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Volumn 42, Issue 6, 2012, Pages 686-691

Leucocyte recruitment in inflammation and novel endogenous negative regulators thereof

Author keywords

Inflammation; Integrin; Leukocyte adhesion; Leukocyte endothelial interactions

Indexed keywords

BETA2 INTEGRIN; CHEMOKINE; CHEMOKINE RECEPTOR; DEVELOPMENTAL ENDOTHELIAL LOCUS 1 PROTEIN; GLYCOPROTEIN; GROWTH DIFFERENTIATION FACTOR 15; IMMUNOGLOBULIN; INTEGRIN; LEUKOCYTE MIGRATION INHIBITION FACTOR; PENTRAXIN 3; SELECTIN; UNCLASSIFIED DRUG;

EID: 84860892863     PISSN: 00142972     EISSN: 13652362     Source Type: Journal    
DOI: 10.1111/j.1365-2362.2012.02677.x     Document Type: Review
Times cited : (40)

References (78)
  • 1
    • 70350450886 scopus 로고    scopus 로고
    • Novel aspects in the regulation of the leukocyte adhesion cascade
    • Chavakis E, Choi EY, Chavakis T. Novel aspects in the regulation of the leukocyte adhesion cascade. Thromb Haemost 2009;102:191-7.
    • (2009) Thromb Haemost , vol.102 , pp. 191-197
    • Chavakis, E.1    Choi, E.Y.2    Chavakis, T.3
  • 2
    • 30044447736 scopus 로고    scopus 로고
    • Immune cell migration in inflammation: present and future therapeutic targets
    • Luster AD, Alon R, von Andrian UH. Immune cell migration in inflammation: present and future therapeutic targets. Nat Immunol 2005;6:1182-90.
    • (2005) Nat Immunol , vol.6 , pp. 1182-1190
    • Luster, A.D.1    Alon, R.2    von Andrian, U.H.3
  • 3
    • 68149162037 scopus 로고    scopus 로고
    • Leukocyte-endothelial interactions in inflammation
    • Langer HF, Chavakis T. Leukocyte-endothelial interactions in inflammation. J Cell Mol Med 2009;13:1211-20.
    • (2009) J Cell Mol Med , vol.13 , pp. 1211-1220
    • Langer, H.F.1    Chavakis, T.2
  • 4
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: the leukocyte adhesion cascade updated
    • Ley K, Laudanna C, Cybulsky MI, Nourshargh S. Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat Rev Immunol 2007;7:678-89.
    • (2007) Nat Rev Immunol , vol.7 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 5
    • 34447300158 scopus 로고    scopus 로고
    • Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium
    • Vestweber D. Adhesion and signaling molecules controlling the transmigration of leukocytes through endothelium. Immunol Rev 2007;218:178-96.
    • (2007) Immunol Rev , vol.218 , pp. 178-196
    • Vestweber, D.1
  • 6
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: lectins that initiate cell adhesion under flow
    • McEver RP. Selectins: lectins that initiate cell adhesion under flow. Curr Opin Cell Biol 2002;14:581-6.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 7
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi T. Intracellular signalling controlling integrin activation in lymphocytes. Nat Rev Immunol 2005;5:546-59.
    • (2005) Nat Rev Immunol , vol.5 , pp. 546-559
    • Kinashi, T.1
  • 8
    • 18244364123 scopus 로고    scopus 로고
    • Lymphocyte arrest requires instantaneous induction of an extended LFA-1 conformation mediated by endothelium-bound chemokines
    • Shamri R, Grabovsky V, Gauguet JM, Feigelson S, Manevich E, Kolanus W et al. Lymphocyte arrest requires instantaneous induction of an extended LFA-1 conformation mediated by endothelium-bound chemokines. Nat Immunol 2005;6:497-506.
    • (2005) Nat Immunol , vol.6 , pp. 497-506
    • Shamri, R.1    Grabovsky, V.2    Gauguet, J.M.3    Feigelson, S.4    Manevich, E.5    Kolanus, W.6
  • 9
    • 33846027057 scopus 로고    scopus 로고
    • Phospholipase C, calcium, and calmodulin are critical for alpha4beta1 integrin affinity up-regulation and monocyte arrest triggered by chemoattractants
    • Hyduk SJ, Chan JR, Duffy ST, Chen M, Peterson MD, Waddell TK et al. Phospholipase C, calcium, and calmodulin are critical for alpha4beta1 integrin affinity up-regulation and monocyte arrest triggered by chemoattractants. Blood 2007;109:176-84.
    • (2007) Blood , vol.109 , pp. 176-184
    • Hyduk, S.J.1    Chan, J.R.2    Duffy, S.T.3    Chen, M.4    Peterson, M.D.5    Waddell, T.K.6
  • 10
    • 33744551677 scopus 로고    scopus 로고
    • Rap1 regulation of RIAM and cell adhesion
    • Lafuente E, Boussiotis VA. Rap1 regulation of RIAM and cell adhesion. Methods Enzymol 2006;407:345-58.
