Summary
Type 1 and Type 2 fibres of skeletal muscle (human m. vastus lateralis), selectively depleted of glycogen by sustained submaximal muscular exercise (running 30 km), were identified at light and electron microscopical level by examination of thin and ultra-thin serial sections treated particularly for visualization of glycogen. Averaged images, obtained by lateral smearing of depleted fibres (Type 1) exhibited five clearly visible cross-bridges in the M-band and had broad Z-bands. Nondepleted fibres (Type 2) showed either three central strong and two weak outer lines in the M-band and intermediate Z-bands (Type 2A), or only three central strong lines in the M-band and narrow Z-bands (Type 2B). The depleted fibres had no subsarcolemmal accumulation of glycogen particles and practically no intermyofibrillar particles. The remaining particles were small in size and seemed almost rudimentary. In nonexercised individuals, a peculiar distribution of individual glycogen particles in the I-band and A-band was found. This distribution was accounted by the structural arrangement of the myofibrillar material.
Similar content being viewed by others
References
Ashby B, Frieden C, Bishoff R (1979) Immunofluorescent and histochemical localization of AMP deaminase in skeletal muscle. J Cell Biol 81:361–373
Bylund AC, Bjurö T, Cederblad G, Holm J, Lundholm K, Sjöström M, Ängquist KA, Scherstén T (1977) Physical training in man. Eur J Appl Physiol 36:151–169
Brooke MH, Kaiser KK (1970) Muscle fiber types. How many and what kind? Arch Neurol. 23:369–379
Costill DL, Gollnick PD, Jansson ED, Saltin B, Stein EM (1973) Glycogen depletion pattern in human muscle fibres during distance running. Acta Physiol Scand 89:374–383
Dubowitz V, Brooke MH (1973) Muscle biopsy: A modern approach. WB Saunders, London Philadelphia Toronto, pp 5–33
Essén B (1978) Glycogen depletion of different fibre types in human skeletal muscle during intermittent and continous exercise. Acta Physiol Scand 103:446–455
Franzini-Armstrong C (1970) Details of the I band structure as revealed by the localization of ferritin. Tissue Cell 2:327–338
Gollnick PD, Piehl K, Saltin B (1974) Selective glycogen depletion pattern in human muscle fibres after exercise of varying intensity and at varying pedalling rates. J Physiol 241:45–57
Heuser J (1981) Quick-freeze, deep-etch preparation of samples for 3-D electron microscopy. Trends Biochem Sci 6:64–68
Hoppeler H, Lüthi P, Claassen H, Weibel ER, Howald H (1973) The ultrastructure of the normal human skeletal muscle. A morphometric analysis on untrained men, women and well-trained orienteers. Pflügers Arch 344:217–232
Knappeis GG, Carlsen F (1968) The ultrastructure of the M-line in skeletal muscle. J Cell Biol 38:202–211
Lazarides E (1980) Intermediate filaments as mechanical integrators of cellular space. Nature 283:249–256
Luther PK, Munro PMG, Squire JN (1981) Three-dimensional structure of the vertebrate muscle A-band. III. M-region structure and myosin filament symmetry. J Mol Biol 151:703–730
Luther PK, Squire JM (1978) Three-dimensional structure of the vertebrate muscle M-region. J Mol Biol 125:313–324
Obinata T, Maruyama K, Sugita H, Kohama K, Ebashi S (1981) Dynamics aspects of structural proteins in vertebrate skeletal muscle. Muscle Nerve 4: 456–488
Pearse AGE (1961) Histochemistry. Theoretical and applied, Appendix 9. Little Brown, Boston, MA, p 832
Pette D (ed.) (1980) Plasticity of muscle. Walter de Gruyter, Berlin
Prince FP, Hikida RS, Hagerman FC, Staron RS, Allen WH (1981) A morphometric analysis of human muscle fibers with relation to fiber types and adaptations to exercise. J Neurol Sci 49:165–179
Sjöström M, Kidman S, Henriksson-Larsén K, Ängquist KA (1982) Z- and M-band appearance in different histochemically defined types of human skeletal muscle fibres. J Histochem Cytochem 30:1–11
Sjöström M, Squire JM (1977a) Fine structure of the A-band in cryo-sections. I. The structure of the A-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J Mol Biol 109:49–68
Sjöström M, Squire JM (1977b) Cryo-ultramicrotomy and myofibrillar fine structure: a review. J Microsc 111:239–278
Somlyo AV, Gonzales-Serratos H, Shuman H, McClellan G, Somlyo (1981) Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: an electron-probe study. J Cell Biol 90:577–594
Squire J, Edman A-C, Freundlich A, Harford J, Sjöström M (1982) Muscle structure, cryomethods and image analysis. J Microsc 125:215–225
Squire JM, Harford JJ, Edman A-C, Sjöström M (1982) Fine structure of the A-band in cryosections. III. Crossbridge distribution and the axial structure of the human C-zone. J Mol Biol 155:467–494
Strehler EE, Pelloni G, Heizmann CW, Eppenberger HM (1980) Biochemical and ultrastructural aspects of Mr 165,000 M-protein in cross-striated muscle. J Cell Biol 86:775–783
Thiéry JP (1967) Mise en évidence des polysaccharides sur coupes fines en microscopie électronique. J Microsc 6:987
Trinick J, Lowey S (1977) M-protein from chicken pectoralis muscle: isolation and characterization. J Mol Biol 131:343–368
Trinick JA (1981) End-filaments: A new structural element of vertebrate skeletal muscle thick filaments. J Mol Biol 151:309–314
Weibel E (ed.) (1979) Stereological methods, Vol 1. Academic Press, New York
Yarom R, Meiri V (1971) N lines in striated muscle: a site of intracellular Ca2+ Nature (New Biol) 234:254–256
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Sjöström, M., Fridén, J. & Ekblom, B. Fine structural details of human muscle fibres after fibre type specific glycogen depletion. Histochemistry 76, 425–438 (1982). https://doi.org/10.1007/BF00489899
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00489899