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Recognition Sites of RGD-Dependent Integrins

  • Chapter
Integrin-Ligand Interaction

Abstract

The tripeptide motif Arg-Gly-Asp (RGD) was identified more than 12 years ago as a minimal essential peptide sequence inhibiting cell adhesion to fibronectin.1–3 Subsequently, short RGD-peptides were found to inhibit the binding of other major cell-adhesive proteins like vitronectin, fibrinogen or van Willebrand factor, indicating the central biological importance of this simple peptide motif as the basic unit of a widespread cellular recognition system.4–7 In the last 10 years, with the rapid accumulation of available protein sequence information and the discovery of various families of adhesion receptors, these initial findings have been corroborated.8,9 However, apart from RGD, other important cell adhesion motifs have been identified and we know today that cell adhesion to an extracellular matrix protein can involve a series of different receptor-ligand interactions. Therefore RGD-recognition is not the unique mechanism for interactions of proteins with cells, but it is unique with respect to its broad distribution in biological organisms and its usage by a large number of different cell-adhesive proteins and cell-adhesion receptors.

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References

  1. Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984; 309: 30–3.

    CAS  PubMed  Google Scholar 

  2. Pierschbacher MD, Ruoslahti E. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity. Proc Natl Acad Sci USA 1984; 81: 5985–8.

    CAS  PubMed  Google Scholar 

  3. Yamada KM, Kennedy DW. Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function. J Cell Biol 1984; 99: 29–36.

    CAS  PubMed  Google Scholar 

  4. Suzuki S, Oldberg A, Hayman EG et al. Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J 1985; 4: 2519–24.

    Google Scholar 

  5. Gartner TK, Bennett JS. The tetrapeptide analogue of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets. J Biol Chem 1985; 260: 11891–4.

    CAS  PubMed  Google Scholar 

  6. Plow EF, Pierschbacher MD, Ruoslahti E et al. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc Natl Acad Sci USA 1985; 82: 8057–61.

    CAS  PubMed  Google Scholar 

  7. Ruoslahti E, Pierschbacher MD. Arg-GlyAsp: a versatile cell recognition signal. Cell 1986; 44: 517–8.

    CAS  PubMed  Google Scholar 

  8. Springer TA. Adhesion receptors of the immune system. Nature 1990; 346: 425–34.

    CAS  PubMed  Google Scholar 

  9. Albelda SM, Buck CA. Integrins and other cell adhesion molecules. FASEB J 1990; 4: 2868–80.

    Google Scholar 

  10. Hautanen A, Gailit J, Mann DM et al. Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor. J Biol Chem 1989; 264: 1437–42.

    CAS  PubMed  Google Scholar 

  11. Bowditch RD, Halloran CE, Aota S et al. Integrin allb33 (platelet GPIIb-IIIa) recognizes multiple sites in fibronectin. J Biol Chem 1991; 266: 23323–8.

    CAS  PubMed  Google Scholar 

  12. Bowditch RD, Hariharan M, Tominna EF et al. Identification of a novel binding site in fibronectin. Differential utilisation by [33 integrins. J Biol Chem 1994; 269: 10856–63.

    CAS  PubMed  Google Scholar 

  13. Aota S, Nagai T, Yamada KM. Characterization of regions of fibronectin besides the arginine-glycine-aspartic acid sequence required for adhesive function of the cell-binding domain using site-directed mutagenesis. J Biol Chem 1991; 266: 15938–43.

    CAS  PubMed  Google Scholar 

  14. Aota S, Nomizu M, Yamada KM. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem 1994; 269: 24756–61.

    CAS  PubMed  Google Scholar 

  15. Nagai T, Yamakawa N, Aota S et al. Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly. J Cell Biol 1991; 114: 1295–305.

    CAS  PubMed  Google Scholar 

  16. Pytela R, Pierschbacher MD, 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 USA 1985; 82: 5766–70.

    CAS  PubMed  Google Scholar 

  17. Pytela R, Pierschbacher MD, Ginsberg MH et al. Platelet membrane glycoprotein IIb/ IIIa: member of a family of Arg-Gly-Asp specific adhesion receptors. Science 1986; 231: 1559–62.

    CAS  PubMed  Google Scholar 

  18. Hu DD, Hoyer JR, Smith JW. Ca’’ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin aß,(33. J Biol Chem 1995; 270: 9917–25.

    CAS  PubMed  Google Scholar 

  19. Pfaff M, Reinhardt DP, Sakai LY et al. Cell adhesion and integrin binding to recombi-nant human fibrillin-1. FEBS L 1996; 384: 247–50.

    Google Scholar 

  20. Pfaff M, Tangemann K, Müller B et al. Selective recognition of cyclic RGD peptides of NMR defined conformation by aIIb93, a433 and a513î integrins. J Biol Chem 1994; 269: 20233–8.

