Integrin αIIbβ3 and Platelet Function

X Du; Mark H Ginsberg

doi:10.1055/s-0038-1657508

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1997; 78(01): 096-100
DOI: 10.1055/s-0038-1657508

Integrin signalling and vascular function

Schattauer GmbH Stuttgart

Integrin α_IIbβ₃ and Platelet Function

X Du

¹Department of Pharmacology, University of Illinois at Chicago, College of Medicine, Chicago, IL

,

Mark H Ginsberg

²Department of Vascular Biology, The Scripps Research Institute, La Jolla, CA, USA

› Author Affiliations

Abstract

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References

References
1 Ginsberg MH, Du X, O’Toole TE, Loftus JC. Platelet Integrins. Thromb. Haemo stas 1995; 74: 352-359
2 Smyth SS, Joneckis CC, Parise LV. Regulation of vascular integrins. Blood 1993; 81: 2827-2843
3 Phillips DR, Charo IF, Parise LV, Fitzgerald LA. The platelet membrane glycoprotein Ilb-IIIa complex. Blood 1988; 71: 831-843
4 O’Toole TE, Katagiri Y, Faull RJ. et al Integrin cytoplasmic domains mediate inside-out signal transduction. J Cell Biol 1994; 124: 1047-1059
5 Du X, Saido TC, Tsubuki S, Indig FE, Williams MJ, Ginsberg MH. Calpain cleavage of the cytoplasmic domain of the integrin β₃ subunit. J Biol Chem 1995; 270: 26146-26151
6 Weisel JW, Nagaswami C, Vilaire G, Bennett JS. Examination of the platelet membrane glycoprotein Ilb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. J Biol Chem 1992; 267: 16637-16643
7 Du X, Gu M, Weisel JW. et al Long range propagation of conformational changes in integrin α_IIbβ₃ . J Biol Chem 1993; 268: 23087-23092
8 Lam SCT. Isolation and characterization of a chymotryptic fragment of platelet glycoprotein Ilb-IIIa retaining arg-gly-asp binding activity. J Biol Chem 1992; 267: 5649-5655
9 Haas TA, Plow EF. The cytoplasmic domain of α_IIbβ₃ . J Biol Chem 1996; 271: 6017-6026
10 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
11 Lam SC, Plow EF, Smith MA. et al Evidence that Arginyl-Glycyl-Aspartate peptides and fibrinogen gamma chain peptides share a common binding site on platelets. J Biol Chem 1987; 262: 947-950
12 Holmback K, Danton MJS, Suh TT, Daugherty CC, Degen JL. Impaired platelet aggregation and sustained bleeding in mice lacking the fibrinogen motif bound by integrin α_IIbβ₃ . EMBO J 1996; 15: 5760-5771
13 Farrell DH, Thiagarajan P. Binding of recombinant fibrinogen mutants to platelets. J Biol Chem 1994; 269: 226-231
14 Plow EF, Pierschbacher MD, Ruoslahti E, Marguerie GA, Ginsberg MH. Arginyl-Glycyl-Aspartic acid sequences and fibrinogen binding to platelets. Blood 1987; 70: 110-115
15 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 1988; 242: 91-93
16 Bajt ML, Loftus JC. Mutation of a ligand binding domain of β3 integrin. Integral role of oxygenated residues in α_IIbβ₃ (GPIIb-Ilia) receptor function. J Biol Chem 1994; 269: 20913-20919
17 Loftus JC, O’Toole TE, Plow EF, Glass A, Frelinger III AL, Ginsberg MH. A β3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 1990; 249: 915-918
18 Andrieux A, Rabiet MJ, Chapel A, Concord E, Marguerie G. A highly conserved sequence of the Arg-Gly-Asp-binding domain of the integrin beta 3 subunit is sensitive to stimulation. J Biol Chem 1991; 266: 14202-14207
19 D’Souza SE, Haas TA, Piotrowicz RS. et al Ligand and cation binding are dual functions of a discrete segment of the integrin b₃ subunit:Cation displacement is involved in ligand binding. Cell 1994; 79: 659-667
20 Charo IF, Nannizzi L, Phillips DR, Hsu MA, Scarborough RM. Inhibition of fibrinogen binding to GPIIb-IIIa by a GP IlIa peptide. J Biol Chem 1991; 266: 1414-1421
21 Tozer EC, Liddington RC, Sutcliffe MJ, Smeeton AH, Loftus JC. Ligand binding to integrin α_IIbβ₃ is dependent on a MIDAS-like domain in the β₃ subunit. J Biol Chem 1996; 271: 21978-21984
22 Bajt ML, Ginsberg MH, Frelinger III AL, Berndt MC, Loftus JC. A spontaneous mutation of integrin allbb3 (platelet Glycoprotein nb-IIIa) helps define a ligand binding site. J Biol Chem 1992; 267: 3789-3794
23 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 1990; 265: 3440-3446
