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Volumn 3, Issue 2, 2003, Pages 125-140

Inhibition of platelet adhesion to collagen as a new target for antithrombotic drugs

Author keywords

Antiplatelet agent; Antithrombotic; Glycoprotein Ib V IX; Glycoprotein VI; In vivo; Integrin 2 1; Von Willebrand factor

Indexed keywords

ADENOSINE DIPHOSPHATE; ANTICOAGULANT AGENT; ANTITHROMBOCYTIC AGENT; AURINTRICARBOXYLIC ACID; COLLAGEN; FIBRINOGEN; FIBRINOGEN RECEPTOR; FIBRINOLYTIC AGENT; GINKGOLIDE B; GLYCOPROTEIN; GLYCOPROTEIN IB; HIRUDIN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; INTEGRIN; MONOCLONAL ANTIBODY; MONOCROTALINE; RECEPTOR SUBTYPE; RECOMBINANT PROTEIN; SNAKE VENOM; THROMBOCYTE ACTIVATING FACTOR ANTAGONIST; THROMBOCYTE RECEPTOR; TRIFLAVIN; VERY LATE ACTIVATION ANTIGEN 2; VON WILLEBRAND FACTOR;

EID: 0038780817     PISSN: 15680061     EISSN: None     Source Type: Journal    
DOI: 10.2174/1568006033481500     Document Type: Review
Times cited : (40)

References (130)
  • 1
    • 0033635085 scopus 로고    scopus 로고
    • Structural determinants within platelet glycoprotein Ibalpha involved in its binding to von Willebrand factor
    • Cauwenberghs, N.; Vanhoorelbeke, K.; Vauterin, S.; Deckmyn, H. Structural determinants within platelet glycoprotein Ibalpha involved in its binding to von Willebrand factor. Platelets, 2000, 11, 373.
    • (2000) Platelets , vol.11 , pp. 373
    • Cauwenberghs, N.1    Vanhoorelbeke, K.2    Vauterin, S.3    Deckmyn, H.4
  • 2
    • 0029000368 scopus 로고
    • Platelet-collagen interactions
    • Kehrel, B. Platelet-collagen interactions. Semin. Thromb. Hemost., 1995, 21, 123.
    • (1995) Semin. Thromb. Hemost. , vol.21 , pp. 123
    • Kehrel, B.1
  • 5
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage, B.; Saldivar, E.; Ruggeri, Z.M. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell, 1996, 84, 289.
    • (1996) Cell , vol.84 , pp. 289
    • Savage, B.1    Saldivar, E.2    Ruggeri, Z.M.3
  • 6
    • 0022922723 scopus 로고
    • Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen
    • Santoro, S.A. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen. Cell, 1986, 46, 913.
    • (1986) Cell , vol.46 , pp. 913
    • Santoro, S.A.1
  • 7
    • 0031973037 scopus 로고    scopus 로고
    • Glycoprotein VI is a major collagen receptor for platelet activation: It recognizes the platelet-activating quaternary structure of collagen, whereas CD36, glycoprotein IIb/IIIa, and von Willebrand factor do not
    • Kehrel, B.; Wierwille, S.; Clemetson, K.J.; Anders, O.; Steiner, M.; Knight, C.G.; Farndale, R.W.; Okuma, M.; Barnes, M.J. Glycoprotein VI is a major collagen receptor for platelet activation: it recognizes the platelet-activating quaternary structure of collagen, whereas CD36, glycoprotein IIb/IIIa, and von Willebrand factor do not. Blood, 1998, 91, 491.
    • (1998) Blood , vol.91 , pp. 491
    • Kehrel, B.1    Wierwille, S.2    Clemetson, K.J.3    Anders, O.4    Steiner, M.5    Knight, C.G.6    Farndale, R.W.7    Okuma, M.8    Barnes, M.J.9
  • 8
    • 0034910567 scopus 로고    scopus 로고
    • A monoclonal antibody to platelet type III collagen-binding protein (TIIICBP) binds to blood and vascular cells, and inhibits platelet vessel-wall interactions
    • Monnet, E.; Depraetere, H.; Legrand, C.; Deckmyn, H.; Fauvel-Lafeve, F. A monoclonal antibody to platelet type III collagen-binding protein (TIIICBP) binds to blood and vascular cells, and inhibits platelet vessel-wall interactions. Thromb. Haemost., 2001, 86, 694.
    • (2001) Thromb. Haemost. , vol.86 , pp. 694
    • Monnet, E.1    Depraetere, H.2    Legrand, C.3    Deckmyn, H.4    Fauvel-Lafeve, F.5
  • 9
    • 0034646596 scopus 로고    scopus 로고
    • A new platelet receptor specific to type III collagen. Type III collagen-binding protein
    • Monnet, E.; Fauvel-Lafeve, F. A new platelet receptor specific to type III collagen. Type III collagen-binding protein. J. Biol. Chem., 2000, 275, 10912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10912
    • Monnet, E.1    Fauvel-Lafeve, F.2
  • 10
    • 0027291222 scopus 로고
    • The role of protein phosphatases 1 and 2A in collagen-platelet interaction
    • Chiang, T.M. The role of protein phosphatases 1 and 2A in collagen-platelet interaction. Arch. Biochem. Biophys., 1993, 302, 56.
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 56
    • Chiang, T.M.1
  • 12
    • 0026557780 scopus 로고
    • Disturbed platelet aggregation to collagen associated with an antibody against an 85-to 90-Kd platelet glycoprotein in a patient with prolonged bleeding time
    • Deckmyn, H.; Van Houtte, E.; Vermylen, J. Disturbed platelet aggregation to collagen associated with an antibody against an 85-to 90-Kd platelet glycoprotein in a patient with prolonged bleeding time. Blood, 1992, 79, 1466.
    • (1992) Blood , vol.79 , pp. 1466
    • Deckmyn, H.1    Van Houtte, E.2    Vermylen, J.3
  • 14
    • 0027125530 scopus 로고
    • The pathogenesis of coronary artery disease and the acute coronary syndromes (1)
    • Fuster, V.; Badimon, L.; Badimon, J.J.; Chesebro, J.H. The pathogenesis of coronary artery disease and the acute coronary syndromes (1). N. Engl. J. Med, 1992, 326, 242.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 242
    • Fuster, V.1    Badimon, L.2    Badimon, J.J.3    Chesebro, J.H.4
  • 15
    • 0001145542 scopus 로고
    • Role of platelets in smooth muscle cell proliferation and migration after vascular injury in rat carotid artery
    • Fingerle, J.; Johnson, R.; Clowes, A.W.; Majesky, M.W.; Reidy, M.A. Role of platelets in smooth muscle cell proliferation and migration after vascular injury in rat carotid artery. Proc. Natl. Acad Sci. USA, 1989, 86, 8412.
    • (1989) Proc. Natl. Acad Sci. USA , vol.86 , pp. 8412
    • Fingerle, J.1    Johnson, R.2    Clowes, A.W.3    Majesky, M.W.4    Reidy, M.A.5
  • 17
    • 0028274014 scopus 로고
    • The platelet glycoprotein Ib-IX complex
    • Lopez, J.A. The platelet glycoprotein Ib-IX complex. Blood Coagul. Fibrinolysis, 1994, 5, 97.
    • (1994) Blood Coagul. Fibrinolysis , vol.5 , pp. 97
    • Lopez, J.A.1
  • 18
    • 0025162162 scopus 로고
    • Identification of a site in the alpha chain of platelet glycoprotein Ib that participates in von Willebrand factor binding
    • Vicente, V.; Houghten, R.A.; Ruggeri, Z.M. Identification of a site in the alpha chain of platelet glycoprotein Ib that participates in von Willebrand factor binding. J. Biol. Chem., 1990, 265, 274.