    CAS  PubMed  Google Scholar 

  21. Staatz WD, Walsh JJ, Pexton T et al. The a2f31 integrin cell surface collagen receptor binds to the ul(I)-CB3 peptide of collagen. J Biol Chem 1990; 265: 4778–81.

    CAS  PubMed  Google Scholar 

  22. Kern A, Eble J, Golbik R et al. Interaction of type IV collagen with the isolated integrins a113i and a2(31. Eur J Biochem 1993; 215: 151–9.

    CAS  PubMed  Google Scholar 

  23. Cardarelli PM, Yamagata S, Taguchi I et al. The collagen receptor a2131, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide. J Biol Chem 1992; 267: 23159–64.

    CAS  PubMed  Google Scholar 

  24. Sanchez-Aparicio P, Dominguez-Jimenez C, Garcia-Pardo A. Activation of the integrin through the (31 subunit induces recognition of the RGDS sequence in fibronectin. J Cell Biol 1.991; 126: 271–9.

    Google Scholar 

  25. Mould AP, Komoriya A, Yamada KM et al. The CS5 peptide is a second site in the IIICS region of fibronectin recognized by the integrin a,ß,. Inhibition of aî(31 function by RGD peptide homologues. J Biol Chem 1991; 266: 3579–85.

    CAS  PubMed  Google Scholar 

  26. Yamada KM. Adhesive recognition sequences. J Biol Chem 1991; 266: 12809–12.

    CAS  PubMed  Google Scholar 

  27. Murakawa M, Okamura T, Kamura T et al. Diversity of primary structures of the carboxy-terminal regions of mammalian fibrinogen Au-chains. Characterization of the partial nucleotide and deduced amino acid sequences in five mammalian species; Rhesus monkey, pig, dog, mouse and Syrian hamster. Thrombosis and Haemostasis 1993; 69: 351–60.

    CAS  PubMed  Google Scholar 

  28. Xu X, Doolittle RF. Presence of a vertebrate fibrinogen-like sequence in an echinoderm. Proc Natl Acad Sei USA 1990; 87: 2097–101.

    CAS  Google Scholar 

  29. Ruppert M, Aigner S, Hubbe M et al. The L1 adhesion molecule is a cellular ligand for VLA-5. J Cell Biol 1995; 131: 1881–91.

    CAS  PubMed  Google Scholar 

  30. Montgomery AMP, Becker JC, Siu C-H et al. Human neural cell adhesion molecule L1 and rat homologue NILE are ligands for integrin u,133. J Cell Biol 1996; 132: 474–85.

    Google Scholar 

  31. Krätzschmar J, Lum L, Blobel CP. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J Biol Chem 1996; 271: 4593–6.

    PubMed  Google Scholar 

  32. Vogel BE, Lee SJ, Hildebrand A et al. A novel integrin specificity exemplified by binding of the a„135 integrin to the basic domain of the HIV Tat protein and vitronectin. J Cell Biol 1993; 121: 461–8.

    CAS  PubMed  Google Scholar 

  33. Springer WR, Cooper DN, Barondes SH. Discoidin I is implicated in cell-substratum attachment and ordered cell migration of Dictyostelium discoideum and resembles fibronectin. Cell 1984; 39: 557–64.

    CAS  PubMed  Google Scholar 

  34. Gabius HJ, Springer WR, Barondes SH. Receptor for the cell binding site of discoidin I. Cell 1985; 42: 449–56.

    CAS  PubMed  Google Scholar 

  35. Leahy DJ, Hendrickson WA, Aukhil I et al. Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 1992; 258: 987–91.

    CAS  PubMed  Google Scholar 

  36. Main AL, Harvey TS, Baron M et al. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell 1992; 71: 671–8.

    CAS  PubMed  Google Scholar 

  37. Dickinson CD, Veerapandian B, Dai XP et al. Crystal structure of the tenth type III cell adhesion module of human fibronectin. J Mol Biol 1994; 236: 1079–92.

    CAS  PubMed  Google Scholar 

  38. Krezel AM, Wagner G, Seymour-Ulmer J et al. Structure of the RGD protein decorsin: conserved motif and distinct function in leech proteins that affect blood clotting. Science 1994; 264: 1944–7.

    CAS  PubMed  Google Scholar 

  39. Acharya R, Fry E, Stuart D et al. The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution. Nature 1989; 337: 709–16.

    CAS  PubMed  Google Scholar 

  40. Logan D, Abu-Ghazaleh R, Blakemore W et al. Structure of a major immunogenic site of foot-and-mouth disease virus. Nature 1993; 362: 566–8.

    CAS  PubMed  Google Scholar 

  41. Leahy DJ, Aukhil I, Erickson HP. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996; 84: 15 5–64.

    Google Scholar 

  42. Pierschbacher MD, Ruoslahti E. Influence of stereochemistry of the sequence Arg-GlyAsp-Xaa on binding specificity in cell adhesion. J Biol Chem 1987; 262: 17294–8.