    • (2006) Methods Enzymol , vol.407 , pp. 345-358
    • Lafuente, E.1    Boussiotis, V.A.2
  • 11
    • 27944476021 scopus 로고    scopus 로고
    • Specific integrin alpha and beta chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms
    • Fagerholm SC, Hilden TJ, Nurmi SM, Gahmberg CG. Specific integrin alpha and beta chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms. J Cell Biol 2005;171:705-15.
    • (2005) J Cell Biol , vol.171 , pp. 705-715
    • Fagerholm, S.C.1    Hilden, T.J.2    Nurmi, S.M.3    Gahmberg, C.G.4
  • 12
    • 43549103373 scopus 로고    scopus 로고
    • Regulation of LFA-1-dependent inflammatory cell recruitment by Cbl-b and 14-3-3 proteins
    • Choi EY, Orlova VV, Fagerholm SC, Nurmi SM, Zhang L, Ballantyne CM et al. Regulation of LFA-1-dependent inflammatory cell recruitment by Cbl-b and 14-3-3 proteins. Blood 2008;111:3607-14.
    • (2008) Blood , vol.111 , pp. 3607-3614
    • Choi, E.Y.1    Orlova, V.V.2    Fagerholm, S.C.3    Nurmi, S.M.4    Zhang, L.5    Ballantyne, C.M.6
  • 13
    • 33748454742 scopus 로고    scopus 로고
    • Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3
    • Han J, Lim CJ, Watanabe N, Soriani A, Ratnikov B, Calderwood DA et al. Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3. Curr Biol 2006;16:1796-806.
    • (2006) Curr Biol , vol.16 , pp. 1796-1806
    • Han, J.1    Lim, C.J.2    Watanabe, N.3    Soriani, A.4    Ratnikov, B.5    Calderwood, D.A.6
  • 14
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee HS, Lim CJ, Puzon-McLaughlin W, Shattil SJ, Ginsberg MH. RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J Biol Chem 2009;284:5119-27.
    • (2009) J Biol Chem , vol.284 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2    Puzon-McLaughlin, W.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 15
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, Ruppert R, Schmidt S, Sixt M et al. Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med 2009;15:300-5.
    • (2009) Nat Med , vol.15 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3    Ruppert, R.4    Schmidt, S.5    Sixt, M.6
  • 16
    • 34250180872 scopus 로고    scopus 로고
    • Spleen tyrosine kinase Syk is necessary for E-selectin-induced alpha(L)beta(2) integrin-mediated rolling on intercellular adhesion molecule-1
    • Zarbock A, Lowell CA, Ley K. Spleen tyrosine kinase Syk is necessary for E-selectin-induced alpha(L)beta(2) integrin-mediated rolling on intercellular adhesion molecule-1. Immunity 2007;26:773-83.
    • (2007) Immunity , vol.26 , pp. 773-783
    • Zarbock, A.1    Lowell, C.A.2    Ley, K.3
  • 17
    • 53349171447 scopus 로고    scopus 로고
    • PSGL-1 engagement by E-selectin signals through Src kinase Fgr and ITAM adapters DAP12 and FcR gamma to induce slow leukocyte rolling
    • Zarbock A, Abram CL, Hundt M, Altman A, Lowell CA, Ley K. PSGL-1 engagement by E-selectin signals through Src kinase Fgr and ITAM adapters DAP12 and FcR gamma to induce slow leukocyte rolling. J Exp Med 2008;205:2339-47.
    • (2008) J Exp Med , vol.205 , pp. 2339-2347
    • Zarbock, A.1    Abram, C.L.2    Hundt, M.3    Altman, A.4    Lowell, C.A.5    Ley, K.6
  • 18
    • 1842684991 scopus 로고    scopus 로고
    • Rolling adhesion through an extended conformation of integrin alphaLbeta2 and relation to alpha I and beta I-like domain interaction
    • Salas A, Shimaoka M, Kogan AN, Harwood C, von Andrian UH, Springer TA. Rolling adhesion through an extended conformation of integrin alphaLbeta2 and relation to alpha I and beta I-like domain interaction. Immunity 2004;20:393-406.
    • (2004) Immunity , vol.20 , pp. 393-406
    • Salas, A.1    Shimaoka, M.2    Kogan, A.N.3    Harwood, C.4    von Andrian, U.H.5    Springer, T.A.6
  • 19
    • 72449156722 scopus 로고    scopus 로고
    • Leukocyte integrins and their ligand interactions
    • Hyun YM, Lefort CT, Kim M. Leukocyte integrins and their ligand interactions. Immunol Res 2009;45:195-208.
    • (2009) Immunol Res , vol.45 , pp. 195-208
    • Hyun, Y.M.1    Lefort, C.T.2    Kim, M.3
  • 20
    • 14644391560 scopus 로고    scopus 로고
    • Targeting leukocyte integrins in human diseases
    • Yonekawa K, Harlan JM. Targeting leukocyte integrins in human diseases. J Leukoc Biol 2005;77:129-40.
