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. 1987 Apr;79(4):1054–1061. doi: 10.1172/JCI112918

Isolation of the thrombospondin membrane receptor.

A S Asch, J Barnwell, R L Silverstein, R L Nachman
PMCID: PMC424283  PMID: 2435757

Abstract

Thrombospondin (TSP), a 450-kD multifunctional glycoprotein with a broad tissue distribution, is secreted upon platelet stimulation, binds to the activated platelet surface, and supports platelet aggregation. We have identified and isolated an 88-kd membrane glycoprotein present in platelets, endothelial cells, monocytes, and a variety of human tumor cell lines that is the membrane binding site for TSP. Endogenous platelet TSP binding to thrombin- and ionophore-stimulated human platelets was inhibited in the presence of the monoclonal antibody OKM5. TSP binding to C32 melanoma cells and HT1080 fibrosarcoma cells was specific and also inhibitable with OKM5 Mab. Cell labeling followed by specific immunoprecipitation demonstrated biosynthesis of a single 88-kD glycoprotein. Binding of TSP to the isolated membrane protein was specific and saturable. These studies identify an 88-kD membrane glycoprotein that reacts with the monoclonal antibody, OKM5, and may function as the cellular TSP receptor.

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Selected References

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

  1. Aiken M. L., Ginsberg M. H., Plow E. F. Identification of a new class of inducible receptors on platelets. Thrombospondin interacts with platelets via a GPIIb-IIIa-independent mechanism. J Clin Invest. 1986 Dec;78(6):1713–1716. doi: 10.1172/JCI112767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ali I. U., Hynes R. O. Effects of LETS glycoprotein on cell motility. Cell. 1978 Jun;14(2):439–446. doi: 10.1016/0092-8674(78)90129-0. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Baenziger N. L., Brodie G. N., Majerus P. W. A thrombin-sensitive protein of human platelet membranes. Proc Natl Acad Sci U S A. 1971 Jan;68(1):240–243. doi: 10.1073/pnas.68.1.240. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Barnwell J. W., Ockenhouse C. F., Knowles D. M., 2nd Monoclonal antibody OKM5 inhibits the in vitro binding of Plasmodium falciparum-infected erythrocytes to monocytes, endothelial, and C32 melanoma cells. J Immunol. 1985 Nov;135(5):3494–3497. [PubMed] [Google Scholar]
  6. Basara M. L., McCarthy J. B., Barnes D. W., Furcht L. T. Stimulation of haptotaxis and migration of tumor cells by serum spreading factor. Cancer Res. 1985 Jun;45(6):2487–2494. [PubMed] [Google Scholar]
  7. Bennett J. S., Hoxie J. A., Leitman S. F., Vilaire G., Cines D. B. Inhibition of fibrinogen binding to stimulated human platelets by a monoclonal antibody. Proc Natl Acad Sci U S A. 1983 May;80(9):2417–2421. doi: 10.1073/pnas.80.9.2417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bennett J. S., Vilaire G. Exposure of platelet fibrinogen receptors by ADP and epinephrine. J Clin Invest. 1979 Nov;64(5):1393–1401. doi: 10.1172/JCI109597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bienz D., Schnippering W., Clemetson K. J. Glycoprotein V is not the thrombin activation receptor on human blood platelets. Blood. 1986 Sep;68(3):720–725. [PubMed] [Google Scholar]
  10. 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]
  11. Coligan J. E., Slayter H. S. Structure of thrombospondin. J Biol Chem. 1984 Mar 25;259(6):3944–3948. [PubMed] [Google Scholar]