    CAS  PubMed  Google Scholar 

  43. Aumailley M, Gurrath M, Müller G et al. Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS L 1991; 291: 50–4.

    Google Scholar 

  44. Samanen J, Ali F, Romoff T et al. Development of a small RGD peptide fibrinogen receptor antagonist with potent antiaggregatory activity in vitro. J Med Chem 1991; 34: 3114–25.

    CAS  PubMed  Google Scholar 

  45. Koivunen E, Gay DA, Ruoslahti E. Selection of peptides binding to the a5131 integrin from phage display library. J Biol Chem 1993; 268: 20205–10.

    CAS  PubMed  Google Scholar 

  46. Huang T-F, Holt JC, Lukasiewicz H et al. Trigramin: a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-Illa complex. J Biol Chem 1987; 262: 16157–63.

    CAS  PubMed  Google Scholar 

  47. Gan Z-R, Gould RJ, Jacobs JW et al. Echistatin: a potent platelet aggregation inhibitor from the venom of the viper Echis carinatus. J Biol Chem 1988; 263: 19827–32.

    CAS  PubMed  Google Scholar 

  48. Calvete JJ, Schäfer W, Soszka T et al. Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeresus albolabris: significance for the expression of platelet aggregation inhibitory activity. Biochemistry 1991; 30: 5225–9.

    CAS  PubMed  Google Scholar 

  49. O’Neil KT, Hoess RH, Jackson SA et al. Identification of novel peptide antagonists for GPIIb/IIIa from a conformationally constrained phage peptide library. Proteins 1992; 14: 509–15.

    PubMed  Google Scholar 

  50. Lee G, Chan W, Hurle MR et al. Strong inhibition of fibrinogen binding to platelet receptor allb13 by RGD sequences installed into a presentation scaffold. Protein Engineering 1993; 6: 745–54.

    CAS  PubMed  Google Scholar 

  51. Yamada T, Matsushima M, Inaka K et al. Structural and functional analyses of the Arg-Gly-Asp sequence introduced into human lysozyme. J Biol Chem 1993; 268: 10588–92.

    CAS  PubMed  Google Scholar 

  52. Smith JW, Tachias K, Madison EL. Protein loop grafting to construct a variant of tissue-type plasminogen activator that binds platelet integrin allb(33. J Biol Chem 1995; 270: 30486–90.

    CAS  PubMed  Google Scholar 

  53. Yamada KM, Kennedy DW. Amino acid sequence specificities of an adhesive recognition signal. J Cell Biochem 1985; 28: 99–104.

    CAS  PubMed  Google Scholar 

  54. Cheng S, Craig WS, Mullen D et al. Design and synthesis of novel cyclic RGDcontaining peptides as highly potent and selective integrin alIb[33 antagonists. J Med Chem 1994; 37: 1–8.

    CAS  PubMed  Google Scholar 

  55. Craig WS, Cheng S, Mullen D et al. Concept and progress in the development of RGD-containing peptide pharmaceuticals. Biopolymers 1995; 37: 157–75.

    CAS  PubMed  Google Scholar 

  56. Plow EF, Pierschbacher MD, Ruoslahti E et al. Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets. Blood 1987; 70: 110–5.

    CAS  PubMed  Google Scholar 

  57. Kini RM, Evans HJ. A novel approach to the design of potent bioactive peptides by incorporation of proline brackets: anti-platelet effects of Arg-Gly-Asp peptides. FEBS L 1995; 375: 15–7.

    CAS  Google Scholar 

  58. Scarborough RM, Rose JW, Naughton et al. Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms. J Biol Chem 1993; 268: 1058–65.

    CAS  PubMed  Google Scholar 

  59. Pfaff M, McLane MA, Beviglia L et al. Comparison of disintegrins with limited variation in the RGD loop in their binding to purified integrins allb133, (4(33 and a5f31 and in cell adhesion. Cell Adhes Commun 1994; 2: 491–501.

    CAS  PubMed  Google Scholar 

  60. Dennis MS, Carter P, Lazarus RA. Binding interactions of kistrin with platelet glycoprotein lIb-Illa: analysis by site-directed mutagenesis. Proteins 1993; 15: 312–21.

    CAS  PubMed  Google Scholar 

  61. Koivunen E, Wang B, Ruoslahti E. Isolation of a highly specific ligand for the a513, integrin from a phage display library. J Cell Biol 1994; 124: 373–80.

    CAS  PubMed  Google Scholar 

  62. Healy JM, Murayama O, Maeda T et al. Peptide ligands for integrin a,J3; selected from random phage display libraries. Biochemistry 1995; 34: 3948–55.