    • (1990) J. Biol. Chem. , vol.265 , pp. 274
    • Vicente, V.1    Houghten, R.A.2    Ruggeri, Z.M.3
  • 19
    • 0033635085 scopus 로고    scopus 로고
    • Structural determinants within platelet glycoprotein Ibalpha involved in its binding to von Willebrand factor
    • Cauwenberghs, N.; Vanhoorelbeke, K.; Vauterin, S.; Deckmyn, H. Structural determinants within platelet glycoprotein Ibalpha involved in its binding to von Willebrand factor. Platelets, 2000, 11, 373.
    • (2000) Platelets , vol.11 , pp. 373
    • Cauwenberghs, N.1    Vanhoorelbeke, K.2    Vauterin, S.3    Deckmyn, H.4
  • 21
    • 0037144544 scopus 로고    scopus 로고
    • Crystal Structure of the Platelet Glycoprotein Ibalpha N-terminal Domain Reveals an Unmasking Mechanism for Receptor Activation
    • Uff, S.; Clemetson, J.M.; Harrison, T.; Clemetson, K.J.; Emsley, J. Crystal Structure of the Platelet Glycoprotein Ibalpha N-terminal Domain Reveals an Unmasking Mechanism for Receptor Activation. J. Biol. Chem., 2002, 277, 35657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35657
    • Uff, S.1    Clemetson, J.M.2    Harrison, T.3    Clemetson, K.J.4    Emsley, J.5
  • 23
    • 0016862422 scopus 로고
    • Specific roles for platelet surface glycoproteins in platelet function
    • Nurden, A.T.; Caen, J.P. Specific roles for platelet surface glycoproteins in platelet function. Nature, 1975, 255, 720.
    • (1975) Nature , vol.255 , pp. 720
    • Nurden, A.T.1    Caen, J.P.2
  • 25
    • 0026720406 scopus 로고
    • Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness
    • Murata, M.; Furihata, K.; Ishida, F.; Russell, S.R.; Ware, J.; Ruggeri, Z.M. Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness. Blood, 1992, 79, 3086.
    • (1992) Blood , vol.79 , pp. 3086
    • Murata, M.1    Furihata, K.2    Ishida, F.3    Russell, S.R.4    Ware, J.5    Ruggeri, Z.M.6
  • 26
    • 0033162507 scopus 로고    scopus 로고
    • Polymorphisms of platelet membrane glycoprotein Ib alpha and plasma von Willebrand factor antigen in coronary artery disease
    • Ito, T.; Ishida, F.; Shimodaira, S.; Kitano, K. Polymorphisms of platelet membrane glycoprotein Ib alpha and plasma von Willebrand factor antigen in coronary artery disease. Int. J Hematol., 1999, 70, 47.
    • (1999) Int. J Hematol. , vol.70 , pp. 47
    • Ito, T.1    Ishida, F.2    Shimodaira, S.3    Kitano, K.4
  • 27
    • 0032079569 scopus 로고    scopus 로고
    • Inherited platelet glycoprotein polymorphisms and a risk for coronary heart disease in young central Europeans
    • Sperr, W.R.; Huber, K.; Roden, M.; Janisiw, M.; Lang, T.; Graf, S.; Maurer, G.; Mayr, W.R.; Panzer, S. Inherited platelet glycoprotein polymorphisms and a risk for coronary heart disease in young central Europeans. Thromb. Res., 1998, 90, 117.
    • (1998) Thromb. Res. , vol.90 , pp. 117
    • Sperr, W.R.1    Huber, K.2    Roden, M.3    Janisiw, M.4    Lang, T.5    Graf, S.6    Maurer, G.7    Mayr, W.R.8    Panzer, S.9
  • 32
    • 0035928604 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibalpha HPA-2 Met/VNTR B haplotype as a genetic predictor of myocardial infarction and sudden cardiac death
    • Mikkelsson, J.; Perola, M.; Penttila, A.; Karhunen, P.J. Platelet glycoprotein Ibalpha HPA-2 Met/VNTR B haplotype as a genetic predictor of myocardial infarction and sudden cardiac death. Circulation, 2001, 104, 876.
    • (2001) Circulation , vol.104 , pp. 876
    • Mikkelsson, J.1    Perola, M.2    Penttila, A.3    Karhunen, P.J.4
  • 33
    • 0034646267 scopus 로고    scopus 로고
    • Generation and rescue of a murine model of platelet dysfunction: The Bernard-Soulier syndrome
    • Ware, J.; Russell, S.; Ruggeri, Z.M. Generation and rescue of a murine model of platelet dysfunction: the Bernard-Soulier syndrome. Proc. Natl. Acad. Sci. USA, 2000, 97, 2803.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2803
    • Ware, J.1    Russell, S.2    Ruggeri, Z.M.3
  • 34
    • 0032795849 scopus 로고    scopus 로고
    • Glycoprotein V-deficient platelets have undiminished thrombin responsiveness and Do not exhibit a Bernard-Soulier phenotype
    • Kahn, M.L.; Diacovo, T.G.; Bainton, D.F.; Lanza, F.; Trejo, J.; Coughlin, S.R. Glycoprotein V-deficient platelets have undiminished thrombin responsiveness and Do not exhibit a Bernard-Soulier phenotype. Blood, 1999, 94, 4112.
    • (1999) Blood , vol.94 , pp. 4112
    • Kahn, M.L.1    Diacovo, T.G.2    Bainton, D.F.3    Lanza, F.4    Trejo, J.5    Coughlin, S.R.6
  • 37
    • 0028361191 scopus 로고
    • Relative antithrombotic effects of monoclonal antibodies targeting different platelet glycoprotein-adhesive molecule interactions in nonhuman primates
    • Cadroy, Y.; Hanson, S.R.; Kelly, A.B.; Marzec, U.M.; Evatt, B.L.; Kunicki, T.J.; Montgomery, R.R.; Harker, L.A. Relative antithrombotic effects of monoclonal antibodies targeting different platelet glycoprotein-adhesive molecule interactions in nonhuman primates. Blood, 1994, 83, 3218.
    • (1994) Blood , vol.83 , pp. 3218
    • Cadroy, Y.1    Hanson, S.R.2    Kelly, A.B.3    Marzec, U.M.4    Evatt, B.L.5    Kunicki, T.J.6    Montgomery, R.R.7    Harker, L.A.8
  • 39
    • 0024392126 scopus 로고
    • Effects of an antiplatelet glycoprotein Ib antibody on hemostatic function in the guinea pig
    • Becker, B.H.; Miller, J.L. Effects of an antiplatelet glycoprotein Ib antibody on hemostatic function in the guinea pig. Blood, 1989, 74, 690.
    • (1989) Blood , vol.74 , pp. 690
    • Becker, B.H.1    Miller, J.L.2
  • 40
    • 0025800330 scopus 로고
    • Reduction in thrombus formation by PG-1 F(ab′)2, an anti-guinea pig platelet glycoprotein Ib monoclonal antibody
    • Miller, J.L.; Thiam-Cisse, M.; Drouet, L.O. Reduction in thrombus formation by PG-1 F(ab′)2, an anti-guinea pig platelet glycoprotein Ib monoclonal antibody. Arterioscler. Thromb., 1991, 11, 1231.
    • (1991) Arterioscler. Thromb. , vol.11 , pp. 1231
    • Miller, J.L.1    Thiam-Cisse, M.2    Drouet, L.O.3
  • 41
    • 0036162199 scopus 로고    scopus 로고
    • Inhibition of platelet glycoprotein Ib, glycoprotein IIb/IIIa, or both by monoclonal antibodies prevents arterial thrombosis in baboons
    • Wu, D.; Meiring, M.; Kotze, H.F.; Deckmyn, H.; Cauwenberghs, N. Inhibition of platelet glycoprotein Ib, glycoprotein IIb/IIIa, or both by monoclonal antibodies prevents arterial thrombosis in baboons. Arterioscler. Thromb. Vasc. Biol., 2002, 22, 323.
