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Logo of jcellbiolhis Article at jcb.orgThe Rockefeller University PressInstructions to AuthorsContactEditorsThe Journal of Cell Biology
J Cell Biol. 1962 January 1; 12(1): 135–147.
PMCID: PMC2106012
A STUDY OF MYOFIBRIL SARCOMERE STRUCTURE DURING CONTRACTION
Vladimir P. Gilëv
From the Laboratory of Electron Microscopy, Department of Biological Sciences, USSR Academy of Sciences, Moscow
Received June 28, 1961.
Abstract
In the present investigation of cross-striated muscle fibers of axolotl, we succeeded in observing in one field of vision of the electron microscope all the stages of myofibril contraction. This allowed us to avoid errors in establishing the sequence of individual contraction stages. Our studies reveal a new contraction stage which appears at the shortening of the sarcomere below 74 per cent of the "resting length" but prior to the formation of typical "maximally shortened" sarcomeres, characterized by strong "contraction bands." At this stage, in the center of the sarcomere, at either side of the M line, a "secondary anisotropic" band arises which widens with further sarcomere contraction. At either side of this band, at the place of the former ("primary") anisotropic band, a "secondary isotropic" band is formed. A scheme of successive stages of contraction of the sarcomere is presented. The mechanisms of contraction for the first stage (from 100 to 79 per cent of the "resting length") and for the last stage (from 74 to 58 per cent of the "resting length") seem to be different. While the sliding of myofilaments with respect to one another can be assumed for the first stage, it is the spiralization of these structures which is the most likely explanation for the last stage. (An Abstract in German also appears at the end of this article.)
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Selected References
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  • FAWCETT, DW; SELBY, CC. Observations on the fine structure of the turtle atrium. J Biophys Biochem Cytol. 1958 Jan 25;4(1):63–72. [PubMed]
  • HANSON, J. Studies on the cross-striation of the indirect flight myofibrils of the blowfly Calliphora. J Biophys Biochem Cytol. 1956 Nov 25;2(6):691–710. [PubMed]
  • HODGE, AJ. Studies on the structure of muscle. III. Phase contrast and electron microscopy of dipteran plight muscle. J Biophys Biochem Cytol. 1955 Jul 25;1(4):361–380. [PubMed]
  • HUXLEY, HE. The double array of filaments in cross-striated muscle. J Biophys Biochem Cytol. 1957 Sep 25;3(5):631–648. [PubMed]
  • HUXLEY, H; HANSON, J. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature. 1954 May 22;173(4412):973–976. [PubMed]
  • PERRY, SV. Relation between chemical and contractile function and structure of the skeletal muscle cell. Physiol Rev. 1956 Jan;36(1):1–76. [PubMed]
  • PHILPOTT, DE; SZENT-GYORGYI, A. The series elastic component in muscle. Biochim Biophys Acta. 1953 12(1-2):128–133.Sep–Oct; [PubMed]
  • PHILPOTT, DE; SZENT-GYORGYI, A. Observations on the electron microscopic structure of insect muscle. Biochim Biophys Acta. 1955 Oct;18(2):177–182. [PubMed]
  • REVEL, JP; NAPOLITANO, L; FAWCETT, DW. Identification of glycogen in electron micrographs of thin tissue sections. J Biophys Biochem Cytol. 1960 Dec;8:575–589. [PubMed]
  • DE VILLAFRANCA, GW. Observations on the anisotropic band of cross-striated muscle. Exp Cell Res. 1957 Apr;12(2):410–413. [PubMed]
  • WATSON, ML. Staining of tissue sections for electron microscopy with heavy metals. II. Application of solutions containing lead and barium. J Biophys Biochem Cytol. 1958 Nov 25;4(6):727–730. [PubMed]