    CAS  PubMed  Google Scholar 

  63. Barbas CF III, Languino LR, Smith JW. High-affinity self-reactive human antibodies by design and selection: targeting the integrin ligand binding site. Proc Natl Acad Sci USA 1993; 90: 10003–7.

    CAS  PubMed  Google Scholar 

  64. Eggleston DS, Feldman SI1. Structure of the fibrinogen binding sequence: arginylglycylaspartic acid (RGD). hit J Peptide Protein Research 1990; 36: 161–6.

    CAS  Google Scholar 

  65. Verdaguer N, Mateu MG, Andreu D et al. Structure of the major antigenic loop of foot-and-mouth disease virus complexed with a neutralizing antibody. EMBO J 1995; 14: 1690–6.

    CAS  PubMed  Google Scholar 

  66. McDowell RS, Gadek TR. Structural studies of potent constrained RGD peptides. J Am Chem Soc 1992; 111: 9245–53.

    Google Scholar 

  67. Gurrath M, Muller G, Kessler H et al. Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides. Eur J Biochem 1992; 210: 911–21.

    CAS  PubMed  Google Scholar 

  68. Peishoff CE, Ali FE, Bean JW et al. Investigation of conformational specificity at GPIIb/Illa: evaluation of conformationally constrained RGD peptides. J Med Chem 1992; 35: 3962–9.

    CAS  PubMed  Google Scholar 

  69. Ginsberg M, Pierschbacher MD, Ruoslahti E et al. Inhibition of fibronectin binding to platelets by proteolytic fragments and synthetic peptides which support fibroblast adhesion. J Biol Chem 1985; 260: 3931–6.

    CAS  PubMed  Google Scholar 

  70. Farrell DH, Thiagarajan P, Chung DW et al. Role of fibrinogen a and y chain sites in platelet aggregation. Proc Natl Acad Sci USA 1992; 89: 10729–32.

    CAS  PubMed  Google Scholar 

  71. Smith JW, Ruggeri ZM, Kunicki TJ et al. Interaction of integrins a13; and glycoprotein IIb-Ilia with fibrinogen. Differential peptide recognition accounts for distinct binding sites. J Biol Chem 1990; 265: 12267–71.

    CAS  PubMed  Google Scholar 

  72. Scarborough RM, Rose JW, Hsu MA et al. Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus ni. barbouri. J Biol Chem 1991; 266: 9359–62.

    CAS  PubMed  Google Scholar 

  73. Alon R, Bayer EA, Wilchek M. Cell-adhesive properties of streptavidin are mediated by the exposure of an RGD-like RYD site. Eur J Cell Biol 1992; 58: 271–9.

    CAS  PubMed  Google Scholar 

  74. Kodandapani R, Veerapandian B, Kunicki TJ et al. Crystal structure of the OPG2 Fab. An antireceptor antibody that mimics an RGD cell adhesion site. J Biol Chem 1995; 270: 2268–73.

    CAS  PubMed  Google Scholar 

  75. Taub R, Gould RJ, Garsky VM et al. A monoclonal antibody against the platelet fibrinogen receptor contains a sequence that mimics a receptor recognition domain in fibrinogen. J Biol Chem 1989; 264: 259–65.

    CAS  PubMed  Google Scholar 

  76. Soteriadou KP, Remoundos MS, Katsikas MC et al. The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region in fibronectin. J Biol Chem 1992; 267: 13980–5.

    CAS  PubMed  Google Scholar 

  77. Lazarus RA, McDowell RS. Structural and functional aspects of RGD-containing protein antagonists of glycoprotein IIb-Illa. Curr Opin Biotechnol 1993; 4: 438–45.

    CAS  PubMed  Google Scholar 

  78. Ugarova T, Agbanyo FR, Plow EF. Conformational changes in adhesive proteins modulate their adhesive function. Thrombosis and Haemostasis 1995; 74: 253–7.

    CAS  PubMed  Google Scholar 

  79. Ugarova TP, Zamarron C, Veklich Y et al. Conformational transitions in the cell binding domain of fibronectin. Biochemistry 1995; 34: 4457–66.

    CAS  PubMed  Google Scholar 

  80. Fukai F, Ohtaki M, Fujii N et al. Release of biological activities from quiescent fibronectin by a conformational change and limited proteolysis by matrix metalloproteinases. Biochemistry 1995; 34: 11453–9.

    CAS  PubMed  Google Scholar 

  81. Ugarova TP, Budzynski AZ, Shattil SJ et al. Conformational changes in fibrinogen elicited by its interaction with platelet membrane glycoprotein GPIIb-IIIa. J Biol Chem 1993; 268: 21080–7.

    CAS  PubMed  Google Scholar 

  82. Joshi P, Chung CY, Aukhil I et al. Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. J Cell Science 1993; 106: 389–400.

