Advertisement

Biophysics of structure and mechanism

, Volume 9, Issue 2, pp 95–101 | Cite as

The major polypeptide (MIP) of lens fiber junctions and its synthesis in cultured differentiating lens epithelial cells

Article

Abstract

Lens and liver contain many gap junctions, which for a long time have been considered to be very similar. Recent results, however, point to differences on morphological and biochemical levels, especially when the liver gap junction polypeptide (26,000 Daltons) is compared with the main intrinsic polypeptide (MIP) from lens junctions. The lens fiber specific MIP, which represents a marker molecule for lens cell differentiation could be detected by indirect immunofluorescence as well as by immunodiffusion in lens epithelial cells, which differentiated in vitro under distinct culture conditions. The fine structure of these differentiated cells is presented.

Key words

Lens Communicating junctions Polypeptide Synthesis In-vitro-differentiation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Bloemendal H, Vermorken AJM, Kibbelaar M, Dunia I, Benedetti EL (1977) Nomenclature for the polypeptide chains of lens plasma membranes. Exp Eye Res 24: 413–415Google Scholar
  2. Bok D, Dockstader J, Horwitz J (1982) Immunocytochemical localization of the lens main intrinsic polypeptide (MIP 26) in communicating junctions. J Cell Biol 92: 213–220Google Scholar
  3. Broekhuyse RM, Kuhlmann ED, Stols AD (1976) Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranes. Exp Eye Res 23: 365–371Google Scholar
  4. Broekhuyse RM, Kuhlmann ED, Winkens HJ (1979) Lens membranes VII, MIP is an immunological specific component of lens fiber membranes and is identical with 26 K band protein. Exp Eye Res 29: 303–313Google Scholar
  5. Dell'Orco RT (1975) The use of arrested populations of human diploid fibroblasts for the study of senescence in vitro. Adv Exp Med Biol 53: 41–51Google Scholar
  6. Goodenough DA, Dick JSB, Lyons JE (1980) Lens metabolic cooperation: a study of mouse lens transport and permeability visualized with freeze substitution autoradiography and electron microscopy. J Cell Biol 86: 576–589Google Scholar
  7. Henderson D, Eibl H, Weber K (1979) Structure and biochemistry of hepatic gap junctions. J Mol Biol 132: 193–218Google Scholar
  8. Hertzberg EL (1980) Biochemical and immunocytochemical approaches to the study of gap junctional communication. In Vitro 16: 1057–1067Google Scholar
  9. Hertzberg EL, Anderson DJ, Friedlander M, Gilula NB (1982) Comparative analysis of the major polypeptides from liver gap junctions and lens fiber junctions. J Cell Biol 92: 53–59Google Scholar
  10. Hockwin O (1971) Age changes of lens metabolism. In: Brecht H, Rohen JW (eds) Altern und Entwicklung. Schattauer Verlag, Stuttgart, pp 95–129Google Scholar
  11. Horwitz J, Wong MM (1980) Peptide mapping by limited proteolysis in sodiumdodecylsulphate of the main intrinsic polypeptides isolated from human and bovine lens plasma membranes. Biochim Biophys Acta 622: 134–143Google Scholar
  12. Kubawara T (1975) The maturation of the lens cell. A morphologic study. Exp Eye Res 20: 427–443Google Scholar
  13. Nicholson BJ, Hunkapiller MW, Hood LE, Revel JP, Takemoto L (1980) Partial sequencing of the gap junction protein from rat lens and liver. J Cell Biol 87: 1539a (Abstract)Google Scholar
  14. Peracchia C, Peracchia LL (1980) Gap junction dynamics: reversible effects of hydrogen ions. J Cell Biol 87: 719–727Google Scholar
  15. Rae JL (1979) The electrophysiology of the crystalline lens. In: Zadunaisky JA, Davson H (eds) Current topics in eye research. Academic Press, New York, pp 37–90Google Scholar
  16. Rafferty NS, Esson EA (1974) An electron microscope study of adult mouse lens: some ultrastructural specializations. J Ultrastruct Res 46: 239–253Google Scholar
  17. Rink H (1978) The water content of bovine lenses during aging. Interdiscip Top Gerontol 12: 272–277Google Scholar
  18. Rink H, Vornhagen R (1980) Crystallins of rat and bovine lens epithelial cells during aging. In: Regnault F, Hockwin O, Courtois Y (eds) Aging of the lens. Elsevier, North-Holland, Amsterdam, pp 37–51Google Scholar
  19. Takemoto LJ, Hansen JS, Horwitz J (1981) Interspecies conservation of the main intrinsic polypeptide (MIP) of the lens membrane. Comp Biochem Physiol 68B: 101–106Google Scholar
  20. Traub O, Janßen-Timmen U, Drüge P, Dermietzel R, Willecke K (1982) Immunological properties of gap junction protein from mouse liver. J Cell Biochem 19: 27–43Google Scholar
  21. Vornhagen R, Rink H (1981) The expression of crystallins in early and late passages of calf lens epithelial cells grown under different culture conditions. J Cell Biol 24: 25Google Scholar
  22. Vornhagen R, Rink H, Broekhuyse RM (1982) Main intrinsic polypeptide (MIP) a membrane protein as marker molecule for lens cell differentiation. J Cell Biol 27: 33Google Scholar
  23. Willecke K, Traub O, Janßen-Timmen U, Drüge P, Dermietzel R (1982) Expression of gap junction protein in liver and lens tissue. In: Jaenicke L (ed) Biochemistry of differentiation and morphogenesis. Springer, Berlin Heidelberg New YorkGoogle Scholar
  24. Zampighi G, Simon SA, Robertson JD, McIntosh TJ, Costello MJ (1982) On the structural organization of isolated bovine lens fiber junctions. J Cell Biol 93: 175–189Google Scholar
  25. Zigler JS, Horwitz J (1981) Immunochemical studies on the major intrinsic membrane polypeptide from human lens. Invest Ophthalmol 21: 46–51Google Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • H. Rink
    • 1
  1. 1.Institut für StrahlenbiologieUniversität BonnBonnFederal Republic of Germany

Personalised recommendations