Critical residues for ligand binding in blade 2 of the propeller domain of the integrin αIIb subunit

Thrombosis and Haemostasis

Volumn 91, Issue 1, 2004, Pages 111-118

  Tamura, Tatsushiro ^a   Hato, Takaaki ^a   Yamanouchi, Jun ^a   Fujita, Shigeru ^a  

^a EHIME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Adhesion receptors integrins; Cell matrix interactions; Platelet physiology; Protein structure folding

Indexed keywords

ALANINE; ALPHA INTEGRIN; ALPHAIIB BETA3 INTEGRIN; ALPHAIIB INTEGRIN; ARGINYLGLYCYLASPARTYLSERINE; ASPARAGINE; BETA3 INTEGRIN; CD51 ANTIGEN; FIBRINOGEN; GLUTAMINE; HISTIDINE; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

ANIMAL CELL; ARTICLE; BINDING SITE; CELL ADHESION; CHO CELL; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG EFFECT; GENE MUTATION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS;

EID: 1642474427     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th03-06-0392     Document Type: Article

References (41)

1. Giancotti FG, Ruoslahti E. Transduction integrin signaling. Science 1999; 285: 1028-32.
2. Hynes RO. Integrins: Bidirectional, allosteric signaling machines. Cell 2002; 110: 673-87.
3. Gottschalk KE, Kessler H. The structures of integrins and integrin-ligand complexes: Implications for drug design and signal transduction. Angew Chem Int Ed Engl 2002; 41: 3767-74.
4. Coller BS. Anti-GPIIb/IIIa drugs: Current strategies and future directions. Thromb. Haemost. 2001; 86: 427-43.
5. Savage B, Almus-Jacobs F, et al. Specific synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell 1998; 94: 657-66.
6. Ruggeri ZM, Dent JA, Saldivar E. Contribution of distinct adhesive interactions to platelet aggregation in flowing blood. Blood 1999; 94: 172-8.
7. Tsuji S, Sugimoto M, Miyata S, et al. Real-time analysis of mural thrombus formation in various platelet aggregation disorders: Distinct shear-dependent roles of platelet receptors and adhesive proteins under flow. Blood 1999; 94: 968-75.
8. Springer TA. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc Natl Acad Sci USA 1997; 94: 65-72.
9. Humphries MJ. Integrin structure. Biochem. Soc. Trans. 2000; 28: 311-40.
10. Xiong JP, Stehle T, Diefenbach B, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3. Science 2001; 294: 339-45.
11. Xiong JP, Stehle T, Zhang R, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science 2002; 296: 151-5.
12. Felding-Habermann B, Cheresh DA. Vitronectin and its receptors. Curr Opin Cell Biol 1993; 5: 864-8.
13. Wickham TJ, Mathias P, Cheresh DA, et al. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell 1993; 73: 309-19.
14. 3. J Biol Chem 1995; 270: 9917-25.
15. Brooks PC, Stromblad S, Sanders LC, Von Schalscha TL, Aimes RT, Stetler-Stevenson WG, Quigley JP, Cheresh DA. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell 1996; 85: 683-93.
16. Scarborough RM, Naughton MA, Teng W, et al. Design of potent and specific integrin antagonists. Peptide antagonists with high specificity for glycoprotein IIb-IIIa. J Biol Chem 1993; 268: 1066-73.
17. IIb subunit is associated with a variant of Glanzmann thrombasthenia - Critical role of Asp163 in ligand binding. J Clin Invest 1998; 102: 1183-92.
18. Grimaldi CM, Chen FP, Wu CH, et al. Glycoprotein IIb Leu214Pro mutation produces glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa. Blood 1998; 91: 1562-71.
19. Basani RB, French DL, Vilaire G, et al. A naturally occurring mutation near the amino terminus of αIIb defines a new region involved in ligand binding to αIIbβ3. Blood 2000; 95: 180-8.
20. 3(glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J. Biol. Chem. 1996; 271: 18610-5.
21. 3 identifies a novel region important for ligand binding. Blood 1999; 93: 918-24.
22. Kamata T, Tieu KK, Springer TA, et al. Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbβ3 are clustered in the beta- propeller model. J Biol Chem 2001; 276: 44275-83.
23. Shattil SJ, Hoxie JA, Cunningham M, et al. Changes in the platelet membrane glycoprotein IIb-IIIa complex during platelet activation. J Biol Chem 1985; 260: 11107-14.
24. Tokuhira M, Handa M, Kamata T, et al. A novel regulatory epitope defined by a murine monoclonal antibody to the platelet GPIIb-IIIa complex (αIIbβ3 integrin). Thromb Haemost 1996; 76: 1038-46.
25. Yamanouchi J, Hato T, Tamura T, et al. Identification of critical residues for ligand binding in the integrin beta3 I-domain by site-directed mutagenesis. Thromb Haemost 2002; 87: 756-62.
26. Higuchi R, Krummel B, Saiki RK. A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res 1988; 16: 7351-67.
27. IIbβ3. J Cell Biol 1998; 141: 1685-95.
28. O'Toole TE, Katagiri Y, Faull RJ, et al. Integrin cytoplasmic domains mediate inside-out signal transduction. J Cell Biol 1994; 124: 1047-59.
29. 3. J Biol Chem 2000; 275: 7795-802.
30. Hughes PE, Diaz-Gonzalez F, Leong L, et al. Breaking the integrin hinge - A defined structural constraint regulates integrin signaling. J Biol Chem 1996; 271: 6571-4.
31. 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels. Cell 1994; 79: 1157-64.
32. Kiyoi T, Tomiyama Y, Honda S, et al. A naturally occurring Tyr143Hisalpha IIb mutation abolishes alpha IIbbeta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: Comparison with other mutations causing ligand-binding defects. Blood 2003; 101: 3485-91.
33. Morel-Kopp MC, Melchior C, Chen P, et al. A naturally occurring point mutation in the beta3 integrin MIDAS-like domain affects differently alphavbeta3 and alphaIIIbbeta3 receptor function. Thromb Haemost 2001; 86: 1425-34.
34. Arnaout MA, Goodman SL, Xiong JP. Coming to grips with integrin binding to ligands. Curr Opin Cell Biol 2002; 14: 641-51.
35. E chain C-terminal domains. Biochemistry 1999; 38: 5872-7.
36. 1. Cell 2000; 101: 47-56.
37. Takagi J, Petre BM, Walz T, et al. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002; 110: 599-11.
38. Koivunen E, Wang B, Ruoslahti E. Isolation of a highly specific ligand for the alpha 5 beta 1 integrin from a phage display library. J Cell Biol 1994; 124: 373-80.
39. Mould AP, Burrows L, Humphries MJ. Identification of amino acid residues that form part of the ligand-binding pocket of integrin alpha5 beta1. J Biol Chem 1998; 273: 25664-72.
40. Burrows L, Clark K, Mould AP, et al. Fine mapping of inhibitory anti-alpha5 monoclonal antibody epitopes that differentially affect integrin-ligand binding. Biochem J 1999; 344 Pt 2: 527-33.
41. Krukonis ES, Dersch P, Eble JA, Isberg RR. Differential effects of integrin alpha chain mutations on invasin and natural ligand interaction. J Biol Chem 1998; 273: 31837-43.