    CAS  PubMed  Google Scholar 

  83. Aumailley M, Gerl M, Sonnenberg A et al. Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site being exposed in fragment P1. FEBS Letters 1990; 262: 82–6.

    CAS  PubMed  Google Scholar 

  84. Grant DS, Tashiro K, Segui-Real B et al. Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro. Cell 1989; 58: 933–43.

    CAS  PubMed  Google Scholar 

  85. Goodman SL, Aumailley M, von der Mark H. Multiple cell surface receptors for the short arms of laminin: a,[31 integrin and RGD-dependent proteins mediate cell attachment only to domains III in murine tumor laminin. J Cell Biol 1991; 113: 931–41.

    CAS  PubMed  Google Scholar 

  86. Pfaff M, Göhring W, Brown JC et al. Binding of purified collagen receptors (a,(3,, (2131) and RGD-dependent integrins to laminins and laminin fragments. Eur J Biochem 1994; 225: 975–84.

    CAS  PubMed  Google Scholar 

  87. Pfaff M, Aumailley M, Specks U et al. Integrin and Arg-Gly-Asp dependence of cell adhesion to the native and unfolded triple helix of collagen type VI. Exp Cell Res 1993; 206: 167–76.

    CAS  PubMed  Google Scholar 

  88. Sun X, Skorstengaard K, Mosher DF. Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin. J Cell Biol 1992; 118: 693–701.

    CAS  PubMed  Google Scholar 

  89. Rydel TJ, Tulinsky A, Bode W et al. Refined structure of the hirudin-thrombin complex. J Mol Biol 1991; 221 (2): 583–601.

    CAS  PubMed  Google Scholar 

  90. Bar-Shavit R, Eskohjido Y, Fenton JW 2d et al. Thrombin adhesive properties: induction by plasmin and heparan sulfate. J Cell Biol 1993; 123: 1279–87.

    CAS  PubMed  Google Scholar 

  91. Lawler J, Weinstein R, Hynes RO. Cell attachment to thrombospondin: the role of ARG-GLY-ASP, calcium, and integrin receptors. J Cell Biol 1988; 107: 2351–61.

    CAS  PubMed  Google Scholar 

  92. Kouns WC, Kirchhofer D, Hadvary P et al. Reversible conformational changes induced in glycoprotein IIb-IIla by a potent and selective peptidomimetic inhibitor. Blood 1992; 80: 2539–47.

    CAS  PubMed  Google Scholar 

  93. Elices MJ, Urry LA, Hemler ME. Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J Cell Biol 1991; 112: 169–81.

    CAS  PubMed  Google Scholar 

  94. Jones JI, Gockerman A, Busby WH Jr et al. Insulin-like growth factor binding protein 1 stimulates cell migration and binds to the a5131 integrin by means of its ArgGly-Asp sequence. Proc Natl Acad Sci USA 1993; 90: 10553–7.

    CAS  PubMed  Google Scholar 

  95. Müller U, Bossy B, Venstrom K et al. Integrin a8ß, promotes attachment, cell spreading, and neurite outgrowth on fibronectin. Mol Biol Cell 1995; 6: 433–48.

    PubMed  Google Scholar 

  96. Schnapp LM, Hatch N, Ramos DM et al. The human integrin a8ß, functions as a receptor for tenascin, fibronectin, and vitronectin. J Biol Chem 1995; 270: 23196–202.

    CAS  PubMed  Google Scholar 

  97. Marshall JF, Rutherford DC, McCartney ACE et al. a„133 is a receptor for vitronectin and fibrinogen, and acts with 0131 to mediate spreading on fibronectin. J Cell Science 1995; 108: 1227–38.

    CAS  PubMed  Google Scholar 

  98. Hu DD, Lin ECK, Kovach NL et al. A biochemical characterization of the binding of osteopontin to integrins a„ß, and a4135• J Biol Chem 1995; 270: 26232–8.

    CAS  Google Scholar 

  99. Haverstick DM, Cowan JF, Yamada KM et al. Inhibition of platelet adhesion to fibronectin, fibrinogen, and von Willebrand factor substrates by a synthetic tetrapeptide derived from the cell-binding domain of fibronectin. Blood 1985; 66: 946–52.

    CAS  PubMed  Google Scholar 

  100. Berliner S, Niiya K, Roberts JR et al. Generation and characterization of peptide-specific antibodies that inhibit von Willebrand factor binding to glycoprotein IIb-IIIa without interacting with other adhesive molecules. Selectivity is conferred by Pro1743 and other amino acid residues adjacent to the sequence Arg1744-Gly1745-Asp1746. J Biol Chem 1988; 263: 7500–5.

    CAS  PubMed  Google Scholar 

  101. Lawler J, Hynes RO. An integrin receptor on normal and thrombasthenic platelets that binds thrombospondin. Blood 1989; 74: 2022–7.

