173:973–976
Huxley HE, Brown W (1967) The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J Mol Biol 30:383–434
Irish MJ, Wilson FJ (1978) The structure of A band segments from chicken pectoral muscle. Anat Rec 190:429
Irish MJ, Wilson FJ (1979a) The structure of A segments from glycerinated muscle. Tissue Cell 11:201–207
Irish MJ, Wilson FJ (1979b) Immunoelectron microscopy of A band segments from chicken pectoral muscle. Anat Rec 193:573
Irish MJ, Hirabayashi T, Wilson FJ (1977) An effect of avian hereditary muscular dystrophy on the reaction of troponin-C with its antibody. Tissue Cell 9:499–505
Marshall JM, Jr, Holtzer H, Finck H, Pepe F (1959) The distribution of protein antigens in striated myofibrils. Exp Cell Res Suppl 7:219–233
Masaki T, Takaiti O (1974) M-Protein. J Biochem 75:367–380
Ohtsuki I (1974) Localization of troponin in thin filament and tropomyosin paracrystal. J Biochem 75:753–765
Ohtsuki I (1975) Distribution of troponin components in the thin filament studied by immunoelectron microscopy. J Biochem 77:633–639
Ohtsuki I (1979a) Number of anti-troponin striations along the thin filament of chick embryonic breast muscle. J Biochem 85:1377–1378
Ohtsuki I (1979b) Molecular arrangement of troponin-T in the thin filament. J Biochem 86:491–497
Pepe FA (1975) Structure of muscle filaments from immunohistochemical and ultrastructural studies. J Histochem Cytochem 23:543–562
Pepe FA, Huxley HE (1964) Antibody staining of separated thin and thick filaments of striated muscle. In: Gergely J (ed) Biochemistry of Muscle Contraction. Little, Brown &Co., Boston, pp 320–329
Pepe FA, Drucker B (1975) The myosin filament III. C-protein. J Mol Biol 99:609–617
Sjöström M, Squire JM (1977) Fine structure of the A-band in cryo-sections. The structure of the A band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J Mol Biol 109:49–68
Starr R, Offer G (1971) Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett 15:40–44
Wilson FJ, Irish MJ (1979) Preparation and properties of segments of the anisotropic band from skeletal muscle. Abstracts of the XIth International Congress of Biochemistry, Toronto, Canada. 202
Wilson FJ, Hirabayashi T, Cheng M (1977) Distribution of antibodies to the troponin complex, troponin-C and troponin-I in chicken skeletal muscle as determined by a simplified method for immuno-electron microscopy. Tissue Cell 9:273–284
Wilson FJ, Camiscoli D, Irish MJ, Hirabayashi T (1978) Immunohistochemical and ultrastructural distribution of antibodies to troponin-C and troponin-I in normal and dystrophic chicken skeletal muscle. J Histochem Cytochem 26:258–266
Author information
Authors and Affiliations
Additional information
This research was supported in part by General Research Support (RR-5576) from the United States Public Health Service to the College of Medicine and Dentistry of New Jersey, Rutgers Medical School. Paper I in this series is Irish and Wilson (1979a)
Rights and permissions
About this article
Cite this article
Wilson, F.J., Irish, M.J. The structure of segments of the anisotropic band of muscle. Cell Tissue Res. 212, 213–223 (1980). https://doi.org/10.1007/BF00233956
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00233956