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 323
    • Wu, D.1    Meiring, M.2    Kotze, H.F.3    Deckmyn, H.4    Cauwenberghs, N.5
  • 42
    • 0026730092 scopus 로고
    • A monomeric von Willebrand factor fragment, Leu-504--Lys-728, inhibits von Willebrand factor interaction with glycoprotein Ib-IX
    • [corrected]
    • Gralnick, H.R.; Williams, S.; McKeown, L.; Kramer, W.; Krutzsch, H.; Gorecki, M.; Pinet, A.; Garfinkel, L.I. A monomeric von Willebrand factor fragment, Leu-504--Lys-728, inhibits von Willebrand factor interaction with glycoprotein Ib-IX [corrected]. Proc. Natl. Acad Sci. USA, 1992, 89, 7880.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 7880
    • Gralnick, H.R.1    Williams, S.2    McKeown, L.3    Kramer, W.4    Krutzsch, H.5    Gorecki, M.6    Pinet, A.7    Garfinkel, L.I.8
  • 43
    • 0028641293 scopus 로고
    • Abolition of cyclic flow variations in stenosed, endothelium-injured coronary arteries in nonhuman primates with a peptide fragment (VCL) derived from human plasma von Willebrand factor-glycoprotein Ib binding domain
    • McGhie, A.I.; McNatt, J.; Ezov, N.; Cui, K.; Mower, L.K.; Hagay, Y.; Buja, L.M.; Garfinkel, L.I.; Gorecki, M.; Willerson, J.T. Abolition of cyclic flow variations in stenosed, endothelium-injured coronary arteries in nonhuman primates with a peptide fragment (VCL) derived from human plasma von Willebrand factor-glycoprotein Ib binding domain. Circulation, 1994, 90, 2976.
    • (1994) Circulation , vol.90 , pp. 2976
    • McGhie, A.I.1    McNatt, J.2    Ezov, N.3    Cui, K.4    Mower, L.K.5    Hagay, Y.6    Buja, L.M.7    Garfinkel, L.I.8    Gorecki, M.9    Willerson, J.T.10
  • 44
    • 0028240844 scopus 로고
    • Blockade of platelet membrane glycoprotein Ib receptors delays intracoronary thrombogenesis, enhances thrombolysis, and delays coronary artery reocclusion in dogs
    • Yao, S.K.; Ober, J.C.; Garfinkel, L.I.; Hagay, Y.; Ezov, N.; Ferguson, J.J.; Anderson, H.V.; Panet, A.; Gorecki, M.; Buja, L.M.; . Blockade of platelet membrane glycoprotein Ib receptors delays intracoronary thrombogenesis, enhances thrombolysis, and delays coronary artery reocclusion in dogs. Circulation, 1994, 89, 2822.
    • (1994) Circulation , vol.89 , pp. 2822
    • Yao, S.K.1    Ober, J.C.2    Garfinkel, L.I.3    Hagay, Y.4    Ezov, N.5    Ferguson, J.J.6    Anderson, H.V.7    Panet, A.8    Gorecki, M.9    Buja, L.M.10
  • 45
    • 0028804347 scopus 로고
    • Antithrombotic effect of a recombinant von Willebrand factor, VCL, on nitrogen laser-induced thrombus formation in guinea pig mesenteric arteries
    • Azzam, K.; Garfinkel, L.I.; Bal dit, S.C.; Cisse, T.M.; Drouet, L. Antithrombotic effect of a recombinant von Willebrand factor, VCL, on nitrogen laser-induced thrombus formation in guinea pig mesenteric arteries. Thromb. Haemost., 1995, 73, 318.
    • (1995) Thromb. Haemost. , vol.73 , pp. 318
    • Azzam, K.1    Garfinkel, L.I.2    Bal dit, S.C.3    Cisse, T.M.4    Drouet, L.5
  • 47
    • 0032031490 scopus 로고    scopus 로고
    • Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib antagonist from venom of Crotalus atrox
    • Chang, M.C.; Lin, H.K.; Peng, H.C.; Huang, T.F. Antithrombotic effect of crotalin, a platelet membrane glycoprotein Ib antagonist from venom of Crotalus atrox. Blood, 1998, 91, 1582.
    • (1998) Blood , vol.91 , pp. 1582
    • Chang, M.C.1    Lin, H.K.2    Peng, H.C.3    Huang, T.F.4
  • 48
    • 0035127166 scopus 로고    scopus 로고
    • Pharmacological characterization and antithrombotic effect of agkistin, a platelet glycoprotein Ib antagonist
    • Yeh, C.H.; Chang, M.C.; Peng, H.C.; Huang, T.F. Pharmacological characterization and antithrombotic effect of agkistin, a platelet glycoprotein Ib antagonist. Br. J. Pharmacol., 2001, 132, 843.
    • (2001) Br. J. Pharmacol. , vol.132 , pp. 843
    • Yeh, C.H.1    Chang, M.C.2    Peng, H.C.3    Huang, T.F.4
  • 49
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler, J.E. Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem., 1998, 67, 395.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 395
    • Sadler, J.E.1
  • 50
    • 0022649078 scopus 로고
    • von Willebrand factor. A reduced and alkylated 52/48-kDa fragment beginning at amino acid residue 449 contains the domain interacting with platelet glycoprotein Ib
    • Fujimura, Y.; Titani, K.; Holland, L.Z.; Russell, S.R.; Roberts, J.R.; Elder, J.H.; Ruggeri, Z.M.; Zimmerman, T.S. von Willebrand factor. A reduced and alkylated 52/48-kDa fragment beginning at amino acid residue 449 contains the domain interacting with platelet glycoprotein Ib. J. Biol. Chem., 1986, 261, 381.
    • (1986) J. Biol. Chem. , vol.261 , pp. 381
    • Fujimura, Y.1    Titani, K.2    Holland, L.Z.3    Russell, S.R.4    Roberts, J.R.5    Elder, J.H.6    Ruggeri, Z.M.7    Zimmerman, T.S.8
  • 51
    • 0036371063 scopus 로고    scopus 로고
    • Molecular and cellular biology of von Willebrand factor
    • Denis, C.V. Molecular and cellular biology of von Willebrand factor. Int. J. Hematol., 2002, 75, 3.
    • (2002) Int. J. Hematol. , vol.75 , pp. 3
    • Denis, C.V.1
  • 52
    • 0030970681 scopus 로고    scopus 로고
    • von Willebrand factor binds to native collagen VI primarily via its A1 domain
    • Hoylaerts, M.F.; Yamamoto, H.; Nuyts, K.; Vreys, I.; Deckmyn, H.; Vermylen, J. von Willebrand factor binds to native collagen VI primarily via its A1 domain. Biochem. J., 1997, 324 (Pt 1), 185.
    • (1997) Biochem. J. , vol.324 , Issue.PART 1 , pp. 185
    • Hoylaerts, M.F.1    Yamamoto, H.2    Nuyts, K.3    Vreys, I.4    Deckmyn, H.5    Vermylen, J.6
  • 54
    • 0023938680 scopus 로고
    • Generation and characterization of peptide-specific antibodies that inhibit von Willebrand factor binding to glycoprotein IIb-IIIa without interacting with other adhesive molecules. Selectivity is conferred by Pro1743 and other amino acid residues adjacent to the sequence Arg1744- Gly1745-Asp1746
    • Berliner, S.; Niiya, K.; Roberts, J.R.; Houghten, R.A.; Ruggeri, Z.M. Generation and characterization of peptide-specific antibodies that inhibit von Willebrand factor binding to glycoprotein IIb-IIIa without interacting with other adhesive molecules. Selectivity is conferred by Pro1743 and other amino acid residues adjacent to the sequence Arg1744- Gly1745-Asp1746. J. Biol. Chem., 1988, 263, 7500.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7500
    • Berliner, S.1    Niiya, K.2    Roberts, J.R.3    Houghten, R.A.4    Ruggeri, Z.M.5
  • 55
    • 0028201807 scopus 로고
    • A revised classification of von Willebrand disease
    • For the Subcommittee on von Willebrand Factor of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis
    • Sadler, J.E. A revised classification of von Willebrand disease. For the Subcommittee on von Willebrand Factor of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb. Haemost., 1994, 71, 520.
