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Volumn 58, Issue , 1995, Pages 345-416

Leukocyte migration and adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIAL LEUKOCYTE ADHESION MOLECULE 1; HOMING RECEPTOR; INTEGRIN; SELECTIN;

EID: 0028883140     PISSN: 00652776     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0065-2776(08)60623-9     Document Type: Review
Times cited : (315)

References (337)
  • 1
    • 0027667808 scopus 로고
    • How the immune system develops
    • I.L. Weissman M.D. Cooper How the immune system develops Sci. Am. 269 3 1993 33 39
    • (1993) Sci. Am. , vol.269 , Issue.3 , pp. 33-39
    • Weissman, I.L.1    Cooper, M.D.2
  • 2
    • 85113063060 scopus 로고
    • W.E. Paul Fundamental Immunology 3rd ed. 1993 Raven Press New York
    • (1993)
    • Paul, W.E.1
  • 3
    • 0345865947 scopus 로고
    • Lymphocyte locomotion, lymphatic tissues and lymphocyte circulation in the rat
    • A.O. Anderson N.D. Anderson J.D. White Lymphocyte locomotion, lymphatic tissues and lymphocyte circulation in the rat J.B. Hay Animal Models of Immunological Processes 1982 Academic Press New York 25 95
    • (1982) , pp. 25-95
    • Anderson, A.O.1    Anderson, N.D.2    White, J.D.3
  • 4
    • 0026342111 scopus 로고
    • Leukocyte—endothelial cell recognition: Three (or more) steps to specificity and diversity
    • E.C. Butcher Leukocyte—endothelial cell recognition: Three (or more) steps to specificity and diversity Cell 67 1991 1033 1036
    • (1991) Cell , vol.67 , pp. 1033-1036
    • Butcher, E.C.1
  • 5
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • T.A. Springer Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm Cell 76 1994 301 314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 6
    • 85113046682 scopus 로고
    • D. Dunon C.R. Mackay B.A. Imhof Adhesion in Leukocyte Homing and Differentiation 1993 Springer Verlag New York 260
    • (1993) , pp. 260
    • Dunon, D.1    Mackay, C.R.2    Imhof, B.A.3
  • 7
    • 85113043584 scopus 로고
    • D.W. Fawcett A Textbook of Histology 12 ed. 1994 Chapman & Hall New York 964
    • (1994) , pp. 964
    • Fawcett, D.W.1
  • 8
    • 0023158008 scopus 로고
    • Isolation and culture of high endothelial cells from rat endothelial cells from lymph nodes
    • A. Ager Isolation and culture of high endothelial cells from rat endothelial cells from lymph nodes J. Cell Sci 87 1987 133 144
    • (1987) J. Cell Sci , vol.87 , pp. 133-144
    • Ager, A.1
  • 9
    • 0025343120 scopus 로고
    • Naive and memory T cells show distinct pathways of lymphocyte recirculation
    • C.R. Mackay W.L. Marston L. Dudler Naive and memory T cells show distinct pathways of lymphocyte recirculation J. Exp. Med 171 1990 801 817
    • (1990) J. Exp. Med , vol.171 , pp. 801-817
    • Mackay, C.R.1    Marston, W.L.2    Dudler, L.3
  • 10
    • 0001512851 scopus 로고
    • The origin of cells in the efferent lymph from a single lymph node
    • J.G. Hall B. Morris The origin of cells in the efferent lymph from a single lymph node J. Exp. Med 121 1965 901 910
    • (1965) J. Exp. Med , vol.121 , pp. 901-910
    • Hall, J.G.1    Morris, B.2
  • 12
    • 0026810631 scopus 로고
    • The dynamics of immunological memory
    • D. Gray The dynamics of immunological memory Sem. Immunol 4 1992 29 34
    • (1992) Sem. Immunol , vol.4 , pp. 29-34
    • Gray, D.1
  • 13
    • 0028012618 scopus 로고
    • T cell migration during development: Homing is not related to TCR V β1 repertoire selection
    • D. Dunon J. Schwager J.P. Dangy M.D. Cooper B.A. Imhof T cell migration during development: Homing is not related to TCR V β1 repertoire selection EMBO J 13 1994 808 815
    • (1994) EMBO J , vol.13 , pp. 808-815
    • Dunon, D.1    Schwager, J.2    Dangy, J.P.3    Cooper, M.D.4    Imhof, B.A.5
  • 14
    • 0016892242 scopus 로고
    • Lymphopoiesis and lymphocyte recirculation in the sheep fetus
    • L.D. Pearson M.W. Simpson Morgan B. Morris Lymphopoiesis and lymphocyte recirculation in the sheep fetus J. Exp. Med 143 1976 167 186
    • (1976) J. Exp. Med , vol.143 , pp. 167-186
    • Pearson, L.D.1    Simpson Morgan, M.W.2    Morris, B.3
  • 15
    • 0027302705 scopus 로고
    • Immunological memory
    • C.R. Mackay Immunological memory Adv. Immunol 53 1993 217 265
    • (1993) Adv. Immunol , vol.53 , pp. 217-265
    • Mackay, C.R.1
  • 16
    • 0026445567 scopus 로고
    • Lifespan of human lymphocyte subsets defined by CD45 isoforms
    • C.A. Michie A. McLean C. Alcock P.C.L. Beverley Lifespan of human lymphocyte subsets defined by CD45 isoforms Nature 360 1992 264 265
    • (1992) Nature , vol.360 , pp. 264-265
    • Michie, C.A.1    McLean, A.2    Alcock, C.3    Beverley, P.C.L.4
  • 17
    • 0026816125 scopus 로고
    • Function of CD4 T cell subsets in vivo: Expression of CD45R isoforms
    • E.B. Bell Function of CD4 T cell subsets in vivo: Expression of CD45R isoforms Sem. Immunol 4 1992 43 50
    • (1992) Sem. Immunol , vol.4 , pp. 43-50
    • Bell, E.B.1
  • 18
    • 0028267677 scopus 로고
    • Turnover of naive- and memory-phenotype T cells
    • D.F. Tough J. Sprent Turnover of naive- and memory-phenotype T cells J. Exp. Med 179 1994 1127 1135
    • (1994) J. Exp. Med , vol.179 , pp. 1127-1135
    • Tough, D.F.1    Sprent, J.2
  • 19
    • 0026593810 scopus 로고
    • Tissue-specific migration pathways by phenotypically distinct subpopulations of memory T cells
    • C.R. Mackay W.L. Marston L. Dudler O. Spertini T.F. Tedder W.R. Hein Tissue-specific migration pathways by phenotypically distinct subpopulations of memory T cells Eur. J. Immunol 22 1992 887 895
    • (1992) Eur. J. Immunol , vol.22 , pp. 887-895
    • Mackay, C.R.1    Marston, W.L.2    Dudler, L.3    Spertini, O.4    Tedder, T.F.5    Hein, W.R.6
  • 20
    • 0026705574 scopus 로고
    • Homing of blood, splenic, and lung emigrant lymphoblasts: Comparison with the behaviour of lymphocytes from these sources
    • R.M. Binns S.T. Licence R. Pabst Homing of blood, splenic, and lung emigrant lymphoblasts: Comparison with the behaviour of lymphocytes from these sources Int. Immunol 4 1992 1011 1019
    • (1992) Int. Immunol , vol.4 , pp. 1011-1019
    • Binns, R.M.1    Licence, S.T.2    Pabst, R.3
  • 22
    • 0015722745 scopus 로고
    • Maturation of B lymphocytes in the rat. I. Migration pattern, tissue distribution, and turnover rate of unprimed and primed B lymphocytes involved in the adoptive antidinitrophenyl response
    • S. Strober J. Dilley Maturation of B lymphocytes in the rat. I. Migration pattern, tissue distribution, and turnover rate of unprimed and primed B lymphocytes involved in the adoptive antidinitrophenyl response J. Exp. Med 138 1973 1331 1344
    • (1973) J. Exp. Med , vol.138 , pp. 1331-1344
    • Strober, S.1    Dilley, J.2
  • 23
    • 45549118928 scopus 로고
    • The spleen in lymphocyte migration
    • R. Pabst The spleen in lymphocyte migration Immunol. Today 9 1988 43 45
    • (1988) Immunol. Today , vol.9 , pp. 43-45
    • Pabst, R.1
  • 24
    • 0028243311 scopus 로고
    • B- and T-lymphocyte subset numbers in the migrating lymphocyte pool of the rat: The influence of interferon-γ on its mobilization monitored through blood and lymph
    • J. Westermann J. Matyas S. Persin P. Van der Meide C. Heerwagen R. Pabst B- and T-lymphocyte subset numbers in the migrating lymphocyte pool of the rat: The influence of interferon-γ on its mobilization monitored through blood and lymph Scand. J. Immunol 39 1994 395 402
    • (1994) Scand. J. Immunol , vol.39 , pp. 395-402
    • Westermann, J.1    Matyas, J.2    Persin, S.3    Van der Meide, P.4    Heerwagen, C.5    Pabst, R.6
  • 25
    • 0028328763 scopus 로고
    • Migration of so-called naive and memory T lymphocytes from blood to lymph in the rat
