메뉴 건너뛰기




Volumn 5, Issue 10, 2005, Pages 760-771

Cell-surface enzymes in control of leukocyte trafficking

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; CELL ENZYME; CHEMOATTRACTANT; CHEMOKINE; DIPEPTIDYL PEPTIDASE IV INHIBITOR; DIPROTIN A; ENZYME INHIBITOR; INTEGRIN; MEMBRANE ENZYME; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NUCLEOTIDASE; OXIDOREDUCTASE; PEPTIDASE; PROTEINASE; SELECTIN; VASCULAR ADHESION PROTEIN 1;

EID: 25844523991     PISSN: 14741733     EISSN: None     Source Type: Journal    
DOI: 10.1038/nri1705     Document Type: Review
Times cited : (231)

References (135)
  • 1
    • 0242551584 scopus 로고    scopus 로고
    • Homing and cellular traffic in lymph nodes
    • von Andrian, U. H. & Mempel, T. R. Homing and cellular traffic in lymph nodes. Nature Rev. Immunol. 3, 867-878 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 867-878
    • Von Andrian, U.H.1    Mempel, T.R.2
  • 2
    • 0038180539 scopus 로고    scopus 로고
    • Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response
    • Muller, W. A. Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. Trends Immunol. 24, 327-334 (2003).
    • (2003) Trends Immunol. , vol.24 , pp. 327-334
    • Muller, W.A.1
  • 3
    • 2442519018 scopus 로고    scopus 로고
    • Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation
    • Ley, K. & Kansas, G. S. Selectins in T-cell recruitment to non-lymphoid tissues and sites of inflammation. Nature Rev. Immunol. 4, 325-335 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 325-335
    • Ley, K.1    Kansas, G.S.2
  • 5
    • 0036166387 scopus 로고    scopus 로고
    • Chemokines and the tissue-specific migration of lymphocytes
    • Kunkel, E. J. & Butcher, E. C. Chemokines and the tissue-specific migration of lymphocytes. Immunity 16, 1-4 (2002).
    • (2002) Immunity , vol.16 , pp. 1-4
    • Kunkel, E.J.1    Butcher, E.C.2
  • 6
    • 0842324615 scopus 로고    scopus 로고
    • Chemokines: Multiple levels of leukocyte migration control
    • Moser, B., Wolf, M., Walz, A. & Loetscher, P. Chemokines: multiple levels of leukocyte migration control. Trends Immunol. 25, 75-84 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 75-84
    • Moser, B.1    Wolf, M.2    Walz, A.3    Loetscher, P.4
  • 7
    • 0035253835 scopus 로고    scopus 로고
    • Nucleotide receptors: An emerging family of regulatory molecules in blood cells
    • Di Virgilio, F. et al. Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood 97, 587-600 (2001).
    • (2001) Blood , vol.97 , pp. 587-600
    • Di Virgilio, F.1
  • 8
    • 0031908460 scopus 로고    scopus 로고
    • Ecto-enzymes of lymphoid cells
    • Goding, J. W. & Howard, M. C. Ecto-enzymes of lymphoid cells. Immunol. Rev. 161, 5-10 (1998).
    • (1998) Immunol. Rev. , vol.161 , pp. 5-10
    • Goding, J.W.1    Howard, M.C.2
  • 9
    • 1842430537 scopus 로고    scopus 로고
    • Ecto-ADP-ribosyltransferases (ARTs): Emerging actors in cell communication and signaling
    • Seman, M., Adriouch, S., Haag, F. & Koch-Nolte, F. Ecto-ADP-ribosyltransferases (ARTs): emerging actors in cell communication and signaling. Curr. Med. Chem. 11, 857-872 (2004).
    • (2004) Curr. Med. Chem. , vol.11 , pp. 857-872
    • Seman, M.1    Adriouch, S.2    Haag, F.3    Koch-Nolte, F.4
  • 10
    • 0035422806 scopus 로고    scopus 로고
    • Cell surface monoamine oxidases: Enzymes in search of a function
    • Jalkanen, S. & Salmi, M. Cell surface monoamine oxidases: enzymes in search of a function. EMBO J. 20, 3893-3901 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3893-3901
    • Jalkanen, S.1    Salmi, M.2
  • 11
    • 0035905372 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV-like molecules: Homologous proteins or homologous activities?
    • Sedo, A. & Malik, R. Dipeptidyl peptidase IV-like molecules: homologous proteins or homologous activities? Biochim. Biophys. Acta 1550, 107-116 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 107-116
    • Sedo, A.1    Malik, R.2
  • 12
    • 1942485497 scopus 로고    scopus 로고
    • Structure and enzymology of ADP-ribosyl cyclases: Conserved enzymes that produce multiple calcium mobilizing metabolites
    • Schuber, F. & Lund, F. E. Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites. Curr. Mol. Med. 4, 249-261 (2004).
    • (2004) Curr. Mol. Med. , vol.4 , pp. 249-261
    • Schuber, F.1    Lund, F.E.2
  • 14
    • 0035173647 scopus 로고    scopus 로고
    • Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo
    • Partida-Sanchez, S. et al. Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo. Nature Med. 7, 1209-1216 (2001). This paper shows that, in vivo, the absence of CD38 impairs leukocyte trafficking as a consequence of defects in chemotaxis.
    • (2001) Nature Med. , vol.7 , pp. 1209-1216
    • Partida-Sanchez, S.1
  • 15
    • 10244222236 scopus 로고    scopus 로고
    • Endogenous adenosine produced during hypoxia attenuates neutrophil accumulation: Coordination by extracellular nucleotide metabolism
    • Eltzschig, H. K. et al. Endogenous adenosine produced during hypoxia attenuates neutrophil accumulation: coordination by extracellular nucleotide metabolism. Blood 104, 3986-3992 (2004). This work shows that an increase in leukocyte infiltration occurs under hypoxic conditions in CD73-deficient mice.
    • (2004) Blood , vol.104 , pp. 3986-3992
    • Eltzschig, H.K.1
  • 16
    • 19944434024 scopus 로고    scopus 로고
    • Absence of the endothelial oxidase AOC3 leads to abnormal leukocyte traffic in vivo
    • Stolen, C. M. et al. Absence of the endothelial oxidase AOC3 leads to abnormal leukocyte traffic in vivo. Immunity 22, 105-115 (2005). This report describes the importance of VAP1 in leukocyte migration under physiological and pathological conditions.
