Structural Studies of Glycerinated Skeletal Muscle. I. A-Band Length and Cross-Bridge Period in ATP-Contracted Fibers

  • Paul Dreizen
  • Lawrence Herman
  • Jacob E. Berger
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


An electron microscope study is reported of structural changes during ATP-induced contraction of glycerinated rabbit psoas. In the absence of ATP, A-band length is constant at sarcomere lengths above 1.9 μm, with average length of 1.54 μ. In ATP-treated fibers, A-band length is also constant at sarcomere lengths above 2.0 μm, but the apparent length of A-band decreases to approximately 1.3 μm, as sarcomere length decreases from 1.9 μm to 1.5 μ. The occurrence of short A-bands cannot be attributed to crumpling of thick filaments against Z-lines, since I-bands remain patent; nor to the presence of heterogeneous filaments, since resting muscle does not show comparable heterogeneity, nor to compressive artifacts, which are minor when knife edge is oriented parallel with fiber axis during microtomy. The decrease of A-band length appears related, at least in part, to disarray of terminal cross-bridges as the thick filaments encroach upon the N-line, a structure which becomes evident within the I-band during contraction of glycerinated fibers. In preliminary studies, optical transforms of A-bands from individual sarcomeres reveal a characteristic myosin layer-line pattern as low as 1.5 μm sarcomere length. A cross-bridge repeat of 143 Å is obtained for sarcomeres above 1.6 μm length; however, an appreciable proportion of sarcomeres in the range from 1.5 μm to 1.9 μ length generate meridional reflections less than 143 Å, and as low as 130 Å.