  12. Coller B. S., Peerschke E. I., Scudder L. E., Sullivan C. A. A murine monoclonal antibody that completely blocks the binding of fibrinogen to platelets produces a thrombasthenic-like state in normal platelets and binds to glycoproteins IIb and/or IIIa. J Clin Invest. 1983 Jul;72(1):325–338. doi: 10.1172/JCI110973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Dixit V. M., Haverstick D. M., O'Rourke K. M., Hennessy S. W., Grant G. A., Santoro S. A., Frazier W. A. A monoclonal antibody against human thrombospondin inhibits platelet aggregation. Proc Natl Acad Sci U S A. 1985 May;82(10):3472–3476. doi: 10.1073/pnas.82.10.3472. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Doolittle R. F., Watt K. W., Cottrell B. A., Strong D. D., Riley M. The amino acid sequence of the alpha-chain of human fibrinogen. Nature. 1979 Aug 9;280(5722):464–468. doi: 10.1038/280464a0. [DOI] [PubMed] [Google Scholar]
  15. Edelman G. M. Cell adhesion and the molecular processes of morphogenesis. Annu Rev Biochem. 1985;54:135–169. doi: 10.1146/annurev.bi.54.070185.001031. [DOI] [PubMed] [Google Scholar]
  16. Fitzgerald L. A., Charo I. F., Phillips D. R. Human and bovine endothelial cells synthesize membrane proteins similar to human platelet glycoproteins IIb and IIIa. J Biol Chem. 1985 Sep 15;260(20):10893–10896. [PubMed] [Google Scholar]
  17. George J. N., Nurden A. T., Phillips D. R. Molecular defects in interactions of platelets with the vessel wall. N Engl J Med. 1984 Oct 25;311(17):1084–1098. doi: 10.1056/NEJM198410253111705. [DOI] [PubMed] [Google Scholar]
  18. Gerrard J. M., Phillips D. R., Rao G. H., Plow E. F., Walz D. A., Ross R., Harker L. A., White J. G. Biochemical studies of two patients with the gray platelet syndrome. Selective deficiency of platelet alpha granules. J Clin Invest. 1980 Jul;66(1):102–109. doi: 10.1172/JCI109823. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ginsberg M. H., Forsyth J., Lightsey A., Chediak J., Plow E. F. Reduced surface expression and binding of fibronectin by thrombin-stimulated thrombasthenic platelets. J Clin Invest. 1983 Mar;71(3):619–624. doi: 10.1172/JCI110808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ginsberg M., Pierschbacher M. D., Ruoslahti E., Marguerie G., Plow E. Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion. J Biol Chem. 1985 Apr 10;260(7):3931–3936. [PubMed] [Google Scholar]
  21. Hagen I. Effects of thrombin on washed, human platelets: changes in the subcellular fractions. Biochim Biophys Acta. 1975 Jun 12;392(2):242–254. doi: 10.1016/0304-4165(75)90006-9. [DOI] [PubMed] [Google Scholar]
  22. Jaffe E. A., Leung L. L., Nachman R. L., Levin R. I., Mosher D. F. Thrombospondin is the endogenous lectin of human platelets. Nature. 1982 Jan 21;295(5846):246–248. doi: 10.1038/295246a0. [DOI] [PubMed] [Google Scholar]
  23. Jaffe E. A., Ruggiero J. T., Falcone D. J. Monocytes and macrophages synthesize and secrete thrombospondin. Blood. 1985 Jan;65(1):79–84. [PubMed] [Google Scholar]
  24. Jaffe E. A., Ruggiero J. T., Leung L. K., Doyle M. J., McKeown-Longo P. J., Mosher D. F. Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix. Proc Natl Acad Sci U S A. 1983 Feb;80(4):998–1002. doi: 10.1073/pnas.80.4.998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Karpatkin S., Pearlstein E. Role of platelets in tumor cell metastases. Ann Intern Med. 1981 Nov;95(5):636–641. doi: 10.7326/0003-4819-95-5-636. [DOI] [PubMed] [Google Scholar]
