메뉴 건너뛰기




Volumn 93, Issue 3, 1999, Pages 918-924

A mutation in the α subunit of the platelet integrin α(IIb)β3 identifies a novel region important for ligand binding

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; INTEGRIN;

EID: 0032936519     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v93.3.918     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0030857775 scopus 로고    scopus 로고
    • Hematologically important mutations: Glanzmann thrombasthenia
    • French DL, Coller BS: Hematologically important mutations: Glanzmann thrombasthenia. Blood Cells Mol Dis 23:39, 1997
    • (1997) Blood Cells Mol Dis , vol.23 , pp. 39
    • French, D.L.1    Coller, B.S.2
  • 2
    • 0024280898 scopus 로고
    • Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor
    • D'Souza SE, Ginsberg MH, Burke TA, Lam SC, Plow EF: Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science 242:91, 1988
    • (1988) Science , vol.242 , pp. 91
    • D'Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Lam, S.C.4    Plow, E.F.5
  • 6
    • 0026720994 scopus 로고
    • A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg-214Trp mutation
    • Lanza F, Stierle A, Fournier D, Morales M, Andre G, Nurden AT, Cazenave JP: A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg-214Trp mutation. J Clin Invest 89:1995, 1992
    • (1992) J Clin Invest , vol.89 , pp. 1995
    • Lanza, F.1    Stierle, A.2    Fournier, D.3    Morales, M.4    Andre, G.5    Nurden, A.T.6    Cazenave, J.P.7
  • 9
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee JO, Rieu P, Arnaout MA, Liddington R: Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80:631, 1995
    • (1995) Cell , vol.80 , pp. 631
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 10
    • 0027972994 scopus 로고
    • Integrin-mediated cell adhesion: The extracellular face
    • Loftus JC, Smith JW, Ginsberg MH: Integrin-mediated cell adhesion: The extracellular face. J Biol Chem 269:25235, 1994
    • (1994) J Biol Chem , vol.269 , pp. 25235
    • Loftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 17
    • 0025216612 scopus 로고
    • The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit
    • D'Souza SE, Ginsberg MH, Burke TA, Plow EF: The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit. J Biol Chem 265:3440, 1990
    • (1990) J Biol Chem , vol.265 , pp. 3440
    • D'Souza, S.E.1    Ginsberg, M.H.2    Burke, T.A.3    Plow, E.F.4
  • 18
    • 0026035464 scopus 로고
    • A discrete sequence in a platelet integrin is involved in ligand recognition
    • D'Souza SE, Ginsberg MH, Matsueda GR, Plow EF: A discrete sequence in a platelet integrin is involved in ligand recognition. Nature 350:66, 1991
    • (1991) Nature , vol.350 , pp. 66
    • D'Souza, S.E.1    Ginsberg, M.H.2    Matsueda, G.R.3    Plow, E.F.4
  • 19
    • 0026719991 scopus 로고
    • A peptide corresponding to GPIIb alpha 300-312, a presumptive fibrinogen gamma-chain binding site on the platelet integrin GPIIb/IIIa, inhibits the adhesion of platelets to at least four adhesive ligands
    • Taylor DB, Gartner TK: A peptide corresponding to GPIIb alpha 300-312, a presumptive fibrinogen gamma-chain binding site on the platelet integrin GPIIb/IIIa, inhibits the adhesion of platelets to at least four adhesive ligands. J Biol Chem 267:11729, 1992
    • (1992) J Biol Chem , vol.267 , pp. 11729
    • Taylor, D.B.1    Gartner, T.K.2
  • 20
    • 0029780525 scopus 로고    scopus 로고
    • 3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3)
    • 3 (glycoprotein IIb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J Biol Chem 271:18610, 1996
    • (1996) J Biol Chem , vol.271 , pp. 18610
    • Kamata, T.1    Irie, A.2    Tokuhira, M.3    Takada, Y.4
  • 22
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a β-propeller domain
    • Springer TA: Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a β-propeller domain. Proc Natl Acad Sci USA 94:65, 1997
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 65
    • Springer, T.A.1
  • 23
    • 0022180156 scopus 로고
    • Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation
    • Shattil SJ, Hoxie JA, Cunningham M, Brass LF: Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation. J Biol Chem 260:11107, 1985
    • (1985) J Biol Chem , vol.260 , pp. 11107
    • Shattil, S.J.1    Hoxie, J.A.2    Cunningham, M.3    Brass, L.F.4
  • 24
    • 0021027332 scopus 로고
    • Interaction of AP-2, a monoclonal antibody specific for the human platelet glycoprotein IIb-IIIa complex, with intact platelets
