메뉴 건너뛰기




Volumn 8, Issue 11, 2010, Pages 2530-2541

Platelet endothelial cell adhesion molecule-1 regulates collagen-stimulated platelet function by modulating the association of phosphatidylinositol 3-kinase with Grb-2-associated binding protein-1 and linker for activation of T cells

Author keywords

GPVI; Inhibitory; ITIM; PECAM 1; Signaling

Indexed keywords

CD31 ANTIGEN; COLLAGEN; GLYCOPROTEIN VI; GLYCOPROTEIN VI FC RECEPTOR GAMMA; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2 ASSOCIATED BINDING PROTEIN 1; LAT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P85; PROTEIN TYROSINE PHOSPHATASE SHP; UNCLASSIFIED DRUG;

EID: 78149258905     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2010.04025.x     Document Type: Article
Times cited : (41)

References (52)
  • 1
    • 0030013876 scopus 로고    scopus 로고
    • Individually distinct Ig homology domains in PECAM-1 regulate homophilic binding and modulate receptor affinity
    • Sun Q-H, DeLisser HM, Zukowski MM, Paddock C, Albelda SM, Newman PJ. Individually distinct Ig homology domains in PECAM-1 regulate homophilic binding and modulate receptor affinity. J Biol Chem 1996; 271: 11090-8.
    • (1996) J Biol Chem , vol.271 , pp. 11090-8
    • Sun, Q.1    DeLisser, H.M.2    Zukowski, M.M.3    Paddock, C.4    Albelda, S.M.5    Newman, P.J.6
  • 2
    • 0029780520 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression
    • Sun J, Williams J, Yan H-C, Amin KM, Albelda SM, DeLisser HM. Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression. J Biol Chem 1996; 271: 18561-70.
    • (1996) J Biol Chem , vol.271 , pp. 18561-70
    • Sun, J.1    Williams, J.2    Yan, H.3    Amin, K.M.4    Albelda, S.M.5    DeLisser, H.M.6
  • 3
    • 0030838730 scopus 로고    scopus 로고
    • Residues on both faces of the first immunoglobulin fold contribute to homophilic binding sites on PECAM-1/CD31
    • Newton JP, Buckley CD, Jones EY, Simmons DL. Residues on both faces of the first immunoglobulin fold contribute to homophilic binding sites on PECAM-1/CD31. J Biol Chem 1997; 272: 20555-63.
    • (1997) J Biol Chem , vol.272 , pp. 20555-63
    • Newton, J.P.1    Buckley, C.D.2    Jones, E.Y.3    Simmons, D.L.4
  • 4
    • 0021984667 scopus 로고
    • A novel leukocyte differentiation antigen: two monoclonal antibodies, TM2 and TM3, define 120-kDa molecule present on neutrophils, monocytes, platelets and activated lymphoblasts
    • Ohto H, Maeda H, Shibata Y, Chen RF, Ozaki Y, Higashihara M, Takeuchi A, Tohyama H. A novel leukocyte differentiation antigen: two monoclonal antibodies, TM2 and TM3, define 120-kDa molecule present on neutrophils, monocytes, platelets and activated lymphoblasts. Blood 1985; 66: 873-81.
    • (1985) Blood , vol.66 , pp. 873-81
    • Ohto, H.1    Maeda, H.2    Shibata, Y.3    Chen, R.F.4    Ozaki, Y.5    Higashihara, M.6    Takeuchi, A.7    Tohyama, H.8
  • 5
  • 6
    • 0034282684 scopus 로고    scopus 로고
    • Collagen, convulxin and thrombin stimulate aggregation-independent tyrosine phosphorylation of CD31 in platelets. Evidence for the involvement of Src family kinases
    • Cicmil M, Thomas JM, Sage T, Barry FA, Leduc M, Bon C, Gibbins JM. Collagen, convulxin and thrombin stimulate aggregation-independent tyrosine phosphorylation of CD31 in platelets. Evidence for the involvement of Src family kinases. J Biol Chem 2000; 275: 27339-47.