  26. Kinoshita T., Medof M. E., Silber R., Nussenzweig V. Distribution of decay-accelerating factor in the peripheral blood of normal individuals and patients with paroxysmal nocturnal hemoglobinuria. J Exp Med. 1985 Jul 1;162(1):75–92. doi: 10.1084/jem.162.1.75. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Knowles D. M., 2nd, Tolidjian B., Marboe C., D'Agati V., Grimes M., Chess L. Monoclonal anti-human monocyte antibodies OKM1 and OKM5 possess distinctive tissue distributions including differential reactivity with vascular endothelium. J Immunol. 1984 May;132(5):2170–2173. [PubMed] [Google Scholar]
  28. Lacovara J., Cramer E. B., Quigley J. P. Fibronectin enhancement of directed migration of B16 melanoma cells. Cancer Res. 1984 Apr;44(4):1657–1663. [PubMed] [Google Scholar]
  29. 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]
  30. Lahav J., Schwartz M. A., Hynes R. O. Analysis of platelet adhesion with a radioactive chemical crosslinking reagent: interaction of thrombospondin with fibronectin and collagen. Cell. 1982 Nov;31(1):253–262. doi: 10.1016/0092-8674(82)90425-1. [DOI] [PubMed] [Google Scholar]
  31. Lawler J. W., Slayter H. S., Coligan J. E. Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. J Biol Chem. 1978 Dec 10;253(23):8609–8616. [PubMed] [Google Scholar]
  32. Lawler J., Derick L. H., Connolly J. E., Chen J. H., Chao F. C. The structure of human platelet thrombospondin. J Biol Chem. 1985 Mar 25;260(6):3762–3772. [PubMed] [Google Scholar]
  33. 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]
  34. Lesot H., Kühl U., Mark K. Isolation of a laminin-binding protein from muscle cell membranes. EMBO J. 1983;2(6):861–865. doi: 10.1002/j.1460-2075.1983.tb01514.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Leung L. L., Nachman R. L. Complex formation of platelet thrombospondin with fibrinogen. J Clin Invest. 1982 Sep;70(3):542–549. doi: 10.1172/JCI110646. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Leung L. L., Nachman R. L., Harpel P. C. Complex formation of platelet thrombospondin with histidine-rich glycoprotein. J Clin Invest. 1984 Jan;73(1):5–12. doi: 10.1172/JCI111206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Leung L. L. Role of thrombospondin in platelet aggregation. J Clin Invest. 1984 Nov;74(5):1764–1772. doi: 10.1172/JCI111595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Liotta L. A., Horan Hand P., Rao C. N., Bryant G., Barsky S. H., Schlom J. Monoclonal antibodies to the human laminin receptor recognize structurally distinct sites. Exp Cell Res. 1985 Jan;156(1):117–126. doi: 10.1016/0014-4827(85)90266-6. [DOI] [PubMed] [Google Scholar]
  39. Majack R. A., Cook S. C., Bornstein P. Platelet-derived growth factor and heparin-like glycosaminoglycans regulate thrombospondin synthesis and deposition in the matrix by smooth muscle cells. J Cell Biol. 1985 Sep;101(3):1059–1070. doi: 10.1083/jcb.101.3.1059. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Malinoff H. L., McCoy J. P., Jr, Varani J., Wicha M. S. Metastatic potential of murine fibrosarcoma cells is influenced by cell surface laminin. Int J Cancer. 1984 May 15;33(5):651–655. doi: 10.1002/ijc.2910330516. [DOI] [PubMed] [Google Scholar]
  41. Malinoff H. L., Wicha M. S. Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J Cell Biol. 1983 May;96(5):1475–1479. doi: 10.1083/jcb.96.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Margossian S. S., Lawler J. W., Slayter H. S. Physical characterization of platelet thrombospondin. J Biol Chem. 1981 Jul 25;256(14):7495–7500. [PubMed] [Google Scholar]
  43. Marguerie G. A., Plow E. F., Edgington T. S. Human platelets possess an inducible and saturable receptor specific for fibrinogen. J Biol Chem. 1979 Jun 25;254(12):5357–5363. [PubMed] [Google Scholar]