    • J. Westermann S. Persin J. Matyas P. Van der Meide R. Pabst Migration of so-called naive and memory T lymphocytes from blood to lymph in the rat J. Immunol 152 1994 1744 1750
    • (1994) J. Immunol , vol.152 , pp. 1744-1750
    • Westermann, J.1    Persin, S.2    Matyas, J.3    Van der Meide, P.4    Pabst, R.5
  • 26
    • 0026499960 scopus 로고
    • Endothelial cell interactions with granulocytes: Tethering and signaling molecules
    • G.A. Zimmerman S.M. Prescott T.M. McIntyre Endothelial cell interactions with granulocytes: Tethering and signaling molecules Immunol. Today 13 1992 93 100
    • (1992) Immunol. Today , vol.13 , pp. 93-100
    • Zimmerman, G.A.1    Prescott, S.M.2    McIntyre, T.M.3
  • 27
    • 0027507615 scopus 로고
    • Interactions between neutrophils and endothelial cells
    • C. Godin A. Caprani J. Dufaux P. Flaud Interactions between neutrophils and endothelial cells J. Cell Sci 106 1993 441 452
    • (1993) J. Cell Sci , vol.106 , pp. 441-452
    • Godin, C.1    Caprani, A.2    Dufaux, J.3    Flaud, P.4
  • 29
    • 0017088029 scopus 로고
    • Lymphocyte homing into lymph nodes: In vitro demonstration of selective affinity of recirculating lymphocytes for high endothelial venules
    • H.B. Stamper J.J. Woodruff Lymphocyte homing into lymph nodes: In vitro demonstration of selective affinity of recirculating lymphocytes for high endothelial venules J. Exp. Med 144 1976 828 833
    • (1976) J. Exp. Med , vol.144 , pp. 828-833
    • Stamper, H.B.1    Woodruff, J.J.2
  • 30
    • 0020577072 scopus 로고
    • A cell-surface molecule involved in organ-specific homing of lymphocytes
    • W.M. Gallatin I.L. Weissman E.C. Butcher A cell-surface molecule involved in organ-specific homing of lymphocytes Nature 304 1983 30 34
    • (1983) Nature , vol.304 , pp. 30-34
    • Gallatin, W.M.1    Weissman, I.L.2    Butcher, E.C.3
  • 32
    • 0024584481 scopus 로고
    • Mouse lymph node homing receptor cDNA clone encodes a glycoprote in revealing tandem interaction domains
    • M.H. Siegelman M. van den Rijn I.L. Weissman Mouse lymph node homing receptor cDNA clone encodes a glycoprote in revealing tandem interaction domains Science 243 1989 1165 1172
    • (1989) Science , vol.243 , pp. 1165-1172
    • Siegelman, M.H.1    van den Rijn, M.2    Weissman, I.L.3
  • 34
    • 0024328263 scopus 로고
    • Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins
    • T.F. Tedder C.M. Isaacs T.J. Ernst G.D. Demetri D.A. Adler C.M. Disteche Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins J. Exp. Med 170 1989 123 133
    • (1989) J. Exp. Med , vol.170 , pp. 123-133
    • Tedder, T.F.1    Isaacs, C.M.2    Ernst, T.J.3    Demetri, G.D.4    Adler, D.A.5    Disteche, C.M.6
  • 35
    • 0024424889 scopus 로고
    • Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor
    • D. Camerini S.P. James I. Stamenkovic B. Seed Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor Nature 342 1989 78 82
    • (1989) Nature , vol.342 , pp. 78-82
    • Camerini, D.1    James, S.P.2    Stamenkovic, I.3    Seed, B.4
  • 36
    • 0024558097 scopus 로고
    • Cloning of GMP-140, a granule membrane protein of platelets and endothelium: Sequence similarity to proteins involved in cell adhesion and inflammation
    • G.I. Johnston R.G. Cook R.P. McEver Cloning of GMP-140, a granule membrane protein of platelets and endothelium: Sequence similarity to proteins involved in cell adhesion and inflammation Cell 56 1989 1033 1044
    • (1989) Cell , vol.56 , pp. 1033-1044
    • Johnston, G.I.1    Cook, R.G.2    McEver, R.P.3
  • 37
    • 0026718810 scopus 로고
    • Cloning of the mouse endothelial selectins: Expression of both E and P-selectin is inducible by tumor necrosis factor-α
    • A. Weller S. Isenmann D. Vestweber Cloning of the mouse endothelial selectins: Expression of both E and P-selectin is inducible by tumor necrosis factor-α J. Biol. Chem 267 1992 15176 15183
    • (1992) J. Biol. Chem , vol.267 , pp. 15176-15183
    • Weller, A.1    Isenmann, S.2    Vestweber, D.3
  • 38
    • 0024601050 scopus 로고
    • Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins
    • M.P. Bevilacqua S. Stengelin M.A. Gimbrone B. Seed Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins Science 243 1989 1160 1165
    • (1989) Science , vol.243 , pp. 1160-1165
    • Bevilacqua, M.P.1    Stengelin, S.2    Gimbrone, M.A.3    Seed, B.4
  • 40
    • 0026426731 scopus 로고
    • Sticky sugars for selectins
    • T. Springer L.A. Lasky Sticky sugars for selectins Nature 349 1991 196 197
    • (1991) Nature , vol.349 , pp. 196-197
    • Springer, T.1    Lasky, L.A.2
  • 41
    • 0026445723 scopus 로고
    • Selectins: Interpreters of cell-specific carbohydrate information during inflammation
    • L.A. Lasky Selectins: Interpreters of cell-specific carbohydrate information during inflammation Science 258 1992 964 969
    • (1992) Science , vol.258 , pp. 964-969
    • Lasky, L.A.1
  • 44
    • 0024420563 scopus 로고
    • Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors
    • T.K. Kishimoto M.A. Jutila E.L. Berg E.C. Butcher Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors Science 245 1989 1238 1241
    • (1989) Science , vol.245 , pp. 1238-1241
    • Kishimoto, T.K.1    Jutila, M.A.2    Berg, E.L.3    Butcher, E.C.4
  • 45
    • 0024351649 scopus 로고
    • Function and regulation of the neutrophil MEL-14 antigen in vivo: Comparison with LFA-1 and MAC-1
    • M.A. Jutila L. Rott E.L. Berg E.C. Butcher Function and regulation of the neutrophil MEL-14 antigen in vivo: Comparison with LFA-1 and MAC-1 J. Immunol 143 1989 3318 3324
    • (1989) J. Immunol , vol.143 , pp. 3318-3324
    • Jutila, M.A.1    Rott, L.2    Berg, E.L.3    Butcher, E.C.4
  • 46
    • 0023179057 scopus 로고
    • Leukocyte—endothelial cell recognition: Evidence of a common molecular mechanism shared by neutrophils, lymphocytes, and other leukocytes
    • D.M. Lewinsohn R.F. Bargatze E.C. Butcher Leukocyte—endothelial cell recognition: Evidence of a common molecular mechanism shared by neutrophils, lymphocytes, and other leukocytes J. Immunol 138 1987 4313 4321
    • (1987) J. Immunol , vol.138 , pp. 4313-4321
    • Lewinsohn, D.M.1    Bargatze, R.F.2    Butcher, E.C.3
  • 47
    • 0024460326 scopus 로고
    • Demonstration that a lectin-like receptor (gp90MEL) directly mediates adhesion of lymphocytes to high endothelial venules of lymph nodes
    • J.S. Geoffroy S.D. Rosen Demonstration that a lectin-like receptor (gp90MEL) directly mediates adhesion of lymphocytes to high endothelial venules of lymph nodes J. Cell Biol 109 1989 2463 2469
    • (1989) J. Cell Biol , vol.109 , pp. 2463-2469
    • Geoffroy, J.S.1    Rosen, S.D.2
  • 48
    • 0027720288 scopus 로고
    • Interferon-α induces the expression of the L-selectin homing receptor in human B lymphoid cells
    • S.S. Evans R.P. Collea M.M. Appenheimer S.O. Gollnick Interferon-α induces the expression of the L-selectin homing receptor in human B lymphoid cells J. Cell. Biol 123 1993 1889 1893
    • (1993) J. Cell. Biol , vol.123 , pp. 1889-1893
    • Evans, S.S.1    Collea, R.P.2    Appenheimer, M.M.3    Gollnick, S.O.4
  • 49
    • 0026050582 scopus 로고
    • Homing receptors reexamined: Mouse LECAM-1 (MEL-14 antigen) is involved in lymphocyte migration into gut-associated lymphoid tissue
    • A. Hamann W.D. Jablonski P. Jonas H.G. Thiele Homing receptors reexamined: Mouse LECAM-1 (MEL-14 antigen) is involved in lymphocyte migration into gut-associated lymphoid tissue Eur. J. Immunol 21 1991 2925 2929
    • (1991) Eur. J. Immunol , vol.21 , pp. 2925-2929
    • Hamann, A.1    Jablonski, W.D.2    Jonas, P.3    Thiele, H.G.4
  • 50