    • (2000) J Biol Chem , vol.275 , pp. 27339-47
    • Cicmil, M.1    Thomas, J.M.2    Sage, T.3    Barry, F.A.4    Leduc, M.5    Bon, C.6    Gibbins, J.M.7
  • 7
    • 0036090191 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule-1 signalling inhibits the activation of human platelets
    • Cicmil M, Thomas JM, Leduc M, Bon C, Gibbins JM. Platelet endothelial cell adhesion molecule-1 signalling inhibits the activation of human platelets. Blood 2002; 99: 137-44.
    • (2002) Blood , vol.99 , pp. 137-44
    • Cicmil, M.1    Thomas, J.M.2    Leduc, M.3    Bon, C.4    Gibbins, J.M.5
  • 8
    • 0035869434 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule-1 serves as an inhibitory receptor that modulates platelet responses to collagen
    • Patil S, Newman DK, Newman PJ. Platelet endothelial cell adhesion molecule-1 serves as an inhibitory receptor that modulates platelet responses to collagen. Blood 2001; 97: 1727-32.
    • (2001) Blood , vol.97 , pp. 1727-32
    • Patil, S.1    Newman, D.K.2    Newman, P.J.3
  • 10
    • 0031114043 scopus 로고    scopus 로고
    • Endothelial cell tube formation depends on cadherin and CD31 interactions with filamentous actin
    • Matsumura PW, Wolff K, Petzelbauer P. Endothelial cell tube formation depends on cadherin and CD31 interactions with filamentous actin. J Immunol 1997; 158: 3408-16.
    • (1997) J Immunol , vol.158 , pp. 3408-16
    • Matsumura, P.W.1    Wolff, K.2    Petzelbauer, P.3
  • 11
    • 0030053824 scopus 로고    scopus 로고
    • Molecular cloning and expression of murine vascular endothelial cadherin in early stage development of the cardiovascular system
    • Breier G, Breviario F, Caveda L, Berthier R, Schnürch H, Gotsch U, Vestweber D, Risau W, Dejana E. Molecular cloning and expression of murine vascular endothelial cadherin in early stage development of the cardiovascular system. Blood 1996; 87: 630-41.
    • (1996) Blood , vol.87 , pp. 630-41
    • Breier, G.1    Breviario, F.2    Caveda, L.3    Berthier, R.4    Schnürch, H.5    Gotsch, U.6    Vestweber, D.7    Risau, W.8    Dejana, E.9
  • 13
    • 0027431090 scopus 로고
    • Murine platelet endothelial cell adhesion molecule (PECAM-1/CD31) modulates β2 integrins on lymphokine-activated killer cells
    • Piali L, Albelda SM, Baldwin HS, Hammel P, Gisler RH, Imhof BA. Murine platelet endothelial cell adhesion molecule (PECAM-1/CD31) modulates β2 integrins on lymphokine-activated killer cells. Eur J Immunol 1993; 23: 2464-71.
    • (1993) Eur J Immunol , vol.23 , pp. 2464-71
    • Piali, L.1    Albelda, S.M.2    Baldwin, H.S.3    Hammel, P.4    Gisler, R.H.5    Imhof, B.A.6
  • 14
    • 0033565294 scopus 로고    scopus 로고
    • A new role for platelet-endothelial cell adhesion molecule-1 (CD31): inhibition of TCR-mediated signal transduction
    • Newton-Nash DK, Newman PJ. A new role for platelet-endothelial cell adhesion molecule-1 (CD31): inhibition of TCR-mediated signal transduction. J Immunol 1999; 163: 682-8.
    • (1999) J Immunol , vol.163 , pp. 682-8
    • Newton-Nash, D.K.1    Newman, P.J.2
  • 15
    • 0035871812 scopus 로고    scopus 로고
    • Inhibition of antigen-receptor signaling by platelet endothelial cell-adhesion molecule-1 (CD31) requires an intact ITIM, SHP-2, and p56Lck
    • Newman DK, Hamilton CA, Armstrong MJ, Newman PJ. Inhibition of antigen-receptor signaling by platelet endothelial cell-adhesion molecule-1 (CD31) requires an intact ITIM, SHP-2, and p56Lck. Blood 2000; 97: 2351-7.
    • (2000) Blood , vol.97 , pp. 2351-7
    • Newman, D.K.1    Hamilton, C.A.2    Armstrong, M.J.3    Newman, P.J.4
  • 16
    • 0027248750 scopus 로고
    • PECAM-1 is required for transendothelial migration of leukocytes
    • Muller WA, Weigl SA, Deng X, Phillips DM. PECAM-1 is required for transendothelial migration of leukocytes. J Exp Med 1993; 178: 449-60.