    • (2005) Immunity , vol.22 , pp. 105-115
    • Stolen, C.M.1
  • 17
    • 0141457730 scopus 로고    scopus 로고
    • Mechanisms of release of nucleotides and integration of their action as P2X- and P2Y-receptor activating molecules
    • Lazarawski, E. R., Boucher, R. C. & Harden, T. K. Mechanisms of release of nucleotides and integration of their action as P2X- and P2Y-receptor activating molecules. Mol. Pharmacol. 64, 785-795 (2003).
    • (2003) Mol. Pharmacol. , vol.64 , pp. 785-795
    • Lazarawski, E.R.1    Boucher, R.C.2    Harden, T.K.3
  • 18
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • Ralevic, V. & Burnstock, G. Receptors for purines and pyrimidines. Pharmacol. Rev. 50, 413-492 (1998).
    • (1998) Pharmacol. Rev. , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 19
    • 0035655395 scopus 로고    scopus 로고
    • Rapid secretion of interleukin-1β by microvesicle shedding
    • MacKenzie, A. et al. Rapid secretion of interleukin-1β by microvesicle shedding. Immunity 15, 825-835 (2001).
    • (2001) Immunity , vol.15 , pp. 825-835
    • MacKenzie, A.1
  • 20
    • 0036682506 scopus 로고    scopus 로고
    • Nucleotides induce chemotaxis and actin polymerization in immature but not mature human dendritic cells via activation of pertussis toxin-sensitive P2y receptors
    • Idzko, M. et al. Nucleotides induce chemotaxis and actin polymerization in immature but not mature human dendritic cells via activation of pertussis toxin-sensitive P2y receptors. Blood 100, 925-932 (2002).
    • (2002) Blood , vol.100 , pp. 925-932
    • Idzko, M.1
  • 22
    • 0031908461 scopus 로고    scopus 로고
    • Ecto-ATPase: An activation marker necessary for effector cell function
    • Dombrowski, K. E., Ke, Y., Brewer, K. A. & Kapp, J. A. Ecto-ATPase: an activation marker necessary for effector cell function. Immunol. Rev. 161, 111-118 (1998).
    • (1998) Immunol. Rev. , vol.161 , pp. 111-118
    • Dombrowski, K.E.1    Ke, Y.2    Brewer, K.A.3    Kapp, J.A.4
  • 23
    • 0035910015 scopus 로고    scopus 로고
    • Disordered cellular migration and angiogenesis in cd39-null mice
    • Goepfert, C. et al. Disordered cellular migration and angiogenesis in cd39-null mice. Circulation 104, 3109-3115 (2001). This study shows that CD39-deficient monocytes and macrophages have impaired transmigration in vitro and diminished influx to angiogenic sites in vivo.
    • (2001) Circulation , vol.104 , pp. 3109-3115
    • Goepfert, C.1
  • 24
    • 1642281919 scopus 로고    scopus 로고
    • Beneficial effects of CD39/ectonucleoside triphosphate diphosphohydrolase-1 in murine intestinal ischemia-reperfusion injury
    • Guckelberger, O. et al. Beneficial effects of CD39/ectonucleoside triphosphate diphosphohydrolase-1 in murine intestinal ischemia-reperfusion injury. Thromb. Haemost. 91, 576-586 (2004).
    • (2004) Thromb. Haemost. , vol.91 , pp. 576-586
    • Guckelberger, O.1
  • 25
    • 0036102125 scopus 로고    scopus 로고
    • CD39 is the dominant Langerhans cell-associated ecto-NTPDase: Modulatory roles in inflammation and immune responsiveness
    • Mizumoto, N. et al. CD39 is the dominant Langerhans cell-associated ecto-NTPDase: modulatory roles in inflammation and immune responsiveness. Nature Med. 8, 358-365 (2002).
    • (2002) Nature Med. , vol.8 , pp. 358-365
    • Mizumoto, N.1
  • 26
    • 0027440443 scopus 로고
    • Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium
    • Airas, L., Salmi, M. & Jalkanen, S. Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium. J. Immunol. 151, 4228-4238 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 4228-4238
    • Airas, L.1    Salmi, M.2    Jalkanen, S.3
  • 27
    • 0028838712 scopus 로고
    • CD73 is involved in lymphocyte binding to the endothelium: Characterization of lymphocyte-vascular adhesion protein 2 identifies it as CD73
    • Airas, L. et al. CD73 is involved in lymphocyte binding to the endothelium: characterization of lymphocyte-vascular adhesion protein 2 identifies it as CD73. J. Exp. Med. 182, 1603-1608 (1995).
    • (1995) J. Exp. Med. , vol.182 , pp. 1603-1608
    • Airas, L.1
  • 28
    • 0031933227 scopus 로고    scopus 로고
    • Ecto-enzyme and signaling functions of lymphocyte CD73
    • Resta, R., Yamashita, Y. & Thompson, L. F. Ecto-enzyme and signaling functions of lymphocyte CD73. Immunol. Rev. 161, 95-109 (1998).
    • (1998) Immunol. Rev. , vol.161 , pp. 95-109
    • Resta, R.1    Yamashita, Y.2    Thompson, L.F.3
  • 29
    • 0029992387 scopus 로고    scopus 로고
    • 2 integrins and L-selectin of human polymorphonuclear leukocytes in vitro
    • 2 integrins and L-selectin of human polymorphonuclear leukocytes in vitro. J. Leukoc. Biol. 59, 671-682 (1996).
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 671-682
    • Thiel, M.1
  • 31
    • 0035924320 scopus 로고    scopus 로고
    • Role of G-protein-coupled adenosine receptors in down regulation of inflammation and protection from tissue damage
    • Ohta, A. & Sitkovsky, M. Role of G-protein-coupled adenosine receptors in down regulation of inflammation and protection from tissue damage. Nature 414, 916-920 (2001).
    • (2001) Nature , vol.414 , pp. 916-920
    • Ohta, A.1    Sitkovsky, M.2
  • 32
    • 0029968687 scopus 로고    scopus 로고
    • Adenosine inhibits cytokine release and expression of adhesion molecules by activated human endothelial cells
    • Bouma, M. G., van den Wildenberg, F. A. & Buurman, W. A. Adenosine inhibits cytokine release and expression of adhesion molecules by activated human endothelial cells. Am. J. Physiol. 270, C522-C529 (1996).
    • (1996) Am. J. Physiol. , vol.270
    • Bouma, M.G.1    Van Den Wildenberg, F.A.2    Buurman, W.A.3
  • 33
    • 0036550315 scopus 로고    scopus 로고
    • Role of vasodilator-stimulated phosphoprotein in PKA-induced changes in endothelial junctional permeability
    • Comerford, K. M., Lawrence, D. W., Synnestvedt, K., Levi, B. P. & Colgan, S. P. Role of vasodilator-stimulated phosphoprotein in PKA-induced changes in endothelial junctional permeability. FASEB J. 16, 583-585 (2002).
