메뉴 건너뛰기




Volumn 108, Issue 12, 2006, Pages 3746-3752

P-selectin glycoprotein ligand 1 and β2-integrins cooperate in the adhesion of leukocytes to von Willebrand factor

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA9BETA1 INTEGRIN; ALPHALBETA2 INTEGRIN; ALPHAMBETA2 INTEGRIN; ALPHAXBETA2 INTEGRIN; BETA1 INTEGRIN; BETA2 INTEGRIN; NEUTROPHIL INHIBITORY FACTOR; P SELECTIN GLYCOPROTEIN LIGAND 1; PHORBOL 13 ACETATE 12 MYRISTATE; RECOMBINANT P SELECTIN GLYCOPROTEIN LIGAND 1; RECOMBINANT PROTEIN; VERY LATE ACTIVATION ANTIGEN 4; VON WILLEBRAND FACTOR;

EID: 33750688949     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-03-010322     Document Type: Article
Times cited : (150)

References (40)
  • 1
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 1994;76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 2
    • 0030854107 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology: role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver RP, Cummings RD. Perspectives series: cell adhesion in vascular biology: role of PSGL-1 binding to selectins in leukocyte recruitment. J Clin Invest. 1997;100:485-491.
    • (1997) J Clin Invest , vol.100 , pp. 485-491
    • McEver, R.P.1    Cummings, R.D.2
  • 3
    • 0032698482 scopus 로고    scopus 로고
    • P-selectin-beta 2-integrin cross-talk: A molecular mechanism for polymorphonuclear leukocyte recruitment at the site of vascular damage
    • Cerletti C, Evangelista V, de Gaetano G. P-selectin-beta 2-integrin cross-talk: a molecular mechanism for polymorphonuclear leukocyte recruitment at the site of vascular damage. Thromb Haemost. 1999;82:787-793.
    • (1999) Thromb Haemost , vol.82 , pp. 787-793
    • Cerletti, C.1    Evangelista, V.2    De Gaetano, G.3
  • 4
    • 0030854195 scopus 로고    scopus 로고
    • Leukocyte adhesion: CD11/CD18 integrins and intercellular adhesion molecules
    • Gahmberg CG. Leukocyte adhesion: CD11/CD18 integrins and intercellular adhesion molecules. Curr Opin Cell Biol. 1997;9:643-650.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 643-650
    • Gahmberg, C.G.1
  • 5
    • 0034964396 scopus 로고    scopus 로고
    • Recognition of fibrinogen by leukocyte integrins
    • Ugarova TP, Yakubenko VP. Recognition of fibrinogen by leukocyte integrins. Ann N Y Acad Sci. 2001;936:368-385.
    • (2001) Ann N Y Acad Sci , vol.936 , pp. 368-385
    • Ugarova, T.P.1    Yakubenko, V.P.2
  • 6
    • 10644294901 scopus 로고    scopus 로고
    • Promotion of leukocyte adhesion by a novel interaction between vitronectin and the β2 integrin Mac-1 (αMβ2, CD11b/CD18)
    • Kanse SM, Matz RL, Preissner KT, Peter K. Promotion of leukocyte adhesion by a novel interaction between vitronectin and the β2 integrin Mac-1 (αMβ2, CD11b/CD18). Arterioscler Thromb Vasc Biol. 2004;24:2251-2256.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2251-2256
    • Kanse, S.M.1    Matz, R.L.2    Preissner, K.T.3    Peter, K.4
  • 7
    • 0036718520 scopus 로고    scopus 로고
    • The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1
    • Santoso S, Sachs UJ, Kroll H, et al. The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1. J Exp Med. 2002;196:679-691.
    • (2002) J Exp Med , vol.196 , pp. 679-691
    • Santoso, S.1    Sachs, U.J.2    Kroll, H.3
  • 8
    • 0034679329 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibα is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18)
    • Simon DI, Chen Z, Xu H, et al. Platelet glycoprotein Ibα is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18). J Exp Med. 2000;192:193-204.
