Functional and structural correlations of individual αIIbβ3 molecules

Blood

Volumn 104, Issue 13, 2004, Pages 3979-3985

  Litvinov, Rustem I ^b   Nagaswami, Chandrasekaran ^b   Vilaire, Gaston ^b   Shuman, Henry ^b   Bennett, Joel S ^b   Weisel, John W ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2 INTEGRIN; DITHIOTHREITOL; FIBRINOGEN; INTEGRIN; INTEGRIN ALPHA2BBETA3; MANGANESE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; CONTROLLED STUDY; CORRELATION ANALYSIS; EQUILIBRIUM CONSTANT; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROBABILITY; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; THROMBOCYTE; TRANSMISSION ELECTRON MICROSCOPY;

EID: 10244224019     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2004-04-1411     Document Type: Article

References (51)

1. Shattil SJ, Kashiwagi H, Pampori N. Integrin signaling: the platelet paradigm. Blood. 1998;91:2645-2657.
2. Bennett JS. Structural biology of glycoprotein IIb-IIIa. Trends Cardiovasc Med. 1996;6:31-37.
3. Shimaoka M, Takagi J, Springer TA. Conformational regulation of integrin structure and function. Annu Rev Biophys Biomol Struct. 2002;31:485-516.
4. i-coupled pathways is essential for agonist-induced αvβ3 activation on human platelets. J Thrombos Haemostas. 2003;1:814-820.
5. Macintyre DE, Gordon JL. Evidence for two populations of disulfide bonds in blood platelets. Biochem Soc Trans. 1974;2:873-875.
6. Zucker MB, Masiello NC. Platelet aggregation caused by dithiothreitol. Thromb Haemostas. 1984;51:119-124.
7. Peerschke EI. Stabilization of platelet-fibrinogen interactions: modulation by divalent cations. J Lab Clin Med. 1993;121:135-141.
8. Kirchhofer D, Gailit J, Ruoslahti E, Grzesiak J, Pierschbacher MD. Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa. J Biol Chem. 1990;265:18525-18530.
9. Smith J, Piotrowicz R, Mathis D. A mechanism for divalent cation regulation of beta 3-integrins. J Biol Chem. 1994;267:960-967.
10. Suehiro K, Smith JW, Plow EF. The ligand recognition specificity of beta3 integrins. J Biol Chem. 1996;271:10365-10371.
11. Cierniewski CS, Byzova T, Papierak M, et al. Peptide ligands can bind to distinct sites in integrin alphaIIbbeta3 and elicit different functional responses. J Biol Chem. 1999;274:16923-16932.
12. Yan B, Hu DD, Knowles SK, Smith JW. Probing chemical and conformational differences in the resting and active conformers of platelet integrin alpha(IIb)beta(3). J Biol Chem. 2000;275:7249-7260.
13. Takagi J, Petre B, Walz T, Springer T. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell. 2002;110:599-611.
14. 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.
15. Adair BD, Yeager M. Three-dimensional model of the human platelet integrin alpha IIbbeta 3 based on electron cryomicroscopy and x-ray crystallography. Proc Natl Acad Sci U S A. 2002;99:14059-14064.
16. Yan B, Smith JW. Mechanism of integrin activation by disulfide bond reduction. Biochemistry. 2001;40:8861-8867.
17. Chen P, Melchior C, Brons NH, Schlegel N, Caen J, Kieffer N. Probing conformational changes in the I-like domain and the cysteine-rich repeat of human beta 3 integrins following disulfide bond disruption by cysteine mutations: identification of cysteine 598 involved in alphaIIbbeta3 activation. J Biol Chem. 2001;276:38628-38635.
18. Litvinov RI, Shuman H, Bennett JS, Weisel JW. Binding strength and activation state of single fibrinogen-integrin pairs on living cells. Proc Natl Acad Sci U S A. 2002;99:7426-7431.
19. Fowler WE, Erickson HP. Trinodular structure of fibrinogen. Confirmation by both shadowing and negative stain electron microscopy. J Mol Biol. 1979;134:241-249.
20. Weisel JW, Stauffacher CV, Bullitt E, Cohen C. A model for fibrinogen: domains and sequence. Science. 1985;230:1388-1391.
21. Veklich YI, Gorkun OV, Medved LV, Nieuwenhuizen W, Weisel JW. Carboxyl-terminal portions of the alpha chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated alpha C fragments on polymerization. J Biol Chem. 1993;268:13577-13585.
22. 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. 1992;267:18844-18851.
23. Weisel JW, Nagaswami C, Vilaire G, Bennett JS. Examination of the platelet membrane glycoprotein IIb/IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. J Biol Chem. 1992;267:16637-16643.
24. Zaner KS. Physics of actin networks. I. Rheology of semi-dilute F-actin. Biophys J. 1995;68:1019-1026.