    • (2005) J Leukoc Biol , vol.77 , pp. 129-140
    • Yonekawa, K.1    Harlan, J.M.2
  • 21
    • 10744229528 scopus 로고    scopus 로고
    • The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: a novel pathway for inflammatory cell recruitment
    • Chavakis T, Bierhaus A, Al-Fakhri N, Schneider D, Witte S, Linn T et al. The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: a novel pathway for inflammatory cell recruitment. J Exp Med 2003;198:1507-15.
    • (2003) J Exp Med , vol.198 , pp. 1507-1515
    • Chavakis, T.1    Bierhaus, A.2    Al-Fakhri, N.3    Schneider, D.4    Witte, S.5    Linn, T.6
  • 22
    • 41549101916 scopus 로고    scopus 로고
    • ICAM-5--a novel two-facetted adhesion molecule in the mammalian brain
    • Gahmberg CG, Tian L, Ning L, Nyman-Huttunen H. ICAM-5--a novel two-facetted adhesion molecule in the mammalian brain. Immunol Lett 2008;117:131-5.
    • (2008) Immunol Lett , vol.117 , pp. 131-135
    • Gahmberg, C.G.1    Tian, L.2    Ning, L.3    Nyman-Huttunen, H.4
  • 24
    • 0021707124 scopus 로고
    • Inherited deficiency of the Mac-1, LFA-1, p150,95 glycoprotein family and its molecular basis
    • Springer TA, Thompson WS, Miller LJ, Schmalstieg FC, Anderson DC. Inherited deficiency of the Mac-1, LFA-1, p150, 95 glycoprotein family and its molecular basis. J Exp Med 1984;160:1901-18.
    • (1984) J Exp Med , vol.160 , pp. 1901-1918
    • Springer, T.A.1    Thompson, W.S.2    Miller, L.J.3    Schmalstieg, F.C.4    Anderson, D.C.5
  • 25
    • 0033519360 scopus 로고    scopus 로고
    • Lymphocyte migration in lymphocyte function-associated antigen (LFA)-1-deficient mice
    • Berlin-Rufenach C, Otto F, Mathies M, Westermann J, Owen MJ, Hamann A et al. Lymphocyte migration in lymphocyte function-associated antigen (LFA)-1-deficient mice. J Exp Med 1999;189:1467-78.
    • (1999) J Exp Med , vol.189 , pp. 1467-1478
    • Berlin-Rufenach, C.1    Otto, F.2    Mathies, M.3    Westermann, J.4    Owen, M.J.5    Hamann, A.6
  • 26
    • 0035876921 scopus 로고    scopus 로고
    • The differential roles of LFA-1 and Mac-1 in host defense against systemic infection with Streptococcus pneumoniae
    • Prince JE, Brayton CF, Fossett MC, Durand JA, Kaplan SL, Smith CW et al. The differential roles of LFA-1 and Mac-1 in host defense against systemic infection with Streptococcus pneumoniae. J Immunol 2001;166:7362-9.
    • (2001) J Immunol , vol.166 , pp. 7362-7369
    • Prince, J.E.1    Brayton, C.F.2    Fossett, M.C.3    Durand, J.A.4    Kaplan, S.L.5    Smith, C.W.6
  • 30
    • 34347251966 scopus 로고    scopus 로고
    • Suppression of established experimental autoimmune uveitis by anti-LFA-1alpha Ab
    • Ke Y, Sun D, Zhang P, Jiang G, Kaplan HJ, Shao H. Suppression of established experimental autoimmune uveitis by anti-LFA-1alpha Ab. Invest Ophthalmol Vis Sci 2007;48:2667-75.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 2667-2675
    • Ke, Y.1    Sun, D.2    Zhang, P.3    Jiang, G.4    Kaplan, H.J.5    Shao, H.6
  • 31
    • 33645881090 scopus 로고    scopus 로고
    • Suppression of experimental autoimmune encephalomyelitis by extracellular adherence protein of Staphylococcus aureus
    • Xie C, Alcaide P, Geisbrecht BV, Schneider D, Herrmann M, Preissner KT et al. Suppression of experimental autoimmune encephalomyelitis by extracellular adherence protein of Staphylococcus aureus. J Exp Med 2006;203:985-94.
    • (2006) J Exp Med , vol.203 , pp. 985-994
    • Xie, C.1    Alcaide, P.2    Geisbrecht, B.V.3    Schneider, D.4    Herrmann, M.5    Preissner, K.T.6
  • 32
    • 27744451956 scopus 로고    scopus 로고
    • Critical requirement of CD11b (Mac-1) on T cells and accessory cells for development of experimental autoimmune encephalomyelitis
    • Bullard DC, Hu X, Schoeb TR, Axtell RC, Raman C, Barnum SR. Critical requirement of CD11b (Mac-1) on T cells and accessory cells for development of experimental autoimmune encephalomyelitis. J Immunol 2005;175:6327-33.