    • (2002) FASEB J. , vol.16 , pp. 583-585
    • Comerford, K.M.1    Lawrence, D.W.2    Synnestvedt, K.3    Levi, B.P.4    Colgan, S.P.5
  • 34
    • 10644240767 scopus 로고    scopus 로고
    • Crucial role for ecto-5′-nucleotidase (CD73) in vascular leakage during hypoxia
    • Thompson, L. F. et al. Crucial role for ecto-5′-nucleotidase (CD73) in vascular leakage during hypoxia. J. Exp. Med. 200, 1395-1405 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 1395-1405
    • Thompson, L.F.1
  • 35
    • 1642444080 scopus 로고    scopus 로고
    • IFN-α induced adenosine production on the endothelium: A mechanism mediated by CD73 (ecto-5′-nucleotidase) up-regulation
    • Niemela, J. et al. IFN-α induced adenosine production on the endothelium: a mechanism mediated by CD73 (ecto-5′-nucleotidase) up-regulation. J. Immunol. 172, 1646-1653 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 1646-1653
    • Niemela, J.1
  • 36
    • 0034669958 scopus 로고    scopus 로고
    • CD73 engagement promotes lymphocyte binding to endothelial cells via a lymphocyte function-associated antigen-1-dependent mechanism
    • Airas, L., Niemela, J. & Jalkanen, S. CD73 engagement promotes lymphocyte binding to endothelial cells via a lymphocyte function-associated antigen-1-dependent mechanism. J. Immunol. 165, 5411-5417 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 5411-5417
    • Airas, L.1    Niemela, J.2    Jalkanen, S.3
  • 37
    • 0031047221 scopus 로고    scopus 로고
    • Differential regulation and function of CD73, a glycosyl- phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endothelial cells
    • Airas, L. et al. Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endothelial cells. J. Cell Biol. 136, 421-431 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 421-431
    • Airas, L.1
  • 38
    • 0043092170 scopus 로고    scopus 로고
    • Adherent leukocytes prevent adenosine formation and impair endothelial barrier function by ecto-5′-nucleotidase/CD73-dependent mechanism
    • Henttinen, T., Jalkanen, S. & Yegutkin, G. G. Adherent leukocytes prevent adenosine formation and impair endothelial barrier function by ecto-5′-nucleotidase/CD73-dependent mechanism. J. Biol. Chem. 278, 24888-24895 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 24888-24895
    • Henttinen, T.1    Jalkanen, S.2    Yegutkin, G.G.3
  • 39
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • Kameoka, J., Tanaka, T., Nojima, Y., Schlossman, S. F. & Morimoto, C. Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261, 466-469 (1993).
    • (1993) Science , vol.261 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 40
    • 6344283049 scopus 로고    scopus 로고
    • Targeted disruption of cd73/ecto-5′-nucleotidase alters thromboregulation and augments vascular inflammatory response
    • Koszalka, P. et al. Targeted disruption of cd73/ecto-5′- nucleotidase alters thromboregulation and augments vascular inflammatory response. Circ. Res. 95, 814-821 (2004). This paper describes the increased attachment of leukocytes to inflamed endothelia in CD73-deficient mice.
    • (2004) Circ. Res. , vol.95 , pp. 814-821
    • Koszalka, P.1
  • 41
    • 0038664247 scopus 로고    scopus 로고
    • Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/phosphodiesterase family
    • Goding, J. W., Grobben, B. & Siegers, H. Physiological and pathophysiological functions of the ecto-nucleotide pyrophosphatase/ phosphodiesterase family. Biochim. Biophys. Acta 1638, 1-19 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1638 , pp. 1-19
    • Goding, J.W.1    Grobben, B.2    Siegers, H.3
  • 42
    • 0037131366 scopus 로고    scopus 로고
    • Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase
    • Tokumura, A. et al. Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. J. Biol. Chem. 277, 39436-39442 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39436-39442
    • Tokumura, A.1
  • 43
    • 0141593615 scopus 로고    scopus 로고
    • Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator of migration, sphingosine-1-phosphate
    • Clair, T. et al. Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator of migration, sphingosine-1-phosphate. Cancer Res. 63, 5446-5453 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 5446-5453
    • Clair, T.1
  • 44
    • 2942716957 scopus 로고    scopus 로고
    • Lysophospholipase D and its role in LPA production
    • Xie, Y. & Meier, K. E. Lysophospholipase D and its role in LPA production. Cell. Signal. 16, 975-981 (2004).
    • (2004) Cell. Signal. , vol.16 , pp. 975-981
    • Xie, Y.1    Meier, K.E.2
  • 45
    • 21844457949 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and its receptors: An autocrine and paracrine network
    • Rosen, H. & Goetzl, E. J. Sphingosine 1-phosphate and its receptors: an autocrine and paracrine network. Nature Rev. Immunol. 5, 560-570 (2005).
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 560-570
    • Rosen, H.1    Goetzl, E.J.2
  • 46
    • 0032754759 scopus 로고    scopus 로고
    • Ecto-protein kinases: Ecto-domain phosphorylation as a novel target for pharmacological manipulation?
    • Redegeld, F. A., Caldwell, C. C. & Sitkovsky, M. V. Ecto-protein kinases: ecto-domain phosphorylation as a novel target for pharmacological manipulation? Trends Pharmacol. Sci. 20, 453-459 (1999).
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 453-459
    • Redegeld, F.A.1    Caldwell, C.C.2    Sitkovsky, M.V.3
  • 47
    • 0036798380 scopus 로고    scopus 로고
    • The evidence for two opposite, ATP-generating and ATP-consuming, extracellular pathways on endothelial and lymphoid cells
    • Yegutkin, G. G., Henttinen, T., Samburski, S. S., Spychala, J. & Jalkanen, S. The evidence for two opposite, ATP-generating and ATP-consuming, extracellular pathways on endothelial and lymphoid cells. Biochem. J. 367, 121-128 (2002).
    • (2002) Biochem. J. , vol.367 , pp. 121-128
    • Yegutkin, G.G.1    Henttinen, T.2    Samburski, S.S.3    Spychala, J.4    Jalkanen, S.5
  • 48
    • 0035177850 scopus 로고    scopus 로고
    • Human CD38: A (r)evolutionary story of enzymes and receptors
    • Deaglio, S., Mehta, K. & Malavasi, F. Human CD38: a (r)evolutionary story of enzymes and receptors. Leuk. Res. 25, 1-12 (2001).
