A two-amino acid insertion in the Cys146-Cys167 loop of the α(IIb) subunit is associated with a variant of Glanzmann thrombasthenia: Critical role of Asp163 in ligand binding

Journal of Clinical Investigation

Volumn 102, Issue 6, 1998, Pages 1183-1192

  Honda, Shigenori ^a   Tomiyama, Yoshiaki ^a   Shiraga, Masamichi ^a   Tadokoro, Seiji ^a   Takamatsu, Junki ^b   Saito, Hidehiko ^c   Kurata, Yoshiyuki ^d   Matsuzawa, Yuji ^a  

^a OSAKA UNIVERSITY   (Japan)

^b NAGOYA UNIVERSITY HOSPITAL   (Japan)

^c NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d OSAKA UNIVERSITY HOSPITAL   (Japan)

Author keywords

Bleeding disorder; In vitro mutagenesis; Integrin; Platelet; propeller

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; CYSTEINE; EPITOPE; FIBRINOGEN RECEPTOR; GLUTAMIC ACID; INTEGRIN; MESSENGER RNA; SERINE; THREONINE;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; CASE REPORT; CONTROLLED STUDY; FEMALE; GENE EXPRESSION; GENE INSERTION; GENETIC VARIABILITY; GLANZMANN DISEASE; HUMAN; HUMAN CELL; LIGAND BINDING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS;

EID: 0032531105     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI3206     Document Type: Article

References (53)

1. Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
2. Ruoslahti, E. 1991. Integrins. J. Clin. Invest. 87:1-5.
3. Loftus, J.C., and R.C. Linddington. 1997. New insights into integrinligand interaction. J. Clin. Invest. 99:2302-2306.
4. 2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi. J. Biol. Chem. 270:12531-12535.
5. 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72:857-867.
6. Lee, J.-O., P. Rieu, M.A. Arnaout, and R. Liddington. 1995. Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18). Cell. 80:631-638.
7. Phillips, D.R., I.F. Charo, and R.M. Scarborough. 1991. GPIIb-IIIa: the responsive integrin. Cell. 65:359-362.
8. D'Souza, S.E., M.H. Ginsberg, T.A. Burke, S.C.-T. Lam, and E.F. Plow. 1988. Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science. 242:91-93.
9. Charo, I.F., L. Nannizzi, D.R. Phillips, M.A. Hsu, and R.M. Scarborough. 1991. Inhibition of fibrinogen binding to GPIIb-IIIa by a GPIIIa peptide. J. Biol. Chem. 266:1415-1421.
10. 3 integrin. J. Biol. Chem. 269:20913-20919.
11. D'Souza, S.E., M.H. Ginsberg, T.A. Burke, and E.F. Plow. 1990. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit. J. Biol. Chem. 265:3440-3446.
12. D'Souza, S.E., M.H. Ginsberg, G.R. Matsueda, and E.F. Plow. 1991. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature. 350:66-68.
13. (2+)-binding properties of the platelet glycoprotein IIb ligand-interacting domain. J. Biol. Chem. 267:1001-1007.
14. 3. J. Biol. Chem. 271:2033-2039.
15. 3. J. Biol. Chem. 271:30544-30547.
16. 3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J. Biol. Chem. 271:18610-18615.
17. 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science. 249:915-918.
18. 3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site. J. Biol. Chem. 267:3789-3794.
19. 214Trp mutation. J. Clin. Invest. 89:1995-2004.
20. 3 (glycoprotein IIb-IIIa) in a variant of Grantzmann thrombasthenia. Proc. Natl. Acad. Sci. USA. 89:10169-10173.
21. Baker, E.K., E.C. Tozer, M. Pfaff, S.J. Shattil, J.C. Loftus, and M.H. Ginsberg. 1997. A genetic analysis of integrin function: Glanzmann thrombasthenia in vitro. Proc. Natl. Acad. Sci. USA. 94:1973-1978.
22. Calvete, J.J., M.V. Alvarez, G. Rivas, C.-L. Hew, A. Menschen, and J. Gonzalez-Rodriguez. 1989. Interchain and intrachain disulphide bonds in human platelet glycoprotein IIb: localization of the epitopes for several monoclonal antibodies. Biochem. J. 261:551.
23. Springer, T.A. 1997. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc. Natl. Acad. Sci. USA. 94: 65-72.
24. Tomiyama, Y., T. Tsubakio, R.S. Piotrowicz, Y. Kurata, J.C. Loftus, and T.J. Kunicki. 1992. The Arg-Gly-Asp (RGD) recognition site of platelet glycoprotein IIb-IIIa on nonactivated platelets is accessible to high-affinity macromolecules. Blood. 79:2303-2312.
25. Shattil, S.J., J.A. Hoxie, M. Cunningham, and L.F. Brass. 1985. Changes in the platelet membrane glycoprotein IIb-IIIa complex during platelet activation. J. Biol. Chem. 260:11107-11114.
26. Bennett, J.S., S.J. Shattil, J.W. Power, and T.K. Gartner. 1988. Interaction of fibrinogen with its platelet receptor: differential effects of α and γ chain fibrinogen peptides on the glycoprotein IIb-IIIa. J. Biol. Chem. 263:12948-12953.
27. 3. J. Biol. Chem. 267:18085-18092.
28. Taub, R., R.J. Gould, V.M. Garsky, T.M. Ciccarone, J. Hoxie, P.A. Friedman, and S.J. Shattil. 1989. A monoclonal antibody against the platelet fibrinogen receptor contains a sequence that mimics a receptor recognition domain in fibrinogen. J. Biol. Chem. 264:259-265.
29. Kodandapani, R., B. Veerapandian, T.J. Kunicki, and K.R. Ely. 1995. Crystal structure of the OPG2 Fab. An antireceptor antibody that mimics an RGD cell adhesion site. J. Biol. Chem. 270:2268-2273.
30. Pidard, D., R.R. Montgomery, J.S. Bennett, and T.J. Kunicki. 1983. Interaction of AP2, a monoclonal antibody specific for the human platelet glycoprotein GPIIb-IIIa complex, with intact platelet. J. Biol. Chem. 258:12582-12586.
31. 3 subunit. J. Biol. Chem. 270:11947-11954.
32. Ginsberg, M.H., A. Lightsey, T.J. Kunicki, A. Kaufmann, G. Marguerie, and E.F. Plow. 1986. Divalent cation regulation of the surface orientation of platelet membrane glycoprotein IIb: correlation with fibrinogen binding function and definition of a novel variant of Glanzmann's thrombasthenia. J. Clin. Invest. 78:1103-1111.
33. Loftus, J.C., E.F. Plow, A.L. Frelinger III, S.E. D'Souza, D. Dixon, J. Lacy, J. Sorge, and M.H. Ginsberg. 1987. Molecular cloning and chemical synthesis of a region of platelet glycoprotein IIb involved in adhesive function. Proc. Natl. Acad. Sci. USA. 84:7114-7118.
34. Newmann, P.J., R.W. Allen, R.A. Kahn, and T.J. Kunicki. 1985. Quantitation of membrane glycoprotein IIIa on intact human platelets using the monoclonal antibody. AP3. Blood. 65:227-232.
35. McEver, R.R., E.M. Bennett, and M.N. Martin. 1983. Identification of two structurally and functionally distinct sites on human platelet membrane glycoprotein IIb-IIIa using monoclonal antibodies. J. Biol. Chem. 258:5269-5275.
36. 3 integrin). Thromb. Haemost. 76:1038-1046.
37. Aoki, T., D. Cox, K. Senzaki, J. Seki, A. Tanaka, H. Takasugi, and Y. Motoyama. 1996. The anti-platelet and anti-thrombotic effects of FK633, a peptide-minetic GPIIb/IIIa antagonist. Thromb. Res. 81:439-450.
38. 2+ exchanger. Blood. 88:2594-2602.
39. Zucker, M.B., and N.C. Masiello. 1984. Platelet aggregation caused by dithiothreitol. Thromb. Haemost. 51:119-124.
40. Tomiyama, Y., H. Kashiwagi, S. Kosugi, S. Kinoshita, Y. Kanayama, Y. Kurata, and Y. Malsuzawa. 1994. Demonstration of a marked reduction in the amount of GPIIb in most type II patients with Glanzmann's thrombasthenia. Br. J. Haematol. 87:119-124.
41. Tomiyama, Y., H. Kashiwagi, S. Kosugi, M. Shiraga, Y. Kanayama, Y. Kurata, and Y. Matsuzuwa. 1995. Abnormal processing of the glycoprotein IIb transcript due to a nonsense mutation in exon 17 associated with Glanzmann thrombasthenia. Thromb. Haemost. 73:756-762.
42. Rosa, J.P., P.F. Bray, O. Gayet, G.I. Johnston, R.G. Cook, K. W. Jackson, M.A. Shuman, and R.P. McEver. 1988. Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17. Blood. 72:593-600.
43. Heidenreich, R., R. Eisman, S. Surrey, K. Delgrosso, J.S. Bennett, E. Schwartz, and M. Poncz. 1990. Organization of the gene for platelet glycoprotein IIb. Biochemistry. 29:1232-1244.
44. Higuchi, R., B. Krummel, and R.K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interaction. Nucleic Acids Res. 16:7351-7367.
45. 478C→T substitution (prorine→serine) in CD36 cDNA account for CD36 deficiency. J. Clin. Invest. 95:1040-1046.
46. Frelinger III, A.L., S.C.-T. Lam, E.F. Plow, M.A. Smith, J.C. Loftus, and M.H. Ginsborg. 1988. Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. J. Biol. Chem. 263:12397-12402.
47. Kouns, W.C., B. Steiner, T.J. Kunicki, S. Moog, J. Jutzi, L.K. Jennings, J.-P. Czenave, and F. Lanza. 1994. Activation of the fibrinogen binding site on platelets isolated from a patient with the Strasbourg I variant of Glanzmann's thrombasthenia. Blood. 84:1108-1115.
48. Irie, A., T. Kamata, W. Puzon-McLaughlin, and Y. Takada. 1995. Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the inlegrin α4 and α5 subunits. EMBO (Eur. Mol. Biol. Organ.) J. 14:5557-5568.
49. Irie, A., T. Kamata, and Y. Takada. 1997. Multiple loop structures critical for ligand binding of the integrin α4 subunit in the upper face of the β-propeller model 1. Proc. Natl. Acad. Sci. USA. 94:7198-7203.
50. Basani, R., J.S. Bennett, and M. Poncz. 1997. A Glanzmann thrombasthenia variant due to αIIb mutation suggests that an additional N-terminal loop is involved in ligand-binding. Blood. 90:26a. (Abstr.).
51. Grimaldi, C.M., F. Chen, C. Wu, H.J. Weiss, B.S. Coller, and D.L. French. 1998. Glycoprotein IIb Leu214Pro mutation produced Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/ IIIa. Blood. 91:1562-1571.
52. 3 subunit: cation displacement is involved in ligand binding, Cell. 79:659-667.
53. Coller, B.S. 1997. Platelet GPIIb/IIIa antagonists: the first anti-integrin receptor therapeutics. J. Clin. Invest. 99:1467-1470.