Thin Filament Fiber Axis Sarcomere Length Thick Filament Knife Edge 
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  1. Berger, J.E., Zobel, C.R. and Engler, P.E. (1966). Laser as light source for optical diffractometers; Fourier analysis of electron micrographs. Science 153: 168–170.PubMedCrossRefGoogle Scholar
  2. Berger, J.E. and Harker, D. (1967). Optical diffractometer for production of Fourier transforms of electron micrographs. Rev. Sci. Inst. 38: 292–293.CrossRefGoogle Scholar
  3. Craig, R. (1977). Structure of A-segments from frog and rabbit skeletal muscle. J. Mol. Biol. 109: 69–81.PubMedCrossRefGoogle Scholar
  4. Franzini-Armstrong, C. and Porter, K.R. (1964). The Z-disc of skeletal muscle fibers. Z. Zellforsch. 61: 661–672.PubMedCrossRefGoogle Scholar
  5. Franzini-Armstrong, C. (1970). Details of the I-band structure as revealed by the localization of ferritin. Tissue and Cell. 2: 327–338.PubMedCrossRefGoogle Scholar
  6. Hanson, J. and Huxley, H.E. (1955). The structural basis of contraction in striated muscle. Symp. Soc. Expt. Biology. 9: 228–264.Google Scholar
  7. Hanson, J. (1988). X-ray diffraction of muscle. Quart. Rev. Biophysics. 1: 177–216.CrossRefGoogle Scholar
  8. Haselgrove, J.C. and Huxley, H.E. (1973). X-ray evidence for radial cross-bridge movement and the sliding filament model in actively contracting skeletal muscle. J. Mol. Biol. 77: 549–568.PubMedCrossRefGoogle Scholar
  9. Haselgrove, J.C. (1975). X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J. Mol. Biol. 92: 113–143.PubMedCrossRefGoogle Scholar
  10. Herman, L. and Dreizen, P. (1971). Electron microscopic studies of skeletal and cardiac muscle of a benthic fish. I. Myofibrillar structure in resting and contracted muscle. Amer. Zoologist. 11: 543–557.Google Scholar
  11. Huxley, A.F. and Niedergerke, R. (1954). Structural changes in muscle during contraction. Interference microscopy of living muscle fibers. Nature. 173: 971–973.PubMedCrossRefGoogle Scholar
  12. Huxley, H.E. and Hanson, J. (1954). Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature. 173: 973–976.PubMedCrossRefGoogle Scholar
  13. Huxley, H.E. (1957). The double array of filaments in cross-striated muscle. J. Biophys. Biochem. Cytology. 3: 631–647.CrossRefGoogle Scholar
  14. Huxley, H.E. (1980). Muscle Cells. In: The Cell, Vol. 4, pp. 365–481, ed. Brachet, J. and Mirsky, A.R. New York, Academic Press.Google Scholar
  15. Huxley, H.E. (1963). Electron microscopic studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7: 281–308.PubMedCrossRefGoogle Scholar
  16. Huxley, H.E. (1965). Structural evidence concerning the mechanism of contraction in striated muscle. In: Muscle. pp. 3–28. Paul, W.M., Daniel, E.E., Kay, C.M., and Monkton, G. Oxford, Pergamon Press.Google Scholar
  17. Huxley, H.E. and Brown, W. (1967). The low-angle X-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor. J. Molec. Biol. 30: 383–434.PubMedCrossRefGoogle Scholar
  18. Huxley, H.E. (1968). Structural difference between resting and rigor muscle; evidence from intensity changes in the low-angle equatorial X-ray diagram. J. Molec. Biol. 37: 507–520.PubMedCrossRefGoogle Scholar
  19. Kensler, R.W. and Levine, R.J.C. (1982). An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments. J. Cell Biol. 92: 443–451.PubMedCrossRefGoogle Scholar
  20. Klug, A. and Berger, J.E. (1964). An optical method for the analysis of periodicities in electron micrographs, and some observations on the mechanism of negative staining. J. Mol. Biol. 10: 565–569.PubMedCrossRefGoogle Scholar
  21. Knappeis, G.G. and Carlsen, F. (1962). The ultrastructure of the Z-disc in skeletal muscle. J. Cell Biol. 13: 323–335.PubMedCrossRefGoogle Scholar
  22. Luft, J.H. (1961). Improvements in epoxy resin embedding methods. J. Biophys. Biochem. Cytology. 9: 409–414.CrossRefGoogle Scholar
  23. O’Brien, E.J., Bennett, P.M. and Hanson, J. (1971). Optical diffraction studies of myofibrillar structure. Phil. Trans. Roy. Soc. Lond. B. 261: 201–208.CrossRefGoogle Scholar
  24. Page, S.G. and Huxley, H.E. (1963). Filament lengths in striated muscle. J. Cell Biology. 19: 369–390.CrossRefGoogle Scholar
  25. Page, S.G. (1968). Fine structure of tortoise skeletal muscle. J. Physiol. 197: 709–715.PubMedGoogle Scholar
  26. Reynolds, E.S. (1963). The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biology. 17: 208–212.CrossRefGoogle Scholar
  27. Sabatini, D.D., Bensch, K.G. and Barnett, R.J. (1963). Cytochemistry and electron microscopy. The preservation of cellular structures and enzymatic activity by aldehyde fixation. J. Cell Biology. 17: 19–58.CrossRefGoogle Scholar
  28. Samosudova, N.V. and Frank, G.M. (1971). Change in the ultrastructure of contractile apparatus of striated muscle under toxic contraction. Biophysika. 16: 244.Google Scholar
  29. Samosudova, N.V., Lyudkovskaya, R.G. and Frank, G.M. (1972). Ultrastructural studies of slow and intermediate isolated frog muscle fibers under toxic contraction. Biophysika. 17: 1055.Google Scholar
  30. Sjostrand, F.S. and Jagendorf-Elfvin, M. (1967). Ultrastructural studies of the contraction-relaxation cycle of glycerinated rabbit psoas muscle. I. The ultrastructure of glycerinated fibers contracted by treatment with ATP. J. Ultrastruct. Research. 17: 348–378.CrossRefGoogle Scholar
  31. Squire, J. (1981). The Structural Basis of Muscular Contraction. New York, Plenum Press.CrossRefGoogle Scholar
  32. Stempak, J.G. and Ward, R.T. (1964). An improved staining method for electron microscopy. J. Cell Biology. 22: 697–701.CrossRefGoogle Scholar
  33. Yarom, R. and Meiri, U. (1971). N-lines in striated muscle: a ffite of intracellular Ca2+. Nature. 234: 254–256.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Paul Dreizen
    • 1
  • Lawrence Herman
    • 2
  • Jacob E. Berger
    • 3
  1. 1.Biophysics Program and Department of MedicineState University of New York, Downstate Medical CenterBrooklynUSA
  2. 2.Department of AnatomyNew York Medical CollegeValhallaUSA
  3. 3.Center for Crystallographic ResearchRoswell Park Memorial InstituteBuffaloUSA

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