Download PDF
Thromb Haemost 1997; 78(01): 096-100
DOI: 10.1055/s-0038-1657508
Integrin signalling and vascular function
Schattauer GmbH Stuttgart

Integrin αIIbβ3 and Platelet Function

X Du
1   Department of Pharmacology, University of Illinois at Chicago, College of Medicine, Chicago, IL
,
Mark H Ginsberg
2   Department of Vascular Biology, The Scripps Research Institute, La Jolla, CA, USA
› Author Affiliations
Further Information

Publication History

Publication Date:
12 July 2018 (online)

  PDF Download  Permissions and Reprints
 

  • References

  • 1 Ginsberg MH, Du X, O’Toole TE, Loftus JC. Platelet Integrins. Thromb. Haemo stas 1995; 74: 352-359
    PubMedGoogle Scholar
  • 2 Smyth SS, Joneckis CC, Parise LV. Regulation of vascular integrins. Blood 1993; 81: 2827-2843
    PubMedGoogle Scholar
  • 3 Phillips DR, Charo IF, Parise LV, Fitzgerald LA. The platelet membrane glycoprotein Ilb-IIIa complex. Blood 1988; 71: 831-843
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 7 Du X, Gu M, Weisel JW. et al Long range propagation of conformational changes in integrin αIIbβ3 . J Biol Chem 1993; 268: 23087-23092
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 9 Haas TA, Plow EF. The cytoplasmic domain of αIIbβ3 . J Biol Chem 1996; 271: 6017-6026
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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 αIIbβ3 . EMBO J 1996; 15: 5760-5771
    PubMedGoogle Scholar
  • 13 Farrell DH, Thiagarajan P. Binding of recombinant fibrinogen mutants to platelets. J Biol Chem 1994; 269: 226-231
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 16 Bajt ML, Loftus JC. Mutation of a ligand binding domain of β3 integrin. Integral role of oxygenated residues in αIIbβ3 (GPIIb-Ilia) receptor function. J Biol Chem 1994; 269: 20913-20919
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 21 Tozer EC, Liddington RC, Sutcliffe MJ, Smeeton AH, Loftus JC. Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit. J Biol Chem 1996; 271: 21978-21984
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 25 Loftus JC, Halloran CE, Ginsberg MH, Feigen LP, Zablocki JA, Smith JW. The amino-terminal one-third of αIIb defines the ligand recognition specificity of integrin αIIbβ3*. Journal of Biol Chem 1996; 271: 2033-2039
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 28 Phillips DR, Charo IF, Scarborough RM. GPIIb-IIIa: The responsive integrin. Cell 1991; 65: 359-362
    CrossrefPubMedGoogle Scholar
  • 29 Savage B, Shattil SJ, Ruggeri ZM. Modulation of platelet function through adhesion receptors. A dual role for glycoprotein Ilb-IIIa (integrinαIIbβ3) mediated by fibrinogen and glycoprotein Ib-von Willebrandractor. J Biol Chem 1992; 267: 11300-11306
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 32 Du X, Plow EF, Frelinger III AL, O’Toole TE, Loftus JC, Ginsberg MH. Ligands “activate” integrin αIIbβ3(platelet GPIIb-IIIa). Cell 1991; 65: 409-416
    CrossrefPubMedGoogle Scholar
  • 33 Shattil SJ, Brass LF. Induction of the fibrinogen receptor on human platelets by intracellular mediators. J Biol Chem 1987; 262: 0992-1000
    PubMedGoogle Scholar
  • 34 Hillery CA, Smyth SS, Parise LV. Phosphorylation of human platelet glycoprotein IlIa (GPIIIa). J Biol Chem 1991; 266: 14663-14669
    PubMedGoogle Scholar
  • 35 van Willigen G, Hers I, Gorter G, Akkerman JWN. Exposure of the ligand-binding sites on platelet integrin αIIbβ3 by phosphorylation of the β3 subunit. Biochem J 1996; 314: 768-779
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 41 O’Toole TE, Mandelman D, Forsyth J, Shattil SJ, Plow EF, Ginsberg MH. Modulation of the affinity of integrin αIIbβ3 (GPIIb-IIIa) by the cytoplasmic domain of αIIb . Science 1991; 254: 845-847
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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 αvβ3-dependent ligand binding. J Cell Biol 1993; 123: 485-496
    CrossrefPubMedGoogle Scholar
  • 48 Shattil SJ, Ginsberg MH, Brugge JS. Adhesive signaling in blood platelets. Curr Opin Cell Biol 1994; 06: 695-704
    CrossrefPubMedGoogle Scholar
  • 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
    Google Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 54 Knezevic I, Leisner T, Lam S. Direct binding of the platelet integrin αIIbβ3 (GPIIb-IIIa) to talin. J Biol Chem 1996; 271: 16416-16421
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 60 Law DA, Nannizzi-Alalmo L, Phillips DR. Outside-in integrin signal transduction: αIIbβ3(GPIIb-IIIa) tyrosine phosphorylation induced by platelet aggregation. J Biol Chem 1996; 271: 10811-10815
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    CrossrefPubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar
  • 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
    PubMedGoogle Scholar