    • (2005) J Immunol , vol.175 , pp. 6327-6333
    • Bullard, D.C.1    Hu, X.2    Schoeb, T.R.3    Axtell, R.C.4    Raman, C.5    Barnum, S.R.6
  • 33
    • 34250779802 scopus 로고    scopus 로고
    • Natalizumab for multiple sclerosis
    • Ransohoff RM. Natalizumab for multiple sclerosis. N Engl J Med 2007;356:2622-9.
    • (2007) N Engl J Med , vol.356 , pp. 2622-2629
    • Ransohoff, R.M.1
  • 35
    • 33745313872 scopus 로고    scopus 로고
    • The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating beta 2 integrin affinity and valency in neutrophils, but are required for beta 2 integrin-mediated outside-in signaling involved in sustained adhesion
    • Giagulli C, Ottoboni L, Caveggion E, Rossi B, Lowell C, Constantin G et al. The Src family kinases Hck and Fgr are dispensable for inside-out, chemoattractant-induced signaling regulating beta 2 integrin affinity and valency in neutrophils, but are required for beta 2 integrin-mediated outside-in signaling involved in sustained adhesion. J Immunol 2006;177:604-11.
    • (2006) J Immunol , vol.177 , pp. 604-611
    • Giagulli, C.1    Ottoboni, L.2    Caveggion, E.3    Rossi, B.4    Lowell, C.5    Constantin, G.6
  • 36
    • 33747149898 scopus 로고    scopus 로고
    • Impaired integrin-dependent function in Wiskott-Aldrich syndrome protein-deficient murine and human neutrophils
    • Zhang H, Schaff UY, Green CE, Chen H, Sarantos MR, Hu Y et al. Impaired integrin-dependent function in Wiskott-Aldrich syndrome protein-deficient murine and human neutrophils. Immunity 2006;25:285-95.
    • (2006) Immunity , vol.25 , pp. 285-295
    • Zhang, H.1    Schaff, U.Y.2    Green, C.E.3    Chen, H.4    Sarantos, M.R.5    Hu, Y.6
  • 37
    • 33751525386 scopus 로고    scopus 로고
    • Intraluminal crawling of neutrophils to emigration sites: a molecularly distinct process from adhesion in the recruitment cascade
    • Phillipson M, Heit B, Colarusso P, Liu L, Ballantyne CM, Kubes P. Intraluminal crawling of neutrophils to emigration sites: a molecularly distinct process from adhesion in the recruitment cascade. J Exp Med 2006;203:2569-75.
    • (2006) J Exp Med , vol.203 , pp. 2569-2575
    • Phillipson, M.1    Heit, B.2    Colarusso, P.3    Liu, L.4    Ballantyne, C.M.5    Kubes, P.6
  • 38
    • 4544314167 scopus 로고    scopus 로고
    • Locomotion of monocytes on endothelium is a critical step during extravasation
    • Schenkel AR, Mamdouh Z, Muller WA. Locomotion of monocytes on endothelium is a critical step during extravasation. Nat Immunol 2004;5:393-400.
    • (2004) Nat Immunol , vol.5 , pp. 393-400
    • Schenkel, A.R.1    Mamdouh, Z.2    Muller, W.A.3
  • 39
    • 14644441615 scopus 로고    scopus 로고
    • Transmigration through venular walls: a key regulator of leukocyte phenotype and function
    • Nourshargh S, Marelli-Berg FM. Transmigration through venular walls: a key regulator of leukocyte phenotype and function. Trends Immunol 2005;26:157-65.
    • (2005) Trends Immunol , vol.26 , pp. 157-165
    • Nourshargh, S.1    Marelli-Berg, F.M.2
  • 40
    • 80052026271 scopus 로고    scopus 로고
    • The junctional adhesion molecule JAM-C regulates polarized transendothelial migration of neutrophils in vivo
    • Woodfin A, Voisin MB, Beyrau M, Colom B, Caille D, Diapouli FM et al. The junctional adhesion molecule JAM-C regulates polarized transendothelial migration of neutrophils in vivo. Nat Immunol 2011;12:761-9.
    • (2011) Nat Immunol , vol.12 , pp. 761-769
    • Woodfin, A.1    Voisin, M.B.2    Beyrau, M.3    Colom, B.4    Caille, D.5    Diapouli, F.M.6
  • 41
    • 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 et al. 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. 4721-4727
    • Huang, M.T.1    Larbi, K.Y.2    Scheiermann, C.3    Woodfin, A.4    Gerwin, N.5    Haskard, D.O.6
  • 42
    • 19944428045 scopus 로고    scopus 로고
    • Coordinated redistribution of leukocyte LFA-1 and endothelial cell ICAM-1 accompany neutrophil transmigration
    • Shaw SK, Ma S, Kim MB, Rao RM, Hartman CU, Froio RM et al. Coordinated redistribution of leukocyte LFA-1 and endothelial cell ICAM-1 accompany neutrophil transmigration. J Exp Med 2004;200:1571-80.