  44. McCarthy J. B., Furcht L. T. Laminin and fibronectin promote the haptotactic migration of B16 mouse melanoma cells in vitro. J Cell Biol. 1984 Apr;98(4):1474–1480. doi: 10.1083/jcb.98.4.1474. [DOI] [PMC free article] [PubMed] [Google Scholar]
  45. McCarthy J. B., Hagen S. T., Furcht L. T. Human fibronectin contains distinct adhesion- and motility-promoting domains for metastatic melanoma cells. J Cell Biol. 1986 Jan;102(1):179–188. doi: 10.1083/jcb.102.1.179. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. McCarthy J. B., Palm S. L., Furcht L. T. Migration by haptotaxis of a Schwann cell tumor line to the basement membrane glycoprotein laminin. J Cell Biol. 1983 Sep;97(3):772–777. doi: 10.1083/jcb.97.3.772. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. McPherson G. A. A practical computer-based approach to the analysis of radioligand binding experiments. Comput Programs Biomed. 1983 Aug-Oct;17(1-2):107–113. doi: 10.1016/0010-468x(83)90031-4. [DOI] [PubMed] [Google Scholar]
  48. McPherson J., Sage H., Bornstein P. Isolation and characterization of a glycoprotein secreted by aortic endothelial cells in culture. Apparent identity with platelet thrombospondin. J Biol Chem. 1981 Nov 10;256(21):11330–11336. [PubMed] [Google Scholar]
  49. Mollenhauer J., Bee J. A., Lizarbe M. A., von der Mark K. Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen. J Cell Biol. 1984 Apr;98(4):1572–1579. doi: 10.1083/jcb.98.4.1572. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Mosher D. F., Doyle M. J., Jaffe E. A. Synthesis and secretion of thrombospondin by cultured human endothelial cells. J Cell Biol. 1982 May;93(2):343–348. doi: 10.1083/jcb.93.2.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Mumby S. M., Raugi G. J., Bornstein P. Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen. J Cell Biol. 1984 Feb;98(2):646–652. doi: 10.1083/jcb.98.2.646. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Munson P. J., Rodbard D. Ligand: a versatile computerized approach for characterization of ligand-binding systems. Anal Biochem. 1980 Sep 1;107(1):220–239. doi: 10.1016/0003-2697(80)90515-1. [DOI] [PubMed] [Google Scholar]
  53. Nachman R. L., Leung L. L. Complex formation of platelet membrane glycoproteins IIb and IIIa with fibrinogen. J Clin Invest. 1982 Feb;69(2):263–269. doi: 10.1172/JCI110448. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Nurden A. T., Kunicki T. J., Dupuis D., Soria C., Caen J. P. Specific protein and glycoprotein deficiencies in platelets isolated from two patients with the gray platelet syndrome. Blood. 1982 Apr;59(4):709–718. [PubMed] [Google Scholar]
  55. Phillips D. R., Jennings L. K., Prasanna H. R. Ca2+-mediated association of glycoprotein G (thrombinsensitive protein, thrombospondin) with human platelets. J Biol Chem. 1980 Dec 25;255(24):11629–11632. [PubMed] [Google Scholar]
  56. 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]
  57. Pierschbacher M. D., Ruoslahti E., Sundelin J., Lind P., Peterson P. A. The cell attachment domain of fibronectin. Determination of the primary structure. J Biol Chem. 1982 Aug 25;257(16):9593–9597. [PubMed] [Google Scholar]
  58. Pierschbacher M. D., Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc Natl Acad Sci U S A. 1984 Oct;81(19):5985–5988. doi: 10.1073/pnas.81.19.5985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. 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]
  60. Plow E. F., McEver R. P., Coller B. S., Woods V. L., Jr, Marguerie G. A., Ginsberg M. H. Related binding mechanisms for fibrinogen, fibronectin, von Willebrand factor, and thrombospondin on thrombin-stimulated human platelets. Blood. 1985 Sep;66(3):724–727. [PubMed] [Google Scholar]
