Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.
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Journal: 1979/December - Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
PUBMED: 291010
Abstract:
Fibronectin mediates the adhesion of cells to collagen by first binding to the collagen substrate, followed by attachment of the cells to the fibronectin-collagen complex. Bovine brain gangliosides were found to block fibronectin-mediated cell adhesion to collagen in a concentration-dependent manner. The gangliosides did not block the binding of fibronectin to collagen but did prevent the attachment of the cells to the fibronectin-collagen complex. Of the individual gangliosides tested, GT1 and GD1a were the most effective inhibitors followed by GD1b greater than GM1 greater than GM2; GM3 was not an inhibitor. The inhibition of cell adhesion also was observed with the oligosaccharide portion of the gangliosides, but not with ceramides or with a variety of free sugars or glycosaminoglycans. Mild periodate oxidation of mixed gangliosides or of GD1a modified their sialic acid residues and the oxidized gangliosides were no longer inhibitory; subsequent reduction with NaBH4 did not restore the inhibitory activity of the modified gangliosides. These results suggest that specific gangliosides or related sialic acid-containing glycoconjugates on the cell surface may act as the receptors for fibronectin.
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Proc Natl Acad Sci U S A 76(7): 3367-3371
PMID: 291010

Ganglioside inhibition of fibronectin-mediated cell adhesion to collagen.