    • (1994) Thromb. Haemost. , vol.71 , pp. 520
    • Sadler, J.E.1
  • 56
    • 0031047775 scopus 로고    scopus 로고
    • Von Willebrand's disease
    • Ewenstein, B.M. Von Willebrand's disease. Annu. Rev. Med, 1997, 48, 525.
    • (1997) Annu. Rev. Med. , vol.48 , pp. 525
    • Ewenstein, B.M.1
  • 57
    • 0033385938 scopus 로고    scopus 로고
    • Insights from von Willebrand disease animal models
    • Denis, C.V.; Wagner, D.D. Insights from von Willebrand disease animal models. Cell Mol. Life Sci., 1999, 56, 977.
    • (1999) Cell Mol. Life Sci. , vol.56 , pp. 977
    • Denis, C.V.1    Wagner, D.D.2
  • 59
    • 0025328434 scopus 로고
    • von Willebrand factor and occlusive arterial thrombosis. A study in normal and von Willebrand's disease pigs with diet-induced hypercholesterolemia and atherosclerosis
    • Nichols, T.C.; Bellinger, D.A.; Tate, D.A.; Reddick, R.L.; Read, M.S.; Koch, G.G.; Brinkhous, K.M.; Griggs, T.R. von Willebrand factor and occlusive arterial thrombosis. A study in normal and von Willebrand's disease pigs with diet-induced hypercholesterolemia and atherosclerosis. Arteriosclerosis, 1990, 10, 449.
    • (1990) Arteriosclerosis , vol.10 , pp. 449
    • Nichols, T.C.1    Bellinger, D.A.2    Tate, D.A.3    Reddick, R.L.4    Read, M.S.5    Koch, G.G.6    Brinkhous, K.M.7    Griggs, T.R.8
  • 60
    • 0026012551 scopus 로고
    • The porcine model for the understanding of thrombogenesis and atherogenesis
    • Fuster, V.; Badimon, L.; Badimon, J.J.; Ip, J.H.; Chesebro, J.H. The porcine model for the understanding of thrombogenesis and atherogenesis. Mayo Clin. Proc., 1991, 66, 818.
    • (1991) Mayo Clin. Proc. , vol.66 , pp. 818
    • Fuster, V.1    Badimon, L.2    Badimon, J.J.3    Ip, J.H.4    Chesebro, J.H.5
  • 63
    • 0026738642 scopus 로고
    • Antihemostatic and antithrombotic effects of monoclonal antibodies against von Willebrand factor in nonhuman primates
    • Krupski, W.C.; Bass, A.; Cadroy, Y.; Kelly, A.B.; Harker, L.A.; Hanson, S.R. Antihemostatic and antithrombotic effects of monoclonal antibodies against von Willebrand factor in nonhuman primates. Surgery, 1992, 112, 433.
    • (1992) Surgery , vol.112 , pp. 433
    • Krupski, W.C.1    Bass, A.2    Cadroy, Y.3    Kelly, A.B.4    Harker, L.A.5    Hanson, S.R.6
  • 64
    • 0033289760 scopus 로고    scopus 로고
    • Inhibition of thrombus formation by anti-Willebrand monoclonal antibodies in the guinea pig
    • Cisse-Thiam, M.; Girma, J.P.; Meyer, D.; Drouet, L. [Inhibition of thrombus formation by anti-Willebrand monoclonal antibodies in the guinea pig]. Dakar Med., 1999, 44, 45.
    • (1999) Dakar Med. , vol.44 , pp. 45
    • Cisse-Thiam, M.1    Girma, J.P.2    Meyer, D.3    Drouet, L.4
  • 65
    • 0030800626 scopus 로고    scopus 로고
    • Anti-thrombotic effects and bleeding risk of AJvW-2, a monoclonal antibody against human von Willebrand factor
    • Kageyama, S.; Yamamoto, H.; Nagano, M.; Arisaka, H.; Kayahara, T.; Yoshimoto, R. Anti-thrombotic effects and bleeding risk of AJvW-2, a monoclonal antibody against human von Willebrand factor. Br. J. Pharmacol., 1997, 122, 165.
    • (1997) Br. J. Pharmacol. , vol.122 , pp. 165
    • Kageyama, S.1    Yamamoto, H.2    Nagano, M.3    Arisaka, H.4    Kayahara, T.5    Yoshimoto, R.6
  • 67
    • 0035279906 scopus 로고    scopus 로고
    • Anti-human vWF monoclonal antibody, AJvW-2 Fab, inhibits repetitive coronary artery thrombosis without bleeding time prolongation in dogs
    • Kageyama, S.; Yamamoto, H.; Nakazawa, H.; Yoshimoto, R. Anti-human vWF monoclonal antibody, AJvW-2 Fab, inhibits repetitive coronary artery thrombosis without bleeding time prolongation in dogs. Thromb. Res., 2001, 101, 395.
    • (2001) Thromb. Res. , vol.101 , pp. 395
    • Kageyama, S.1    Yamamoto, H.2    Nakazawa, H.3    Yoshimoto, R.4
  • 69
    • 0037123856 scopus 로고    scopus 로고
    • Effect of a humanized monoclonal antibody to von Willebrand factor in a canine model of coronary arterial thrombosis
    • Kageyama, S.; Matsushita, J.; Yamamoto, H. Effect of a humanized monoclonal antibody to von Willebrand factor in a canine model of coronary arterial thrombosis. Eur. J. Pharmacol., 2002, 443, 143.
    • (2002) Eur. J. Pharmacol. , vol.443 , pp. 143
    • Kageyama, S.1    Matsushita, J.2    Yamamoto, H.3
  • 70
    • 0024231915 scopus 로고
    • Aurin tricarboxylic acid: A novel inhibitor of the association of von Willebrand factor and platelets
    • Phillips, M.D.; Moake, J.L.; Nolasco, L.; Turner, N. Aurin tricarboxylic acid: a novel inhibitor of the association of von Willebrand factor and platelets. Blood, 1988, 72, 1898.
    • (1988) Blood , vol.72 , pp. 1898
    • Phillips, M.D.1    Moake, J.L.2    Nolasco, L.3    Turner, N.4
  • 71
    • 0026469379 scopus 로고
    • Aurin tricarboxylic acid inhibits platelet adhesion to collagen by binding to the 509-695 disulphide loop of von Willebrand factor and competing with glycoprotein Ib
    • Girma, J.P.; Fressinaud, E.; Christoplic, O.; Rouault, C.; Obert, B.; Takahashi, Y.; Meyer, D. Aurin tricarboxylic acid inhibits platelet adhesion to collagen by binding to the 509-695 disulphide loop of von Willebrand factor and competing with glycoprotein Ib. Thromb. Haemost., 1992, 68, 707.
    • (1992) Thromb. Haemost. , vol.68 , pp. 707
    • Girma, J.P.1    Fressinaud, E.2    Christoplic, O.3    Rouault, C.4    Obert, B.5    Takahashi, Y.6    Meyer, D.7
  • 72
    • 0026045619 scopus 로고
    • Isolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers
    • Weinstein, M.; Vosburgh, E.; Phillips, M.; Turner, N.; Chute-Rose, L.; Moake, J. Isolation from commercial aurintricarboxylic acid of the most effective polymeric inhibitors of von Willebrand factor interaction with platelet glycoprotein Ib. Comparison with other polyanionic and polyaromatic polymers. Blood, 1991, 78, 2291.