    • (2001) Leuk. Res. , vol.25 , pp. 1-12
    • Deaglio, S.1    Mehta, K.2    Malavasi, F.3
  • 49
    • 0035815670 scopus 로고    scopus 로고
    • ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase act as a redox sensor. A primary role for cyclic ADP-ribose in hypoxic pulmonary vasoconstriction
    • Wilson, H. L. et al. ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase act as a redox sensor. A primary role for cyclic ADP-ribose in hypoxic pulmonary vasoconstriction. J. Biol. Chem. 276, 11180-11188 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11180-11188
    • Wilson, H.L.1
  • 50
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • Lee, H. C. Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu. Rev. Pharmacol. Toxicol. 41, 317-345 (2001).
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 51
    • 1842587485 scopus 로고    scopus 로고
    • Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR)
    • Guse, A. H. Biochemistry, biology, and pharmacology of cyclic adenosine diphosphoribose (cADPR). Curr. Med. Chem. 11, 847-855 (2004).
    • (2004) Curr. Med. Chem. , vol.11 , pp. 847-855
    • Guse, A.H.1
  • 52
    • 0242683360 scopus 로고    scopus 로고
    • Leukocyte polarization in cell migration and immune interactions
    • Sánchez-Madrid, F. & del Pozo, M. A. Leukocyte polarization in cell migration and immune interactions. EMBO J. 18, 501-511 (1999).
    • (1999) EMBO J. , vol.18 , pp. 501-511
    • Sánchez-1    Madrid, F.2    Del Pozo, M.A.3
  • 53
    • 0034635221 scopus 로고    scopus 로고
    • Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant- mediated signal transduction
    • Li, Z. et al. Roles of PLC-β2 and -β3 and PI3Kγ in chemoattractant-mediated signal transduction. Science 287, 1046-1049 (2000).
    • (2000) Science , vol.287 , pp. 1046-1049
    • Li, Z.1
  • 54
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield, I., Cabanas, C., Craig, A. & Hogg, N. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J. Cell Biol. 116, 219-226 (1992).
    • (1992) J. Cell Biol. , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 56
    • 12144285678 scopus 로고    scopus 로고
    • Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38: Impact on the development of humoral immunity
    • Partida-Sanchez, S. et al. Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38: impact on the development of humoral immunity. Immunity 20, 279-291 (2004). The importance of CD38 in DC trafficking was uncovered by this elegant study.
    • (2004) Immunity , vol.20 , pp. 279-291
    • Partida-Sanchez, S.1
  • 58
    • 0028243646 scopus 로고
    • + lymphocytes. Role of the human CD38 molecule
    • + lymphocytes. Role of the human CD38 molecule. J. Immunol. 153, 952-959 (1994).
    • (1994) J. Immunol. , vol.153 , pp. 952-959
    • Dianzani, U.1
  • 59
    • 0031930758 scopus 로고    scopus 로고
    • Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member
    • Deaglio, S. et al. Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member; J. Immunol. 160, 395-402 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 395-402
    • Deaglio, S.1
  • 60
    • 10244246553 scopus 로고    scopus 로고
    • CD157 is an important mediator of neutrophil adhesion and migration
    • Funaro, A. et al. CD157 is an important mediator of neutrophil adhesion and migration. Blood 104, 4269-4278 (2004).
    • (2004) Blood , vol.104 , pp. 4269-4278
    • Funaro, A.1
  • 61
    • 0029980483 scopus 로고    scopus 로고
    • Mouse T cell membrane proteins Rt6-1 and R16-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins
    • Koch-Nolte, F et al. Mouse T cell membrane proteins Rt6-1 and R16-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271, 7686-7693 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 7686-7693
    • Koch-Nolte, F.1
  • 62
    • 0027960632 scopus 로고
    • Premature stop codons inactivate the RT6 genes of the human and chimpanzee species
    • Haag, F., Koch-Nolte, F., Kuhl, M., Lorenzen, S. & Thiele, H. G. Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. J. Mol. Biol. 243, 537-546 (1994).
    • (1994) J. Mol. Biol. , vol.243 , pp. 537-546
    • Haag, F.1    Koch-Nolte, F.2    Kuhl, M.3    Lorenzen, S.4    Thiele, H.G.5
  • 63
    • 0030587933 scopus 로고    scopus 로고
    • Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells
    • Nemoto, E., Yu, Y. & Dennert, G. Cell surface ADP-ribosyltransferase regulates lymphocyte function-associated molecule-1 (LFA-1) function in T cells. J. Immunol. 157, 3341-3349 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 3341-3349
    • Nemoto, E.1    Yu, Y.2    Dennert, G.3
  • 64
    • 0032080818 scopus 로고    scopus 로고
    • Expression of ADP-ribosyltransferase on normal T lymphocytes and effects of nicotinamide adenine dinucleotide on their function
    • Okamoto, S., Azhipa, O., Yu, Y., Russo, E. & Dennert, G. Expression of ADP-ribosyltransferase on normal T lymphocytes and effects of nicotinamide adenine dinucleotide on their function. J. Immunol. 160, 4190-4198 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 4190-4198
    • Okamoto, S.1    Azhipa, O.2    Yu, Y.3    Russo, E.4    Dennert, G.5
  • 65
    • 0034617096 scopus 로고    scopus 로고
    • Interaction of two classes of ADP-ribose transfer reactions in immune signaling
    • Han, M. K., Cho, Y. S., Kim, Y. S., Yim, C. Y. & Kim, U. H. Interaction of two classes of ADP-ribose transfer reactions in immune signaling. J. Biol. Chem. 275, 20799-20805 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 20799-20805
    • Han, M.K.1    Cho, Y.S.2    Kim, Y.S.3    Yim, C.Y.4    Kim, U.H.5
  • 66
    • 0142188258 scopus 로고    scopus 로고
    • 7 purinoceptor
    • 7 purinoceptor. Immunity 19, 571-582 (2003).
    • (2003) Immunity , vol.19 , pp. 571-582
    • Seman, M.1
  • 67
    • 0037108511 scopus 로고    scopus 로고
    • A natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X- Receptor
    • Adriouch, S. et al. A natural P451L mutation in the cytoplasmic domain impairs the function of the mouse P2X- receptor. J. Immunol. 169, 4108-4112 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 4108-4112
    • Adriouch, S.1
  • 68
    • 0036838081 scopus 로고    scopus 로고
    • Generation and characterization of ecto-ADP-ribosyltransferase ART2.1/ART2.2-deficient mice
    • Ohlrogge, W. et al. Generation and characterization of ecto-ADP-ribosyltransferase ART2.1/ART2.2-deficient mice. Mol. Cell. Biol. 22, 7535-7542 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7535-7542
    • Ohlrogge, W.1
  • 69
    • 0142254121 scopus 로고    scopus 로고
    • Regulation of the immune response by the interaction of chemokines and proteases
    • Struyf, S., Proost, P. & Van Damme, J. Regulation of the immune response by the interaction of chemokines and proteases. Adv. Immunol. 81, 1-44 (2003).