    • (1993) J Exp Med , vol.178 , pp. 449-60
    • Muller, W.A.1    Weigl, S.A.2    Deng, X.3    Phillips, D.M.4
  • 18
    • 34548825638 scopus 로고    scopus 로고
    • JAM-A mediates neutrophil transmigration in a stimulus-specific manner in vivo: evidence for sequential roles for JAM-A and PECAM-1 in neutrophil transmigration
    • Woodfin A, Reichel C, Khandoga A, Corada M, Voisin M-B, Scheiermann C, Haskard DO, Dejana E, Krombach F, Nourshargh S. JAM-A mediates neutrophil transmigration in a stimulus-specific manner in vivo: evidence for sequential roles for JAM-A and PECAM-1 in neutrophil transmigration. Blood 2007; 110: 1848-56.
    • (2007) Blood , vol.110 , pp. 1848-56
    • Woodfin, A.1    Reichel, C.2    Khandoga, A.3    Corada, M.4    Voisin, M.5    Scheiermann, C.6    Haskard, D.O.7    Dejana, E.8    Krombach, F.9    Nourshargh, S.10
  • 19
    • 33745115094 scopus 로고    scopus 로고
    • ICAM-2 mediates neutrophil transmigration in vivo: evidence for stimulus specificity and a role in PECAM-1-independent transmigration
    • Huang MT, Larbi KY, Scheiermann C, Woodfin A, Gerwin N, Haskard DO, Nourshargh S. ICAM-2 mediates neutrophil transmigration in vivo: evidence for stimulus specificity and a role in PECAM-1-independent transmigration. Blood 2006; 107: 4721-7.
    • (2006) Blood , vol.107 , pp. 4721-7
    • Huang, M.T.1    Larbi, K.Y.2    Scheiermann, C.3    Woodfin, A.4    Gerwin, N.5    Haskard, D.O.6    Nourshargh, S.7
  • 20
    • 0037370631 scopus 로고    scopus 로고
    • Lack of platelet endothelial cell adhesion molecule-1 attenuates foreign body inflammation because of decreased angiogenesis
    • Solowiej A, Biswas P, Graesser D, Madri JA. Lack of platelet endothelial cell adhesion molecule-1 attenuates foreign body inflammation because of decreased angiogenesis. Am J Pathol 2003; 162: 953-62.
    • (2003) Am J Pathol , vol.162 , pp. 953-62
    • Solowiej, A.1    Biswas, P.2    Graesser, D.3    Madri, J.A.4
  • 23
    • 0030936012 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase SHP-2 binds PECAM-1 and forms a distinct signaling complex during platelet aggregation: evidence for a mechanistic link between PECAM-1 and integrin-mediated cellular signaling
    • Jackson DE, Ward CM, Wang R, Newman PJ. The protein-tyrosine phosphatase SHP-2 binds PECAM-1 and forms a distinct signaling complex during platelet aggregation: evidence for a mechanistic link between PECAM-1 and integrin-mediated cellular signaling. J Biol Chem 1997; 272: 6986-93.
    • (1997) J Biol Chem , vol.272 , pp. 6986-93
    • Jackson, D.E.1    Ward, C.M.2    Wang, R.3    Newman, P.J.4
  • 24
    • 0032884256 scopus 로고    scopus 로고
    • Thrombin-induced association of SHP-2 with multiple tyrosine-phosphorylated proteins in human platelets
    • Edmead CE, Crosby DA, Southcott M, Poole AW. Thrombin-induced association of SHP-2 with multiple tyrosine-phosphorylated proteins in human platelets. FEBS Lett 1999; 459: 27-32.
    • (1999) FEBS Lett , vol.459 , pp. 27-32
    • Edmead, C.E.1    Crosby, D.A.2    Southcott, M.3    Poole, A.W.4
  • 25
    • 0032894612 scopus 로고    scopus 로고
    • Switched at birth: a new family for PECAM-1
    • Newman PJ. Switched at birth: a new family for PECAM-1. J Clin Invest 1999; 103: 5-9.