    • (2004) J Exp Med , vol.200 , pp. 1571-1580
    • Shaw, S.K.1    Ma, S.2    Kim, M.B.3    Rao, R.M.4    Hartman, C.U.5    Froio, R.M.6
  • 43
    • 0037434714 scopus 로고    scopus 로고
    • Targeted recycling of PECAM from endothelial surface-connected compartments during diapedesis
    • Mamdouh Z, Chen X, Pierini LM, Maxfield FR, Muller WA. Targeted recycling of PECAM from endothelial surface-connected compartments during diapedesis. Nature 2003;421:748-53.
    • (2003) Nature , vol.421 , pp. 748-753
    • Mamdouh, Z.1    Chen, X.2    Pierini, L.M.3    Maxfield, F.R.4    Muller, W.A.5
  • 44
    • 34548167543 scopus 로고    scopus 로고
    • The neutrophil-specific antigen CD177 is a counter-receptor for platelet endothelial cell adhesion molecule-1 (CD31)
    • Sachs UJ, Andrei-Selmer CL, Maniar A, Weiss T, Paddock C, Orlova VV et al. The neutrophil-specific antigen CD177 is a counter-receptor for platelet endothelial cell adhesion molecule-1 (CD31). J Biol Chem 2007;282:23603-12.
    • (2007) J Biol Chem , vol.282 , pp. 23603-23612
    • Sachs, U.J.1    Andrei-Selmer, C.L.2    Maniar, A.3    Weiss, T.4    Paddock, C.5    Orlova, V.V.6
  • 45
    • 77956524006 scopus 로고    scopus 로고
    • CD99 and CD99L2 act at the same site as, but independently of PECAM-1 during leukocyte diapedesis
    • Bixel MG, Li H, Petri B, Khandoga AG, Khandoga A, Zarbock A et al. CD99 and CD99L2 act at the same site as, but independently of PECAM-1 during leukocyte diapedesis. Blood 2010;116:1172-84.
    • (2010) Blood , vol.116 , pp. 1172-1184
    • Bixel, M.G.1    Li, H.2    Petri, B.3    Khandoga, A.G.4    Khandoga, A.5    Zarbock, A.6
  • 46
    • 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, Linder M, Ruf A, Preissner KT 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;196:679-91.
    • (2002) J Exp Med , vol.196 , pp. 679-691
    • Santoso, S.1    Sachs, U.J.2    Kroll, H.3    Linder, M.4    Ruf, A.5    Preissner, K.T.6
  • 47
    • 0036008013 scopus 로고    scopus 로고
    • JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes
    • Ostermann G, Weber KS, Zernecke A, Schroder A, Weber C. JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes. Nat Immunol 2002;3:151-8.
    • (2002) Nat Immunol , vol.3 , pp. 151-158
    • Ostermann, G.1    Weber, K.S.2    Zernecke, A.3    Schroder, A.4    Weber, C.5
  • 49
    • 34547859252 scopus 로고    scopus 로고
    • Regulation of vascular endothelial permeability by junctional adhesion molecules (JAM)
    • Orlova VV, Chavakis T. Regulation of vascular endothelial permeability by junctional adhesion molecules (JAM). Thromb Haemost 2007;98:327-32.
    • (2007) Thromb Haemost , vol.98 , pp. 327-332
    • Orlova, V.V.1    Chavakis, T.2
  • 50
    • 23044465208 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A-deficient polymorphonuclear cells show reduced diapedesis in peritonitis and heart ischemia-reperfusion injury
    • Corada M, Chimenti S, Cera MR, Vinci M, Salio M, Fiordaliso F et al. Junctional adhesion molecule-A-deficient polymorphonuclear cells show reduced diapedesis in peritonitis and heart ischemia-reperfusion injury. Proc Natl Acad Sci U S A 2005;102:10634-9.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10634-10639
    • Corada, M.1    Chimenti, S.2    Cera, M.R.3    Vinci, M.4    Salio, M.5    Fiordaliso, F.6
  • 51
    • 11144304343 scopus 로고    scopus 로고
    • The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo
    • Chavakis T, Keiper T, Matz-Westphal R, Hersemeyer K, Sachs UJ, Nawroth PP et al. The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. J Biol Chem 2004;279:55602-8.
    • (2004) J Biol Chem , vol.279 , pp. 55602-55608
    • Chavakis, T.1    Keiper, T.2    Matz-Westphal, R.3    Hersemeyer, K.4    Sachs, U.J.5    Nawroth, P.P.6
  • 52
    • 18644384462 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation
    • Aurrand-Lions M, Lamagna C, Dangerfield JP, Wang S, Herrera P, Nourshargh S et al. Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation. J Immunol 2005;174:6406-15.