    • 0025299180 scopus 로고
    • A homing receptor-IgG chimera as a probe for adhesive ligands of lymph node high endothelial venules
    • S.R. Watson Y. Imai C. Fennie J.S. Geoffroy S.D. Rosen L.A. Lasky A homing receptor-IgG chimera as a probe for adhesive ligands of lymph node high endothelial venules J. Cell. Biol 110 1990 2221 2229
    • (1990) J. Cell. Biol , vol.110 , pp. 2221-2229
    • Watson, S.R.1    Imai, Y.2    Fennie, C.3    Geoffroy, J.S.4    Rosen, S.D.5    Lasky, L.A.6
  • 51
    • 0026088467 scopus 로고
    • Neutrophil influx into an inflammatory site inhibited by a soluble homing receptor-IgG chimaera
    • S.R. Watson C. Fennie L.A. Lasky Neutrophil influx into an inflammatory site inhibited by a soluble homing receptor-IgG chimaera Nature 349 1991 164 167
    • (1991) Nature , vol.349 , pp. 164-167
    • Watson, S.R.1    Fennie, C.2    Lasky, L.A.3
  • 52
    • 0025210021 scopus 로고
    • Identification of a human peripheral lymph node homing receptor: a rapidly down-regulated adhesion molecule
    • T.K. Kishimoto M.A. Jutila E.C. Butcher Identification of a human peripheral lymph node homing receptor: a rapidly down-regulated adhesion molecule Proc. Natl. Acad. Sci. USA 87 1990 2244 2248
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2244-2248
    • Kishimoto, T.K.1    Jutila, M.A.2    Butcher, E.C.3
  • 53
    • 0026660377 scopus 로고
    • Soluble L-selectin is present in human plasma at high levels and retains functional activity
    • B. Schleiffenbaum O. Spertini T.F. Tedder Soluble L-selectin is present in human plasma at high levels and retains functional activity J. Cell Biol 119 1992 229 238
    • (1992) J. Cell Biol , vol.119 , pp. 229-238
    • Schleiffenbaum, B.1    Spertini, O.2    Tedder, T.F.3
  • 55
    • 0025119997 scopus 로고
    • PADGEM-dependent adhesion of platelets to monocytes and neutrophils is mediated by a lineage-specific carbohydrate, LNF III (CD15)
    • E. Larsen T. Palabrica S. Sajer G.E. Gilbert D.D. Wagner B.C. Furie B. Furie PADGEM-dependent adhesion of platelets to monocytes and neutrophils is mediated by a lineage-specific carbohydrate, LNF III (CD15) Cell 63 1990 467 474
    • (1990) Cell , vol.63 , pp. 467-474
    • Larsen, E.1    Palabrica, T.2    Sajer, S.3    Gilbert, G.E.4    Wagner, D.D.5    Furie, B.C.6    Furie, B.7
  • 56
    • 0026938894 scopus 로고
    • Leukocyte—endothelial cell interactions
    • R.P. McEver Leukocyte—endothelial cell interactions Curr. Opin. Cell Biol 4 1992 840 849
    • (1992) Curr. Opin. Cell Biol , vol.4 , pp. 840-849
    • McEver, R.P.1
  • 58
    • 0027374172 scopus 로고
    • P-selectin mediates neutrophil rolling on histamine-stimulated endothelial cells
    • D.A. Jones O. Abbassi L.V. McIntire R.P. McEver C.W. Smith P-selectin mediates neutrophil rolling on histamine-stimulated endothelial cells Biophys. J 65 1993 1560 1569
    • (1993) Biophys. J , vol.65 , pp. 1560-1569
    • Jones, D.A.1    Abbassi, O.2    McIntire, L.V.3    McEver, R.P.4    Smith, C.W.5
  • 59
    • 0027272394 scopus 로고
    • Selectin-mediated rolling of neutrophils on immobilized platelets
    • S.M. Buttrum R. Hatton G.B. Nash Selectin-mediated rolling of neutrophils on immobilized platelets Blood 82 1993 1165 1174
    • (1993) Blood , vol.82 , pp. 1165-1174
    • Buttrum, S.M.1    Hatton, R.2    Nash, G.B.3
  • 60
    • 0027186297 scopus 로고
    • Activated platelets induce superoxide anion release by monocytes and neutrophils through P-selectin (CD62)
    • K. Nagata T. Tsuji N. Todoroki Y. Katagiri K. Tanoue H. Yamazaki N. Hanai T. Irimura Activated platelets induce superoxide anion release by monocytes and neutrophils through P-selectin (CD62) J. Immunol 151 1993 3267 3273
    • (1993) J. Immunol , vol.151 , pp. 3267-3273
    • Nagata, K.1    Tsuji, T.2    Todoroki, N.3    Katagiri, Y.4    Tanoue, K.5    Yamazaki, H.6    Hanai, N.7    Irimura, T.8
  • 62
    • 0027182466 scopus 로고
    • The cytoplasmic domain of P-selectin is phosphorylated on serine and threonine residues
    • T. Fujimoto R.P. McEver The cytoplasmic domain of P-selectin is phosphorylated on serine and threonine residues Blood 82 1993 1758 1766
    • (1993) Blood , vol.82 , pp. 1758-1766
    • Fujimoto, T.1    McEver, R.P.2
  • 63
    • 0028140035 scopus 로고
    • The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes
    • S.A. Green H. Setiadi R.P. McEver R.B. Kelly The cytoplasmic domain of P-selectin contains a sorting determinant that mediates rapid degradation in lysosomes J. Cell Biol 124 1994 435 448
    • (1994) J. Cell Biol , vol.124 , pp. 435-448
    • Green, S.A.1    Setiadi, H.2    McEver, R.P.3    Kelly, R.B.4
  • 65
    • 0027223996 scopus 로고
    • Neuropeptides induce rapid expression of endothelial cell adhesion molecules and elicit granulocytic infiltration in human skin
    • C.H. Smith J.N. Barker R.W. Morris D.M. MacDonald T.H. Lee Neuropeptides induce rapid expression of endothelial cell adhesion molecules and elicit granulocytic infiltration in human skin J. Immunol 151 1993 3274 3782
    • (1993) J. Immunol , vol.151 , pp. 3274-3782
    • Smith, C.H.1    Barker, J.N.2    Morris, R.W.3    MacDonald, D.M.4    Lee, T.H.5
  • 66
    • 0026486191 scopus 로고
    • Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: A mechanism for stabilizing neutrophil adhesion
    • Y. Sugama C. Tiruppathi K. Janakidevi T.T. Andersen J.W. Fenton II A.B. Malik Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: A mechanism for stabilizing neutrophil adhesion J. Cell Biol 119 1992 935 944
    • (1992) J. Cell Biol , vol.119 , pp. 935-944
    • Sugama, Y.1    Tiruppathi, C.2    Janakidevi, K.3    Andersen, T.T.4    Fenton, J.W.5    Malik, A.B.6
  • 67
    • 0028242968 scopus 로고
    • Expression of P-selectin on endothelial cells is upregulated by LPS and TNF-α in vivo
    • U. Gotsch U. Jäger M. Dominis D. Vestweber Expression of P-selectin on endothelial cells is upregulated by LPS and TNF-α in vivo Cell Adhesion Commun 1993 in press
    • (1993) Cell Adhesion Commun
    • Gotsch, U.1    Jäger, U.2    Dominis, M.3    Vestweber, D.4
  • 68
    • 0027381402 scopus 로고
    • Characterization of the promoter for the human P-selectin gene
    • J. Pan R.P. McEver Characterization of the promoter for the human P-selectin gene J. Biol. Chem 268 1993 22600 22608
    • (1993) J. Biol. Chem , vol.268 , pp. 22600-22608
    • Pan, J.1    McEver, R.P.2
  • 74
    • 0025786799 scopus 로고
    • Four molecular pathways of T cell adhesion to endothelial cells: Roles of LFA-1, VCAM-1, and ELAM-1 and changes in pathway hierarchy under different activation conditions
    • Y. Shimizu W. Newman T.V. Gopal K.J. Horgan N. Graber L.D. Beall S.G. van S. Shaw Four molecular pathways of T cell adhesion to endothelial cells: Roles of LFA-1, VCAM-1, and ELAM-1 and changes in pathway hierarchy under different activation conditions J. Cell Biol 113 1991 1203 1212
    • (1991) J. Cell Biol , vol.113 , pp. 1203-1212
    • Shimizu, Y.1    Newman, W.2    Gopal, T.V.3    Horgan, K.J.4    Graber, N.5    Beall, L.D.6    van, S.G.7    Shaw, S.8
  • 76
    • 0027233024 scopus 로고
    • Nickel chloride and cobalt chloride, two common contact sensitizers, directly induce expression of intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and endothelial leukocyte adhesion molecule (ELAM-1) by endothelial cells
    • M. Goebeler G. Meinardus-Hager J. Roth S. Goerdt C. Sorg Nickel chloride and cobalt chloride, two common contact sensitizers, directly induce expression of intercellular adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1), and endothelial leukocyte adhesion molecule (ELAM-1) by endothelial cells J. Invest. Dermatol 100 1993 759 765
