Species differences in small molecule binding to άIIbΒ3 are the result of sequence differences in 2 loops of the άIIb Β propeller

Blood

Volumn 113, Issue 4, 2009, Pages 902-910

  Basani, Ramesh B ^a   Zhu, Hua ^b   Thornton, Michael A ^a,c   Soto, Cinque S ^b   DeGrado, William F ^b   Kowalska, M Anna ^a   Bennett, Joel S ^b   Poncz, Mortimer ^a  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c FLORIDA A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ALPHA 2B BETA 3 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; DISINTEGRIN; ECHISTATIN; EPTIFIBATIDE; LYMPHOCYTE ANTIGEN; TIROFIBAN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR; DRUG DERIVATIVE; FIBRINOGEN; FIBRINOGEN RECEPTOR; PEPTIDE; RECOMBINANT PROTEIN; TYROSINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL EXPERIMENT; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; FEMALE; HEMOSTASIS; HUMAN; HUMAN CELL; INFECTION PREVENTION; LIGAND BINDING; MACROMOLECULE; MALE; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; SPECIES DIFFERENCE; STRUCTURE ANALYSIS; ANIMAL; CELL LINE; CHEMISTRY; DRUG EFFECT; GENETICS; HAMSTER; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; RAT; SEQUENCE ALIGNMENT; THROMBOCYTE AGGREGATION;

ADENOSINE DIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CONSERVED SEQUENCE; CRICETINAE; FIBRINOGEN; HUMANS; MICE; MOLECULAR SEQUENCE DATA; PEPTIDES; PLATELET AGGREGATION; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX; PROTEIN BINDING; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; TYROSINE;

EID: 59649120717     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-09-177337     Document Type: Article

References (48)

