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. 1988 Oct 1;107(4):1541–1549. doi: 10.1083/jcb.107.4.1541

Evidence that an RGD-dependent receptor mediates the binding of oligodendrocytes to a novel ligand in a glial-derived matrix

PMCID: PMC2115253  PMID: 2459131

Abstract

A simple adhesion assay was used to measure the interaction between rat oligodendrocytes and various substrata, including a matrix secreted by glial cells. Oligodendrocytes bound to surfaces coated with fibronectin, vitronectin and a protein component of the glial matrix. The binding of cells to all of these substrates was inhibited by a synthetic peptide (GRGDSP) modeled after the cell-binding domain of fibronectin. The component of the glial matrix responsible for the oligodendrocyte interaction is a protein which is either secreted by the glial cells or removed from serum by products of these cultures; serum alone does not promote adhesion to the same extent as the glial- derived matrix. The interaction of cells with this glial-derived matrix requires divalent cations and is not mediated by several known RGD- containing extracellular proteins, including fibronectin, vitronectin, thrombospondin, type I and type IV collagen, and tenascin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Akiyama S. K., Yamada S. S., Yamada K. M. Characterization of a 140-kD avian cell surface antigen as a fibronectin-binding molecule. J Cell Biol. 1986 Feb;102(2):442–448. doi: 10.1083/jcb.102.2.442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Asch A. S., Leung L. L., Shapiro J., Nachman R. L. Human brain glial cells synthesize thrombospondin. Proc Natl Acad Sci U S A. 1986 May;83(9):2904–2908. doi: 10.1073/pnas.83.9.2904. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boucaut J. C., Darribère T., Poole T. J., Aoyama H., Yamada K. M., Thiery J. P. Biologically active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos. J Cell Biol. 1984 Nov;99(5):1822–1830. doi: 10.1083/jcb.99.5.1822. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bradel E. J., Prince F. P. Cultured neonatal rat oligodendrocytes elaborate myelin membrane in the absence of neurons. J Neurosci Res. 1983;9(4):381–392. doi: 10.1002/jnr.490090404. [DOI] [PubMed] [Google Scholar]
  5. Cardwell M. C., Rome L. H. RGD-containing peptides inhibit the synthesis of myelin-like membrane by cultured oligodendrocytes. J Cell Biol. 1988 Oct;107(4):1551–1559. doi: 10.1083/jcb.107.4.1551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Carey D. J., Todd M. S., Rafferty C. M. Schwann cell myelination: induction by exogenous basement membrane-like extracellular matrix. J Cell Biol. 1986 Jun;102(6):2254–2263. doi: 10.1083/jcb.102.6.2254. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chiquet M., Fambrough D. M. Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits. J Cell Biol. 1984 Jun;98(6):1937–1946. doi: 10.1083/jcb.98.6.1937. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Dedhar S., Ruoslahti E., Pierschbacher M. D. A cell surface receptor complex for collagen type I recognizes the Arg-Gly-Asp sequence. J Cell Biol. 1987 Mar;104(3):585–593. doi: 10.1083/jcb.104.3.585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Erickson H. P., Taylor H. C. Hexabrachion proteins in embryonic chicken tissues and human tumors. J Cell Biol. 1987 Sep;105(3):1387–1394. doi: 10.1083/jcb.105.3.1387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gabius H. J., Springer W. R., Barondes S. H. Receptor for the cell binding site of discoidin I. Cell. 1985 Sep;42(2):449–456. doi: 10.1016/0092-8674(85)90102-3. [DOI] [PubMed] [Google Scholar]
  11. Gospodarowicz D. J. Extracellular matrices and the control of cell proliferation and differentiation in vitro. Prog Clin Biol Res. 1984;145:103–128. [PubMed] [Google Scholar]