    • (1993) J. Invest. Dermatol , vol.100 , pp. 759-765
    • Goebeler, M.1    Meinardus-Hager, G.2    Roth, J.3    Goerdt, S.4    Sorg, C.5
  • 77
    • 0027221555 scopus 로고
    • Transforming growth factor-beta inhibits E-selectin expression on human endothelial cells
    • J.R. Gamble Y. Khew-Goodall M.A. Vadas Transforming growth factor-beta inhibits E-selectin expression on human endothelial cells J. Immunol 150 1993 4494 4503
    • (1993) J. Immunol , vol.150 , pp. 4494-4503
    • Gamble, J.R.1    Khew-Goodall, Y.2    Vadas, M.A.3
  • 78
    • 0026059613 scopus 로고
    • Cellular activation of latent TGFβ requires binding to the cation independent mannose 6 phosphate/IGF type II receptor
    • P.A. Dennis D.B. Rifkin Cellular activation of latent TGFβ requires binding to the cation independent mannose 6 phosphate/IGF type II receptor Proc. Natl. Acad. Sci. USA 88 1991 580 587
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 580-587
    • Dennis, P.A.1    Rifkin, D.B.2
  • 79
    • 0027365599 scopus 로고
    • Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells
    • N. Marui M.K. Offermann R. Swerlick C. Kunsch C.A. Rosen M. Ahmad R.W. Alexander R.M. Medford Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells J. Clin. Invest 92 1993 1866 1874
    • (1993) J. Clin. Invest , vol.92 , pp. 1866-1874
    • Marui, N.1    Offermann, M.K.2    Swerlick, R.3    Kunsch, C.4    Rosen, C.A.5    Ahmad, M.6    Alexander, R.W.7    Medford, R.M.8
  • 81
    • 0026039789 scopus 로고
    • The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and non myeloid cells
    • Q. Zhou K.L. Moore D.F. Smith A. Varki R.P. McEver R.D. Cummings The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and non myeloid cells J. Cell Biol 115 1991 557 564
    • (1991) J. Cell Biol , vol.115 , pp. 557-564
    • Zhou, Q.1    Moore, K.L.2    Smith, D.F.3    Varki, A.4    McEver, R.P.5    Cummings, R.D.6
  • 83
    • 0027407945 scopus 로고
    • The HNK-1 reactive sulfoglucuronyl glycolipids are ligands for L-selectin and P-selectin but not E-selectin
    • L.K. Needham R.L. Schnaar The HNK-1 reactive sulfoglucuronyl glycolipids are ligands for L-selectin and P-selectin but not E-selectin Proc. Natl. Acad. Sci. USA 90 1993 1359 1363
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1359-1363
    • Needham, L.K.1    Schnaar, R.L.2
  • 84
  • 85
    • 0027655844 scopus 로고
    • L-selectin and its biological ligands
    • S. Rosen L-selectin and its biological ligands Histochemistry 100 1993 185 191
    • (1993) Histochemistry , vol.100 , pp. 185-191
    • Rosen, S.1
  • 86
    • 0027647924 scopus 로고
    • Cell surface lectins in the immune system
    • S. Rosen Cell surface lectins in the immune system Sem. Immunol 5 1993 237 247
    • (1993) Sem. Immunol , vol.5 , pp. 237-247
    • Rosen, S.1
  • 88
    • 0027185994 scopus 로고
    • L- and E-selectin can recognize the same naturally occurring ligands on high endothelial venules
    • R.E. Mebius S.R. Watson L- and E-selectin can recognize the same naturally occurring ligands on high endothelial venules J. Immunol 151 1993 3252 3260
    • (1993) J. Immunol , vol.151 , pp. 3252-3260
    • Mebius, R.E.1    Watson, S.R.2
  • 93
    • 0027207679 scopus 로고
    • MAdCAM-1 has homology to immunoglobulin and mucin-like adhesion receptors and to IgA-1
    • M.G. Briskin L.M. McEvoy E.C. Butcher MAdCAM-1 has homology to immunoglobulin and mucin-like adhesion receptors and to IgA-1 Nature 363 1993 461 464
    • (1993) Nature , vol.363 , pp. 461-464
    • Briskin, M.G.1    McEvoy, L.M.2    Butcher, E.C.3
  • 94
    • 0026656908 scopus 로고
    • Identification of a soluble form of a ligand for the lymphocyte homing receptor
    • M. Brustein G. Kraal R.E. Mebius S.R. Watson Identification of a soluble form of a ligand for the lymphocyte homing receptor J. Exp. Med 176 1992 1415 1419
    • (1992) J. Exp. Med , vol.176 , pp. 1415-1419
    • Brustein, M.1    Kraal, G.2    Mebius, R.E.3    Watson, S.R.4
  • 95
    • 0028197560 scopus 로고
    • Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
    • M. Lenter A. Levinovitz S. Isenmann D. Vestweber Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells J. Cell. Biol 125 1994 471 481
    • (1994) J. Cell. Biol , vol.125 , pp. 471-481
    • Lenter, M.1    Levinovitz, A.2    Isenmann, S.3    Vestweber, D.4
  • 96
    • 0027133074 scopus 로고
    • Expression of GlyCAM-1, an endothelial ligand for L-selectin, is affected by afferent lymphatic flow
    • R.E. Mebius D. Dowbenko A. Williams C. Fennie L.A. Lasky S.R. Watson Expression of GlyCAM-1, an endothelial ligand for L-selectin, is affected by afferent lymphatic flow J. Immunol 151 1993 6769 6776
    • (1993) J. Immunol , vol.151 , pp. 6769-6776
    • Mebius, R.E.1    Dowbenko, D.2    Williams, A.3    Fennie, C.4    Lasky, L.A.5    Watson, S.R.6
  • 99
    • 0027271974 scopus 로고
    • Reciprocal of CD34 and cell adhesion ELAM-1 on vascular endothelium in acute cutaneous graft-versus-host disease
    • J. Norton J.P. Sloane D. Delia M.F. Greaves Reciprocal of CD34 and cell adhesion ELAM-1 on vascular endothelium in acute cutaneous graft-versus-host disease J. Pathol 170 1993 173 177
    • (1993) J. Pathol , vol.170 , pp. 173-177
    • Norton, J.1    Sloane, J.P.2    Delia, D.3    Greaves, M.F.4
  • 100
  • 101
    • 0024543127 scopus 로고
    • The mucosal vascular addressin is a tissue-specific endothelial cell adhesion molecule for circulating lymphocytes
    • M. Nakache E.L. Berg P.R. Streeter E.C. Butcher The mucosal vascular addressin is a tissue-specific endothelial cell adhesion molecule for circulating lymphocytes Nature 337 1989 179 181
    • (1989) Nature , vol.337 , pp. 179-181
    • Nakache, M.1    Berg, E.L.2    Streeter, P.R.3    Butcher, E.C.4
  • 106
    • 0025939215 scopus 로고
    • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140
    • L.J. Picker R.A. Warnock A.R. Burns C.M. Doerschuk E.L. Berg E.C. Butcher The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140 Cell 66 1991 921 933
    • (1991) Cell , vol.66 , pp. 921-933
    • Picker, L.J.1    Warnock, R.A.2    Burns, A.R.3    Doerschuk, C.M.4    Berg, E.L.5    Butcher, E.C.6
  • 107
    • 0025912259 scopus 로고
    • Antibodies against human neutrophil LECAM-1 (LAM-1/Leu-8/DREG-56 antigen) and endothelial cell ELAM-1 inhibit a common CD18-independent adhesion pathway, in vitro
    • T.K. Kishimoto R.A. Warnock M.A. Jutila E.C. Butcher C. Lane D.C. Anderson C.W. Smith Antibodies against human neutrophil LECAM-1 (LAM-1/Leu-8/DREG-56 antigen) and endothelial cell ELAM-1 inhibit a common CD18-independent adhesion pathway, in vitro Blood 78 1991 805 811
    • (1991) Blood , vol.78 , pp. 805-811
    • Kishimoto, T.K.1    Warnock, R.A.2    Jutila, M.A.3    Butcher, E.C.4    Lane, C.5    Anderson, D.C.6    Smith, C.W.7
  • 108
    • 0025751637 scopus 로고
    • The cutaneous lymphocyte antigen is a skin lymphocyte homing receptor for the vascular lectin endothelial cell-leukocyte adhesion molecule 1
    • E.L. Berg T. Yoshino L.S. Rott M.K. Robinson R.A. Warnock T.K. Kishimoto L.J. Picker E.C. Butcher The cutaneous lymphocyte antigen is a skin lymphocyte homing receptor for the vascular lectin endothelial cell-leukocyte adhesion molecule 1 J. Exp. Med 174 1991 1461 1466
    • (1991) J. Exp. Med , vol.174 , pp. 1461-1466
    • Berg, E.L.1    Yoshino, T.2    Rott, L.S.3    Robinson, M.K.4    Warnock, R.A.5    Kishimoto, T.K.6    Picker, L.J.7    Butcher, E.C.8
  • 109
    • 0027211784 scopus 로고
    • Control of lymphocyte recirculation in man. II. Differential regulation of the cutaneous lymphocyte-associated antigen (CLA), a tissue-selective homing receptor for skin-homing T cells