    • (1999) J Clin Invest , vol.103 , pp. 5-9
    • Newman, P.J.1
  • 26
    • 0038120892 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology
    • Newman PJ, Newman DK. Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology. Arterioscler Thromb Vasc Biol 2003; 23: 953-64.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 953-64
    • Newman, P.J.1    Newman, D.K.2
  • 27
    • 0141867737 scopus 로고    scopus 로고
    • PECAM-1: old friend, new partners
    • Ilan N, Madri JA. PECAM-1: old friend, new partners. Curr Opin Cell Biol 2003; 15: 515-24.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 515-24
    • Ilan, N.1    Madri, J.A.2
  • 28
    • 0030716868 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase SHP-2 associates with tyrosine-phosphorylated adhesion molecule PECAM-1 (CD31)
    • Sagawa K, Kimura T, Swieter M, Siraganian RP. The protein-tyrosine phosphatase SHP-2 associates with tyrosine-phosphorylated adhesion molecule PECAM-1 (CD31). J Biol Chem 1997; 272: 31086-91.
    • (1997) J Biol Chem , vol.272 , pp. 31086-91
    • Sagawa, K.1    Kimura, T.2    Swieter, M.3    Siraganian, R.P.4
  • 29
    • 0030855963 scopus 로고    scopus 로고
    • Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet endothelial cell-adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2
    • Jackson DE, Kupcho KR, Newman PJ. Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet endothelial cell-adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2. J Biol Chem 1997; 272: 24868-75.
    • (1997) J Biol Chem , vol.272 , pp. 24868-75
    • Jackson, D.E.1    Kupcho, K.R.2    Newman, P.J.3
  • 30
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
    • Feng GS, Hui CC, Pawson T. SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases. Science 1993; 259: 1607-11.
    • (1993) Science , vol.259 , pp. 1607-11
    • Feng, G.S.1    Hui, C.C.2    Pawson, T.3
  • 31
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew
    • Freeman RM, Plutzky J Jr, Neel BG. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc Natl Acad Sci USA 1992; 89: 11239-43.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11239-43
    • Freeman, R.M.1    Plutzky Jr, J.2    Neel, B.G.3
  • 32
    • 0027399168 scopus 로고
    • Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation
    • Vogel W, Lammers R, Huang J, Ullrich A. Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science 1993; 259: 1611-14.
    • (1993) Science , vol.259 , pp. 1611-14
    • Vogel, W.1    Lammers, R.2    Huang, J.3    Ullrich, A.4
  • 33
    • 0034572534 scopus 로고    scopus 로고
    • The SHP-2 tyrosine phosphatase: signalling mechanisms and biological functions
    • Kui QC. The SHP-2 tyrosine phosphatase: signalling mechanisms and biological functions. Cell Res 2000; 10: 279-88.
    • (2000) Cell Res , vol.10 , pp. 279-88
    • Kui, Q.C.1
  • 34
    • 0034681445 scopus 로고    scopus 로고
    • Requirement for protein-tyrosine phosphatase SHP-2 in insulin-induced activation of c-jun NH2-terminal kinase
    • Fukunaga K, Noguchi T, Takeda H, Matozaki T, Hayashi Y, Itoh H, Kasuga M. Requirement for protein-tyrosine phosphatase SHP-2 in insulin-induced activation of c-jun NH2-terminal kinase. J Biol Chem 2000; 275: 5208-13.
    • (2000) J Biol Chem , vol.275 , pp. 5208-13
    • Fukunaga, K.1    Noguchi, T.2    Takeda, H.3    Matozaki, T.4    Hayashi, Y.5    Itoh, H.6    Kasuga, M.7
  • 35
    • 0033602224 scopus 로고    scopus 로고
    • Immune signalling: SHP-2 docks at multiple ports
    • Huyer G, Alexander DR. Immune signalling: SHP-2 docks at multiple ports. Curr Biol 1999; 9: 129-32.
    • (1999) Curr Biol , vol.9 , pp. 129-32
    • Huyer, G.1    Alexander, D.R.2
  • 38
    • 0036258332 scopus 로고    scopus 로고
    • Receptor-specific regulation of phosphatidylinositol 3′-kinase activation by the protein tyrosine phosphatase SHP-2
    • Zhang SQ, Tsiaras WG, Araki T, Wen G, Minichiello L, Klein R, Neel BG. Receptor-specific regulation of phosphatidylinositol 3′-kinase activation by the protein tyrosine phosphatase SHP-2. Mol Cell Biol 2002; 22: 4062-72.