Abstract

Fibronectin mediates the adhesion of cells to collagen by first binding to the collagen substrate, followed by attachment of the cells to the fibronectin-collagen complex. Bovine brain gangliosides were found to block fibronectin-mediated cell adhesion to collagen in a concentration-dependent manner. The gangliosides did not block the binding of fibronectin to collagen but did prevent the attachment of the cells to the fibronectin-collagen complex. Of the individual gangliosides tested, GT1 and GD1a were the most effective inhibitors followed by GD1b greater than GM1 greater than GM2; GM3 was not an inhibitor. The inhibition of cell adhesion also was observed with the oligosaccharide portion of the gangliosides, but not with ceramides or with a variety of free sugars or glycosaminoglycans. Mild periodate oxidation of mixed gangliosides or of GD1a modified their sialic acid residues and the oxidized gangliosides were no longer inhibitory; subsequent reduction with NaBH4 did not restore the inhibitory activity of the modified gangliosides. These results suggest that specific gangliosides or related sialic acid-containing glycoconjugates on the cell surface may act as the receptors for fibronectin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Grinnell F. Cellular adhesiveness and extracellular substrata. Int Rev Cytol. 1978;53:65–144. [PubMed] [Google Scholar]
  • Klebe RJ. Isolation of a collagen-dependent cell attachment factor. Nature. 1974 Jul 19;250(463):248–251. [PubMed] [Google Scholar]
  • Yamada KM, Kennedy DW. Fibroblast cellular and plasma fibronectins are similar but not identical. J Cell Biol. 1979 Feb;80(2):492–498.[PMC free article] [PubMed] [Google Scholar]
  • Pearlstein E. Substrate activation of cell adhesion factor as a prerequisite for cell attachment. Int J Cancer. 1978 Jul 15;22(1):32–35. [PubMed] [Google Scholar]
  • Klebe RJ. Cell attachment to collagen: the requirement for energy. J Cell Physiol. 1975 Oct;86(2 Pt 1):231–236. [PubMed] [Google Scholar]
  • Engvall E, Ruoslahti E, Miller EJ. Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J Exp Med. 1978 Jun 1;147(6):1584–1595.[PMC free article] [PubMed] [Google Scholar]
  • Kleinman HK, McGoodwin EB. Localization of the cell attachment region in types I and II collagens. Biochem Biophys Res Commun. 1976 Sep 20;72(2):426–432. [PubMed] [Google Scholar]
  • Dessau W, Adelmann BC, Timpl R. Identification of the sites in collagen alpha-chains that bind serum anti-gelatin factor (cold-insoluble globulin). Biochem J. 1978 Jan 1;169(1):55–59.[PMC free article] [PubMed] [Google Scholar]
  • Kleinman HK, McGoodwin EB, Martin GR, Klebe RJ, Fietzek PP, Woolley DE. Localization of the binding site for cell attachment in the alpha1(I) chain of collagen. J Biol Chem. 1978 Aug 25;253(16):5642–5646. [PubMed] [Google Scholar]
  • Hopper KE, Adelmann BC, Gentner G, Gay S. Recongnition by guinea-pig peritoneal exudate cells of conformationally different states of the collagen molecule. Immunology. 1976 Feb;30(2):249–259.[PMC free article] [PubMed] [Google Scholar]
  • Engvall E, Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer. 1977 Jul 15;20(1):1–5. [PubMed] [Google Scholar]
  • Ruoslahti E, Vaheri A. Interaction of soluble fibroblast surface antigen with fribrinogen and fibrin. J Exp Med. 1975 Feb 1;141(2):497–501.[PMC free article] [PubMed] [Google Scholar]
  • Fishman PH, Brady RO. Biosynthesis and function of gangliosides. Science. 1976 Nov 26;194(4268):906–915. [PubMed] [Google Scholar]
  • Van Heyningen WE, Carpenter CC, Pierce NF, Greenough WB., 3rd Deactivation of cholera toxin by ganglioside. J Infect Dis. 1971 Oct;124(4):415–418. [PubMed] [Google Scholar]
  • Pacuszka T, Duffard RO, Nishimura RN, Brady RO, Fishman PH. Biosynthesis of bovine thyroid gangliosides. J Biol Chem. 1978 Aug 25;253(16):5839–5846. [PubMed] [Google Scholar]
  • Fishman PH, Moss J, Osborne JC., Jr Interaction of choleragen with the oligosaccharide of ganglioside GM1: evidence for multiple oligosaccharide binding sites. Biochemistry. 1978 Feb 21;17(4):711–716. [PubMed] [Google Scholar]
  • Veh R, Corfield AP, Sander M, Schauer R. Neuraminic acid-specific modification and tritium labelling of gangliosides. Biochim Biophys Acta. 1976 Jan 18;486(1):145–160. [PubMed] [Google Scholar]
  • Moss J, Manganiello VC, Fishman PH. Enzymatic and chemical oxidation of gangliosides in cultured cells: effects of choleragen. Biochemistry. 1977 May 3;16(9):1876–1881. [PubMed] [Google Scholar]
  • AMINOFF D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J. 1961 Nov;81:384–392.[PMC free article] [PubMed] [Google Scholar]
  • Fishman PH, Brady RO, Bradley RM, Aaronson SA, Todaro GJ. Absence of a specific ganglioside galactosyltransferase in mouse cells transformed by murine sarcoma virus. Proc Natl Acad Sci U S A. 1974 Feb;71(2):298–301.[PMC free article] [PubMed] [Google Scholar]
  • Henneberry RC, Fishman PH, Freese E. Morphological changes in cultured mammalian cells: prevention by the calcium ionophore A23187. Cell. 1975 May;5(1):1–9. [PubMed] [Google Scholar]
  • Cuatrecasas P. Gangliosides and membrane receptors for cholera toxin. Biochemistry. 1973 Aug 28;12(18):3558–3566. [PubMed] [Google Scholar]
  • Hollenberg MD, Fishman PH, Bennett V, Cuatrecasas P. Cholera toxin and cell growth: role of membrane gangliosides. Proc Natl Acad Sci U S A. 1974 Oct;71(10):4224–4228.[PMC free article] [PubMed] [Google Scholar]
  • Moss J, Fishman PH, Manganiello VC, Vaughan M, Brady RO. Functional incorporation of ganglioside into intact cells: induction of choleragen responsiveness. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1034–1037.[PMC free article] [PubMed] [Google Scholar]
  • Lingwood CA, Hakomori S. Selective inhibition of cell growth and associated changes in glycolipid metabolism induced by monovalent antibodies to glycolipids. Exp Cell Res. 1977 Sep;108(2):385–391. [PubMed] [Google Scholar]
  • Brady RO, Fishman PH. Biosynthesis of glycolipids in virus-transformed cells. Biochim Biophys Acta. 1974 Sep 9;355(2):121–148. [PubMed] [Google Scholar]
  • Hynes RO. Alteration of cell-surface proteins by viral transformation and by proteolysis. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3170–3174.[PMC free article] [PubMed] [Google Scholar]
  • Gahmberg CG, Hakomori S. Organization of glycolipids and glycoproteins in surface membranes: dependency on cell cycle and on transformation. Biochem Biophys Res Commun. 1974 Jul 10;59(1):283–291. [PubMed] [Google Scholar]
  • Vaheri A, Ruoslahti E. Fibroblast surface antigen produced but not retained by virus-transformed human cells. J Exp Med. 1975 Aug 1;142(2):530–535.[PMC free article] [PubMed] [Google Scholar]
  • Langenbach R, Kennedy S. Gangliosides and their cell density-dependent changes in control and chemically transformed C3H/10T1/2 cells. Exp Cell Res. 1978 Mar 15;112(2):361–372. [PubMed] [Google Scholar]
  • Yogeeswaran G, Hakomori S. Cell contact-dependent ganglioside changes in mouse 3T3 gibroblasts and a suppressed sialidase activity on cell contact. Biochemistry. 1975 May 20;14(10):2151–2156. [PubMed] [Google Scholar]
  • Chen LB, Moser FG, Chen AB, Mosesson MW. Distribution of cell surface LETS protein in co-cultures of normal and transformed cells. Exp Cell Res. 1977 Sep;108(2):375–383. [PubMed] [Google Scholar]
  • Huang RT. Cell adhesion mediated by glycolipids. Nature. 1978 Dec 7;276(5688):624–626. [PubMed] [Google Scholar]
Copyright notice
Abstract
Fibronectin mediates the adhesion of cells to collagen by first binding to the collagen substrate, followed by attachment of the cells to the fibronectin-collagen complex. Bovine brain gangliosides were found to block fibronectin-mediated cell adhesion to collagen in a concentration-dependent manner. The gangliosides did not block the binding of fibronectin to collagen but did prevent the attachment of the cells to the fibronectin-collagen complex. Of the individual gangliosides tested, GT1 and GD1a were the most effective inhibitors followed by GD1b greater than GM1 greater than GM2; GM3 was not an inhibitor. The inhibition of cell adhesion also was observed with the oligosaccharide portion of the gangliosides, but not with ceramides or with a variety of free sugars or glycosaminoglycans. Mild periodate oxidation of mixed gangliosides or of GD1a modified their sialic acid residues and the oxidized gangliosides were no longer inhibitory; subsequent reduction with NaBH4 did not restore the inhibitory activity of the modified gangliosides. These results suggest that specific gangliosides or related sialic acid-containing glycoconjugates on the cell surface may act as the receptors for fibronectin.
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