Abstract
The structural simplicity of the Z line in fish muscle fibers allows direct visualization of its basic geometry. Models which postulate termination of the I filaments at the edges of the Z line and the direct linkage of I filaments belonging to the two adjacent sarcomeres by Z filaments crossing the whole width of the Z line give the best fit to the electron micrographs. The structure of fish Z lines is not significantly altered by the use of different fixation procedures and by changes in sarcomere length.
Full Text
The Full Text of this article is available as a PDF (1.5 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- CARLSEN F., KNAPPEIS G. G., BUCHTHAL F. Ultrastructure of the resting and contracted striated muscle fiber at different degrees of stretch. J Biophys Biochem Cytol. 1961 Oct;11:95–117. doi: 10.1083/jcb.11.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Elliott G. F., Lowy J., Millman B. M. X-ray diffraction from living striated muscle during contraction. Nature. 1965 Jun 26;206(991):1357–1358. doi: 10.1038/2061357a0. [DOI] [PubMed] [Google Scholar]
- FRANZINI-ARMSTRONG C., PORTER K. R. SARCOLEMMAL INVAGINATIONS CONSTITUTING THE T SYSTEM IN FISH MUSCLE FIBERS. J Cell Biol. 1964 Sep;22:675–696. doi: 10.1083/jcb.22.3.675. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FRANZINI-ARMSTRONG C., PORTER K. R. THE Z DISC OF SKELETAL MUSCLE FIBRILS. Z Zellforsch Mikrosk Anat. 1964;61:661–672. doi: 10.1007/BF00342617. [DOI] [PubMed] [Google Scholar]
- Gauthier G. F. On the relationship of ultrastructural and cytochemical features of color in mammalian skeletal muscle. Z Zellforsch Mikrosk Anat. 1969;95(3):462–482. doi: 10.1007/BF00995217. [DOI] [PubMed] [Google Scholar]
- Goll D. E., Mommaerts W. F., Reedy M. K., Seraydarian K. Studies on alpha-actinin-like proteins liberated during trypsin digestion of alpha-actinin and of myofibrils. Biochim Biophys Acta. 1969 Feb 4;175(1):174–194. doi: 10.1016/0005-2795(69)90156-1. [DOI] [PubMed] [Google Scholar]
- HUXLEY H. E. X-ray analysis and the problem of muscle. Proc R Soc Lond B Biol Sci. 1953 Mar 11;141(902):59–62. doi: 10.1098/rspb.1953.0017. [DOI] [PubMed] [Google Scholar]
- KNAPPEIS G. G., CARLSEN F. The ultrastructure of the Z disc in skeletal muscle. J Cell Biol. 1962 May;13:323–335. doi: 10.1083/jcb.13.2.323. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kelly D. E., Cahill M. A. Filamentous and matrix components of skeletal muscle Z-disks. Anat Rec. 1972 Apr;172(4):623–642. doi: 10.1002/ar.1091720403. [DOI] [PubMed] [Google Scholar]
- Kelly D. E. Myofibrillogenesis and Z-band differentiation. Anat Rec. 1969 Mar;163(3):403–425. doi: 10.1002/ar.1091630305. [DOI] [PubMed] [Google Scholar]
- Landon D. N. The influence of fixation upon the fine structure of the Z-disk of rat striated muscle. J Cell Sci. 1970 Jan;6(1):257–276. doi: 10.1242/jcs.6.1.257. [DOI] [PubMed] [Google Scholar]
- Locke M., Krishnan N., McMahon J. T. A routine method for obtaining high contrast without staining sections. J Cell Biol. 1971 Aug;50(2):540–544. doi: 10.1083/jcb.50.2.540. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MARKHAM R., HITCHBORN J. H., HILLS G. J., FREY S. THE ANATOMY OF THE TOBACCO MOSAIC VIRUS. Virology. 1964 Mar;22:342–359. doi: 10.1016/0042-6822(64)90025-x. [DOI] [PubMed] [Google Scholar]
- Macdonald R. D., Engel A. G. Observations on organization of Z-disk components and on rod-bodies of Z-disk origin. J Cell Biol. 1971 Feb;48(2):431–437. doi: 10.1083/jcb.48.2.431. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Masaki T., Endo M., Ebashi S. Localization of 6S component of a alpha-actinin at Z-band. J Biochem. 1967 Nov;62(5):630–632. doi: 10.1093/oxfordjournals.jbchem.a128717. [DOI] [PubMed] [Google Scholar]
- Moore P. B., Huxley H. E., DeRosier D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J Mol Biol. 1970 Jun 14;50(2):279–295. doi: 10.1016/0022-2836(70)90192-0. [DOI] [PubMed] [Google Scholar]
- PAGE S. G., HUXLEY H. E. FILAMENT LENGTHS IN STRIATED MUSCLE. J Cell Biol. 1963 Nov;19:369–390. doi: 10.1083/jcb.19.2.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pepe F. A. Some aspects of the structural organization of the myofibril as revealed by antibody--staining methods. J Cell Biol. 1966 Mar;28(3):505–525. doi: 10.1083/jcb.28.3.505. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peracchia C., Mittler B. S. Fixation by means of glutaraldehyde-hydrogen peroxide reaction products. J Cell Biol. 1972 Apr;53(1):234–238. doi: 10.1083/jcb.53.1.234. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rowe R. W. Ultrastructure of the Z line of skeletal muscle fibers. J Cell Biol. 1971 Dec;51(3):674–685. doi: 10.1083/jcb.51.3.674. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sato T. A modified method for lead staining of thin sections. J Electron Microsc (Tokyo) 1968;17(2):158–159. [PubMed] [Google Scholar]
- Schiaffino S., Hanzlíková V., Pierobon S. Relations between structure and function in rat skeletal muscle fibers. J Cell Biol. 1970 Oct;47(1):107–119. doi: 10.1083/jcb.47.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stromer M. H., Goll D. E. Studies on purified -actinin. II. Electron microscopic studies on the competitive binding of -actinin and tropomyosin to Z-line extracted myofibrils. J Mol Biol. 1972 Jun 28;67(3):489–494. doi: 10.1016/0022-2836(72)90465-2. [DOI] [PubMed] [Google Scholar]
- Stromer M. H., Hartshorne D. J., Mueller H., Rice R. V. The effect of various protein fractions on Z- and M-line reconstitution. J Cell Biol. 1969 Jan;40(1):167–178. doi: 10.1083/jcb.40.1.167. [DOI] [PMC free article] [PubMed] [Google Scholar]