    • (2003) Adv. Immunol. , vol.81 , pp. 1-44
    • Struyf, S.1    Proost, P.2    Van Damme, J.3
  • 71
    • 0035839639 scopus 로고    scopus 로고
    • Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family
    • Lambeir, A. M. et al. Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. J. Biol. Chem. 276, 29839-29845 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29839-29845
    • Lambeir, A.M.1
  • 72
    • 0037777665 scopus 로고    scopus 로고
    • Cell surface peptidase CD26/DPPIV mediates G-CSF mobilization of mouse progenitor cells
    • Christopherson, K. W. 2nd, Cooper, S. & Broxmeyer, H. E. Cell surface peptidase CD26/DPPIV mediates G-CSF mobilization of mouse progenitor cells. Blood 101, 4680-4686 (2003).
    • (2003) Blood , vol.101 , pp. 4680-4686
    • Christopherson II, K.W.1    Cooper, S.2    Broxmeyer, H.E.3
  • 73
    • 0036659179 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine
    • Ludwig, A., Schiemann, F., Mentlein, R., Lindner, B. & Brandt, E. Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine. J. Leukoc. Biol. 72, 183-191 (2002).
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 183-191
    • Ludwig, A.1    Schiemann, F.2    Mentlein, R.3    Lindner, B.4    Brandt, E.5
  • 74
    • 13144283654 scopus 로고    scopus 로고
    • Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage
    • Shioda, T. et al. Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1α (SDF-1α) and SDF-1β are abolished by CD26/dipeptidyl peptidase IV-mediated cleavage. Proc. Natl Acad. Sci. USA 95, 6331-6336 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6331-6336
    • Shioda, T.1
  • 75
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz, T. et al. Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J. Exp. Med. 186, 1865-1872 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1865-1872
    • Oravecz, T.1
  • 76
    • 0032992914 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: Possible mechanism for the switch from innate to acquired immune response
    • Iwata, S. et al. CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: possible mechanism for the switch from innate to acquired immune response. Int. Immunol. 11, 417-426 (1999).
    • (1999) Int. Immunol. , vol.11 , pp. 417-426
    • Iwata, S.1
  • 77
    • 11244266087 scopus 로고    scopus 로고
    • CD26 (dipeptidyl-peptidase IV)-dependent recruitment of T cells in a rat asthma model
    • Kruschinski, C. et al. CD26 (dipeptidyl-peptidase IV)-dependent recruitment of T cells in a rat asthma model. Clin. Exp. Immunol. 139, 17-24 (2005).
    • (2005) Clin. Exp. Immunol. , vol.139 , pp. 17-24
    • Kruschinski, C.1
  • 78
    • 13244297075 scopus 로고    scopus 로고
    • Circulating CD26 is negatively associated with inflammation in human and experimental arthritis
    • Busso, N. et al. Circulating CD26 is negatively associated with inflammation in human and experimental arthritis. Am. J. Pathol. 166, 433-442 (2005).
    • (2005) Am. J. Pathol. , vol.166 , pp. 433-442
    • Busso, N.1
  • 80
    • 0036346299 scopus 로고    scopus 로고
    • Soluble CD26/dipeptidyl peptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin-like growth factor II receptor
    • Ikushima, H. et al. Soluble CD26/dipeptidyl peptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate/insulin- like growth factor II receptor. Cell. Immunol. 215, 106-110 (2002).
    • (2002) Cell. Immunol. , vol.215 , pp. 106-110
    • Ikushima, H.1
  • 81
    • 0032508633 scopus 로고    scopus 로고
    • Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin
    • Cheng, H. C., Abdel-Ghany, M., Elble, R. C. & Pauli, B. U. Lung endothelial dipeptidyl peptidase IV promotes adhesion and metastasis of rat breast cancer cells via tumor cell surface-associated fibronectin. J. Biol. Chem. 273, 24207-24215 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 24207-24215
    • Cheng, H.C.1    Abdel-Ghany, M.2    Elble, R.C.3    Pauli, B.U.4
  • 82
    • 0037291715 scopus 로고    scopus 로고
    • The multifunctional or moonlighting protein CD26/DPPIV
    • Boonacker, E. & Van Noorden, C. J. The multifunctional or moonlighting protein CD26/DPPIV. Eur. J. Cell Biol. 82, 53-73 (2003).
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 53-73
    • Boonacker, E.1    Van Noorden, C.J.2
  • 83
    • 0028832073 scopus 로고
    • Inactivation of interleukin-8 by aminopeptidase N (CD13)
    • Kanayama, N. et al. Inactivation of interleukin-8 by aminopeptidase N (CD13). J. Leukoc. Biol. 57, 129-134 (1995).
    • (1995) J. Leukoc. Biol. , vol.57 , pp. 129-134
    • Kanayama, N.1
  • 84
    • 0025986666 scopus 로고
    • CD10 (CALLA)/neutral endopeptidase 24.11 modulates inflammatory peptide-induced changes in neutrophil morphology, migration, and adhesion proteins and is itself regulated by neutrophil activation
    • Shipp, M. A., Stefano, G. B., Switzer, S. N., Griffin, J. D. & Reinherz, E. L. CD10 (CALLA)/neutral endopeptidase 24.11 modulates inflammatory peptide-induced changes in neutrophil morphology, migration, and adhesion proteins and is itself regulated by neutrophil activation. Blood 78, 1834-1841 (1991).
    • (1991) Blood , vol.78 , pp. 1834-1841
    • Shipp, M.A.1    Stefano, G.B.2    Switzer, S.N.3    Griffin, J.D.4    Reinherz, E.L.5
  • 85
    • 0034889163 scopus 로고    scopus 로고
    • Deletion of neutral endopeptidase exacerbates intestinal inflammation induced by Clostridium difficile toxin A
    • Kirkwood, K. S. et al. Deletion of neutral endopeptidase exacerbates intestinal inflammation induced by Clostridium difficile toxin A. Am. J. Physiol. Gastrointest. Liver Physiol. 281, G544-G551 (2001).
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.281
    • Kirkwood, K.S.1
  • 86
    • 0035955760 scopus 로고    scopus 로고
    • Novel clinical markers of vascular wall inflammation
    • Blake, G. J. & Ridker, P. M. Novel clinical markers of vascular wall inflammation. Circ. Res. 89, 763-771 (2001).