    • (1991) Blood , vol.78 , pp. 2291
    • Weinstein, M.1    Vosburgh, E.2    Phillips, M.3    Turner, N.4    Chute-Rose, L.5    Moake, J.6
  • 73
    • 0025270361 scopus 로고
    • Aurintricarboxylic acid in a canine model of coronary artery thrombosis
    • Strony, J.; Phillips, M.; Brands, D.; Moake, J.; Adelman, B. Aurintricarboxylic acid in a canine model of coronary artery thrombosis. Circulation, 1990, 81, 1106.
    • (1990) Circulation , vol.81 , pp. 1106
    • Strony, J.1    Phillips, M.2    Brands, D.3    Moake, J.4    Adelman, B.5
  • 74
    • 0028120330 scopus 로고
    • Inhibition by aurintricarboxylic acid of von Willebrand factor binding to platelet GPIb, platelet retention, and thrombus formation in vivo
    • Kawasaki, T.; Kaku, S.; Kohinata, T.; Sakai, Y.; Taniuchi, Y.; Kawamura, K.; Yano, S.; Takenaka, T.; Fujimura, Y. Inhibition by aurintricarboxylic acid of von Willebrand factor binding to platelet GPIb, platelet retention, and thrombus formation in vivo. Am. J. Hematol., 1994, 47, 6.
    • (1994) Am. J. Hematol. , vol.47 , pp. 6
    • Kawasaki, T.1    Kaku, S.2    Kohinata, T.3    Sakai, Y.4    Taniuchi, Y.5    Kawamura, K.6    Yano, S.7    Takenaka, T.8    Fujimura, Y.9
  • 75
    • 0029901051 scopus 로고    scopus 로고
    • A comparative study of the antithrombotic effect of aurintricarboxylic acid on arterial thrombosis in rats and guinea pigs
    • Takiguchi, Y.; Shimazawa, M.; Nakashima, M. A comparative study of the antithrombotic effect of aurintricarboxylic acid on arterial thrombosis in rats and guinea pigs. Br. J. Pharmacol., 1996, 118, 1633.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 1633
    • Takiguchi, Y.1    Shimazawa, M.2    Nakashima, M.3
  • 76
    • 0026639850 scopus 로고
    • Unexpected effects of aurin tricarboxylic acid on human platelets
    • Kinlough-Rathbone, R.L.; Packham, M.A. Unexpected effects of aurin tricarboxylic acid on human platelets. Thromb. Haemost., 1992, 68, 189.
    • (1992) Thromb. Haemost. , vol.68 , pp. 189
    • Kinlough-Rathbone, R.L.1    Packham, M.A.2
  • 77
    • 0030044552 scopus 로고    scopus 로고
    • The antithrombotic effect of aurin tricarboxylic acid in the guinea pig is not solely due to its interaction with the von Willebrand factor-GPIb axis
    • Azzam, K.; Cisse-Thiam, M.; Drouet, L. The antithrombotic effect of aurin tricarboxylic acid in the guinea pig is not solely due to its interaction with the von Willebrand factor-GPIb axis. Thromb. Haemost., 1996, 75, 203.
    • (1996) Thromb. Haemost. , vol.75 , pp. 203
    • Azzam, K.1    Cisse-Thiam, M.2    Drouet, L.3
  • 78
    • 0029123084 scopus 로고
    • Aurintricarboxylic acid reduces platelet deposition in stenosed and endothelially injured rabbit carotid arteries more effectively than other antiplatelet interventions
    • Golino, P.; Ragni, M.; Cirillo, P.; Pascucci, I.; Ezekowitz, M.D.; Pawashe, A.; Scognamiglio, A.; Pace, L.; Guarino, A.; Chiariello, M. Aurintricarboxylic acid reduces platelet deposition in stenosed and endothelially injured rabbit carotid arteries more effectively than other antiplatelet interventions. Thromb. Haemost., 1995, 74, 974.
    • (1995) Thromb. Haemost. , vol.74 , pp. 974
    • Golino, P.1    Ragni, M.2    Cirillo, P.3    Pascucci, I.4    Ezekowitz, M.D.5    Pawashe, A.6    Scognamiglio, A.7    Pace, L.8    Guarino, A.9    Chiariello, M.10
  • 80
    • 0028919848 scopus 로고
    • Aurintricarboxylic acid prevents acute rethrombosis in a canine model of arterial thrombosis
    • Strony, J.; Song, A,; Rusterholtz, L.; Adelman, B. Aurintricarboxylic acid prevents acute rethrombosis in a canine model of arterial thrombosis. Arterioscler. Thromb. Vasc. Biol., 1995, 15, 359.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 359
    • Strony, J.1    Song, A.2    Rusterholtz, L.3    Adelman, B.4
  • 81
    • 0027156469 scopus 로고
    • Aurintricarboxylic acid protects hippocampal neurons from glutamate excitotoxicity in vitro
    • Samples, S.D.; Dubinsky, J.M. Aurintricarboxylic acid protects hippocampal neurons from glutamate excitotoxicity in vitro. J. Neurochem., 1993, 61, 382.
    • (1993) J. Neurochem. , vol.61 , pp. 382
    • Samples, S.D.1    Dubinsky, J.M.2
  • 82
    • 0036171227 scopus 로고    scopus 로고
    • Aurintricarboxylic acid induces a distinct activation of the IGF-I receptor signaling within MDA-231 cells
    • Haimsohn, M.; Beery, R.; Karasik, A.; Kanety, H.; Geier, A. Aurintricarboxylic acid induces a distinct activation of the IGF-I receptor signaling within MDA-231 cells. Endocrinology, 2002, 143, 837.
    • (2002) Endocrinology , vol.143 , pp. 837
    • Haimsohn, M.1    Beery, R.2    Karasik, A.3    Kanety, H.4    Geier, A.5
  • 83
    • 0037093219 scopus 로고    scopus 로고
    • Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons
    • Wu, D.; Vanhoorelbeke, K.; Cauwenberghs, N.; Meiring, M.; Depraetere, H.; Kotze, H.F.; Deckmyn, H. Inhibition of the von Willebrand (VWF)-collagen interaction by an antihuman VWF monoclonal antibody results in abolition of in vivo arterial platelet thrombus formation in baboons. Blood, 2002, 99, 3623.
    • (2002) Blood , vol.99 , pp. 3623
    • Wu, D.1    Vanhoorelbeke, K.2    Cauwenberghs, N.3    Meiring, M.4    Depraetere, H.5    Kotze, H.F.6    Deckmyn, H.7
  • 85
    • 0035491108 scopus 로고    scopus 로고
    • Saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion, decreases platelet aggregation and intimal hyperplasia in a rat carotid endarterectomy model
    • Cruz, C.P.; Eidt, J.; Drouilhet, J.; Brown, A.T.; Wang, Y.; Barnes, C.S.; Moursi, M.M. Saratin, an inhibitor of von Willebrand factor-dependent platelet adhesion, decreases platelet aggregation and intimal hyperplasia in a rat carotid endarterectomy model. J. Vasc. Surg., 2001, 34, 724.
    • (2001) J. Vasc. Surg. , vol.34 , pp. 724
    • Cruz, C.P.1    Eidt, J.2    Drouilhet, J.3    Brown, A.T.4    Wang, Y.5    Barnes, C.S.6    Moursi, M.M.7
  • 86
    • 0029077090 scopus 로고
    • VCL, an antagonist of the platelet GPlb receptor, markedly inhibits platelet adhesion and intimal thickening after balloon injury in the rat
    • Zahger, D.; Fishbein, M.C.; Garfinkel, L.I.; Shall, P.K.; Forrester, J.S.; Regnstrom, J.; Yano, J.; Cercek, B. VCL, an antagonist of the platelet GPlb receptor, markedly inhibits platelet adhesion and intimal thickening after balloon injury in the rat. Circulation, 1995, 92, 1269.