    • L.J. Picker J.R. Treer B. Ferguson-Darnell P.A. Collins P.R. Bergstresser L.W.M.M. Terstappen Control of lymphocyte recirculation in man. II. Differential regulation of the cutaneous lymphocyte-associated antigen (CLA), a tissue-selective homing receptor for skin-homing T cells J. Immunol 150 1993 1122 1136
    • (1993) J. Immunol , vol.150 , pp. 1122-1136
    • Picker, L.J.1    Treer, J.R.2    Ferguson-Darnell, B.3    Collins, P.A.4    Bergstresser, P.R.5    Terstappen, L.W.M.M.6
  • 110
    • 0025290056 scopus 로고
    • A unique phenotype of skin-associated lymphocytes in humans. Preferential expression of the HECA-452 epitope by benign and malignant T cells at cutaneous sites
    • L.J. Picker S.A. Michie L.S. Rott E.C. Butcher A unique phenotype of skin-associated lymphocytes in humans. Preferential expression of the HECA-452 epitope by benign and malignant T cells at cutaneous sites Am. J. Pathol 136 1990 1053 1068
    • (1990) Am. J. Pathol , vol.136 , pp. 1053-1068
    • Picker, L.J.1    Michie, S.A.2    Rott, L.S.3    Butcher, E.C.4
  • 111
    • 0027449670 scopus 로고
    • Differentiation-dependent expression of sialyl stage-specific embryonic antigen-1 and I-antigens on human lymphoid cells and its implications for carbohydrate-mediated adhesion to vascular endothelium
    • K. Ohmori A. Takada T. Yoneda Y. Buma K. Hirashima K. Tsyuoka A. Hasegawa R. Kannagi Differentiation-dependent expression of sialyl stage-specific embryonic antigen-1 and I-antigens on human lymphoid cells and its implications for carbohydrate-mediated adhesion to vascular endothelium Blood 81 1993 101 111
    • (1993) Blood , vol.81 , pp. 101-111
    • Ohmori, K.1    Takada, A.2    Yoneda, T.3    Buma, Y.4    Hirashima, K.5    Tsyuoka, K.6    Hasegawa, A.7    Kannagi, R.8
  • 113
    • 0027323990 scopus 로고
    • Bovine γ/δ T cells bind E-selecting via a novel glycoprotein receptor: Characterization of a lymphocyte/E-selectin interaction in an animal model
    • B. Walchek G. Watts M.A. Jutila Bovine γ / δ T cells bind E-selecting via a novel glycoprotein receptor: Characterization of a lymphocyte/E-selectin interaction in an animal model J. Exp. Med 178 1993 853 863
    • (1993) J. Exp. Med , vol.178 , pp. 853-863
    • Walchek, B.1    Watts, G.2    Jutila, M.A.3
  • 114
    • 0027483361 scopus 로고
    • Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells
    • A. Levinovitz J. Muhlhoff S. Isenmann D. Vestweber Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells J. Cell Biol 121 1993 449 459
    • (1993) J. Cell Biol , vol.121 , pp. 449-459
    • Levinovitz, A.1    Muhlhoff, J.2    Isenmann, S.3    Vestweber, D.4
  • 115
    • 0026770377 scopus 로고
    • Integrins, versatility, modulation, and signaling in cell adhesion
    • R. Hynes Integrins, versatility, modulation, and signaling in cell adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.1
  • 116
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • S.M. Albelda C.A. Buck Integrins and other cell adhesion molecules FASEB J 4 1990 2868 2880
    • (1990) FASEB J , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 118
    • 0028281362 scopus 로고
    • Integrin LFA-1 a subunit contains an ICAM-1 binding sites in domains V and VI
    • P. Stanley P.A. Bates J. Harvey R.I. Bennett N. Hogg Integrin LFA-1 a subunit contains an ICAM-1 binding sites in domains V and VI EMBO J 13 1994 1790 1798
    • (1994) EMBO J , vol.13 , pp. 1790-1798
    • Stanley, P.1    Bates, P.A.2    Harvey, J.3    Bennett, R.I.4    Hogg, N.5
  • 119
    • 0024571518 scopus 로고
    • Primary structure of the leukocyte function-associated molecule-α subunit: An integrin with an embedded domain defining a protein superfamily
    • R.S. Larson A.L. Corbi L. Berman T. Springer Primary structure of the leukocyte function-associated molecule-α subunit: An integrin with an embedded domain defining a protein superfamily J. Cell. Biol 108 1989 703 712
    • (1989) J. Cell. Biol , vol.108 , pp. 703-712
    • Larson, R.S.1    Corbi, A.L.2    Berman, L.3    Springer, T.4
  • 120
    • 0027496638 scopus 로고
    • Mutation of putative divalent cation sites in the α4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin
    • A. Masumoto M.E. Hemler Mutation of putative divalent cation sites in the α 4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin J. Cell Biol 123 1993 245 253
    • (1993) J. Cell Biol , vol.123 , pp. 245-253
    • Masumoto, A.1    Hemler, M.E.2
  • 122
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • I. Dransfield C. Cabanas A. Craig N. Hogg Divalent cation regulation of the function of the leukocyte integrin LFA-1 J. Cell Biol 116 1992 219 226
    • (1992) J. Cell Biol , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 123
    • 0025009813 scopus 로고
    • Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa
    • D. Kirchhofer J. Gailit E. Ruoslahti J. Grzesiak M.D. Pierschbacker Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa J. Biol. Chem 265 1990 18525 18530
    • (1990) J. Biol. Chem , vol.265 , pp. 18525-18530
    • Kirchhofer, D.1    Gailit, J.2    Ruoslahti, E.3    Grzesiak, J.4    Pierschbacker, M.D.5
  • 124
    • 0028180208 scopus 로고
    • The integrin chains β1 and α6 associate with the chaperone calnexin prior to integrin assembly
    • M. Lenter V. Vestweber The integrin chains β1 and α6 associate with the chaperone calnexin prior to integrin assembly J. Biol. Chem 269 1994 12263 12268
    • (1994) J. Biol. Chem , vol.269 , pp. 12263-12268
    • Lenter, M.1    Vestweber, V.2
  • 125
    • 0025807704 scopus 로고
    • TNFα and IFNγ modulate expression of the vitronectin receptor (integrin β3) in human endothelial cells
    • P. Defilippi G. Truffa G. Stefanuto F. Altruda L. Silengo G. Tarone TNFα and IFN γ modulate expression of the vitronectin receptor (integrin β3) in human endothelial cells J. Biol. Chem 266 1991 7638 7645
    • (1991) J. Biol. Chem , vol.266 , pp. 7638-7645
    • Defilippi, P.1    Truffa, G.2    Stefanuto, G.3    Altruda, F.4    Silengo, L.5    Tarone, G.6
  • 126
    • 0026611378 scopus 로고
    • α6/β1 integrin (laminin receptor) is down regulated by TNFα and IL-1β in human endothelial cells
    • P. Defilippi L. Silengo G. Tarone α6/β1 integrin (laminin receptor) is down regulated by TNFα and IL-1β in human endothelial cells J. Biol. Chem 267 1992 18303 18307
    • (1992) J. Biol. Chem , vol.267 , pp. 18303-18307
    • Defilippi, P.1    Silengo, L.2    Tarone, G.3
  • 127
    • 0027421094 scopus 로고
    • A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1
    • M. Lenter H. Uhlig A. Hamann P. Jenö B.A. Imhof D. Vestweber A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1 Proc. Natl. Acad. Sci. USA 90 1993 51 55
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 51-55
    • Lenter, M.1    Uhlig, H.2    Hamann, A.3    Jenö, P.4    Imhof, B.A.5    Vestweber, D.6
  • 128
    • 0027431097 scopus 로고
    • Post-receptor occupany events in leukocytes during beta 1 integrin-ligand interactions
    • P. Sanchez-Mateos A.G. Arroyo M.A. Balboa F. Sanchez-Madrid Post-receptor occupany events in leukocytes during beta 1 integrin-ligand interactions Eur. J. Immunol 23 1993 2642 2648
    • (1993) Eur. J. Immunol , vol.23 , pp. 2642-2648
    • Sanchez-Mateos, P.1    Arroyo, A.G.2    Balboa, M.A.3    Sanchez-Madrid, F.4
  • 129
    • 0026512171 scopus 로고
    • A monoclonal antibody to beta 1 integrin (CD29) stimulated VLA-dependent adherence of leukocytes to human unbilical vein endothelial cells and matrix components
    • N.L. Kovach T.M. Carlos E. Yee J.M. Harlan A monoclonal antibody to beta 1 integrin (CD29) stimulated VLA-dependent adherence of leukocytes to human unbilical vein endothelial cells and matrix components J. Cell Biol 116 1992 499 509