    • (2000) J Exp Med , vol.192 , pp. 193-204
    • Simon, D.I.1    Chen, Z.2    Xu, H.3
  • 9
    • 0141498240 scopus 로고    scopus 로고
    • Von Willebrand factor, platelets and endothelial cell interactions
    • Ruggeri ZM. Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost. 2003;1:1335-1342.
    • (2003) J Thromb Haemost , vol.1 , pp. 1335-1342
    • Ruggeri, Z.M.1
  • 10
    • 14544302314 scopus 로고    scopus 로고
    • New concepts in von Willebrand disease
    • Sadler JE. New concepts in von Willebrand disease. Annu Rev Med. 2005;56:173-191.
    • (2005) Annu Rev Med , vol.56 , pp. 173-191
    • Sadler, J.E.1
  • 11
    • 0033385938 scopus 로고    scopus 로고
    • Insights from von Willebrand disease animal models
    • Denis CV, Wagner DD. Insights from von Willebrand disease animal models. Cell Mol Life Sci. 1999;56:977-990.
    • (1999) Cell Mol Life Sci , vol.56 , pp. 977-990
    • Denis, C.V.1    Wagner, D.D.2
  • 12
    • 0035957410 scopus 로고    scopus 로고
    • Defect in regulated secretion of P-selectin affects leukocyte recruitment in von Willebrand factor-deficient mice
    • Denis CV, Andre P, Saffaripour S, Wagner DD. Defect in regulated secretion of P-selectin affects leukocyte recruitment in von Willebrand factor-deficient mice. Proc Natl Acad Sci U S A. 2001;98:4072-4077.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4072-4077
    • Denis, C.V.1    Andre, P.2    Saffaripour, S.3    Wagner, D.D.4
  • 13
    • 0024580737 scopus 로고
    • PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells
    • Bonfanti R, Furie BC, Furie B, Wagner DD. PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells. Blood. 1989;73:1109-1112.
    • (1989) Blood , vol.73 , pp. 1109-1112
    • Bonfanti, R.1    Furie, B.C.2    Furie, B.3    Wagner, D.D.4
  • 14
    • 0036371063 scopus 로고    scopus 로고
    • Molecular and cellular biology of von Willebrand factor
    • Denis CV. Molecular and cellular biology of von Willebrand factor. Int J Hematol. 2002;75:3-8.
    • (2002) Int J Hematol , vol.75 , pp. 3-8
    • Denis, C.V.1
  • 15
    • 0035469891 scopus 로고    scopus 로고
    • Localized reduction of atherosclerosis in von Willebrand factor-deficient mice
    • Methia N, Andre P, Denis CV, Economopoulos M, Wagner DD. Localized reduction of atherosclerosis in von Willebrand factor-deficient mice. Blood. 2001;98:1424-1428.
    • (2001) Blood , vol.98 , pp. 1424-1428
    • Methia, N.1    Andre, P.2    Denis, C.V.3    Economopoulos, M.4    Wagner, D.D.5
  • 16
    • 0030887708 scopus 로고    scopus 로고
    • Propolypeptide of von Willebrand factor is a novel ligand for very late antigen-4 integrin
    • Isobe T, Hisaoka T, Shimizu A, et al. Propolypeptide of von Willebrand factor is a novel ligand for very late antigen-4 integrin. J Biol Chem. 1997;272:8447-8453.
    • (1997) J Biol Chem , vol.272 , pp. 8447-8453
    • Isobe, T.1    Hisaoka, T.2    Shimizu, A.3
  • 17
    • 0034604565 scopus 로고    scopus 로고
    • Tissue transglutaminase, coagulation factor XIII, and the pro-polypeptide of von Willebrand factor are all ligands for the integrins α9β1 and α4β1
    • Takahashi H, Isobe T, Horibe S, et al. Tissue transglutaminase, coagulation factor XIII, and the pro-polypeptide of von Willebrand factor are all ligands for the integrins α9β1 and α4β1. J Biol Chem. 2000;275:23589-23595.