    • (1995) Circulation , vol.92 , pp. 1269
    • Zahger, D.1    Fishbein, M.C.2    Garfinkel, L.I.3    Shall, P.K.4    Forrester, J.S.5    Regnstrom, J.6    Yano, J.7    Cercek, B.8
  • 87
    • 0030761798 scopus 로고    scopus 로고
    • Inhibition of von Willebrand factor binding to platelet GP lb by a fractionated aurintricarboxylic acid prevents restenosis after vascular injury in hamster carotid artery
    • Matsuno, H.; Kozawa, O.; Niwa, M.; Uematsu, T. Inhibition of von Willebrand factor binding to platelet GP lb by a fractionated aurintricarboxylic acid prevents restenosis after vascular injury in hamster carotid artery. Circulation, 1997, 96, 1299.
    • (1997) Circulation , vol.96 , pp. 1299
    • Matsuno, H.1    Kozawa, O.2    Niwa, M.3    Uematsu, T.4
  • 88
    • 0031967214 scopus 로고    scopus 로고
    • Multiple inhibition of platelet activation by aurintricarboxylic acid prevents vascular stenosis after endothelial injury in hamster carotid artery
    • Matsuno, H.; Kozawa, O.; Niwa, M.; Tanabe, K.; Ichimaru, K.; Takiguchi, Y.; Yokota, M.; Hayashi, H.; Uematsu, T. Multiple inhibition of platelet activation by aurintricarboxylic acid prevents vascular stenosis after endothelial injury in hamster carotid artery. Thromb. Haemost., 1998, 79, 865.
    • (1998) Thromb. Haemost. , vol.79 , pp. 865
    • Matsuno, H.1    Kozawa, O.2    Niwa, M.3    Tanabe, K.4    Ichimaru, K.5    Takiguchi, Y.6    Yokota, M.7    Hayashi, H.8    Uematsu, T.9
  • 89
    • 0033793186 scopus 로고    scopus 로고
    • Anti-human von willebrand factor monoclonal antibody AJvW-2 prevents thrombus deposition and neointinia formation after balloon injury in guinea pigs
    • Kageyama, S.; Yamamoto, H.; Yoshimoto, R. Anti-human von willebrand factor monoclonal antibody AJvW-2 prevents thrombus deposition and neointinia formation after balloon injury in guinea pigs. Arterioscler. Thromb. Vasc. Biol., 2000, 20, 2303.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2303
    • Kageyama, S.1    Yamamoto, H.2    Yoshimoto, R.3
  • 90
    • 0024847956 scopus 로고
    • The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor oil others
    • Elices, M.J.; Hemler, M.E. The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor oil others. Proc. Natl. Acad Sci. USA, 1989, 86, 9906.
    • (1989) Proc. Natl. Acad Sci. USA , vol.86 , pp. 9906
    • Elices, M.J.1    Hemler, M.E.2
  • 91
    • 0028075817 scopus 로고
    • Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner
    • Kamata, T.; Takada, Y. Direct binding of collagen to the I domain of integrin alpha 2 beta 1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner. J. Biol. Chem., 1994, 269, 26006.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26006
    • Kamata, T.1    Takada, Y.2
  • 93
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight, C.G.; Morton, L.F.; Peachey, A.R.; Tuckwell, D.S.; Farndale, R.W.; Barnes, M.J. The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J. Biol. Chem., 2000, 275, 35.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 95
    • 0026590333 scopus 로고
    • Glycoprotein Ia/IIa-mediated activation-dependent platelet adhesion to collagen
    • Kainoh, M.; Ikeda, Y.; Nishio, S.; Nakadate, T. Glycoprotein Ia/IIa-mediated activation-dependent platelet adhesion to collagen. Thromb. Res., 1992, 65, 165.
    • (1992) Thromb. Res. , vol.65 , pp. 165
    • Kainoh, M.1    Ikeda, Y.2    Nishio, S.3    Nakadate, T.4
  • 96
    • 0034441740 scopus 로고    scopus 로고
    • Activation of the platelet collagen receptor integrin alpha(2)beta(1): Its mechanism and participation in the physiological functions of platelets
    • Jung, S.M.; Moroi, M. Activation of the platelet collagen receptor integrin alpha(2)beta(1): its mechanism and participation in the physiological functions of platelets. Trends Cardiovasc. Med., 2000, 10, 285.
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 285
    • Jung, S.M.1    Moroi, M.2
  • 97
    • 0022353697 scopus 로고
    • Human blood platelets showing no response to collagen fail to express surface glycoprotein Ia
    • Nieuwenhuis, H.K.; Akkerman, J.W.; Houdijk, W.P.; Sixma, J.J. Human blood platelets showing no response to collagen fail to express surface glycoprotein Ia. Nature, 1985, 318, 470.
    • (1985) Nature , vol.318 , pp. 470
    • Nieuwenhuis, H.K.1    Akkerman, J.W.2    Houdijk, W.P.3    Sixma, J.J.4
  • 98
    • 0023897855 scopus 로고
    • Deficiency of intact thrombospondin and membrane glycoprotein Ia in platelets with defective collagen-induced aggregation and spontaneous loss of disorder
    • Kehrel, B.; Balleisen, L.; Kokott, R.; Mesters, R.; Stenzinger, W.; Clemetson, K.J.; van de, L.J. Deficiency of intact thrombospondin and membrane glycoprotein Ia in platelets with defective collagen-induced aggregation and spontaneous loss of disorder. Blood, 1988, 71, 1074.
    • (1988) Blood , vol.71 , pp. 1074
    • Kehrel, B.1    Balleisen, L.2    Kokott, R.3    Mesters, R.4    Stenzinger, W.5    Clemetson, K.J.6    van de, L.J.7
  • 99
    • 0028957133 scopus 로고
    • Platelet unresponsiveness to collagen: Involvement of glycoprotein Ia- IIa (alpha 2 beta 1 integrin) deficiency associated with a myeloproliferative disorder
    • Handa, M.; Watanabe, K.; Kawai, Y.; Kamata, T.; Koyama, T.; Nagai, H.; Ikeda, Y. Platelet unresponsiveness to collagen: involvement of glycoprotein Ia- IIa (alpha 2 beta 1 integrin) deficiency associated with a myeloproliferative disorder. Thromb. Haemost., 1995, 73, 521.
    • (1995) Thromb. Haemost. , vol.73 , pp. 521
    • Handa, M.1    Watanabe, K.2    Kawai, Y.3    Kamata, T.4    Koyama, T.5    Nagai, H.6    Ikeda, Y.7
  • 100
    • 0025042513 scopus 로고
    • Lack of platelet response to collagen associated with an autoantibody against glycoprotein Ia: A novel cause of acquired qualitative platelet dysfunction
    • Deckmyn, H.; Chew, S.L.; Vermylen, J. Lack of platelet response to collagen associated with an autoantibody against glycoprotein Ia: a novel cause of acquired qualitative platelet dysfunction. Thromb. Haemost., 1990, 64, 74.
    • (1990) Thromb. Haemost. , vol.64 , pp. 74
    • Deckmyn, H.1    Chew, S.L.2    Vermylen, J.3
  • 101
    • 0030942489 scopus 로고    scopus 로고
    • Hereditary variation in platelet integrin alpha 2 beta 1 density is associated with two silent polymorphisms in the alpha 2 gene coding sequence
    • Kunicki, T.J.; Kritzik, M.; Annis, D.S.; Nugent, D.J. Hereditary variation in platelet integrin alpha 2 beta 1 density is associated with two silent polymorphisms in the alpha 2 gene coding sequence. Blood, 1997, 89, 1939.