    • (1992) J. Cell Biol , vol.116 , pp. 499-509
    • Kovach, N.L.1    Carlos, T.M.2    Yee, E.3    Harlan, J.M.4
  • 130
    • 0027679403 scopus 로고
    • Integrin cytoplasmic domains: mediators of cytoskeletal linkages extra- and intracellular initiated transmembrane signaling
    • S.K. Sastry A.F. Horwitz Integrin cytoplasmic domains: mediators of cytoskeletal linkages extra- and intracellular initiated transmembrane signaling Curr. Opin. Cell. Biol 5 1993 819 831
    • (1993) Curr. Opin. Cell. Biol , vol.5 , pp. 819-831
    • Sastry, S.K.1    Horwitz, A.F.2
  • 133
    • 0025806144 scopus 로고
    • Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit
    • M.L. Hibbs H. Xu S.A. Stacker T.A. Springer Regulation of adhesion of ICAM-1 by the cytoplasmic domain of LFA-1 integrin beta subunit Science 251 1991 1611 1613
    • (1991) Science , vol.251 , pp. 1611-1613
    • Hibbs, M.L.1    Xu, H.2    Stacker, S.A.3    Springer, T.A.4
  • 134
    • 0025990521 scopus 로고
    • The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: Sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site
    • M. Hibbs S. Jakes S.A. Stacker R.W. Wallace T.A. Springer The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: Sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site J. Exp. Med 174 1991 1227 1238
    • (1991) J. Exp. Med , vol.174 , pp. 1227-1238
    • Hibbs, M.1    Jakes, S.2    Stacker, S.A.3    Wallace, R.W.4    Springer, T.A.5
  • 136
    • 0027332373 scopus 로고
    • Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of α subunit
    • L.M. Shaw A.M. Mercurio Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of α subunit J. Cell Biol 123 1993 1017 1025
    • (1993) J. Cell Biol , vol.123 , pp. 1017-1025
    • Shaw, L.M.1    Mercurio, A.M.2
  • 137
    • 0027258613 scopus 로고
    • Inside-out integrin signaling in macrophages
    • L.M. Shaw M.M. Lotz A.M. Mercurio Inside-out integrin signaling in macrophages J. Biol. Chem 268 1993 11401 11408
    • (1993) J. Biol. Chem , vol.268 , pp. 11401-11408
    • Shaw, L.M.1    Lotz, M.M.2    Mercurio, A.M.3
  • 139
    • 0027513263 scopus 로고
    • Cell adhesion in the immune system
    • C.R. Mackay B.A. Imhof Cell adhesion in the immune system Immunol. Today 14 1993 99 102
    • (1993) Immunol. Today , vol.14 , pp. 99-102
    • Mackay, C.R.1    Imhof, B.A.2
  • 141
    • 0027431090 scopus 로고
    • Murine platelet endothelial cell adhesion molecule (PECAM-1)/CD31 modulates β2 integrins on lymphokine-activated killer cells
    • L. Piali S.M. Albelda H.S. Baldwin P. Hammel R.H. Gisler B.A. Imhof Murine platelet endothelial cell adhesion molecule (PECAM-1)/CD31 modulates β2 integrins on lymphokine-activated killer cells Eur. J. Immunol 23 1993 2464 2471
    • (1993) Eur. J. Immunol , vol.23 , pp. 2464-2471
    • Piali, L.1    Albelda, S.M.2    Baldwin, H.S.3    Hammel, P.4    Gisler, R.H.5    Imhof, B.A.6
  • 142
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokines-CXC and CC chemokines
    • M. Baggiolini B. Dewald B. Moser Interleukin-8 and related chemotactic cytokines-CXC and CC chemokines Adv. Immunol 55 1994 97 179
    • (1994) Adv. Immunol , vol.55 , pp. 97-179
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 143
    • 0002640866 scopus 로고
    • Proinflammatory cytokines and immunity
    • S.K. Durum J.J. Oppenheim Proinflammatory cytokines and immunity W.E. Paul Fundamental Immunology 3rd ed 1993 Raven press New York 801 835
    • (1993) , pp. 801-835
    • Durum, S.K.1    Oppenheim, J.J.2
  • 144
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • C.H. Damsky Z. Werb Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information Curr. Opin. Cell. Biol 4 1992 772 781
    • (1992) Curr. Opin. Cell. Biol , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 145
    • 0026665562 scopus 로고
    • Signaling from LFA-1 contribute signal transduction through CD2 alternative pathway in T cell activation
    • A. Yamada T. Kaneyuki Y. Torimoto J.F. Daley C.M. Prado M.M. Yokyama Signaling from LFA-1 contribute signal transduction through CD2 alternative pathway in T cell activation Cell. Immunol 142 1992 145 158
    • (1992) Cell. Immunol , vol.142 , pp. 145-158
    • Yamada, A.1    Kaneyuki, T.2    Torimoto, Y.3    Daley, J.F.4    Prado, C.M.5    Yokyama, M.M.6
  • 146
    • 0027212509 scopus 로고
    • Laminin regulates a tumor cell chemotaxis receptor through the laminin-binding integrin subunit alpha 6
    • C.H. Blood B.R. Zetter Laminin regulates a tumor cell chemotaxis receptor through the laminin-binding integrin subunit alpha 6 Cancer Res 53 1993 2661 2666
    • (1993) Cancer Res , vol.53 , pp. 2661-2666
    • Blood, C.H.1    Zetter, B.R.2
  • 148
    • 0024358179 scopus 로고
    • Heterogenous distribution and transmembrane signaling properties of lymphocyte function-associated antigen (LFA-1) in human lymphocyte subsets
    • R. Pardi J.R. Bender C. Dettori E. Giannazza E.G. Engelman Heterogenous distribution and transmembrane signaling properties of lymphocyte function-associated antigen (LFA-1) in human lymphocyte subsets J. Immunol 143 1989 3157 3166
    • (1989) J. Immunol , vol.143 , pp. 3157-3166
    • Pardi, R.1    Bender, J.R.2    Dettori, C.3    Giannazza, E.4    Engelman, E.G.5
  • 149
    • 0026535397 scopus 로고
    • Ligation of VLA-4 on T cell stimulates tyrosine phosphorylation of a 105-kD protein
    • Y. Nojima D.M. Rothstein K. Sugita S.F. Schlossman C. Morimoto Ligation of VLA-4 on T cell stimulates tyrosine phosphorylation of a 105-kD protein J. Exp. Med 175 1992 1045 1053
    • (1992) J. Exp. Med , vol.175 , pp. 1045-1053
    • Nojima, Y.1    Rothstein, D.M.2    Sugita, K.3    Schlossman, S.F.4    Morimoto, C.5
  • 150
    • 0027291705 scopus 로고
    • Focal adhesion kinase: an integrin-linked protein tyrosine kinase
    • M.D. Schaller J.T. Parsons Focal adhesion kinase: an integrin-linked protein tyrosine kinase Trends Cell. Biol 3 1993 258 262
    • (1993) Trends Cell. Biol , vol.3 , pp. 258-262
    • Schaller, M.D.1    Parsons, J.T.2
  • 151
    • 0026476697 scopus 로고
    • Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • I. Zachary E. Rozengurt Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes Cell 71 1992 891 894
    • (1992) Cell , vol.71 , pp. 891-894
    • Zachary, I.1    Rozengurt, E.2
  • 152
    • 0001909033 scopus 로고
    • Primary immunodeficiency diseases
    • R.H. Buckley Primary immunodeficiency diseases W.E. Paul 3rd ed. Fundamental Immunology 1993 Raven Press New York 1353 1374
    • (1993) , pp. 1353-1374
    • Buckley, R.H.1
  • 153
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • T. Springer Adhesion receptors of the immune system Nature 346 1990 425 434
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.1
  • 155
    • 0024469059 scopus 로고
    • Peyer's patch-specific lymphocyte homing receptors consist of a VLA-4-like alpha chain associated with either of two integrin beta chains, one of which is novel
    • B. Holzmann I.L. Weissman Peyer's patch-specific lymphocyte homing receptors consist of a VLA-4-like alpha chain associated with either of two integrin beta chains, one of which is novel EMBO J 8 1989 1735 1741
    • (1989) EMBO J , vol.8 , pp. 1735-1741
    • Holzmann, B.1    Weissman, I.L.2
  • 157
    • 0027373310 scopus 로고
    • Expression of a protective intestinal immune response can be inhibited at three distinct sites by treatment with anti-alpha 4 integrin
    • R.G. Bell T. Issekutz Expression of a protective intestinal immune response can be inhibited at three distinct sites by treatment with anti-alpha 4 integrin J. Immunol 151 1993 4790 4802
    • (1993) J. Immunol , vol.151 , pp. 4790-4802