    CAS  PubMed  Google Scholar 

  102. Pfaff M, Sasaki T, Tangemann K et al. Integrin-binding and cell-adhesion studies of fibulins reveal a particular affinity for aIIb(33. Exp Cell Res 1995; 219: 87–92.

    CAS  PubMed  Google Scholar 

  103. Cheresh DA. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc Natl Acad Sci USA 1987; 84: 6471–5.

    CAS  PubMed  Google Scholar 

  104. Cheresh DA, Spiro RC. Biosynthetic and functional properties of an Arg-Gly-Aspdirected receptor involved in human melanoma cell attachment to vitronectin, fibrinogen, and von Willebrand factor. J Biol Chem 1987; 262: 17703–11.

    CAS  PubMed  Google Scholar 

  105. Bar-Shavit R, Sabbah V, Lampugnani MG et al. An Arg-Gly-Asp sequence within thrombin promotes endothelial cell adhesion. J Cell Biol 1991; 112: 335–44.

    CAS  PubMed  Google Scholar 

  106. Charo IF, Nannizzi L, Smith JW et al. The vitronectin receptor a4ß3 binds fibronectin and acts in concert with a5133 in promoting cellular attachment and spreading on fibronectin. J Cell Biol 1990; 111: 2795–800.

    CAS  PubMed  Google Scholar 

  107. Oldberg A, Franzen A, Heinegard D et al. Identification of a bone sialoprotein receptor in osteosarcoma cells. J Biol Chem 1988; 263: 19433–6.

    CAS  PubMed  Google Scholar 

  108. Prieto AL, Edelman GM, Crossin KL. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc Natl Acad Sci USA 1993; 90: 10154–8.

    CAS  PubMed  Google Scholar 

  109. Sakamoto H, Broekelmann T, Cheresh DA et al. Cell-type specific recognition of RGDand non-RGD-containing cell binding domains in fibrillin-1. J Biol Chem 1996; 271: 4916–22.

    CAS  PubMed  Google Scholar 

  110. Hayashi K, Madri JA, Yurchenco PD. Endothelial cells interact with the core protein of basement membrane perlecan through 131 and 133 integrins: an adhesion modulated by glycosaminoglycan. J Cell Biol 1992; 119: 945–59.

    CAS  PubMed  Google Scholar 

  111. Horton MA, Spragg JH, Bodary SC et al. Recognition of cryptic sites in human and mouse laminins by rat osteoclasts is mediated by 133 and 131 integrins. Bone 1994; 15: 639–46.

    CAS  PubMed  Google Scholar 

  112. Busk M, Pytela R, Sheppard D. Characterization of the integrin av(36 as a fibronectinbinding protein. J Biol Chem 1992; 267: 5790–6.

    CAS  PubMed  Google Scholar 

  113. Nishimura SL, Sheppard D, Pytela R. Integrin av138. Interaction with vitronectin and functional divergence of the 138 cytoplasmic domain. J Biol Chem 1994; 269: 28708–15.

    CAS  PubMed  Google Scholar 

  114. Gresham HD, Goodwin JL, Allen PM et al. A novel member of the integrin receptor family mediates Arg-Gly-Asp-stimulated neutrophil phagocytosis. J Cell Biol 1989; 108: 1935–43.

    CAS  PubMed  Google Scholar 

  115. Senior RM, Gresham HD, Griffin GL et al. Entactin stimulates neutrophil adhesion and chemotaxis through interactions between its Arg-Gly-Asp (RGD) domain and the leukocyte response integrin. J Clin Invest 1992; 90: 2251–7.

    CAS  PubMed  Google Scholar 

  116. Bunch TA, Brower DL. Drosophila PS2 integrin mediates RGD-dependent cell-matrix interactions. Development 1992; 116: 239–47.

    CAS  PubMed  Google Scholar 

  117. Fogerty FJ, Fessler LI, Bunch TA et al. Tiggrin, a novel Drosophila extracellular matrix protein that functions as a ligand for Drosophila aPS2fIPS integrins. Development 1994; 120: 1747–58.

    CAS  PubMed  Google Scholar 

  118. Ziegler U, Stidwill RP. The attachment of nematocytes from the primitive invertebrate Hydra to fibronectin is specific and RGDdependent. Exp Cell Res 1992; 202: 281–6.

    CAS  PubMed  Google Scholar 

  119. Santoni G, Gismondi A, Liu JH et al. Candida albicans expresses a fibronectin receptor antigenically related to a5ß1 integrin. Microbiol 1994; 140: 2971–9.

    CAS  Google Scholar 

  120. Carreno MP, Gresham HD, Brown EJ. Isolation of leukocyte response integrin: a novel RGD-binding protein involved in regulation of phagocytic function. Clin Immunol Immunopathol 1993; 69: 43–51.