    • (2005) J Immunol , vol.174 , pp. 6406-6415
    • Aurrand-Lions, M.1    Lamagna, C.2    Dangerfield, J.P.3    Wang, S.4    Herrera, P.5    Nourshargh, S.6
  • 53
    • 79958863561 scopus 로고    scopus 로고
    • A novel function of Junctional Adhesion Molecule-C in mediating melanoma cell metastasis
    • Langer HF, Orlova VV, Xie C, Kaul S, Schneider D, Lonsdorf AS et al. A novel function of Junctional Adhesion Molecule-C in mediating melanoma cell metastasis. Cancer Res 2011;71:4096-105.
    • (2011) Cancer Res , vol.71 , pp. 4096-4105
    • Langer, H.F.1    Orlova, V.V.2    Xie, C.3    Kaul, S.4    Schneider, D.5    Lonsdorf, A.S.6
  • 55
    • 80054935637 scopus 로고    scopus 로고
    • Stabilizing the VE-cadherin-catenin complex blocks leukocyte extravasation and vascular permeability
    • Schulte D, Kuppers V, Dartsch N, Broermann A, Li H, Zarbock A et al. Stabilizing the VE-cadherin-catenin complex blocks leukocyte extravasation and vascular permeability. EMBO J 2011;30:4157-70.
    • (2011) EMBO J , vol.30 , pp. 4157-4170
    • Schulte, D.1    Kuppers, V.2    Dartsch, N.3    Broermann, A.4    Li, H.5    Zarbock, A.6
  • 56
    • 33751546663 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C regulates vascular endothelial permeability by modulating VE-cadherin-mediated cell-cell contacts
    • Orlova VV, Economopoulou M, Lupu F, Santoso S, Chavakis T. Junctional adhesion molecule-C regulates vascular endothelial permeability by modulating VE-cadherin-mediated cell-cell contacts. J Exp Med 2006;203:2703-14.
    • (2006) J Exp Med , vol.203 , pp. 2703-2714
    • Orlova, V.V.1    Economopoulou, M.2    Lupu, F.3    Santoso, S.4    Chavakis, T.5
  • 57
    • 33745813930 scopus 로고    scopus 로고
    • ESAM supports neutrophil extravasation, activation of Rho, and VEGF-induced vascular permeability
    • Wegmann F, Petri B, Khandoga AG, Moser C, Khandoga A, Volkery S et al. ESAM supports neutrophil extravasation, activation of Rho, and VEGF-induced vascular permeability. J Exp Med 2006;203:1671-7.
    • (2006) J Exp Med , vol.203 , pp. 1671-1677
    • Wegmann, F.1    Petri, B.2    Khandoga, A.G.3    Moser, C.4    Khandoga, A.5    Volkery, S.6
  • 58
    • 12444321548 scopus 로고    scopus 로고
    • New aspects of integrin-mediated leukocyte adhesion in inflammation: regulation by haemostatic factors and bacterial products
    • Rhee JS, Santoso S, Herrmann M, Bierhaus A, Kanse SM, May AE et al. New aspects of integrin-mediated leukocyte adhesion in inflammation: regulation by haemostatic factors and bacterial products. Curr Mol Med 2003;3:387-92.
    • (2003) Curr Mol Med , vol.3 , pp. 387-392
    • Rhee, J.S.1    Santoso, S.2    Herrmann, M.3    Bierhaus, A.4    Kanse, S.M.5    May, A.E.6
  • 59
    • 34548566416 scopus 로고    scopus 로고
    • The anti-inflammatory activities of Staphylococcus aureus
    • Chavakis T, Preissner KT, Herrmann M. The anti-inflammatory activities of Staphylococcus aureus. Trends Immunol 2007;28:408-18.
    • (2007) Trends Immunol , vol.28 , pp. 408-418
    • Chavakis, T.1    Preissner, K.T.2    Herrmann, M.3
  • 60
    • 0036061581 scopus 로고    scopus 로고
    • Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes
    • Chavakis T, Hussain M, Kanse SM, Peters G, Bretzel RG, Flock JI et al. Staphylococcus aureus extracellular adherence protein serves as anti-inflammatory factor by inhibiting the recruitment of host leukocytes. Nat Med 2002;8:687-93.
    • (2002) Nat Med , vol.8 , pp. 687-693
    • Chavakis, T.1    Hussain, M.2    Kanse, S.M.3    Peters, G.4    Bretzel, R.G.5    Flock, J.I.6
  • 61
    • 33645512039 scopus 로고    scopus 로고
    • The extracellular adherence protein (Eap) of Staphylococcus aureus inhibits wound healing by interfering with host defense and repair mechanisms
    • Athanasopoulos AN, Economopoulou M, Orlova VV, Sobke A, Schneider D, Weber H et al. The extracellular adherence protein (Eap) of Staphylococcus aureus inhibits wound healing by interfering with host defense and repair mechanisms. Blood 2006;107:2720-7.