  12. Grumet M., Hoffman S., Crossin K. L., Edelman G. M. Cytotactin, an extracellular matrix protein of neural and non-neural tissues that mediates glia-neuron interaction. Proc Natl Acad Sci U S A. 1985 Dec;82(23):8075–8079. doi: 10.1073/pnas.82.23.8075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Horwitz A., Duggan K., Greggs R., Decker C., Buck C. The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin. J Cell Biol. 1985 Dec;101(6):2134–2144. doi: 10.1083/jcb.101.6.2134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Humphries M. J., Akiyama S. K., Komoriya A., Olden K., Yamada K. M. Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion. J Cell Biol. 1986 Dec;103(6 Pt 2):2637–2647. doi: 10.1083/jcb.103.6.2637. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hynes R. O. Integrins: a family of cell surface receptors. Cell. 1987 Feb 27;48(4):549–554. doi: 10.1016/0092-8674(87)90233-9. [DOI] [PubMed] [Google Scholar]
  16. Kleinman H. K., McGarvey M. L., Hassell J. R., Star V. L., Cannon F. B., Laurie G. W., Martin G. R. Basement membrane complexes with biological activity. Biochemistry. 1986 Jan 28;25(2):312–318. doi: 10.1021/bi00350a005. [DOI] [PubMed] [Google Scholar]
  17. Kleinman H. K., McGoodwin E. B., Rennard S. I., Martin G. R. Preparation of collagen substrates for cell attachment: effect of collagen concentration and phosphate buffer. Anal Biochem. 1979 Apr 15;94(2):308–312. doi: 10.1016/0003-2697(79)90365-8. [DOI] [PubMed] [Google Scholar]
  18. Künemund V., Jungalwala F. B., Fischer G., Chou D. K., Keilhauer G., Schachner M. The L2/HNK-1 carbohydrate of neural cell adhesion molecules is involved in cell interactions. J Cell Biol. 1988 Jan;106(1):213–223. doi: 10.1083/jcb.106.1.213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  20. Lawler J., Hynes R. O. The structure of human thrombospondin, an adhesive glycoprotein with multiple calcium-binding sites and homologies with several different proteins. J Cell Biol. 1986 Nov;103(5):1635–1648. doi: 10.1083/jcb.103.5.1635. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Liesi P., Kirkwood T., Vaheri A. Fibronectin is expressed by astrocytes cultured from embryonic and early postnatal rat brain. Exp Cell Res. 1986 Mar;163(1):175–185. doi: 10.1016/0014-4827(86)90570-7. [DOI] [PubMed] [Google Scholar]
  22. Martini R., Schachner M. Immunoelectron microscopic localization of neural cell adhesion molecules (L1, N-CAM, and MAG) and their shared carbohydrate epitope and myelin basic protein in developing sciatic nerve. J Cell Biol. 1986 Dec;103(6 Pt 1):2439–2448. doi: 10.1083/jcb.103.6.2439. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. McCarthy K. D., de Vellis J. Preparation of separate astroglial and oligodendroglial cell cultures from rat cerebral tissue. J Cell Biol. 1980 Jun;85(3):890–902. doi: 10.1083/jcb.85.3.890. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. McGarvey M. L., Baron-Van Evercooren A., Kleinman H. K., Dubois-Dalcq M. Synthesis and effects of basement membrane components in cultured rat Schwann cells. Dev Biol. 1984 Sep;105(1):18–28. doi: 10.1016/0012-1606(84)90257-4. [DOI] [PubMed] [Google Scholar]
  25. Merril C. R., Goldman D., Sedman S. A., Ebert M. H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science. 1981 Mar 27;211(4489):1437–1438. doi: 10.1126/science.6162199. [DOI] [PubMed] [Google Scholar]
  26. Naidet C., Sémériva M., Yamada K. M., Thiery J. P. Peptides containing the cell-attachment recognition signal Arg-Gly-Asp prevent gastrulation in Drosophila embryos. Nature. 1987 Jan 22;325(6102):348–350. doi: 10.1038/325348a0. [DOI] [PubMed] [Google Scholar]
  27. Noble M., Albrechtsen M., Møller C., Lyles J., Bock E., Goridis C., Watanabe M., Rutishauser U. Glial cells express N-CAM/D2-CAM-like polypeptides in vitro. Nature. 1985 Aug 22;316(6030):725–728. doi: 10.1038/316725a0. [DOI] [PubMed] [Google Scholar]
  28. Parise L. V., Phillips D. R. Fibronectin-binding properties of the purified platelet glycoprotein IIb-IIIa complex. J Biol Chem. 1986 Oct 25;261(30):14011–14017. [PubMed] [Google Scholar]
  29. Pierschbacher M. D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature. 1984 May 3;309(5963):30–33. doi: 10.1038/309030a0. [DOI] [PubMed] [Google Scholar]