  61. Poste G., Doll J., Hart I. R., Fidler I. J. In vitro selection of murine B16 melanoma variants with enhanced tissue-invasive properties. Cancer Res. 1980 May;40(5):1636–1644. [PubMed] [Google Scholar]
  62. 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]
  63. 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]
  64. 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]
  65. Raugi G. J., Mumby S. M., Abbott-Brown D., Bornstein P. Thrombospondin: synthesis and secretion by cells in culture. J Cell Biol. 1982 Oct;95(1):351–354. doi: 10.1083/jcb.95.1.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Roberts D. D., Sherwood J. A., Spitalnik S. L., Panton L. J., Howard R. J., Dixit V. M., Frazier W. A., Miller L. H., Ginsburg V. Thrombospondin binds falciparum malaria parasitized erythrocytes and may mediate cytoadherence. Nature. 1985 Nov 7;318(6041):64–66. doi: 10.1038/318064a0. [DOI] [PubMed] [Google Scholar]
  67. Ruggeri Z. M., De Marco L., Gatti L., Bader R., Montgomery R. R. Platelets have more than one binding site for von Willebrand factor. J Clin Invest. 1983 Jul;72(1):1–12. doi: 10.1172/JCI110946. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Ruoslahti E. Fibronectin in cell adhesion and invasion. Cancer Metastasis Rev. 1984;3(1):43–51. doi: 10.1007/BF00047692. [DOI] [PubMed] [Google Scholar]
  69. 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]
  70. Sage H., Farin F. M., Striker G. E., Fisher A. B. Granular pneumocytes in primary culture secrete several major components of the extracellular matrix. Biochemistry. 1983 Apr 26;22(9):2148–2155. doi: 10.1021/bi00278a015. [DOI] [PubMed] [Google Scholar]
  71. Schmidt J. A., Udeinya I. J., Leech J. H., Hay R. J., Aikawa M., Barnwell J., Green I., Miller L. H. Plasmodium falciparum malaria. An amelanotic melanoma cell line bears receptors for the knob ligand on infected erythrocytes. J Clin Invest. 1982 Aug;70(2):379–386. doi: 10.1172/JCI110627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Silverstein R. L., Leung L. L., Harpel P. C., Nachman R. L. Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator. J Clin Invest. 1984 Nov;74(5):1625–1633. doi: 10.1172/JCI111578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Situ R., Lee E. C., McCoy J. P., Jr, Varani J. Stimulation of murine tumour cell motility by laminin. J Cell Sci. 1984 Aug;70:167–176. doi: 10.1242/jcs.70.1.167. [DOI] [PubMed] [Google Scholar]
  74. Talle M. A., Rao P. E., Westberg E., Allegar N., Makowski M., Mittler R. S., Goldstein G. Patterns of antigenic expression on human monocytes as defined by monoclonal antibodies. Cell Immunol. 1983 May;78(1):83–99. doi: 10.1016/0008-8749(83)90262-9. [DOI] [PubMed] [Google Scholar]
  75. Terranova V. P., Williams J. E., Liotta L. A., Martin G. R. Modulation of the metastatic activity of melanoma cells by laminin and fibronectin. Science. 1984 Nov 23;226(4677):982–985. doi: 10.1126/science.6505678. [DOI] [PubMed] [Google Scholar]
  76. Wight T. N., Raugi G. J., Mumby S. M., Bornstein P. Light microscopic immunolocation of thrombospondin in human tissues. J Histochem Cytochem. 1985 Apr;33(4):295–302. doi: 10.1177/33.4.3884704. [DOI] [PubMed] [Google Scholar]
  77. Wolff R., Plow E. F., Ginsberg M. H. Interaction of thrombospondin with resting and stimulated human platelets. J Biol Chem. 1986 May 25;261(15):6840–6846. [PubMed] [Google Scholar]
  78. 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]

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