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The fine structure of the bovine Descemet's membrane with special reference to biochemical nature

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Summary

A freeze-etch replica method combined with biochemical analyses was used to investigate the ultrastructural organization of the bovine Descemet's membrane.

The freeze-etch replica observations revealed that the intact Descemet's membranes were composed of stacks of two-dimensionally arranged hexagonal lattices, in which four components were resolved; (1) round densities as nodes, (2) rod-like structures connecting the densities, (3) randomly oriented fine filaments within the lattices, and (4) amorphous materials covering the lattices.

When the membranes were treated with sodium dodecyl sulfate (SDS) and mercaptoethanol, only the amorphous materials were solubilized. However, both the amorphous materials and rod-like structures disappeared in SDS-mercaptoethanol-urea-treated membranes. When the membranes were treated with a very low concentration (0.0005%) of collagenase, rod-like structures and round densities remained insoluble. If the concentration was raised to 0.01%, only the round densities persisted.

Comparing these data with the amino acid analysis of each fraction, the following conclusions may be drawn: rod-like structures and fine filaments contain collagenous proteins of different solubility, while round densities and amorphous materials are non-collagenous in nature.

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References

  • Alitalo K, Vaheri A, Kreig T, Timpl R (1980) Biosynthesis of two subunits of type IV procollagen and of other basement membrane proteins by a human tumor cell line. Eur J Biochem 109:247–255

    Google Scholar 

  • Bailey AJ, Robins SP, Balian G (1974) Biological significance of the intermolecular crosslinks of collagen. Nature (London) 251:105–109

    Google Scholar 

  • Bernfield MR, Banerjee SD, Cohn RH (1972) Dependence of salivary epithelial morphology and branching morphogenesis upon acid mucopolysaccharide-protein (proteoglycan) at the epithelial surface. J Cell Biol 52:674–689

    Google Scholar 

  • Bornstein P, Traub W (1979) The chemistry and biology of collagen. In: Neurath H, Hill RL, Boeder C-L (eds) The proteins. Vol 4. Academic Press, New York, pp 412–632

    Google Scholar 

  • Brendel K, Meezan E, Nagle RB (1978) The acellular perfused kidney: A model for basement membrane permeability. In: Kefalides NA (ed) Biology and chemistry of basement membranes. Academic Press, New York, pp 177–193

    Google Scholar 

  • Carlson EC, Meezan E, Brendel K, Kenney MC (1981) Ultrastructural analysis of control and enzymetreated isolated renal basement membranes. Anat Rec 200:421–436

    Google Scholar 

  • Chung E, Rhodes RK, Miller EJ (1976) Isolation of three collagenous components of probable basement membrane origin from several tissues. Biochem Biophys Res Commun 71:1167–1174

    Google Scholar 

  • Dohlman C-H, Balazs EA (1955) Chemical studies on Descemet's membrane of the bovine cornea. Arch Biochem Biophys 57:445–457

    Google Scholar 

  • Fairbanks G, Steck TL, Wallach DHF (1971) Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617

    Google Scholar 

  • Farquhar MG (1978) Structure and function in glomerular capillaries: Role of the basement membrane in glomerular filtration. In: Kefalides NA (ed) Biology and chemistry of basement membranes. Academic Press, New York, pp 43–80

    Google Scholar 

  • Franglen G (1974) Plasma albumin: Aspects of its chemical behavior and structure. In: Allison AC (ed) Structure and function of plasma proteins. Vol 1. Plenum Press, London, pp 265–281

    Google Scholar 

  • Hay ED, Revel J-P (1969) In: Fine structure of the developing avian cornea. S Karger, Basel, Switzerland

    Google Scholar 

  • Heuser JE, Salpeter SR (1979) Organization of acetylcholine receptors in quick frozen, deep-etched, and rotary-replicated Torpedo postsynaptic membrane. J Cell Biol 82:150–173

    Google Scholar 

  • Hudson BG, Spiro RG (1972) Studies on the native and reduced alkylated renal glomerular basement membrane. J Biol Chem 247:4229–4238

    Google Scholar 

  • Hung C-H, Ohno M, Freytag JW, Hudson BG (1977) Intestinal basement membrane of Ascaris suum: Analysis of polypeptide components. J Biol Chem 252:3995–4001

    Google Scholar 

  • Jakus MA (1956) Studies on the cornea: II. The fine structure of Descemet's membrane. J Biophys Biochem Cytol 2 suppl: 243–255

    Google Scholar 

  • Jakus MA (1964) The lens. In: Ocular fine structure. Little Brown, Boston, pp 171–197

    Google Scholar 

  • Kefalides NA (1973) Structure and biosynthesis of basement membranes. Int Rev Connect Tissue Res 6:63–104

    Google Scholar 

  • Kefalides NA, Denduchis B (1969) Structural components of epithelial and endothelial basement membranes. Biochemistry 11:4613–4621

    Google Scholar 

  • Kefalides NA, Cameron JD, Tomichek EA, Yanoff M (1976) Biosynthesis of basement membrane collagen by rabbit corneal endothelium in vitro. J Biol Chem 251:730–733

    Google Scholar 

  • Krakower CA, Greenspon SA (1951) Localization of the nephrotoxic antigen within the isolated renal glomerulus. AMA Arch Pathol 52:629–639

    Google Scholar 

  • Moczar M, Moczar E (1975) Biochemical aspects of the maturation of corneal stroma and Descemet's membrane. Arch Opthalmol (Paris) 35:83–90

    Google Scholar 

  • Olsen BR, Alper R, Kefalides NA (1973) Structural characterization of a soluble fraction from lens-capsule basement membrane. Eur J Biochem 38:220–228

    Google Scholar 

  • Roll FJ, Madri JA, Albert J, Furthmayr H (1980) Codistribution of collagen types IV and AB2 in basement membranes and mesangium of the kidney: An immunoferritin study of ultrathin frozen sections. J Cell Biol 85:597–616

    Google Scholar 

  • Sanes JR, Marshall LM, McMahan UJ (1978) Reinnervation of muscle fiber basal lamina after removal of myofibers: Differentiation of regenerating axons at original synaptic sites. J Cell Biol 78:176–198

    Google Scholar 

  • Sawada H, Yamada E (1981) A freeze-fracture deep-etching replica method with volatile cryoprotectant. J Electr Microsc 30:341–344

    Google Scholar 

  • Terranova VP, Rohrbach DH, Martin GR (1980) Role of laminin in the attachment of PAM 212 (epithelial) cells to basement membrane collagen. Cell 22:719–726

    Google Scholar 

  • Yamada E (1955) The fine structure of the renal glomerulus of the mouse. J Biophys Biochem Cytol 1:551–566

    Google Scholar 

  • Zacharius RM, Zell TE, Morrison JH, Woodlock JJ (1969) Glycoprotein staining following electrophoresis on acrylamide gels. Anal Biochem 30:148–152

    Google Scholar 

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Sawada, H. The fine structure of the bovine Descemet's membrane with special reference to biochemical nature. Cell Tissue Res. 226, 241–255 (1982). https://doi.org/10.1007/BF00218356

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