  30. Pierschbacher M., Hayman E. G., Ruoslahti E. Synthetic peptide with cell attachment activity of fibronectin. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1224–1227. doi: 10.1073/pnas.80.5.1224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Poltorak M., Sadoul R., Keilhauer G., Landa C., Fahrig T., Schachner M. Myelin-associated glycoprotein, a member of the L2/HNK-1 family of neural cell adhesion molecules, is involved in neuron-oligodendrocyte and oligodendrocyte-oligodendrocyte interaction. J Cell Biol. 1987 Oct;105(4):1893–1899. doi: 10.1083/jcb.105.4.1893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Price J., Hynes R. O. Astrocytes in culture synthesize and secrete a variant form of fibronectin. J Neurosci. 1985 Aug;5(8):2205–2211. doi: 10.1523/JNEUROSCI.05-08-02205.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Pytela R., Pierschbacher M. D., Ginsberg M. H., Plow E. F., Ruoslahti E. Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors. Science. 1986 Mar 28;231(4745):1559–1562. doi: 10.1126/science.2420006. [DOI] [PubMed] [Google Scholar]
  34. Pytela R., Pierschbacher M. D., Ruoslahti E. A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc Natl Acad Sci U S A. 1985 Sep;82(17):5766–5770. doi: 10.1073/pnas.82.17.5766. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Pytela R., Pierschbacher M. D., Ruoslahti E. Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell. 1985 Jan;40(1):191–198. doi: 10.1016/0092-8674(85)90322-8. [DOI] [PubMed] [Google Scholar]
  36. Rome L. H., Bullock P. N., Chiappelli F., Cardwell M., Adinolfi A. M., Swanson D. Synthesis of a myelin-like membrane by oligodendrocytes in culture. J Neurosci Res. 1986;15(1):49–65. doi: 10.1002/jnr.490150106. [DOI] [PubMed] [Google Scholar]
  37. Ruoslahti E., Hayman E. G., Pierschbacher M. D. Extracellular matrices and cell adhesion. Arteriosclerosis. 1985 Nov-Dec;5(6):581–594. doi: 10.1161/01.atv.5.6.581. [DOI] [PubMed] [Google Scholar]
  38. Ruoslahti E., Pierschbacher M. D. Arg-Gly-Asp: a versatile cell recognition signal. Cell. 1986 Feb 28;44(4):517–518. doi: 10.1016/0092-8674(86)90259-x. [DOI] [PubMed] [Google Scholar]
  39. Sanes J. R. Roles of extracellular matrix in neural development. Annu Rev Physiol. 1983;45:581–600. doi: 10.1146/annurev.ph.45.030183.003053. [DOI] [PubMed] [Google Scholar]
  40. Schuppan D., Glanville R. W., Timpl R. Covalent structure of mouse type-IV collagen. Isolation, order and partial amino-acid sequence of cyanogen-bromide and tryptic peptides of pepsin fragment P1 from the alpha 1(IV) chain. Eur J Biochem. 1982 Apr;123(3):505–512. [PubMed] [Google Scholar]
  41. Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. doi: 10.1016/0003-2697(85)90442-7. [DOI] [PubMed] [Google Scholar]
  42. Suzuki S., Oldberg A., Hayman E. G., Pierschbacher M. D., Ruoslahti E. Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J. 1985 Oct;4(10):2519–2524. doi: 10.1002/j.1460-2075.1985.tb03965.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Szuchet S., Yim S. H., Monsma S. Lipid metabolism of isolated oligodendrocytes maintained in long-term culture mimics events associated with myelinogenesis. Proc Natl Acad Sci U S A. 1983 Nov;80(22):7019–7023. doi: 10.1073/pnas.80.22.7019. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. Vartanian T., Szuchet S., Dawson G., Campagnoni A. T. Oligodendrocyte adhesion activates protein kinase C-mediated phosphorylation of myelin basic protein. Science. 1986 Dec 12;234(4782):1395–1398. doi: 10.1126/science.2431483. [DOI] [PubMed] [Google Scholar]
  46. Yamada K. M. Cell surface interactions with extracellular materials. Annu Rev Biochem. 1983;52:761–799. doi: 10.1146/annurev.bi.52.070183.003553. [DOI] [PubMed] [Google Scholar]
  47. Yamada K. M., Kennedy D. W. Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function. J Cell Biol. 1984 Jul;99(1 Pt 1):29–36. doi: 10.1083/jcb.99.1.29. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Yamada K. M., Kennedy D. W. Peptide inhibitors of fibronectin, laminin, and other adhesion molecules: unique and shared features. J Cell Physiol. 1987 Jan;130(1):21–28. doi: 10.1002/jcp.1041300105. [DOI] [PubMed] [Google Scholar]
  49. Yim S. H., Szuchet S., Polak P. E. Cultured oligodendrocytes. A role for cell-substratum interaction in phenotypic expression. J Biol Chem. 1986 Sep 5;261(25):11808–11815. [PubMed] [Google Scholar]

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