    • (2001) Circ. Res. , vol.89 , pp. 763-771
    • Blake, G.J.1    Ridker, P.M.2
  • 87
    • 0028909302 scopus 로고
    • Physiological enzymatic cleavage of leukocyte membrane molecules
    • Bazil, V. Physiological enzymatic cleavage of leukocyte membrane molecules. Immunol. Today 16, 135-140 (1995).
    • (1995) Immunol. Today , vol.16 , pp. 135-140
    • Bazil, V.1
  • 88
    • 24044469049 scopus 로고    scopus 로고
    • L-selectin: Mechanisms and physiological significance of ectodomain cleavage
    • Smalley, D. M. & Ley, K. L-selectin: mechanisms and physiological significance of ectodomain cleavage. J. Cell. Mol. Med. 9, 255-266 (2005).
    • (2005) J. Cell. Mol. Med. , vol.9 , pp. 255-266
    • Smalley, D.M.1    Ley, K.2
  • 89
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon, J. J. et al. An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284 (1998). This report shows that CD156b is a sheddase that cleaves the rolling receptor CD62L from the surface of leukocytes.
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1
  • 90
    • 18444368391 scopus 로고    scopus 로고
    • The tumor necrosis factor-α converting enzyme (TACE): A unique metalloproteinase with highly defined substrate selectivity
    • Mohan, M. J. et al. The tumor necrosis factor-α converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity. Biochemistry 41, 9462-9469 (2002).
    • (2002) Biochemistry , vol.41 , pp. 9462-9469
    • Mohan, M.J.1
  • 92
    • 0035437168 scopus 로고    scopus 로고
    • Transendothelial migration of lymphocytes across high endothelial venules into lymph nodes is affected by metalloproteinases
    • Faveeuw, C., Preece, G. & Ager, A. Transendothelial migration of lymphocytes across high endothelial venules into lymph nodes is affected by metalloproteinases. Blood 98, 688-695 (2001).
    • (2001) Blood , vol.98 , pp. 688-695
    • Faveeuw, C.1    Preece, G.2    Ager, A.3
  • 93
    • 0242442699 scopus 로고    scopus 로고
    • L-selectin shedding does not regulate constitutive T cell trafficking but controls the migration pathways of antigen-activated T lymphocytes
    • Galkina, E. et al. L-selectin shedding does not regulate constitutive T cell trafficking but controls the migration pathways of antigen-activated T lymphocytes. J. Exp. Med. 198, 1323-1335 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 1323-1335
    • Galkina, E.1
  • 94
    • 10744227313 scopus 로고    scopus 로고
    • Leukocyte migration is regulated by L-selectin endoproteolytic release
    • Venturi, G. M. et al. Leukocyte migration is regulated by L-selectin endoproteolytic release. Immunity 19, 713-724 (2003).
    • (2003) Immunity , vol.19 , pp. 713-724
    • Venturi, G.M.1
  • 95
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • Itoh, Y. & Seiki, M. MT1-MMP: an enzyme with multidimensional regulation. Trends Biochem. Sci. 29, 285-289 (2004).
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 96
    • 0842347494 scopus 로고    scopus 로고
    • Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-type 1 matrix metalloproteinase
    • Nakamura, H. et al. Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-type 1 matrix metalloproteinase. Cancer Res. 64, 876-882 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 876-882
    • Nakamura, H.1
  • 97
    • 13444273084 scopus 로고    scopus 로고
    • CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase
    • Suenaga, N., Mori, H., Itoh, Y. & Seiki, M. CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase. Oncogene 24, 859-868 (2005). In this work, the authors show that the hemopexin domain of MT-MMPs is involved in the shedding of CD44.
    • (2005) Oncogene , vol.24 , pp. 859-868
    • Suenaga, N.1    Mori, H.2    Itoh, Y.3    Seiki, M.4
  • 98
    • 9144231190 scopus 로고    scopus 로고
    • Mature human thymocytes migrate on laminin-5 with activation of metalloproteinase-14 and cleavage of CD44
    • Vivinus-Nebot, M. et al. Mature human thymocytes migrate on laminin-5 with activation of metalloproteinase-14 and cleavage of CD44. J. Immunol. 172, 1397-1406 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 1397-1406
    • Vivinus-Nebot, M.1
  • 99
    • 0037103183 scopus 로고    scopus 로고
    • Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo
    • McQuibban, G. A. et al. Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo. Blood 100, 1160-1167 (2002).
    • (2002) Blood , vol.100 , pp. 1160-1167
    • McQuibban, G.A.1
  • 100
    • 0042237924 scopus 로고    scopus 로고
    • 3CL1-mediated cell-cell adhesion
    • 3CL1-mediated cell-cell adhesion. Blood 102, 1186-1195 (2003).
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1
  • 101
    • 0027368071 scopus 로고
    • Induction and function of vascular adhesion protein-1 at sites of inflammation
    • Salmi, M., Kalimo, K. & Jalkanen, S. Induction and function of vascular adhesion protein-1 at sites of inflammation. J. Exp. Med. 178, 2255-2260 (1993).
    • (1993) J. Exp. Med. , vol.178 , pp. 2255-2260
    • Salmi, M.1    Kalimo, K.2    Jalkanen, S.3
  • 102
    • 0033888918 scopus 로고    scopus 로고
    • In vivo detection of vascular adhesion protein-1 in experimental inflammation
    • Jaakkola, K. et al. In vivo detection of vascular adhesion protein-1 in experimental inflammation. Am. J. Pathol. 157, 463-471 (2000).
    • (2000) Am. J. Pathol. , vol.157 , pp. 463-471
    • Jaakkola, K.1
  • 103
    • 0032490640 scopus 로고    scopus 로고
    • Cloning of vascular adhesion protein-1 reveals a novel multifunctional adhesion molecule
    • Smith, D. J. et al. Cloning of vascular adhesion protein-1 reveals a novel multifunctional adhesion molecule. J. Exp. Med. 188, 17-27 (1998).
    • (1998) J. Exp. Med. , vol.188 , pp. 17-27
    • Smith, D.J.1
  • 104
  • 105
    • 0035071558 scopus 로고    scopus 로고
    • A cell surface amine oxidase directly controls lymphocyte migration
    • Salmi, M. et al. A cell surface amine oxidase directly controls lymphocyte migration. Immunity 14, 265-276 (2001). This was the first study to show that SSAO activity is required for lymphocyte-endothelial-cell interactions.