24 D’Souza SE, Ginsberg MH, Matsueda GR, Plow EF. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature 1991; 350: 66-68
25 Loftus JC, Halloran CE, Ginsberg MH, Feigen LP, Zablocki JA, Smith JW. The amino-terminal one-third of α_IIb defines the ligand recognition specificity of integrin α_IIbβ₃*. Journal of Biol Chem 1996; 271: 2033-2039
26 Kamata T, Me A, Tokuhira M, Takada Y. Critical residues of integrin allb subunit for binding of allbb3 (glycoprotein Ilb-IIIa) to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2, and LJ-CP3). J Biol Chem 1996; 271: 01-30
27 Kamata T, Puzon W, Takada Y. Identification of Putative Ligand-Binding Sites of the Integrin a4bl (VLA-4, CD49d/CD29). Biochem J 1995; 305: 945-951
28 Phillips DR, Charo IF, Scarborough RM. GPIIb-IIIa: The responsive integrin. Cell 1991; 65: 359-362
29 Savage B, Shattil SJ, Ruggeri ZM. Modulation of platelet function through adhesion receptors. A dual role for glycoprotein Ilb-IIIa (integrin_αIIbβ3) mediated by fibrinogen and glycoprotein Ib-von Willebrandractor. J Biol Chem 1992; 267: 11300-11306
30 Savage B, Saldivar E, Ruggeri ZM. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von willebrand factor. Cell 1996; 84: 289-297
31 Coller BS. Interaction of normal, thrombasthenic, and Bernard-Soulier platelets with immobilized fibrinogen: Defective plate-let-fibrinogen interaction in thrombasthenia. Blood 1980; 55: 169-178
32 Du X, Plow EF, Frelinger III AL, O’Toole TE, Loftus JC, Ginsberg MH. Ligands “activate” integrin α_IIbβ₃(platelet GPIIb-IIIa). Cell 1991; 65: 409-416
33 Shattil SJ, Brass LF. Induction of the fibrinogen receptor on human platelets by intracellular mediators. J Biol Chem 1987; 262: 0992-1000
34 Hillery CA, Smyth SS, Parise LV. Phosphorylation of human platelet glycoprotein IlIa (GPIIIa). J Biol Chem 1991; 266: 14663-14669
35 van Willigen G, Hers I, Gorter G, Akkerman JWN. Exposure of the ligand-binding sites on platelet integrin α_IIbβ₃ by phosphorylation of the β₃ subunit. Biochem J 1996; 314: 768-779
36 Morii N, Teru-uchi T, Tominaga T. et al A rho gene product in human blood platelets. II. Effects of the ADP-ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation. J Biol Chem 1992; 267: 20921-20926
37 Ridley AJ, Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992; 70: 389-399
38 Kovacsovics TJ, Bachelot C, Toker A. et al Phoshoinositide 3-kinase inhibition spares actin assembly in activating platelets, but reverses platelet aggregation. J Biol Chem 1995; 270: 11358-11366
39 Chen Y, Djaffar I, Pidard D. et al Ser-752-Pro mutation in the cytoplasmic domain of integrin b3 subunit and defective activation of platelet integrin allbb3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia. Proc Natl Acad Sci USA 1992; 89: 10169-10173
40 Chen Y, O’Toole TE, Ylanne J, Rosa J, Ginsberg MH. A point mutation in the integrin ²3 cytoplasmic domain (S752-P) impairs bidirectional signaling through αllbβ3 (Platelet glycoprotein IIb-IIIa). Blood 1994; 84: 1857-1865
41 O’Toole TE, Mandelman D, Forsyth J, Shattil SJ, Plow EF, Ginsberg MH. Modulation of the affinity of integrin α_IIbβ₃ (GPIIb-IIIa) by the cytoplasmic domain of α_IIb . Science 1991; 254: 845-847
42 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: 6571-6574
43 Chen Y, O’Toole TE, Shipley T. et al “Inside-Out” signal transduction inhibited by isolated integrin cytoplasmic domains. J Biol Chem 1994; 269: 18307-18310
44 Rojiani MV, Finlay BB, Gray V, Dedhar S. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits. Biochemistry 1991; 30: 9859-9866
45 Opas M, Szewczenko-Pawlikowski M, Jass GK, Mesaeli N, Michalak M. Calreticulin modulates cell adhesiveness via regulation of vinculin expression. J Cell Biol 1996; 135: 1913-1923
46 Shattil SJ, O’Toole TE, Eigenthaler M. et al β₃ endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin β₃ subunit. J Cell Biol 1995; 131: 807-816
47 Lindberg FP, Gresham HD, Schwarz E, Brown EJ. Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in α_vβ₃-dependent ligand binding. J Cell Biol 1993; 123: 485-496