1. Hynes RO. Cellular location of viral transforming proteins. Cell. 1987;48:549-554.
2. Springer TA, Wang JH. The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion. Adv Protein Chem. 2004;68:29-63.
3. Kloczewiak M, Timmons S, Hawiger J. Localization of a site interacting with human platelet receptor on carboxy-terminal segment of human fibrinogen gamma chain. Biochem Biophys Res Commun. 1982;107:181-187.
4. Plow EF, Marguerie G. Inhibition of fibrinogen binding to human platelets by the tetrapeptide glycyl-L-prolyl-L-arginyl-L-proline. Proc Natl Acad Sci U S A. 1982;79:3711-3715.
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: 11891-11894.
6. Haverstick DM, Cowan JF, Yamada KM, Santoro SA. Inhibition of platelet adhesion to fibronectin, fibrinogen, and von Willebrand factor substrates by a synthetic tetrapeptide derived from the cellbinding domain of fibronectin. Blood. 1985;66: 946-952.
7. Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie G, Ginsberg MH. Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets. Proc Natl Acad Sci U S A. 1985;82: 8057-8061.
8. Chung DW, Harris JE, Davie EW. Nucleotide sequences of the three genes coding for human fibrinogen. Adv Exp Med Biol. 1990;281:39-48.
9. Sadler JE, Shelton-Inloes BB, Sorace JM, Harlan JM, Titani K, Davie EW. Cloning and characterization of two cDNAs coding for human von Willebrand factor. Proc Natl Acad Sci U S A. 1985;82: 6394-6398.
10. Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie G, Ginsberg MH. Arginyl-glycyl-aspartic acid sequences and fibrinogen binding to platelets. Blood. 1987;70:110-115.
11. Hartman GD, Egbertson MS, Halczenko W, et al. Non-peptide fibrinogen receptor antagonists. 1. Discovery and design of exosite inhibitors. J Med Chem. 1992;35:4640-4642.
12. Nicolini FA, Lee P, Rios G, Kottke-Marchant K, Topol EJ. Combination of platelet fibrinogen receptor antagonist and direct thrombin inhibitor at low doses markedly improves thrombolysis. Circulation. 1994;89:1802-1809.
13. Harfenist EJ, Packham MA, Mustard JF. Effects of the cell adhesion peptide, Arg-Gly-Asp-Ser, on responses of washed platelets from humans, rabbits, and rats. Blood. 1998;71:132-136.
14. Jennings LK, White MM, Mandrell TD. Interspecies comparison of platelet aggregation, LIBS expression and clot retraction: observed differences in GPIIb-IIIa functional activity. Thromb Haemost. 1995;74:1551-1556.
15. Basani RB, D'Andrea G, Mitra N, et al. RGDcontaining peptides inhibit fibrinogen binding to platelet alpha(IIb)beta3 by inducing an allosteric change in the amino-terminal portion of alpha( IIb). J Biol Chem. 2001;276:13975-13981.
16. Xiao T, Takagi J, Coller BS, Wang JH, Springer TA. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature. 2004;432:59-67.
17. Xiong JP, Stehle T, Diefenbach B, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3. Science. 2001;294:339-345.
18. 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;296:151-155.
19. Poncz M, Newman PJ. Analysis of rodent platelet glycoprotein IIb: evidence for evolutionarily conserved domains and alternative proteolytic processing. Blood. 1990;75:1282-1289.
20. Thornton MA, Poncz M. Characterization of the murine platelet alphaIIb gene and encoded cDNA. Blood. 1990;94:3947-3950.
21. Miyazaki H, Tamura S, Sudo T, Suzuki T. Production and characterization of monoclonal antibodies against rat platelet GPIIb/IIIa. Thromb Res. 1990;59:941-953.
22. Bennett JS, Hoxie JA, Leitman SF, Vilaire G, Cines DB. Inhibition of fibrinogen binding to stimulated human platelets by a monoclonal antibody. Proc Natl Acad Sci U S A. 1983;80:2417-2421.
23. Qi W, Loh E, Vilaire G, Bennett JS. Regulation of alphaIIb beta3 function in human B lymphocytes. J Biol Chem. 1998;273:15271-15278.
24. Zucker MB, Masiello NC. Platelet aggregation caused by dithiothreitol. Thromb Haemost. 1984; 51:119-124.
25. Haverstick DM, Dixit VM, Grant GA, Frazier WA, Santoro SA. Localization of the hemagglutinating activity of platelet thrombospondin to a 140,000- dalton thermolytic fragment. Biochemistry. 1984; 23:5597-5603.
26. McLane MA, Vijay-Kumar S, Marcinkiewicz C, Calvete JJ, Niewiarowski S. Importance of the structure of the RGD-containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 integrins. FEBS Lett. 1996;391:139-143.
27. Thornton MA, Zhang C, Kowalska MA, Poncz M. Identification of distal regulatory regions in the human alpha IIb gene locus necessary for consistent, high-level megakaryocyte expression. Blood. 2002;100:3588-3596.
28. Massberg S, Schurzinger K, Lorenz M, et al. Platelet adhesion via glycoprotein IIb integrin is critical for atheroprogression and focal cerebral ischemia: an in vivo study in mice lacking glycoprotein IIb. Circulation. 2005;112:1180-1188.
29. Bennett JS, Vilaire G. Exposure of platelet fibrinogen receptors by ADP and epinephrine. J Clin Invest. 1979;64:1393-1401.
30. Yin H, Litvinov RI, Vilaire G, et al. Activation of platelet alphaIIbbeta3 by an exogenous peptide corresponding to the transmembrane domain of alphaIIb. J Biol Chem. 2006;281:36732-36741.
31. Kamata T, Irie A, Tokuhira M, Takada Y. Critical residues of integrin alphaIIb subunit for binding of alphaIIbbeta3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J Biol Chem. 1996;271:18610-18615.
32. Kamata T, Tieu KK, Irie A, Springer TA, Takada Y. Amino acid residues in the alpha IIb subunit that are critical for ligand binding to integrin alpha IIb beta 3 are clustered in the beta-propeller model. J Biol Chem. 2001;276:44275-44283.
33. Calvete JJ. Structure-function correlations of snake venom disintegrins. Curr Pharm Des. 2005;11:829-835.
34. Peerlinck K, De Lepeleire I, Goldberg M, et al. MK-383 (L-700,462), a selective nonpeptide platelet glycoprotein IIb/IIIa antagonist, is active in man. Circulation. 1993;88:1512-1517.
35. Egbertson MS, Chang CT, Duggan ME, et al. Non-peptide fibrinogen receptor antagonists. 2. Optimization of a tyrosine template as a mimic for Arg-Gly-Asp. J. Med Chem. 1994;7:2537-2551.
36. Quinn M, Deering A, Stewart M, Cox D, Foley B, Fitzgerald D. Quantifying GPIIb/IIIa receptor binding using 2 monoclonal antibodies: discriminating abciximab and small molecular weight antagonists. Circulation. 1999;99:2231-2238.
37. Beacham DA, Wise RJ, Turci SM, Handin RI. Selective inactivation of the Arg-Gly-Asp-Ser (RGDS) binding site in von Willebrand factor by site-directed mutagenesis. J Biol Chem. 1992; 267:3409-3415.
38. Ginsburg D, Handin RI, Bonthron DT, et al. Human von Willebrand factor (vWF): isolation of complementary DNA (cDNA) clones and chromosomal localization. Science. 1985;228:1401-1406.
39. Thibault G, Tardif P, Lapalme G. Comparative specificity of platelet alpha(IIb)beta(3) integrin antagonists. J Pharmacol Exp Ther. 2001;296: 690-696.
40. Farrell DH, Thiagarajan P, Chung DW, Davie EW. Role of fibrinogen alpha and gamma chain sites in platelet aggregation, Proc Natl Acad Sci U S A. 1992;89:10729-10732.
41. Farrell DH, Thiagarajan P. Binding of recombinant fibrinogen mutants to platelets. J Biol Chem. 1994;269:226-231.
42. Bennett JS, Shattil SJ, Power JW, Gartner TK. Interaction of fibrinogen with its platelet receptor: differential effects of alpha and gamma chain fibrinogen peptides on the glycoprotein IIb-IIIa complex. J Biol Chem. 1988;263:12948-12953.
43. 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: 1066-1073.
44. Farrell DH, Thiagarajan P, Chung DW, Davie EW. Role of fibrinogen alpha and gamma chain sites in platelet aggregation. Proc Natl Acad Sci U S A. 1992;89:10729-10732.
45. Farrell DH, Thiagarajan P. Binding of recombinant fibrinogen mutants to platelets. J Biol Chem. 1994;269:226-231.
46. Rooney MM, Parise LV, Lord ST. Dissecting clot retraction and platelet aggregation: clot retraction does not require an intact fibrinogen gamma chain C terminus. J Biol Chem. 1996;271:8553-8555.
47. Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 2003;22:4607-4615.
48. Mould AP, Barton SJ, Askari JA, Craig SE, Humphries MJ. Role of ADMIDAS cation-binding site in ligand recognition by integrin alpha 5 beta 1. J Biol Chem. 2003;278:51622-51629.