    • (2001) Immunity , vol.14 , pp. 265-276
    • Salmi, M.1
  • 106
    • 23844480355 scopus 로고    scopus 로고
    • H2 lymphocytes in inflamed liver: A role for α-4 integrin and vascular adhesion protein-1
    • H2 lymphocytes in inflamed liver: a role for α-4 integrin and vascular adhesion protein-1. Immunity 23, 153-163 (2005).
    • (2005) Immunity , vol.23 , pp. 153-163
    • Bonder, C.S.1
  • 107
    • 0026757630 scopus 로고
    • A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans
    • Salmi, M. & Jalkanen, S. A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans. Science 257, 1407-1409 (1992).
    • (1992) Science , vol.257 , pp. 1407-1409
    • Salmi, M.1    Jalkanen, S.2
  • 108
    • 0037100288 scopus 로고    scopus 로고
    • Vascular adhesion protein-1 mediates adhesion and transmigration of lymphocytes on human hepatic endothelial cells
    • Lalor, P. F. et al. Vascular adhesion protein-1 mediates adhesion and transmigration of lymphocytes on human hepatic endothelial cells. J. Immunol. 169, 983-992 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 983-992
    • Lalor, P.F.1
  • 109
    • 0032522844 scopus 로고    scopus 로고
    • Vascular adhesion protein-1 and ICAM-1 support the adhesion of tumor-infiltrating lymphocytes to tumor endothelium in human hepatocellular carcinoma
    • Yoong, K. F., McNab, G., Hubscher, S. G. & Adams, D. H. Vascular adhesion protein-1 and ICAM-1 support the adhesion of tumor-infiltrating lymphocytes to tumor endothelium in human hepatocellular carcinoma. J. Immunol. 160, 3978-3988 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 3978-3988
    • Yoong, K.F.1    McNab, G.2    Hubscher, S.G.3    Adams, D.H.4
  • 110
    • 0035124160 scopus 로고    scopus 로고
    • Vascular adhesion protein 1 (VAP-1) functions as a molecular brake during granulocyte rolling and mediates their recruitment in vivo
    • Tohka, S., Laukkanen, M.-L., Jalkanen, S. & Salmi, M. Vascular adhesion protein 1 (VAP-1) functions as a molecular brake during granulocyte rolling and mediates their recruitment in vivo. FASEB J. 15, 373-382 (2001).
    • (2001) FASEB J. , vol.15 , pp. 373-382
    • Tohka, S.1    Laukkanen, M.-L.2    Jalkanen, S.3    Salmi, M.4
  • 111
    • 9644260760 scopus 로고    scopus 로고
    • Blockade of vascular adhesion protein-1 inhibits lymphocyte infiltration in rat liver allograft rejection
    • Martelius, T. et al. Blockade of vascular adhesion protein-1 inhibits lymphocyte infiltration in rat liver allograft rejection. Am. J. Pathol. 165, 1993-2001 (2004).
    • (2004) Am. J. Pathol. , vol.165 , pp. 1993-2001
    • Martelius, T.1
  • 112
    • 14644393680 scopus 로고    scopus 로고
    • Vascular adhesion protein-1 is involved in both acute and chronic inflammation in the mouse
    • Merinen, M. et al. Vascular adhesion protein-1 is involved in both acute and chronic inflammation in the mouse. Am. J. Pathol. 166, 793-800 (2005).
    • (2005) Am. J. Pathol. , vol.166 , pp. 793-800
    • Merinen, M.1
  • 113
    • 1942456908 scopus 로고    scopus 로고
    • Granulocyte transmigration through endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1)
    • Koskinen, K. et al. Granulocyte transmigration through endothelium is regulated by the oxidase activity of vascular adhesion protein-1 (VAP-1). Blood 103, 3388-3395 (2004).
    • (2004) Blood , vol.103 , pp. 3388-3395
    • Koskinen, K.1
  • 114
    • 3042742805 scopus 로고    scopus 로고
    • Semicarbazide sensitive amine oxidase overexpression has dual consequences: Insulin mimicry and diabetes-like complications
    • Stolen, C. M. et al. Semicarbazide sensitive amine oxidase overexpression has dual consequences: insulin mimicry and diabetes-like complications. FASEB J. 18, 702-704 (2004).
    • (2004) FASEB J. , vol.18 , pp. 702-704
    • Stolen, C.M.1
  • 115
    • 23644452808 scopus 로고    scopus 로고
    • Crystal structure of the human vascular adhesion protein-1 : Unique structural features with functional implications
    • Airenne, T. T. et al. Crystal structure of the human vascular adhesion protein-1 : unique structural features with functional implications. Protein Sci. 14, 1964-1974 (2005).
    • (2005) Protein Sci. , vol.14 , pp. 1964-1974
    • Airenne, T.T.1
  • 116
    • 0038798023 scopus 로고    scopus 로고
    • The inhibition of semicarbazide-sensitive amine oxidase by aminohexoses
    • O'Sullivan, J. et al. The inhibition of semicarbazide-sensitive amine oxidase by aminohexoses. Biochim. Biophys. Acta 1647, 367-371 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 367-371
    • O'Sullivan, J.1
  • 117
    • 0036911138 scopus 로고    scopus 로고
    • Hydrogen peroxide as second messenger in lymphocyte activation
    • Reth, M. Hydrogen peroxide as second messenger in lymphocyte activation. Nature Immunol. 3, 1129-1134 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 1129-1134
    • Reth, M.1
  • 118
    • 0037365968 scopus 로고    scopus 로고
    • Specificity of a third kind: Reactive oxygen and nitrogen intermediates in cell signaling
    • Nathan, C. Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling. J. Clin. Invest. 111, 769-778 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 769-778
    • Nathan, C.1
  • 119
    • 0029761141 scopus 로고    scopus 로고
    • Hydrogen peroxide induces leukocyte rolling: Modulation by endogenous antioxidant mechanisms including NO
    • Johnston, B., Kanwar, S. & Kubes, P. Hydrogen peroxide induces leukocyte rolling: modulation by endogenous antioxidant mechanisms including NO. Am. J. Physiol. 271, H614-H621 (1996).
    • (1996) Am. J. Physiol. , vol.271
    • Johnston, B.1    Kanwar, S.2    Kubes, P.3
  • 120
    • 0033067572 scopus 로고    scopus 로고
    • Increases in oxygen tension stimulate expression of ICAM-1 and VCAM-1 on human endothelial cells
    • Willam, C., Schindler, R., Frei, U. & Eckardt, K. U. Increases in oxygen tension stimulate expression of ICAM-1 and VCAM-1 on human endothelial cells. Am. J. Physiol. 276, H2044-H2052 (1999).