    • Bell, R.G.1    Issekutz, T.2
  • 158
    • 0027436423 scopus 로고
    • VLA-4 integrin mediates lymphocyte migration on the inducible endothelial cell ligand VCAM-1 and the extracellular matrix ligand fibronectin
    • P.Y. Chan A. Aruffo VLA-4 integrin mediates lymphocyte migration on the inducible endothelial cell ligand VCAM-1 and the extracellular matrix ligand fibronectin J. Biol. Chem 268 1993 24655 24664
    • (1993) J. Biol. Chem , vol.268 , pp. 24655-24664
    • Chan, P.Y.1    Aruffo, A.2
  • 159
    • 0027189768 scopus 로고
    • Lymphocyte migration across high endothelium is associated with increases in α4β1 integrin (VLA-4) affinity
    • H. Hourihan T.D. Allen A. Ager Lymphocyte migration across high endothelium is associated with increases in α4β1 integrin (VLA-4) affinity J. Cell. Sci 104 1993 1049 1059
    • (1993) J. Cell. Sci , vol.104 , pp. 1049-1059
    • Hourihan, H.1    Allen, T.D.2    Ager, A.3
  • 160
    • 0025871814 scopus 로고
    • EA-1, a novel adhesion molecule involved in the homing of progenitor T lymphocytes to the thymus
    • B.A. Imhof P. Ruiz B. Hesse R. Palacios D. Dunon EA-1, a novel adhesion molecule involved in the homing of progenitor T lymphocytes to the thymus J. Cell Biol 114 1991 1069 1078
    • (1991) J. Cell Biol , vol.114 , pp. 1069-1078
    • Imhof, B.A.1    Ruiz, P.2    Hesse, B.3    Palacios, R.4    Dunon, D.5
  • 161
    • 0027599001 scopus 로고
    • Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for alpha 6 integrins
    • P. Ruiz D. Dunon A. Sonnenberg B.A. Imhof Suppression of mouse melanoma metastasis by EA-1, a monoclonal antibody specific for alpha 6 integrins Cell Adhesion Commun 1 1993 67 81
    • (1993) Cell Adhesion Commun , vol.1 , pp. 67-81
    • Ruiz, P.1    Dunon, D.2    Sonnenberg, A.3    Imhof, B.A.4
  • 162
    • 0027396168 scopus 로고
    • Mechanisms of thymus homing
    • D. Dunon B.A. Imhof Mechanisms of thymus homing Blood 81 1993 1 8
    • (1993) Blood , vol.81 , pp. 1-8
    • Dunon, D.1    Imhof, B.A.2
  • 163
    • 0028205487 scopus 로고
    • Alpha 6 integrin distribution in human embryonic and adult tissues
    • H.J. Terpe H. Stark P. Ruiz B.A. Imhof Alpha 6 integrin distribution in human embryonic and adult tissues Histochemistry 101 1994 41 49
    • (1994) Histochemistry , vol.101 , pp. 41-49
    • Terpe, H.J.1    Stark, H.2    Ruiz, P.3    Imhof, B.A.4
  • 164
    • 0024968166 scopus 로고
    • Identification of a murine Peyer's patch-specific lymphocyte homing receptor as an integrin molecule with an alpha chain homologous to human VLA-4 alpha
    • B. Holzmann B.W. Mclntyre I.L. Weissman Identification of a murine Peyer's patch-specific lymphocyte homing receptor as an integrin molecule with an alpha chain homologous to human VLA-4 alpha Cell 56 1989 37 46
    • (1989) Cell , vol.56 , pp. 37-46
    • Holzmann, B.1    Mclntyre, B.W.2    Weissman, I.L.3
  • 165
    • 0026655693 scopus 로고
    • Cloning and expression of mouse integrin βp (β7): A functional role in Peyer's patch-specific lymphocyte homing
    • M.C. Hu D.T. Crowe I.L. Weissman B. Holzmann Cloning and expression of mouse integrin βp (β7): A functional role in Peyer's patch-specific lymphocyte homing Proc. Natl. Acad. Sci. USA 89 1992 8254 8258
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8254-8258
    • Hu, M.C.1    Crowe, D.T.2    Weissman, I.L.3    Holzmann, B.4
  • 166
    • 0026348317 scopus 로고
    • Cloning and expression of cDNAs for the alpha subunit of the murine lymphocyte-Peyer's patch adhesion molecule
    • H. Neuhaus M.C. Hu M.E. Hemler Y. Takada B. Holzmann I.L. Weissman Cloning and expression of cDNAs for the alpha subunit of the murine lymphocyte-Peyer's patch adhesion molecule J. Cell Biol 115 1991 1149 1158
    • (1991) J. Cell Biol , vol.115 , pp. 1149-1158
    • Neuhaus, H.1    Hu, M.C.2    Hemler, M.E.3    Takada, Y.4    Holzmann, B.5    Weissman, I.L.6
  • 168
    • 0026573191 scopus 로고
    • The human intrepi-thelial lymphocyte marker HML-1 is an integrin consisting of a β7 subunit associated with a distinctive α chain
    • N. Cerf-Bensussan B. Begue J. Gagnon T. Meo The human intrepi-thelial lymphocyte marker HML-1 is an integrin consisting of a β7 subunit associated with a distinctive α chain Eur. J. Immunol 22 1992 273 278
    • (1992) Eur. J. Immunol , vol.22 , pp. 273-278
    • Cerf-Bensussan, N.1    Begue, B.2    Gagnon, J.3    Meo, T.4
  • 169
    • 0027303737 scopus 로고
    • The mucosal T cell integrin αM290β7 recognizes a ligand on mucosal epithelial cell lines
    • K. Roberts P.J. Kilshaw The mucosal T cell integrin αM290β7 recognizes a ligand on mucosal epithelial cell lines Eur. J. Immunol 23 1993 1630 1635
    • (1993) Eur. J. Immunol , vol.23 , pp. 1630-1635
    • Roberts, K.1    Kilshaw, P.J.2
  • 170
    • 0027324601 scopus 로고
    • Integrin αEβ7 mediates adhesion of T lymphocytes to epithelial cells
    • K.L. Cepek C.M. Parker G.L. Madara M.B. Brenner Integrin αEβ7 mediates adhesion of T lymphocytes to epithelial cells J. Immunol 150 1993 3459 3470
    • (1993) J. Immunol , vol.150 , pp. 3459-3470
    • Cepek, K.L.1    Parker, C.M.2    Madara, G.L.3    Brenner, M.B.4
  • 172
    • 0027071814 scopus 로고
    • The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGF alpha into soluble growth factor
    • M.W. Bosenberg A. Pandiella J. Massague The cytoplasmic carboxy-terminal amino acid specifies cleavage of membrane TGF alpha into soluble growth factor Cell 71 1992 1157 1165
    • (1992) Cell , vol.71 , pp. 1157-1165
    • Bosenberg, M.W.1    Pandiella, A.2    Massague, J.3
  • 174
    • 0023874285 scopus 로고
    • ICAM, an adhesion ligand of LFA-1 is homologous to the neural cell adhesion molecule NCAM
    • D. Simmons M.W. Makgoba B. Seed ICAM, an adhesion ligand of LFA-1 is homologous to the neural cell adhesion molecule NCAM Nature 331 1988 624 627
    • (1988) Nature , vol.331 , pp. 624-627
    • Simmons, D.1    Makgoba, M.W.2    Seed, B.3
  • 175
    • 0024592732 scopus 로고
    • Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1
    • D.E. Staunton M.L. Dustin T.A. Springer Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1 Nature 339 1989 61 64
    • (1989) Nature , vol.339 , pp. 61-64
    • Staunton, D.E.1    Dustin, M.L.2    Springer, T.A.3
  • 176
    • 0024385056 scopus 로고
    • Molecular cloning of murine intercellular adhesion molecule (ICAM-1)
    • K.J. Horley C. Carpenito B. Baker F. Takei Molecular cloning of murine intercellular adhesion molecule (ICAM-1) EMBO J 8 1989 2889 2896
    • (1989) EMBO J , vol.8 , pp. 2889-2896
    • Horley, K.J.1    Carpenito, C.2    Baker, B.3    Takei, F.4
  • 177
    • 0025274020 scopus 로고
    • PECAM-1 (CD31) cloning and regulation to adhesion molecules of the immunoglobulin gene superfamily
    • P.J. Newman M.C. Berndt J. Gorski G.C. White S. Lyman C. Paddock W.A. Muller PECAM-1 (CD31) cloning and regulation to adhesion molecules of the immunoglobulin gene superfamily Science 247 1990 1219 1222
    • (1990) Science , vol.247 , pp. 1219-1222
    • Newman, P.J.1    Berndt, M.C.2    Gorski, J.3    White, G.C.4    Lyman, S.5    Paddock, C.6    Muller, W.A.7
  • 178
    • 0024818401 scopus 로고
    • Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes
    • L. Osborn C. Hession R. Tizard C. Vassallo S. Luhowskyj R.G. Chi R. Lobb Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes Cell 59 1989 1203 1211
    • (1989) Cell , vol.59 , pp. 1203-1211
    • Osborn, L.1    Hession, C.2    Tizard, R.3    Vassallo, C.4    Luhowskyj, S.5    Chi, R.G.6    Lobb, R.7
  • 179
    • 0027502563 scopus 로고
    • Cloning and expression of intercellular adhesion molecule 3 reveals strong homology to other immunoglobulin family receptors for lymphocyte function-associated antigen 1