25. Tuszynski JA, Brown JA, Sept D. Models of the collective behavior of proteins in cells: tubulin, actin, and motor proteins. J Biol Phys. 2003;29:401-428.
26. Briehl RW, Mann ES, Josephs R. Length distributions of hemoglobin S fibers. J Mol Biol. 1990; 211:693-698.
27. Masel J, Jansen VA. The kinetics of proteinase K digestion of linear prion polymers. Proc R Soc Lond B Biol Sci. 1999;266:1927-1931.
28. Basani RB, D'Andrea G, Mitra N, et al. RGD-containing 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.
29. Niewiarowski S, Kornecki E, Hershock D, et al. Aggregation of chymotrypsin-treated thrombasthenic platelets is mediated by fibrinogen binding to glycoproteins IIb and IIIa. J Lab Clin Med. 1985;106:651-660.
30. Ginsberg MH, Lightsey A, Kunicki TJ, Kaufmann A, Marguerie G, Plow EF. Divalent cation regulation of the surface orientation of platelet membrane glycoprotein IIb. J Clin Invest. 1986;78:1103-1111.
31. Masumoto A, Hemler ME. Mutation of putative divalent cation sites in the alpha 4 subunit of the integrin VLA-4: distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin. J Cell Biol. 1993;123:245-253.
32. Helluin O, Chan C, Vilaire G, Mousa S, DeGrado WF, Bennett JS. The activation state of αvβ3 regulates platelet and lymphocyte adhesion to intact and thrombin-cleaved osteopontin. J Biol Chem. 2000;275:18337-18343.
33. 3 and to calcium- and integrin-binding protein. J Biol Chem. 1999;274:17257-17266.
34. Kim M, Carman CV, Springer TA. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science. 2003;301:1720-1725.
35. Honda S, Tomiyama Y, Pampori N, et al. Ligand binding to integrin alpha(v)beta(3) requires tyrosine 178 in the alpha(v) subunit. Blood. 2001; 97:175-182.
36. Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 2003;22:4607-4615.
37. Buensuceso C, de Virgilio M, Shattil SJ. Detection of integrin alpha IIbbeta 3 clustering in living cells. J Biol Chem. 2003;278:15217-15224.
38. Xiong JP, Stehle T, Diefenbach B, et al. Crystal structure of the extracellular segment of integrin αVβ3. Science. 2001;294:339-345.
39. Visscher K, Block SM. Versatile optical traps with feedback control. Methods Enzymol. 1998;298:460-489.
40. Weisel JW, Shuman H, Litvinov RI. Protein-protein unbinding induced by force: single-molecule studies. Curr Opin Struct Biol. 2003;13:227-235.
41. Masumoto A, Hemler ME. Multiple activation states of VLA-4. Mechanistic differences between adhesion to CS1/fibronectin and to vascular cell adhesion molecule-1. J Biol Chem. 1993;268:228-234.
42. Chigaev A, Blenc AM, Braaten JV, et al. Real time analysis of the affinity regulation of alpha 4-integrin. The physiologically activated receptor is intermediate in affinity between resting and Mn(2+) or antibody activation. J Biol Chem. 2001;276:48670-48678.
43. Chigaev A, Zwartz GJ, Buranda T, Edwards BS, Prossnitz ER, Sklar LA. Conformational regulation of the alpha 4beta 1-integrin affinity by reducing agents: "inside-out" signaling is independent and additive to reduction-regulated integrin activation. J Biol Chem. 2004;279:32435-32443.
44. Mould AP, Symonds EJ, Buckley PA, et al. Structure of an integrin-ligand complex deduced from solution x-ray scattering and site-directed mutagenesis. J Biol Chem. 2003;278:39993-39999.
45. Li R, Mitra N, Gratkowski H, et al. Activation of integrin alphaIIbbeta3 by modulation of transmembrane helix associations. Science. 2003; 300:795-798.
46. Mould AP, Barton SJ, Askari JA, et al. Conformational changes in the integrin beta A domain provide a mechanism for signal transduction via hybrid domain movement. J Biol Chem. 2003;278:17028-17035.
47. Yang W, Shimaoka M, Chen J, Springer TA. Activation of integrin beta-subunit I-like domains by one-turn C-terminal alpha-helix deletions. Proc Natl Acad Sci U S A. 2004;101:2333-2338.
48. 3 and its ligand and induces selective movements of ligand- occupied integrin. J Biol Chem. 1996;271:7004-7011.
49. 3. J Cell Biol. 1998;141:1685-1695.
50. Hantgan RR, Paumi C, Rocco M, Weisel JW. Effects of ligand-mimetic peptides Arg-Gly-Asp-X (X = Phe, Trp, Ser) on αIIbβ3 integrin conformation and oligomerization. Biochemistry. 1999;38:14461-14474.
51. Hantgan RR, Lyles DS, Mallett TC, Rocco M, Nagaswami C, Weisel JW. Ligand binding promotes the entropy-driven oligomerization of integrin αIIbβ3. J Biol Chem. 2003;278:3417-3426.