    • (1999) Am. J. Physiol. , vol.276
    • Willam, C.1    Schindler, R.2    Frei, U.3    Eckardt, K.U.4
  • 121
    • 0034646464 scopus 로고    scopus 로고
    • Redox regulation of chemokine receptor expression
    • Saccani, A. et al. Redox regulation of chemokine receptor expression. Proc. Natl Acad. Sci. USA 97, 2761-2766 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2761-2766
    • Saccani, A.1
  • 122
    • 0037119473 scopus 로고    scopus 로고
    • 2 activates pro-matrix metalloproteinase-2 through receptor tyrosine kinases/phosphatidylinositol 3-kinase/NF-κB pathway
    • 2 activates pro-matrix metalloproteinase-2 through receptor tyrosine kinases/phosphatidylinositol 3-kinase/NF-κB pathway. J. Biol. Chem. 277, 30271-30282 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30271-30282
    • Yoon, S.O.1    Park, S.J.2    Yoon, S.Y.3    Yun, C.H.4    Chung, A.S.5
  • 123
    • 4944225786 scopus 로고    scopus 로고
    • Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: Role of reactive oxygen species
    • Deem, T. L. & Cook-Mills, J. M. Vascular cell adhesion molecule 1 (VCAM-1) activation of endothelial cell matrix metalloproteinases: role of reactive oxygen species. Blood 104, 2385-2393 (2004).
    • (2004) Blood , vol.104 , pp. 2385-2393
    • Deem, T.L.1    Cook-Mills, J.M.2
  • 124
    • 0035148585 scopus 로고    scopus 로고
    • Extracellular ATP formation on vascular endothelial cells is mediated by ecto-nucleotide kinase activities via phosphotransfer reactions
    • Yegutkin, G. G., Henttinen, T. & Jalkanen, S. Extracellular ATP formation on vascular endothelial cells is mediated by ecto-nucleotide kinase activities via phosphotransfer reactions. FASEB J. 15, 251-260 (2001).
    • (2001) FASEB J. , vol.15 , pp. 251-260
    • Yegutkin, G.G.1    Henttinen, T.2    Jalkanen, S.3
  • 125
    • 0035814940 scopus 로고    scopus 로고
    • The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast
    • Schwartz, B., Olgin, A. K. & Klinman, J. P. The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast. Biochemistry 40, 2954-2963 (2001).
    • (2001) Biochemistry , vol.40 , pp. 2954-2963
    • Schwartz, B.1    Olgin, A.K.2    Klinman, J.P.3
  • 126
    • 20144379146 scopus 로고    scopus 로고
    • CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins
    • Krebs, C. et al. CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins. J. Immunol. 174, 3298-3305 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 3298-3305
    • Krebs, C.1
  • 127
    • 0030588705 scopus 로고    scopus 로고
    • Selective induction of CD73 expression in human lymphocytes by CD38 ligation: A novel pathway linking signal transducers with ecto-enzyme activities
    • Peola, S. et al. Selective induction of CD73 expression in human lymphocytes by CD38 ligation: a novel pathway linking signal transducers with ecto-enzyme activities. J. Immunol. 157, 4354-4362 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 4354-4362
    • Peola, S.1
  • 128
    • 0030586618 scopus 로고    scopus 로고
    • Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1. Possible role in the recycling of nicotinamide adenine dinucleotide metabolites
    • Deterre, P. et al. Coordinated regulation in human T cells of nucleotide-hydrolyzing ecto-enzymatic activities, including CD38 and PC-1. Possible role in the recycling of nicotinamide adenine dinucleotide metabolites. J. Immunol. 157, 1381-1388 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 1381-1388
    • Deterre, P.1
  • 129
    • 20644449872 scopus 로고    scopus 로고
    • Safety of blocking vascular adhesion protein-1 in patients with contact dermatitis
    • Vainio, P. J. et al. Safety of blocking vascular adhesion protein-1 in patients with contact dermatitis. Basic Clin. Pharmacol. Toxicol. 96, 429-435 (2005).
    • (2005) Basic Clin. Pharmacol. Toxicol. , vol.96 , pp. 429-435
    • Vainio, P.J.1
  • 130
    • 20344401109 scopus 로고    scopus 로고
    • Mechanisms, management and future directions for reperfusion injury after acute myocardial infarction
    • Cannon, R. Mechanisms, management and future directions for reperfusion injury after acute myocardial infarction. Nature Clin. Pract. Cardiovasc. Med. 2, 88-94 (2005).
    • (2005) Nature Clin. Pract. Cardiovasc. Med. , vol.2 , pp. 88-94
    • Cannon, R.1
  • 131
    • 0031444134 scopus 로고    scopus 로고
    • ACE-inhibition prevents postischemic coronary leukocyte adhesion and leukocyte-dependent reperfusion injury
    • Kupatt, C. et al. ACE-inhibition prevents postischemic coronary leukocyte adhesion and leukocyte-dependent reperfusion injury. Cardiovasc. Res. 36, 386-395 (1997).
    • (1997) Cardiovasc. Res. , vol.36 , pp. 386-395
    • Kupatt, C.1
  • 132
    • 4644363433 scopus 로고    scopus 로고
    • Role of angiotensin II in ischemia/reperfusion-induced leukocyte-endothelium interactions in the colon
    • Riaz, A. A. et al. Role of angiotensin II in ischemia/reperfusion-induced leukocyte-endothelium interactions in the colon. FASEB J. 18, 881-883 (2004).
    • (2004) FASEB J. , vol.18 , pp. 881-883
    • Riaz, A.A.1
  • 133
    • 0022648659 scopus 로고
    • Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence
    • Schumacher, M. et al. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature 319, 407-409 (1986).
    • (1986) Nature , vol.319 , pp. 407-409
    • Schumacher, M.1
  • 134
    • 0033816854 scopus 로고    scopus 로고
    • Ecto-enzymes: Physiology meets pathology
    • Goding, J. W. Ecto-enzymes: physiology meets pathology. J. Leukoc. Biol. 67, 285-311 (2000).
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 285-311
    • Goding, J.W.1
  • 135
    • 0033499058 scopus 로고    scopus 로고
    • Is the Fischer 344/CRJ rat a protein-knock-out model for dipeptidyl peptidase IV-mediated lung metastasis of breast cancer?
    • Cheng, H. C., Abdel-Ghany, M., Zhang, S. & Pauli, B. U. Is the Fischer 344/CRJ rat a protein-knock-out model for dipeptidyl peptidase IV-mediated lung metastasis of breast cancer? Clin. Exp. Metastasis 17, 609-615 (1999).
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 609-615
    • Cheng, H.C.1    Abdel-Ghany, M.2    Zhang, S.3    Pauli, B.U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.