    • (2000) J Biol Chem , vol.275 , pp. 23589-23595
    • Takahashi, H.1    Isobe, T.2    Horibe, S.3
  • 18
    • 0035947769 scopus 로고    scopus 로고
    • Inhibition of beta(2) integrin-mediated leukocyte cell adhesion by leucine-leucine-glycine motif-containing peptides
    • Koivunen E, Ranta TM, Annila A, et al. Inhibition of beta(2) integrin-mediated leukocyte cell adhesion by leucine-leucine-glycine motif-containing peptides. J Cell Biol. 2001;153:905-916.
    • (2001) J Cell Biol , vol.153 , pp. 905-916
    • Koivunen, E.1    Ranta, T.M.2    Annila, A.3
  • 19
    • 17544399383 scopus 로고    scopus 로고
    • Von Willebrand factor without the A2 domain is resistant to proteolysis
    • Lankhof H, Damas C, Schiphorst ME, et al. von Willebrand factor without the A2 domain is resistant to proteolysis. Thromb Haemost. 1997;77:1008-1013.
    • (1997) Thromb Haemost , vol.77 , pp. 1008-1013
    • Lankhof, H.1    Damas, C.2    Schiphorst, M.E.3
  • 20
    • 0029960408 scopus 로고    scopus 로고
    • A3 domain is essential for interaction of von Willebrand factor with collagen type III
    • Lankhof H, van Hoeijj M, Schiphorst ME, et al. A3 domain is essential for interaction of von Willebrand factor with collagen type III. Thromb Haemost. 1996;75:950-958.
    • (1996) Thromb Haemost , vol.75 , pp. 950-958
    • Lankhof, H.1    Van Hoeijj, M.2    Schiphorst, M.E.3
  • 21
    • 1842530336 scopus 로고    scopus 로고
    • An experimental model to study the in vivo survival of von Willebrand factor: Basic aspects and application to the R1205H mutation
    • Lenting PJ, Westein E, Terraube V, et al. An experimental model to study the in vivo survival of von Willebrand factor: basic aspects and application to the R1205H mutation. J Biol Chem. 2004;279:12102-12109.
    • (2004) J Biol Chem , vol.279 , pp. 12102-12109
    • Lenting, P.J.1    Westein, E.2    Terraube, V.3
  • 22
    • 0038747210 scopus 로고    scopus 로고
    • Characterization of ICAM-4 binding to the I domains of the CD11a/CD18 and CD11b/CD18 leukocyte integrins
    • Ihanus E, Uotila L, Toivanen A, et al. Characterization of ICAM-4 binding to the I domains of the CD11a/CD18 and CD11b/CD18 leukocyte integrins. Eur J Biochem. 2003;270:1710-1723.
    • (2003) Eur J Biochem , vol.270 , pp. 1710-1723
    • Ihanus, E.1    Uotila, L.2    Toivanen, A.3
  • 23
    • 0033574172 scopus 로고    scopus 로고
    • Recombinant soluble form of PSGL-1 accelerates thrombolysis and prevents reocclusion in a porcine model
    • Kumar A, Villani MP, Patel UK, Keith JC Jr, Schaub RG. Recombinant soluble form of PSGL-1 accelerates thrombolysis and prevents reocclusion in a porcine model. Circulation. 1999;99:1363-1369.
    • (1999) Circulation , vol.99 , pp. 1363-1369
    • Kumar, A.1    Villani, M.P.2    Patel, U.K.3    Keith Jr., J.C.4    Schaub, R.G.5
  • 24
    • 0025727990 scopus 로고
    • Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca
    • Fujimura Y, Titani K, Usami Y, et al. Isolation and chemical characterization of two structurally and functionally distinct forms of botrocetin, the platelet coagglutinin isolated from the venom of Bothrops jararaca. Biochemistry. 1991;19:1957-1964.
    • (1991) Biochemistry , vol.19 , pp. 1957-1964
    • Fujimura, Y.1    Titani, K.2    Usami, Y.3
  • 25
    • 0028807440 scopus 로고
    • A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature N terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding
    • De Luca M, Dunlop LC, Andrews RK, et al. A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature N terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding. J Biol Chem. 1995;270:26734-26737.