    CAS  PubMed  Google Scholar 

  121. Obara M, Kang MS, Yamada KM. Site-directed mutagenesis of the cell-binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Cell 1988; 53: 649–57.

    CAS  PubMed  Google Scholar 

  122. Akiyama SK, Hasegawa E, Hasegawa T et al. The interaction of fibronectin fragments with fibroblastic cells. J Biol Chem 1985; 260: 13256–60.

    CAS  PubMed  Google Scholar 

  123. Giancotti FG, Comoglio PM, Tarone G. Fibronectin-plasma membrane interaction in the adhesion of hemopoietic cells. J Cell Biol 1986; 103: 429–37.

    CAS  PubMed  Google Scholar 

  124. Cierniewski CS, Swiatkowska M, Poniatowski J et al. Anti-(Arg-Gly-Asp-Ser) antibody and its interaction with fibronectin, fibrinogen and platelets. Eur J Biochem 1988; 177: 109–15.

    CAS  PubMed  Google Scholar 

  125. Cherny RC, Honan MA, Thiagarajan P. Site-directed mutagenesis of the arginine-glycine-aspartic acid in vitronectin abolishes cell adhesion. J Biol Chem 1993; 268: 9725–9.

    CAS  PubMed  Google Scholar 

  126. Andrieux A, Hudry-Clergeon G, Ryckewaert JJ et al. Amino acid sequences in fibrinogen mediating its interaction with its platelet receptor, GPIIbIIIa. J Biol Chem 1989; 264: 9258–65.

    CAS  PubMed  Google Scholar 

  127. Cheresh DA, Berliner SA, Vicente V et al. Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells. Cell 1989; 58: 945–53.

    CAS  PubMed  Google Scholar 

  128. Lankhof H, Wu YP, Vink T et al. Role of the glycoprotein Ib-binding Al repeat and the RGD sequence in platelet adhesion to human recombinant von Willebrand factor. Blood 1995; 86: 1035–42.

    CAS  PubMed  Google Scholar 

  129. Dejana E, Lampugnani MG, Giorgi M et al. Von Willebrand factor promotes endothelial cell adhesion via an Arg-Gly-Aspdependent mechanism. J Cell Biol 1989; 109: 367–75.

    CAS  PubMed  Google Scholar 

  130. Oldberg A, Franzen A, Heinegard D. Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence. Proc Natl Acad Sci USA 1986; 83: 8819–23.

    CAS  PubMed  Google Scholar 

  131. Xuan JW, Hota C, Shigeyama Yet al. Site-directed mutagenesis of the arginine-glycine-aspartic acid sequence in osteopontin destroys cell adhesion and migration functions. J Cell Biochem 1995; 57: 680–90.

    CAS  PubMed  Google Scholar 

  132. Flores ME, Norgard M, Heinegard D et al. RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein, and fibronectin. Exp Cell Res 1992; 201: 526–30.

    CAS  PubMed  Google Scholar 

  133. Bourdon MA, Ruoslahti E. Tenascin mediates cell attachment through an RGD-dependent receptor. J Cell Biol 1989; 108: 1149–55.

    CAS  PubMed  Google Scholar 

  134. Dahm LM, Bowers CW. Substance P responsiveness of smooth muscle cells is regulated by the integrin ligand, thrombospondin. Proc Natl Acad Sci USA 1996; 93: 1276–81.

    CAS  PubMed  Google Scholar 

  135. Schulze B, Mann K, Pöschl E et al. Structural and functional analysis of the globular domain IVa of the laminin al chain and its impact on an adjacent RGD site. Biochem J 1996; 314: 847–51.

    CAS  PubMed  Google Scholar 

  136. Aumailley M, Mann K, von der Mark H et al. Cell attachment properties of collagen type VI and Arg-Gly-Asp dependent binding to its a2(VI) and a3(VI) chains. Exp Cell Res 1989; 181: 463–74.

    CAS  PubMed  Google Scholar 

  137. Chakravarti S, Tam MF, Chung AE. The basement membrane glycoprotein entactin promotes cell attachment and binds calcium ions. J Biol Chem 1990; 265: 10597–603.

    CAS  PubMed  Google Scholar 

  138. Chakravarti S, Horchar T, Jefferson B et al. Recombinant domain III of perlecan promotes cell attachment through its RGDS sequence. J Biol Chem 1995; 270: 404–9.

    CAS  PubMed  Google Scholar 

  139. Brake DA, Debouck C, Biesecker G. Identification of an Arg-Gly-Asp (RGD) cell adhesion site in human immunodeficiency virus type 1 transactivation protein, tat. J Cell Biol 1990; 111: 1275–81.

    CAS  PubMed  Google Scholar 

  140. Fox G, Parry NR, Barnett PV et al. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J Gen Virol 1989; 70: 625–37.

    CAS  PubMed  Google Scholar 

  141. Mason PW, Rieder E, Baxt B. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc Natl Acad Sci USA 1994; 91: 1932–6.