    • (1997) Blood , vol.89 , pp. 1939
    • Kunicki, T.J.1    Kritzik, M.2    Annis, D.S.3    Nugent, D.J.4
  • 102
    • 0027431790 scopus 로고
    • Variability of integrin alpha 2 beta 1 activity on human platelets
    • Kunicki, T.J.; Orchekowski, R.; Annis, D.; Honda, Y. Variability of integrin alpha 2 beta 1 activity on human platelets. Blood, 1993, 82, 2693.
    • (1993) Blood , vol.82 , pp. 2693
    • Kunicki, T.J.1    Orchekowski, R.2    Annis, D.3    Honda, Y.4
  • 103
    • 0033137301 scopus 로고    scopus 로고
    • Low platelet alpha2beta1 levels in type I von Willebrand disease correlate with impaired platelet function in a high shear stress system
    • Di Paola, J.; Federici, A.B.; Mannucci, P.M.; Canciani, M.T.; Kritzik, M.; Kunicki, T.J.; Nugent, D. Low platelet alpha2beta1 levels in type I von Willebrand disease correlate with impaired platelet function in a high shear stress system. Blood, 1999, 93, 3578.
    • (1999) Blood , vol.93 , pp. 3578
    • Di Paola, J.1    Federici, A.B.2    Mannucci, P.M.3    Canciani, M.T.4    Kritzik, M.5    Kunicki, T.J.6    Nugent, D.7
  • 104
    • 0036192238 scopus 로고    scopus 로고
    • Influence of Platelet Collagen Receptor Polymorphisms on Risk for Arterial Thrombosis
    • Furihata, K.; Nugent, D.J.; Kunicki, T.J. Influence of Platelet Collagen Receptor Polymorphisms on Risk for Arterial Thrombosis. Arch. Pathol. Lab Med., 2002, 126, 305.
    • (2002) Arch. Pathol. Lab. Med. , vol.126 , pp. 305
    • Furihata, K.1    Nugent, D.J.2    Kunicki, T.J.3
  • 105
    • 0033622005 scopus 로고    scopus 로고
    • The impact of the glycoprotein Ia collagen receptor subunit A1648G gene polymorphism on coronary artery disease and acute myocardial infarction
    • Kroll, H.; Gardemann, A.; Fechter, A.; Haberbosch, W.; Santoso, S. The impact of the glycoprotein Ia collagen receptor subunit A1648G gene polymorphism on coronary artery disease and acute myocardial infarction. Thromb. Haemost., 2000, 83, 392.
    • (2000) Thromb. Haemost. , vol.83 , pp. 392
    • Kroll, H.1    Gardemann, A.2    Fechter, A.3    Haberbosch, W.4    Santoso, S.5
  • 106
    • 0037192771 scopus 로고    scopus 로고
    • Integrin {alpha) 2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen
    • Holtkotter, O.; Nieswandt, B.; Smyth, N.; Muller, W.; Hafner, M.; Schulte, V.; Krieg, T.; Eckes, B. Integrin {alpha) 2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen. J. Biol. Chem., 2002.
    • (2002) J. Biol. Chem.
    • Holtkotter, O.1    Nieswandt, B.2    Smyth, N.3    Muller, W.4    Hafner, M.5    Schulte, V.6    Krieg, T.7    Eckes, B.8
  • 108
    • 0035571593 scopus 로고    scopus 로고
    • Variation in human platelet glycoprotein VI content modulates glycoprotein VI-specific prothrombinase activity
    • Furihata, K.; Clemetson, K.J.; Deguchi, H.; Kunicki, T.J. Variation in human platelet glycoprotein VI content modulates glycoprotein VI-specific prothrombinase activity. Arterioscler. Thromb. Vasc. Biol., 2001, 21, 1857.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1857
    • Furihata, K.1    Clemetson, K.J.2    Deguchi, H.3    Kunicki, T.J.4
  • 110
    • 0026705756 scopus 로고
    • An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. II. Cloning of the cDNA and expression
    • Keller, P.M.; Schultz, L.D.; Condra, C.; Karczewski, J.; Connolly, T.M. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. II. Cloning of the cDNA and expression. J. Biol. Chem., 1992, 267, 6899.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6899
    • Keller, P.M.1    Schultz, L.D.2    Condra, C.3    Karczewski, J.4    Connolly, T.M.5
  • 111
    • 0026733452 scopus 로고
    • An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. I. Identification, isolation, and characterization
    • Connolly, T.M.; Jacobs, J.W.; Condra, C. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. I. Identification, isolation, and characterization. J. Biol. Chem., 1992, 267, 6893.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6893
    • Connolly, T.M.1    Jacobs, J.W.2    Condra, C.3
  • 112
    • 0028931844 scopus 로고
    • Calin from Hirudo medicinalis, an inhibitor of platelet adhesion to collagen, prevents platelet-rich thrombosis in hamsters
    • Deckmyn, H.; Stassen, J.M.; Vreys, I.; Van Houtte, E.; Sawyer, R.T.; Vermylen, J. Calin from Hirudo medicinalis, an inhibitor of platelet adhesion to collagen, prevents platelet-rich thrombosis in hamsters. Blood, 1995, 85, 712.
    • (1995) Blood , vol.85 , pp. 712
    • Deckmyn, H.1    Stassen, J.M.2    Vreys, I.3    Van Houtte, E.4    Sawyer, R.T.5    Vermylen, J.6
  • 113
    • 0028928893 scopus 로고
    • Calin from Hirudo medicinalis, an inhibitor of von Willebrand factor binding to collagen under static and flow conditions
    • Harsfalvi, J.; Stassen, J.M.; Hoylaerts, M.F.; Van Houtte, E.; Sawyer, R.T.; Vermylen, J.; Deckmyn, H. Calin from Hirudo medicinalis, an inhibitor of von Willebrand factor binding to collagen under static and flow conditions. Blood, 1995, 85, 705.
    • (1995) Blood , vol.85 , pp. 705
    • Harsfalvi, J.1    Stassen, J.M.2    Hoylaerts, M.F.3    Van Houtte, E.4    Sawyer, R.T.5    Vermylen, J.6    Deckmyn, H.7
  • 114
    • 0032865278 scopus 로고    scopus 로고
    • The collagen-binding leech products rLAPP and calin prevent both von Willebrand factor and alpha2beta1(GPIa/IIa)-I-domain binding to collagen in a different manner
    • Depraetere, H.; Kerekes, A.; Deckmyn, H. The collagen-binding leech products rLAPP and calin prevent both von Willebrand factor and alpha2beta1(GPIa/IIa)-I-domain binding to collagen in a different manner. Thromb. Haemost., 1999, 82, 1160.
    • (1999) Thromb. Haemost. , vol.82 , pp. 1160
    • Depraetere, H.1    Kerekes, A.2    Deckmyn, H.3
  • 115
    • 0027421698 scopus 로고
    • Recombinant leech antiplatelet protein prevents collagen-mediated platelet aggregation but not collagen graft thrombosis in baboons
    • Schaffer, L.W.; Davidson, J.T.; Siegl, P.K.; Gould, R.J.; Nutt, R.F.; Brady, S.F.; Connolly, T.M. Recombinant leech antiplatelet protein prevents collagen-mediated platelet aggregation but not collagen graft thrombosis in baboons. Arterioscler. Thromb., 1993, 13, 1593.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1593
    • Schaffer, L.W.1    Davidson, J.T.2    Siegl, P.K.3    Gould, R.J.4    Nutt, R.F.5    Brady, S.F.6    Connolly, T.M.7
  • 116
    • 0023185207 scopus 로고
    • A novel platelet aggregating factor found in a patient with defective collagen-induced platelet aggregation and autoimmune thrombocytopenia
    • Sugiyama, T.; Okuma, M.; Ushikubi, F.; Sensaki, S.; Kanaji, K.; Uchino, H. A novel platelet aggregating factor found in a patient with defective collagen-induced platelet aggregation and autoimmune thrombocytopenia. Blood, 1987, 69, 1712.