    • (2002) Mol Cell Biol , vol.22 , pp. 4062-72
    • Zhang, S.Q.1    Tsiaras, W.G.2    Araki, T.3    Wen, G.4    Minichiello, L.5    Klein, R.6    Neel, B.G.7
  • 39
    • 0032545307 scopus 로고    scopus 로고
    • The p85 subunit of phosphatidylinositol 3-kinase associates with the Fc receptor gamma-chain and linker for activation of T cells (LAT) in platelets stimulated by collagen and convulxin
    • Gibbins JM, Briddon S, Shutes A, Van Vugt MJ, Van De Winkel JG, Saito T, Watson SP. The p85 subunit of phosphatidylinositol 3-kinase associates with the Fc receptor gamma-chain and linker for activation of T cells (LAT) in platelets stimulated by collagen and convulxin. J Biol Chem 1998; 273: 34437-43.
    • (1998) J Biol Chem , vol.273 , pp. 34437-43
    • Gibbins, J.M.1    Briddon, S.2    Shutes, A.3    Van Vugt, M.J.4    Van De Winkel, J.G.5    Saito, T.6    Watson, S.P.7
  • 41
    • 4444260266 scopus 로고    scopus 로고
    • Platelet adhesion signaling and the regulation of thrombus formation
    • Gibbins JM. Platelet adhesion signaling and the regulation of thrombus formation. J Cell Sci 2004; 117: 3415-25.
    • (2004) J Cell Sci , vol.117 , pp. 3415-25
    • Gibbins, J.M.1
  • 47
    • 0035968279 scopus 로고    scopus 로고
    • Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP-2
    • Cunnick JM, Mei L, Doupnik CA, Wu J. Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP-2. J Biol Chem 2001; 276: 24380-7.
    • (2001) J Biol Chem , vol.276 , pp. 24380-7
    • Cunnick, J.M.1    Mei, L.2    Doupnik, C.A.3    Wu, J.4
  • 48
    • 0035006702 scopus 로고    scopus 로고
    • Role of phosphatidylinositol-3 kinase and its association with Gab1 in thrombopoietin-mediated up-regulation of platelet function
    • Kojima H, Shinagawa A, Shimizu S, Kanada H, Hibi M, Hirano T, Nagasawa T. Role of phosphatidylinositol-3 kinase and its association with Gab1 in thrombopoietin-mediated up-regulation of platelet function. Exp Hematol 2001; 29: 616-22.
    • (2001) Exp Hematol , vol.29 , pp. 616-22
    • Kojima, H.1    Shinagawa, A.2    Shimizu, S.3    Kanada, H.4    Hibi, M.5    Hirano, T.6    Nagasawa, T.7
  • 49
    • 33845974917 scopus 로고    scopus 로고
    • Lipid rafts facilitate the interaction of PECAM-1 with the glycoprotein VI-FcR gamma-chain complex in human platelets
    • Lee FA, Van Lier M, Relou IA, Foley L, Akkerman JW, Heijnem HF, Farndale RW. Lipid rafts facilitate the interaction of PECAM-1 with the glycoprotein VI-FcR gamma-chain complex in human platelets. J Biol Chem 2006; 281: 39330-8.
    • (2006) J Biol Chem , vol.281 , pp. 39330-8
    • Lee, F.A.1    Van Lier, M.2    Relou, I.A.3    Foley, L.4    Akkerman, J.W.5    Heijnem, H.F.6    Farndale, R.W.7
  • 51
    • 70349251723 scopus 로고    scopus 로고
    • Genetic evidence for a predominant role of PI3K beta catalytic activity in ITAM- and integrin-mediated signaling in platelets
    • Canobbio I, Stefanini L, Cipolla L, Ciraolo E, Gruppi C, Balduini C, Hirsch E, Torti M. Genetic evidence for a predominant role of PI3K beta catalytic activity in ITAM- and integrin-mediated signaling in platelets. Blood 2009; 114: 2193-6.
    • (2009) Blood , vol.114 , pp. 2193-6
    • Canobbio, I.1    Stefanini, L.2    Cipolla, L.3    Ciraolo, E.4    Gruppi, C.5    Balduini, C.6    Hirsch, E.7    Torti, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.