    • (2006) Blood , vol.107 , pp. 2720-2727
    • Athanasopoulos, A.N.1    Economopoulou, M.2    Orlova, V.V.3    Sobke, A.4    Schneider, D.5    Weber, H.6
  • 62
    • 0028305898 scopus 로고
    • A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18
    • Moyle M, Foster DL, McGrath DE, Brown SM, Laroche Y, De Meutter J et al. A hookworm glycoprotein that inhibits neutrophil function is a ligand of the integrin CD11b/CD18. J Biol Chem 1994;269:10008-15.
    • (1994) J Biol Chem , vol.269 , pp. 10008-10015
    • Moyle, M.1    Foster, D.L.2    McGrath, D.E.3    Brown, S.M.4    Laroche, Y.5    De Meutter, J.6
  • 63
    • 0032103369 scopus 로고    scopus 로고
    • In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism
    • Zhou MY, Lo SK, Bergenfeldt M, Tiruppathi C, Jaffe A, Xu N et al. In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism. J Clin Invest 1998;101:2427-37.
    • (1998) J Clin Invest , vol.101 , pp. 2427-2437
    • Zhou, M.Y.1    Lo, S.K.2    Bergenfeldt, M.3    Tiruppathi, C.4    Jaffe, A.5    Xu, N.6
  • 64
    • 0028929259 scopus 로고
    • Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X
    • Rozdzinski E, Sandros J, van der Flier M, Young A, Spellerberg B, Bhattacharyya C et al. Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X. J Clin Invest 1995;95:1078-85.
    • (1995) J Clin Invest , vol.95 , pp. 1078-1085
    • Rozdzinski, E.1    Sandros, J.2    van der Flier, M.3    Young, A.4    Spellerberg, B.5    Bhattacharyya, C.6
  • 65
    • 56449122732 scopus 로고    scopus 로고
    • Del-1, an endogenous leukocyte-endothelial adhesion inhibitor, limits inflammatory cell recruitment
    • Choi EY, Chavakis E, Czabanka MA, Langer HF, Fraemohs L, Economopoulou M et al. Del-1, an endogenous leukocyte-endothelial adhesion inhibitor, limits inflammatory cell recruitment. Science 2008;322:1101-4.
    • (2008) Science , vol.322 , pp. 1101-1104
    • Choi, E.Y.1    Chavakis, E.2    Czabanka, M.A.3    Langer, H.F.4    Fraemohs, L.5    Economopoulou, M.6
  • 66
    • 66149128052 scopus 로고    scopus 로고
    • SED1/MFG-E8: a bi-motif protein that orchestrates diverse cellular interactions
    • Raymond A, Ensslin MA, Shur BD. SED1/MFG-E8: a bi-motif protein that orchestrates diverse cellular interactions. J Cell Biochem 2009;106:957-66.
    • (2009) J Cell Biochem , vol.106 , pp. 957-966
    • Raymond, A.1    Ensslin, M.A.2    Shur, B.D.3
  • 67
    • 15444354665 scopus 로고    scopus 로고
    • Cloning and characterization of developmental endothelial locus-1: an embryonic endothelial cell protein that binds the alphavbeta3 integrin receptor
    • Hidai C, Zupancic T, Penta K, Mikhail A, Kawana M, Quertermous EE et al. Cloning and characterization of developmental endothelial locus-1: an embryonic endothelial cell protein that binds the alphavbeta3 integrin receptor. Genes Dev 1998;12:21-33.
    • (1998) Genes Dev , vol.12 , pp. 21-33
    • Hidai, C.1    Zupancic, T.2    Penta, K.3    Mikhail, A.4    Kawana, M.5    Quertermous, E.E.6
  • 68
    • 84859434153 scopus 로고    scopus 로고
    • Developmental Endothelial Locus-1 (Del-1) Mediates Clearance of Platelet Microparticles by the Endothelium
    • Dasgupta SK, Le A, Chavakis T, Rumbaut RE, Thiagarajan P. Developmental Endothelial Locus-1 (Del-1) Mediates Clearance of Platelet Microparticles by the Endothelium. Circulation 2012; doi:
    • (2012) Circulation
    • Dasgupta, S.K.1    Le, A.2    Chavakis, T.3    Rumbaut, R.E.4    Thiagarajan, P.5
  • 69
    • 12144289916 scopus 로고    scopus 로고
    • Developmental endothelial locus-1 (Del-1), a novel angiogenic protein: its role in ischemia
    • Ho HK, Jang JJ, Kaji S, Spektor G, Fong A, Yang P et al. Developmental endothelial locus-1 (Del-1), a novel angiogenic protein: its role in ischemia. Circulation 2004;109:1314-9.