    • (1995) J Biol Chem , vol.270 , pp. 26734-26737
    • De Luca, M.1    Dunlop, L.C.2    Andrews, R.K.3
  • 26
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα: Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibα as a binding site for von Willebrand factor and alpha-thrombin
    • Ward CM, Andrews RK, Smith AI, Berndt MC. Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα: identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibα as a binding site for von Willebrand factor and alpha-thrombin. Biochemistry. 1996;35:4929-4938.
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1    Andrews, R.K.2    Smith, A.I.3    Berndt, M.C.4
  • 27
    • 0029830192 scopus 로고    scopus 로고
    • Core2 beta-6-N-acetylglucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin
    • Kumar R, Camphausen RT, Sullivan FX, Cumming DA. Core2 beta-6-N-acetylglucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin. Blood. 1996;88:3872-3879.
    • (1996) Blood , vol.88 , pp. 3872-3879
    • Kumar, R.1    Camphausen, R.T.2    Sullivan, F.X.3    Cumming, D.A.4
  • 28
    • 0030902446 scopus 로고    scopus 로고
    • Prothrombin conversion under flow conditions by prothrombinase assembled on adherent platelets
    • Billy D, Briede J, Heemskerk JW, Hemker HC, Lindhout T. Prothrombin conversion under flow conditions by prothrombinase assembled on adherent platelets. Blood Coagul Fibrinolysis. 1997;8:168-174.
    • (1997) Blood Coagul Fibrinolysis , vol.8 , pp. 168-174
    • Billy, D.1    Briede, J.2    Heemskerk, J.W.3    Hemker, H.C.4    Lindhout, T.5
  • 29
    • 0032724774 scopus 로고    scopus 로고
    • Neutrophil inhibitory factor abrogates neutrophil adhesion by blockade of CD11a and CD11b beta(2) integrins
    • Lo SK, Rahman A, Xu N, et al. Neutrophil inhibitory factor abrogates neutrophil adhesion by blockade of CD11a and CD11b beta(2) integrins. Mol Pharmacol. 1999;56:926-932.
    • (1999) Mol Pharmacol , vol.56 , pp. 926-932
    • Lo, S.K.1    Rahman, A.2    Xu, N.3
  • 30
    • 0034846702 scopus 로고    scopus 로고
    • Adhesive interactions of leukocytes, platelets, and the vessel wall during hemostasis and inflammation
    • McEver RP. Adhesive interactions of leukocytes, platelets, and the vessel wall during hemostasis and inflammation. Thromb Haemost. 2001;86:746-756.
    • (2001) Thromb Haemost , vol.86 , pp. 746-756
    • McEver, R.P.1
  • 31
    • 10644292431 scopus 로고    scopus 로고
    • Human Pselectin glycoprotein ligand-1 (PSGL-1) interacts with the skin-associated chemokine CCL27 via sulfated tyrosines at the PSGL-1 amino terminus
    • Hirata T, Furukawa Y, Yang BG, et al. Human Pselectin glycoprotein ligand-1 (PSGL-1) interacts with the skin-associated chemokine CCL27 via sulfated tyrosines at the PSGL-1 amino terminus. J Biol Chem. 2004;279:51775-51782.
    • (2004) J Biol Chem , vol.279 , pp. 51775-51782
    • Hirata, T.1    Furukawa, Y.2    Yang, B.G.3
  • 32
    • 0012805136 scopus 로고    scopus 로고
    • Recombinant P-selectin glycoprotein ligand-1 directly inhibits leukocyte rolling by all 3 selectins in vivo: Complete inhibition of rolling is not required for anti-inflammatory effect
    • Hicks AE, Nolan SL, Ridger VC, Hellewell PG, Norman KE. Recombinant P-selectin glycoprotein ligand-1 directly inhibits leukocyte rolling by all 3 selectins in vivo: complete inhibition of rolling is not required for anti-inflammatory effect. Blood. 2003;101:3249-3256.