    • Pidard D, Montgomery RR, Bennett JS, Kunicki TJ: Interaction of AP-2, a monoclonal antibody specific for the human platelet glycoprotein IIb-IIIa complex, with intact platelets. J Biol Chem 258:12582, 1983
    • (1983) J Biol Chem , vol.258 , pp. 12582
    • Pidard, D.1    Montgomery, R.R.2    Bennett, J.S.3    Kunicki, T.J.4
  • 25
    • 0026771879 scopus 로고
    • The Arg-Gly-Asp (RGD) recognition site of platelet glycoprotein IIb-IIIa on nonactivated platelets is accessible to high-affinity macromolecules
    • Tomiyama Y, Tsubakio T, Piotrowicz RS, Kurata Y, Loftus JC, Kunicki TJ: The Arg-Gly-Asp (RGD) recognition site of platelet glycoprotein IIb-IIIa on nonactivated platelets is accessible to high-affinity macromolecules. Blood 79:2303, 1992
    • (1992) Blood , vol.79 , pp. 2303
    • Tomiyama, Y.1    Tsubakio, T.2    Piotrowicz, R.S.3    Kurata, Y.4    Loftus, J.C.5    Kunicki, T.J.6
  • 27
  • 29
    • 0023234083 scopus 로고
    • Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130-kDa alpha subunit
    • Cheresh DA, Harper JR: Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130-kDa alpha subunit. J Biol Chem 262:1434, 1987
    • (1987) J Biol Chem , vol.262 , pp. 1434
    • Cheresh, D.A.1    Harper, J.R.2
  • 30
    • 0026629829 scopus 로고
    • Conformational modulation of purified glycoprotein (GP) IIb-IIIa allows proteolytic generation of active fragments from either active or inactive GPIIb-IIIa
    • Kouns WC, Hadvary P, Haering P, Steiner B: Conformational modulation of purified glycoprotein (GP) IIb-IIIa allows proteolytic generation of active fragments from either active or inactive GPIIb-IIIa. J Biol Chem 267:18844, 1992
    • (1992) J Biol Chem , vol.267 , pp. 18844
    • Kouns, W.C.1    Hadvary, P.2    Haering, P.3    Steiner, B.4
  • 31
    • 0023663947 scopus 로고
    • Evidence that arginyl-glycyl-aspartate peptides and fibrinogen gamma chain peptides share a common binding site on platelets
    • Lam SC, Plow EF, Smith MA, Andrieux A, Ryckwaert JJ, Marguerie G, Ginsberg MH: Evidence that arginyl-glycyl-aspartate peptides and fibrinogen gamma chain peptides share a common binding site on platelets. J Biol Chem 262:947, 1987
    • (1987) J Biol Chem , vol.262 , pp. 947
    • Lam, S.C.1    Plow, E.F.2    Smith, M.A.3    Andrieux, A.4    Ryckwaert, J.J.5    Marguerie, G.6    Ginsberg, M.H.7
  • 34
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar G, Sommer SS: The "megaprimer" method of site-directed mutagenesis. Biotechniques 8:404, 1990
    • (1990) Biotechniques , vol.8 , pp. 404
    • Sarkar, G.1    Sommer, S.S.2
  • 35
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR: Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51, 1989
    • (1989) Gene , vol.77 , pp. 51
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 36
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes PE, O'Toole TE, Ylanne J, Shattil SJ, Ginsberg MH: The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J Biol Chem 270:12411, 1995
    • (1995) J Biol Chem , vol.270 , pp. 12411
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 38
    • 0027483226 scopus 로고
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 72:857, 1993
    • (1993) Cell , vol.72 , pp. 857
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 41
    • 0032032356 scopus 로고    scopus 로고
    • Glyoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa
    • Grimaldi CM, Chen F, Wu C, Weiss HJ, Coller BS, French DL: Glyoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa. Blood 91:1562, 1998
    • (1998) Blood , vol.91 , pp. 1562
    • Grimaldi, C.M.1    Chen, F.2    Wu, C.3    Weiss, H.J.4    Coller, B.S.5    French, D.L.6
  • 44
    • 0024427509 scopus 로고
    • Developmentally regulated alternative splicing of Drosophila integrin PS2α transcripts
    • Brown NH, King DL, Wilcox M, Kafatos FC: Developmentally regulated alternative splicing of Drosophila integrin PS2α transcripts. Cell 59:185, 1989
    • (1989) Cell , vol.59 , pp. 185
    • Brown, N.H.1    King, D.L.2    Wilcox, M.3    Kafatos, F.C.4
  • 45
    • 0029955198 scopus 로고    scopus 로고
    • Alternatively spliced forms of the Drosophila αPS2 subunit of integrin are sufficient for viability and can replace the function of the αPS1 subunit of integrin in the retina
    • Roote CE, Zusman S: Alternatively spliced forms of the Drosophila αPS2 subunit of integrin are sufficient for viability and can replace the function of the αPS1 subunit of integrin in the retina. Development 122:1985, 1996
    • (1996) Development , vol.122 , pp. 1985
    • Roote, C.E.1    Zusman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.