    • (2004) Circulation , vol.109 , pp. 1314-1319
    • Ho, H.K.1    Jang, J.J.2    Kaji, S.3    Spektor, G.4    Fong, A.5    Yang, P.6
  • 70
    • 34548757394 scopus 로고    scopus 로고
    • Discoidin domain of Del1 protein contributes to its deposition in the extracellular matrix
    • Hidai C, Kawana M, Kitano H, Kokubun S. Discoidin domain of Del1 protein contributes to its deposition in the extracellular matrix. Cell Tissue Res 2007;330:83-95.
    • (2007) Cell Tissue Res , vol.330 , pp. 83-95
    • Hidai, C.1    Kawana, M.2    Kitano, H.3    Kokubun, S.4
  • 71
    • 84863393385 scopus 로고    scopus 로고
    • The leukocyte integrin antagonist Del-1 inhibits IL-17-mediated inflammatory bone loss
    • Eskan MA, Jotwani R, Abe T, Chmelar J, Lim JH, Liang S et al. The leukocyte integrin antagonist Del-1 inhibits IL-17-mediated inflammatory bone loss. Nat Immunol 2012;13:465-73.
    • (2012) Nat Immunol , vol.13 , pp. 465-473
    • Eskan, M.A.1    Jotwani, R.2    Abe, T.3    Chmelar, J.4    Lim, J.H.5    Liang, S.6
  • 72
    • 17644423119 scopus 로고    scopus 로고
    • Pentraxins at the crossroads between innate immunity, inflammation, matrix deposition, and female fertility
    • Garlanda C, Bottazzi B, Bastone A, Mantovani A. Pentraxins at the crossroads between innate immunity, inflammation, matrix deposition, and female fertility. Annu Rev Immunol 2005;23:337-66.
    • (2005) Annu Rev Immunol , vol.23 , pp. 337-366
    • Garlanda, C.1    Bottazzi, B.2    Bastone, A.3    Mantovani, A.4
  • 73
    • 38449105896 scopus 로고    scopus 로고
    • Complement dependent amplification of the innate response to a cognate microbial ligand by the long pentraxin PTX3
    • Cotena A, Maina V, Sironi M, Bottazzi B, Jeannin P, Vecchi A et al. Complement dependent amplification of the innate response to a cognate microbial ligand by the long pentraxin PTX3. J Immunol 2007;179:6311-7.
    • (2007) J Immunol , vol.179 , pp. 6311-6317
    • Cotena, A.1    Maina, V.2    Sironi, M.3    Bottazzi, B.4    Jeannin, P.5    Vecchi, A.6
  • 74
    • 58049201685 scopus 로고    scopus 로고
    • The long pentraxin PTX3 as a prototypic humoral pattern recognition receptor: interplay with cellular innate immunity
    • Bottazzi B, Garlanda C, Cotena A, Moalli F, Jaillon S, Deban L et al. The long pentraxin PTX3 as a prototypic humoral pattern recognition receptor: interplay with cellular innate immunity. Immunol Rev 2009;227:9-18.
    • (2009) Immunol Rev , vol.227 , pp. 9-18
    • Bottazzi, B.1    Garlanda, C.2    Cotena, A.3    Moalli, F.4    Jaillon, S.5    Deban, L.6
  • 76
    • 40749084822 scopus 로고    scopus 로고
    • Cardioprotective function of the long pentraxin PTX3 in acute myocardial infarction
    • Salio M, Chimenti S, De Angelis N, Molla F, Maina V, Nebuloni M et al. Cardioprotective function of the long pentraxin PTX3 in acute myocardial infarction. Circulation 2008;117:1055-64.
    • (2008) Circulation , vol.117 , pp. 1055-1064
    • Salio, M.1    Chimenti, S.2    De Angelis, N.3    Molla, F.4    Maina, V.5    Nebuloni, M.6
  • 77
    • 79955703474 scopus 로고    scopus 로고
    • GDF-15 is an inhibitor of leukocyte integrin activation required for survival after myocardial infarction in mice
    • Kempf T, Zarbock A, Widera C, Butz S, Stadtmann A, Rossaint J et al. GDF-15 is an inhibitor of leukocyte integrin activation required for survival after myocardial infarction in mice. Nat Med 2011;17:581-8.
    • (2011) Nat Med , vol.17 , pp. 581-588
    • Kempf, T.1    Zarbock, A.2    Widera, C.3    Butz, S.4    Stadtmann, A.5    Rossaint, J.6
  • 78
    • 33646076691 scopus 로고    scopus 로고
    • The transforming growth factor-beta superfamily member growth-differentiation factor-15 protects the heart from ischemia/reperfusion injury
    • Kempf T, Eden M, Strelau J, Naguib M, Willenbockel C, Tongers J et al. The transforming growth factor-beta superfamily member growth-differentiation factor-15 protects the heart from ischemia/reperfusion injury. Circ Res 2006;98:351-60.
    • (2006) Circ Res , vol.98 , pp. 351-360
    • Kempf, T.1    Eden, M.2    Strelau, J.3    Naguib, M.4    Willenbockel, C.5    Tongers, J.6


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