    • (2003) Blood , vol.101 , pp. 3249-3256
    • Hicks, A.E.1    Nolan, S.L.2    Ridger, V.C.3    Hellewell, P.G.4    Norman, K.E.5
  • 33
    • 12344318633 scopus 로고    scopus 로고
    • PG-M/versican binds to P-selectin glycoprotein ligand-1 and mediates leukocyte aggregation
    • Zheng PS, Vais D, Lapierre D, et al. PG-M/versican binds to P-selectin glycoprotein ligand-1 and mediates leukocyte aggregation. J Cell Sci. 2004;117:5887-5895.
    • (2004) J Cell Sci , vol.117 , pp. 5887-5895
    • Zheng, P.S.1    Vais, D.2    Lapierre, D.3
  • 34
    • 0035907254 scopus 로고    scopus 로고
    • Tyrosine sulfation of glycoprotein I(b)alpha: Role of electrostatic interactions in von Willebrand factor binding
    • Dong J, Ye P, Schade AJ, et al. Tyrosine sulfation of glycoprotein I(b)alpha: role of electrostatic interactions in von Willebrand factor binding. J Biol Chem. 2001;276:16690-16694.
    • (2001) J Biol Chem , vol.276 , pp. 16690-16694
    • Dong, J.1    Ye, P.2    Schade, A.J.3
  • 35
    • 0028863479 scopus 로고
    • PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • Pouyani T, Seed B. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell. 1995;20:333-343.
    • (1995) Cell , vol.20 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 36
    • 0028885684 scopus 로고
    • A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding
    • Sako D, Comess KM, Barone KM, et al. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell. 1995;20:323-331.
    • (1995) Cell , vol.20 , pp. 323-331
    • Sako, D.1    Comess, K.M.2    Barone, K.M.3
  • 37
    • 0032549656 scopus 로고    scopus 로고
    • Identification of N-terminal residues on P-selectin glycoprotein ligand-1 required for binding to P-selectin
    • Liu W, Ramachandran V, Kang J, et al. Identification of N-terminal residues on P-selectin glycoprotein ligand-1 required for binding to P-selectin. J Biol Chem. 1998;20:7078-7087.
    • (1998) J Biol Chem , vol.20 , pp. 7078-7087
    • Liu, W.1    Ramachandran, V.2    Kang, J.3
  • 38
    • 0034816999 scopus 로고    scopus 로고
    • Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin
    • Rodgers SD, Camphausen RT, Hammer DA. Tyrosine sulfation enhances but is not required for PSGL-1 rolling adhesion on P-selectin. Biophys J. 2001;81:2001-2009.
    • (2001) Biophys J , vol.81 , pp. 2001-2009
    • Rodgers, S.D.1    Camphausen, R.T.2    Hammer, D.A.3
  • 39
    • 0141924777 scopus 로고    scopus 로고
    • Targeting platelet-leukocyte interactions: Identification of the integrin Mac-1 binding site for the platelet counter receptor glycoprotein Ibα
    • Ehlers R, Ustinov V, Chen Z, et al. Targeting platelet-leukocyte interactions: identification of the integrin Mac-1 binding site for the platelet counter receptor glycoprotein Ibα. J Exp Med. 2003;198:1077-1088.
    • (2003) J Exp Med , vol.198 , pp. 1077-1088
    • Ehlers, R.1    Ustinov, V.2    Chen, Z.3
  • 40
    • 0027209421 scopus 로고
    • Leukocyte rolling and extravasation are severely compromised in P selectin-deficient mice
    • Mayadas TN, Johnson RC, Rayburn H, Hynes RO, Wagner DD. Leukocyte rolling and extravasation are severely compromised in P selectin-deficient mice. Cell. 1993;74:541-554.
    • (1993) Cell , vol.74 , pp. 541-554
    • Mayadas, T.N.1    Johnson, R.C.2    Rayburn, H.3    Hynes, R.O.4    Wagner, D.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.