    CAS  PubMed  Google Scholar 

  142. Bai M, Harfe B, Freimuth P. Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells. J Virol 1993; 67: 5198–205.

    CAS  PubMed  Google Scholar 

  143. Roivainen M, Hyypia T, Piirainen L et al. RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases. J Virol 1991; 65: 4735–40.

    CAS  PubMed  Google Scholar 

  144. Stanway G, Kalkkinen N, Roivainen M et al. Molecular and biological characteristics of echovirus 22, a representative of a new picornavirus group. J Virol 1994, 68: 8232–8.

    CAS  PubMed  Google Scholar 

  145. Leininger E, Roberts M, Kenimer JG et al. Pertactin, an Arg-Gly-Asp-containing Bordetella pertussis surface protein that promotes adherence of mammalian cells. Proc Natl Acad Sci USA 1991; 88: 345–9.

    CAS  PubMed  Google Scholar 

  146. Reiman DA, Domenighini M, Tuomanen E et al. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc Natl Acad Sci USA 1989; 86: 2637–41.

    Google Scholar 

  147. Ozeki Y, Matsui T, Titani K. Cell adhesive activity of two animal lectins through different recognition mechanisms. FEBS L 1991; 289: 145–7.

    CAS  Google Scholar 

  148. Nichols AJ, Ruffolo RR Jr, Huffman WF et al. Development of GPIIb/IIIa antagonists as antithrombotic drugs. Trends in Pharm Sei 1992; 13: 413–7.

    CAS  Google Scholar 

  149. Coller BS. Antiplatelet agents in the prevention and therapy of thrombosis. Annu Rev Med 1992; 43: 171–80.

    CAS  PubMed  Google Scholar 

  150. Alig L, Edenhofer A, Hadvdry et al. Low molecular weight, non-peptide fibrinogen receptor antagonists. J Med Chem 1992; 35: 4393–407.

    CAS  PubMed  Google Scholar 

  151. Cohen D, Lu HR, Stassen JM et al. Antithrombotic effects and bleeding time prolongation with synthetic platelet GPIIb/ IIla inhibitors in animal models of platelet-mediated thrombosis. Thromb Haemost 1994; 71: 95–102.

    Google Scholar 

  152. Duggan ME, Naylor-Olsen AM, Perkins JJ et al. Non-peptide fibrinogen receptor antagonists. 7. Design and synthesis of a potent, orally active fibrinogen receptor antagonist. J Med Chem 1995; 38: 3332–11.

    CAS  PubMed  Google Scholar 

  153. Humphries MJ, Olden K, Yamada KM. A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells. Science 1986; 233: 467–70.

    CAS  PubMed  Google Scholar 

  154. Dresner-Pollak R, Rosenblatt M. Blockade of osteoclast-mediated hone resorption through occupancy of the integrin receptor: a potential approach to the therapy of osteoporosis. J Cell Biochem 1994; 56: 323–30.

    CAS  PubMed  Google Scholar 

  155. Greenspoon N, Hershkoviz R, Alon R et al. Structural analysis of integrin recognition and the inhibition of integrin-mediated cell functions by novel nonpeptidic surrogates of the Arg-Gly-Asp sequence. Biochem 1993; 32: 1001–8.

    CAS  Google Scholar 

  156. Sawyer RT, Garner RE, Hudson JA. ArgGly-Asp (RGD) peptides alter hepatic killing of Candida albicans in the isolated per-fused mouse liver model. Infection and Immunity 1992; 60: 213–8.

    CAS  PubMed  Google Scholar 

  157. McKenna TS, Lubroth J, Rieder E et al. Receptor binding site-deleted foot-and-mouth disease (FMD) virus protects cattle from FMD. J Virol 1995; 69: 5787–90.

    CAS  PubMed  Google Scholar 

  158. Goligorsky MS, Dißona GF. Pathogenetic role of Arg-Gly-Asp-recognizing integrins in acute renal failure. Proc Natl Acad Sci 1993; 90: 5700–4.

    CAS  PubMed  Google Scholar 

  159. Noiri E, Gailit J, Sheth D et al. Cyclic RGD peptides ameliorate ischemic acute renal failure in rats. Kidney Int 1994; 46: 1050–8.

    CAS  PubMed  Google Scholar 

  160. Pierschbacher MD, Polarek JW, Craig WS et al. Manipulation of cellular interactions with biomaterials toward a therapeutic outcome: a perspective. J Cell Biochem 1994; 56: 150–4.

    CAS  PubMed  Google Scholar 

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Pfaff, M. (1997). Recognition Sites of RGD-Dependent Integrins. In: Integrin-Ligand Interaction. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-4064-6_4

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  • DOI: https://doi.org/10.1007/978-1-4757-4064-6_4

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