    • (1987) Blood , vol.69 , pp. 1712
    • Sugiyama, T.1    Okuma, M.2    Ushikubi, F.3    Sensaki, S.4    Kanaji, K.5    Uchino, H.6
  • 117
    • 0024426540 scopus 로고
    • A patient with platelets deficient in glycoprotein VI that lack both collagen-induced aggregation and adhesion
    • Moroi, M.; Jung, S.M.; Okuma, M.; Shinmyozu, K. A patient with platelets deficient in glycoprotein VI that lack both collagen-induced aggregation and adhesion. J Clin. Invest., 1989, 84, 1440.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1440
    • Moroi, M.1    Jung, S.M.2    Okuma, M.3    Shinmyozu, K.4
  • 118
    • 0026564824 scopus 로고
    • Deficiency of P62, a putative collagen receptor, in platelets from a patient with defective collagen-induced platelet aggregation
    • Ryo, R.; Yoshida, A.; Sugano, W.; Yasunaga, M.; Nakayama, K.; Saigo, K.; Adachi, M.; Yamaguchi, N.; Okuma, M. Deficiency of P62, a putative collagen receptor, in platelets from a patient with defective collagen-induced platelet aggregation. Am. J. Hematol., 1992, 39, 25.
    • (1992) Am. J. Hematol. , vol.39 , pp. 25
    • Ryo, R.1    Yoshida, A.2    Sugano, W.3    Yasunaga, M.4    Nakayama, K.5    Saigo, K.6    Adachi, M.7    Yamaguchi, N.8    Okuma, M.9
  • 119
    • 0028928125 scopus 로고
    • Platelets with 10% of the normal amount of glycoprotein VI have an impaired response to collagen that results in a mild bleeding tendency
    • Arai, M.; Yamamoto, N.; Moroi, M.; Akamatsu, N.; Fukutake, K.; Tanoue, K. Platelets with 10% of the normal amount of glycoprotein VI have an impaired response to collagen that results in a mild bleeding tendency. Br. J. Haematol., 1995, 89, 124.
    • (1995) Br. J. Haematol. , vol.89 , pp. 124
    • Arai, M.1    Yamamoto, N.2    Moroi, M.3    Akamatsu, N.4    Fukutake, K.5    Tanoue, K.6
  • 120
    • 0028986390 scopus 로고
    • Integrin alpha 2 beta 1-independent activation of platelets by simple collagen-like peptides: Collagen tertiary (trip helical) and quaternary (polymeric) structures are sufficient alone for alpha 2 beta 1-independent platelet reactivity
    • Morton, L.F.; Hargreaves, P.G.; Farndale, R.W.; Young, R.D.; Barnes, M.J. Integrin alpha 2 beta 1-independent activation of platelets by simple collagen-like peptides: collagen tertiary (trip helical) and quaternary (polymeric) structures are sufficient alone for alpha 2 beta 1-independent platelet reactivity. Biochem. J., 1995, 306 (Pt 2), 337.
    • (1995) Biochem. J. , vol.306 , Issue.PART 2 , pp. 337
    • Morton, L.F.1    Hargreaves, P.G.2    Farndale, R.W.3    Young, R.D.4    Barnes, M.J.5
  • 121
    • 0033561374 scopus 로고    scopus 로고
    • Monomeric (glycine-prolinehydroxyproline) 1O repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI
    • Asselin, J.; Knight, C.G.; Farndale, R.W.; Barnes, M.J.; Watson, S.P. Monomeric (glycine-prolinehydroxyproline) 1O repeat sequence is a partial agonist of the platelet collagen receptor glycoprotein VI. Biochem. J., 1999, 339 (Pt 2), 413.
    • (1999) Biochem. J. , vol.339 , Issue.PART 2 , pp. 413
    • Asselin, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4    Watson, S.P.5
  • 122
    • 0032828086 scopus 로고    scopus 로고
    • The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors
    • Clemetson, J.M.; Polgar, J.; Magnenat, E.; Wells, T.N.; Clemetson, K.J. The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors. J. Biol. Chem., 1999, 274, 29019.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29019
    • Clemetson, J.M.1    Polgar, J.2    Magnenat, E.3    Wells, T.N.4    Clemetson, K.J.5
  • 124
    • 0034649228 scopus 로고    scopus 로고
    • Molecular cloning, genomic structure, chromosomal localization, and alternative splice forms of the platelet collagen receptor glycoprotein VI
    • Ezumi, Y.; Uchiyama, T.; Takayama, H. Molecular cloning, genomic structure, chromosomal localization, and alternative splice forms of the platelet collagen receptor glycoprotein VI. Biochem. Biophys. Res. Commun., 2000, 277, 27.
    • (2000) Biochem. Biophys. Res. Commun. , vol.277 , pp. 27
    • Ezumi, Y.1    Uchiyama, T.2    Takayama, H.3
  • 125
    • 0000633068 scopus 로고    scopus 로고
    • Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets
    • Gross, B.S.; Melford, S.K.; Watson, S.P. Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets. Eur. J. Biochem., 1999, 263, 612.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 612
    • Gross, B.S.1    Melford, S.K.2    Watson, S.P.3
  • 126
    • 0034604575 scopus 로고    scopus 로고
    • Expression and function of the mouse collagen receptor glycoprotein VI is strictly dependent on its association with the FcRgamma chain
    • Nieswandt, B.; Bergmeier, W.; Schulte, V.; Rackebrandt, K.; Gessner, J.E.; Zirngibl, H. Expression and function of the mouse collagen receptor glycoprotein VI is strictly dependent on its association with the FcRgamma chain. J. Biol. Chem., 2000, 275, 23998.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23998
    • Nieswandt, B.1    Bergmeier, W.2    Schulte, V.3    Rackebrandt, K.4    Gessner, J.E.5    Zirngibl, H.6
  • 127
    • 0037177026 scopus 로고    scopus 로고
    • Platelets activated by collagen through immunoreceptor tyrosine-based activation motif play pivotal role in initiation and generation of neointimal hyperplasia after vascular injury
    • Konishi, H.; Katoh, Y.; Takaya, N.; Kashiwakura, Y.; Itoh, S.; Ra, C.; Daida, H. Platelets activated by collagen through immunoreceptor tyrosine-based activation motif play pivotal role in initiation and generation of neointimal hyperplasia after vascular injury. Circulation, 2002, 105, 912.
    • (2002) Circulation , vol.105 , pp. 912
    • Konishi, H.1    Katoh, Y.2    Takaya, N.3    Kashiwakura, Y.4    Itoh, S.5    Ra, C.6    Daida, H.7
  • 130
    • 0034852807 scopus 로고    scopus 로고
    • Ser968Thr mutation within the A3 domain of von Willebrand factor (VWF) in two related patients leads to a defective binding of VWF to collagen
    • Ribba, A.S.; Loisel, I.; Lavergne, J.M.; Juhan-Vague, I.; Obert, B.; Cherel, G.; Meyer, D.; Girma, J.P. Ser968Thr mutation within the A3 domain of von Willebrand factor (VWF) in two related patients leads to a defective binding of VWF to collagen. Thromb. Haemost., 2001, 86, 848.
    • (2001) Thromb. Haemost. , vol.86 , pp. 848
    • Ribba, A.S.1    Loisel, I.2    Lavergne, J.M.3    Juhan-Vague, I.4    Obert, B.5    Cherel, G.6    Meyer, D.7    Girma, J.P.8


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