48 Shattil SJ, Ginsberg MH, Brugge JS. Adhesive signaling in blood platelets. Curr Opin Cell Biol 1994; 06: 695-704
49 Schwartz MA, Schaller MD, Ginsberg MH. Integrins: Emerging Paradigms of Signal Transduction. In: Spudich JA, Gerhart J, McKnight SL, Schekman R. eds. Annual Review of Cell and Developmental Biology. Palo Alto, California: Annual Reviews Inc; 1995: 549-599
50 Ylanne J, Chen Y, O’Toole TE, Loftus JC, Takada Y, Ginsberg MH. Distinct functions of integrin a and b subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J Cell Biol 1993; 122: 223-233
51 Ylanne J, Huuskonen J, O’Toole TE, Ginsberg MH, Virtanen I, Gahmberg CG. Mutation of the Cytoplasmic Domain of the Integrin β₃ Subunit. J Biol Chem 1995; 270: 9550-9557
52 Burridge K, Fath K, Kelley T, Nuckolls G, Turner N. Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988; 04: 487-525
53 Hartwig J, Bokoch G, Carpenter C. et al Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis inpermeabilized human platelets. Cell 1995; 82: 643-653
54 Knezevic I, Leisner T, Lam S. Direct binding of the platelet integrin α_IIbβ₃ (GPIIb-IIIa) to talin. J Biol Chem 1996; 271: 16416-16421
55 Otey CA, Pavalko FM, Burridge K. An interaction between alpha actinin and the beta 1 integrin subunit in vitro. J Cell Biol 1990; 111: 721-729
56 Ferrell Jr JE, Martin GS. Tyrosine-specific protein phosphorylation is regulated by glycoprotein Ilb-IIIa in platelets. Proc Natl Acad Sci USA 1989; 86: 2234-2238
57 Lipfert L, Haimovich B, Schaller MD, Cobb BS, Parsons JT, Brugge JS. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase ppl25FAK in platelets. J Cell Biol 1992; 119: 905-912
58 Clark EA, Shattil SJ, Ginsberg MH, Bolen J, Brugge JS. Regulation of the protein tyrosine kinase pp72SYK by platelet agonists and the integrin aIIbb3. J Biol Chem 1994; 269: 28859-28864
59 Shattil SJ, Haimovich B, Cunningham M. et al Tyrosine phosphorylation of ppl25FAK in platelets requires coordinated signaling through integrin and agonist receptors. J Biol Chem 1994; 269: 14738-14745
60 Law DA, Nannizzi-Alalmo L, Phillips DR. Outside-in integrin signal transduction: α_IIbβ₃(GPIIb-IIIa) tyrosine phosphorylation induced by platelet aggregation. J Biol Chem 1996; 271: 10811-10815
61 Wary KK, Mainiero F, Isakoff SJ, Marcantonio EE, Giancotti FG. The adaptor protein She couples a class of integrins to the control of cell cycle progression. Cell 1996; 87: 733-743
62 Clark E, Hynes R. Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A2 but not for cytoskeletal organization. J Biol Chem 1996; 271: 14814-14818
63 Chen Q, Lin TH, Der CJ, Juliano RL. Integrin-mediated activation of mitogen-activated protein (MAP) or extracellular signal-related kinase kinase (MEK) and kinase is independent of Ras. J Biol Chem 1996; 271: 18122-18127
64 Chen Q, Kinch MS, Lin TH, Burridge K, Juliano RL. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J Biol Chem 1994; 269: 26602-26605
65 Zhu X, Assoian RK. Integrin-dependent activation of MAP kinase: a link to shape-dependent cell proliferation. Mol Biol Cell 1995; 06: 273-282
66 Fujimoto T, Fujimura K, Kuramoto A. Electrophysiological evidence that glycoprotein Ilb-IIIa complex is involved in calcium channel activation on human platelet plasma membrane. J Biol Chem 1991; 266: 16370-16375
67 Fujimoto T, Fujimura K, Kuramoto A. Functional Ca²⁺ channel produced by purified platelet membrane glycoprotein Ilb-IIIa complex incorporated into planar phospholipid bilayer. Thromb. Haemostas 1991; 66: 598-603
68 Pelletier AJ, Bodary SC, Levinson AD. Signal transduction by the platelet integrin αllbβ3: induction of calcium oscillations required for protein-tyrosine phosphorylation and ligand-induced spreading of stably transfected cells. Mol Biol Cell 1992; 03: 989-998
69 Rybak ME, Renzulli LA, Bruns MJ, Cahaly DP. Platelet glycoproteins IIb and IIIa as a calcium channel in liposomes. Blood 1988; 72: 714-720
70 Schwartz MA, Brown EJ, Fazeli B. A 50-kda integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. J Biol Chem 1993; 268: 19931-19934