350 rub
Journal №1 for 2012 г.
Article in number:
Organization of Cytoskeleton of the Cross-Striated Myocyte
Authors:
Yu.A. Khoroshkov, N.A. Odintsova
Abstract:
Using the scanning and transmissive electron microscopy methods the morphological analysis of structural-functional organization of cytoskeleton of the cross-striated myocyte was made. The structural complexes of cytoskeleton are connected closely with constricting system of myocyte was found. These complexes guarantee total integration and local connections with sarcolemma, stabilize the architectonics of myofibrils and form buffer mechanisms between them. Complexes proteins of cytoskeleton surround myofibrils in the line «Z» area. It are more important elements of integrating system of the constricting apparatus of myocyte. Most large complexes proteins of cytoskeleton are concentrated in the line «Z» area around of the constricting apparatus. It form local connections with sarcolemma. These connections form also less large complexes proteins of cytoskeleton, which are concentrated in the line «M» area. Structural proteins of cytoskeleton form inside and outer carcass of sarcolemma, which fulfils also the supporting function of design myocyte.
Pages: 229-232
References
  1. Зайцев В.В. Цитоскелетная организация клеток нефрона позвоночных // Российские морфологические ведомости. 1999. № 1-2. С.71.
  2. Ломакин А.Ю., Надеждина Е.С. Динамика немембранных компонентов клетки: роль активного транспорта по микротрубочкам // Биохимия. 2010. Т. 75. № 1. С. 12-16.
  3. Branly Crista M., Rock Ronalds. Unconventional myosin traffic in cell reveals a selective actin cytoskeleton // Proc. Natl. Acad. Sci. USA. 2009. V.106. № 24. P. 9685-9690.
  4. King Megan C., Drivas Theodore G., Blober Gunter. A network of nuclear envelope membrane proteins linking centromers to microtubule // Cell. 2008. V. 134. P. 427-438.
  5. Yoshina Hisaho, Suzuki Reiko. Adhesion structures and their cytoskeleton membrane interactions at podosomes of osteoclastis in culture // Cell and Tissue Res. 2008. V. 331. № 3. P. 625-641.
  6. Buvridge K., Fath K., Kelly F., Naekalls G., Turner C. Focal adhesion: transmembrane junctions between the extracellular matrix and cytoskeleton // Annu. Rev.Cell Biol. 1988. № 4. P. 487-526.
  7. Фултон А. Цитоскелет. Архитектура и хореография клетки. М.: Мир. 1987. 320 с.
  8. Gastellani L., Offer G., Elliott A., Brien E. Structure and filamin and F-actin heavy merofilamin complex // J. Muscle Res. Cell Mot. 1981.V.2. P.193-202.
  9. Kimura S., Maruyama K. Preparation of native connectin from chicken breast muscle // J. Biochem. 1983. V. 94. P. 2083-2085.
  10. Maruyama K. Elastic structure of connectin in muscle. In: Muscle contraction. Its regulatory mechanisms. Berlin. 1980. P. 485-496.
  11. Nelson J., Lazarides E. Goblin (ankyrin) in striated muscle identification of the potential membrane receptor for erythroid spectrin in muscle cell. // Proc. Natl. Acad. Sci. USA. 1984. V. 81. P. 3292-3296.
  12. Thornell E., Ericsson A., Edstrom L. Intermediate filaments in human myophathies / In: Cell and Muscle Motility, 1983. New York, London. V. 4. P. 85-136.
  13. Birchmeier W. Cytoskeleton. Structure and function // Trends Biochem. Sci. 1984. V. 9. № 4. P.192-195.
  14. Pardo J.V., Siliciano I.D. A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements («costameres») mark sites of attachement between myofibrils and sarcolemma // Proc. Natl. Acad. Sci. NSA. 1983. V. 80. P. 1008-1012.
  15. Pardo J.V., Siliciano I.D. Vinculin is a component of extensive network of myofibrilla sarcolemma attachment regions in cardiac muscle fibers // J. Cell. Biol. 1983. V. 4. P. 1081-1087.
  16. Gruig S.V., Pardo J.V. Gama-actin, spectrin and intermediate filament proteins localize with vinculin at costameres myofibril to sarcolemma attachment sites // J. Cell Motility. 1983. V. 3. P. 449-462.
  17. Wang K. Membrane skeleton of skeletal muscle // Nature. 1983. V. 304. P. 485-486.