    • A.R. de Fougerolles L.B. Klickstein T. Springer Cloning and expression of intercellular adhesion molecule 3 reveals strong homology to other immunoglobulin family receptors for lymphocyte function-associated antigen 1 J. Exp. Med 177 1993 1187 1192
    • (1993) J. Exp. Med , vol.177 , pp. 1187-1192
    • de Fougerolles, A.R.1    Klickstein, L.B.2    Springer, T.3
  • 180
    • 0027512971 scopus 로고
    • Location of the domains of ICAM-1 by immunolabeling and single-molecule electron microscopy
    • T. Kirchhausen D.E. Staunton T.A. Springer Location of the domains of ICAM-1 by immunolabeling and single-molecule electron microscopy J. Leukocyte Biol 53 1993 342 346
    • (1993) J. Leukocyte Biol , vol.53 , pp. 342-346
    • Kirchhausen, T.1    Staunton, D.E.2    Springer, T.A.3
  • 181
    • 0023644247 scopus 로고
    • Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1)
    • S.D. Marlin T.A. Springer Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1) Cell 51 1987 813 819
    • (1987) Cell , vol.51 , pp. 813-819
    • Marlin, S.D.1    Springer, T.A.2
  • 182
    • 0024296564 scopus 로고
    • Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families
    • D.E. Staunton S.D. Marlin C. Stratowa M.L. Dustin T.A. Springer Primary structure of ICAM-1 demonstrates interaction between members of the immunoglobulin and integrin supergene families Cell 52 1988 925 933
    • (1988) Cell , vol.52 , pp. 925-933
    • Staunton, D.E.1    Marlin, S.D.2    Stratowa, C.3    Dustin, M.L.4    Springer, T.A.5
  • 184
    • 0025269047 scopus 로고
    • The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus [published erratum appears in Cell 1990 61(2), 1157]
    • D.E. Staunton M.L. Dustin H.P. Erickson T.A. Springer The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus [published erratum appears in Cell 1990 61 (2), 1157] Cell 61 1990 243 254
    • (1990) Cell , vol.61 , pp. 243-254
    • Staunton, D.E.1    Dustin, M.L.2    Erickson, H.P.3    Springer, T.A.4
  • 187
    • 0026542081 scopus 로고
    • The binding site in ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site
    • A.R. Berendt A. McDowall A.G. Craig P.A. Bates M.J.E. Sternberg K. Marsh C.I. Newbold N. Hogg The binding site in ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site Cell 68 1992 71 81
    • (1992) Cell , vol.68 , pp. 71-81
    • Berendt, A.R.1    McDowall, A.2    Craig, A.G.3    Bates, P.A.4    Sternberg, M.J.E.5    Marsh, K.6    Newbold, C.I.7    Hogg, N.8
  • 188
    • 0026580223 scopus 로고
    • Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus
    • C.F. Ockenhouse R. Begateri T.A. Springer D.E. Staunton Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus Cell 68 1992 63 69
    • (1992) Cell , vol.68 , pp. 63-69
    • Ockenhouse, C.F.1    Begateri, R.2    Springer, T.A.3    Staunton, D.E.4
  • 191
    • 0026794252 scopus 로고
    • The importance of cross-linking in the homotypic aggregation of lymphocyte induced by antileukosialin (CD43) antibodies
    • J.G. Cyster A.F. Williams The importance of cross-linking in the homotypic aggregation of lymphocyte induced by antileukosialin (CD43) antibodies Eur. J. Immunol 22 1992 2565 2572
    • (1992) Eur. J. Immunol , vol.22 , pp. 2565-2572
    • Cyster, J.G.1    Williams, A.F.2
  • 192
    • 0022574146 scopus 로고
    • Induction by IL 1 and interferon-gamma: Tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1)
    • M.L. Dustin R. Rothlein A.K. Bhan C.A. Dinarello T.A. Springer Induction by IL 1 and interferon-gamma: Tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1) J. Immunol 137 1986 245 254
    • (1986) J. Immunol , vol.137 , pp. 245-254
    • Dustin, M.L.1    Rothlein, R.2    Bhan, A.K.3    Dinarello, C.A.4    Springer, T.A.5
  • 193
    • 0023250759 scopus 로고
    • Deacylatedlipopolysachar-ide inhibits neutrophil adherence to endothelium induced by lipopolysaccharide in vitro
    • T.H. Pohlman R.S. Munford J.M. Harlan Deacylatedlipopolysachar-ide inhibits neutrophil adherence to endothelium induced by lipopolysaccharide in vitro J. Exp. Med 165 1987 1393 1402
    • (1987) J. Exp. Med , vol.165 , pp. 1393-1402
    • Pohlman, T.H.1    Munford, R.S.2    Harlan, J.M.3
  • 195
    • 0026546311 scopus 로고
    • Tumor necrosis factor mediates experimental pulmonary edema by ICAM-1 and CD18-dependent mechanisms
    • S.K. Lo J. Everitt J. Gu A.B. Malik Tumor necrosis factor mediates experimental pulmonary edema by ICAM-1 and CD18-dependent mechanisms J. Clin. Invest 89 1992 981 988
    • (1992) J. Clin. Invest , vol.89 , pp. 981-988
    • Lo, S.K.1    Everitt, J.2    Gu, J.3    Malik, A.B.4
  • 196
    • 0023807438 scopus 로고
    • Induction of cellular adhesion molecule-1 on primary and continuous cell lines by proinflammatory cytokines. Regulation by pharmcologic agents and neutralizing antibodies
    • R. Rohlein M. Czajkowski M.M. O'Neill S.D. Marlin E. Mainolki M.J. Merluzzi Induction of cellular adhesion molecule-1 on primary and continuous cell lines by proinflammatory cytokines. Regulation by pharmcologic agents and neutralizing antibodies J. Immunol 141 1988 1665 1669
    • (1988) J. Immunol , vol.141 , pp. 1665-1669
    • Rohlein, R.1    Czajkowski, M.2    O'Neill, M.M.3    Marlin, S.D.4    Mainolki, E.5    Merluzzi, M.J.6
  • 198
    • 0025860094 scopus 로고
    • Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1
    • A.R. de Fougerolles S.A. Stacker R. Schwarting T.A. Springer Characterization of ICAM-2 and evidence for a third counter-receptor for LFA-1 J. Exp. Med 174 1991 253 267
    • (1991) J. Exp. Med , vol.174 , pp. 253-267
    • de Fougerolles, A.R.1    Stacker, S.A.2    Schwarting, R.3    Springer, T.A.4
  • 199
    • 0027982997 scopus 로고
    • Characterization of the function of intercellular adhesion molecules (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses
    • A.R. de Fougerolles X. Quin T.A. Springer Characterization of the function of intercellular adhesion molecules (ICAM)-3 and comparison with ICAM-1 and ICAM-2 in immune responses J. Exp. Med 179 1994 619 629
    • (1994) J. Exp. Med , vol.179 , pp. 619-629
    • de Fougerolles, A.R.1    Quin, X.2    Springer, T.A.3
  • 200
    • 0026604790 scopus 로고
    • Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes
    • A.R. de Fougerolles T.A. Springer Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes J. Exp. Med 175 1992 185 190
    • (1992) J. Exp. Med , vol.175 , pp. 185-190
    • de Fougerolles, A.R.1    Springer, T.A.2
  • 202
    • 0025132002 scopus 로고
    • Association of intercellular adhesion molecule 1 with the multichain high-affinity interleu-kin 2 receptor
    • J. Burton C.K. Goldman P. Rao M. Moos T.A. Waldmann Association of intercellular adhesion molecule 1 with the multichain high-affinity interleu-kin 2 receptor Proc. Natl. Acad. Sci. USA 87 1990 7329 7333
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7329-7333
    • Burton, J.1    Goldman, C.K.2    Rao, P.3    Moos, M.4    Waldmann, T.A.5
  • 205
    • 0025161990 scopus 로고
    • VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site
    • M.J. Elices L. Osborn Y. Takada C. Crouse S. Luhowskyj M.E. Hemler R.R. Lobb VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/fibronectin binding site Cell 60 1990 577 584
    • (1990) Cell , vol.60 , pp. 577-584
    • Elices, M.J.1    Osborn, L.2    Takada, Y.3    Crouse, C.4    Luhowskyj, S.5    Hemler, M.E.6    Lobb, R.R.7
  • 206
    • 0026574125 scopus 로고
    • Role of integrin alpha 4 beta 7/alpha 4 beta P in lymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering
    • C. Ruegg A.A. Postigo E.E. Sikorski E.C. Butcher R. Pytela D.J. Erle Role of integrin alpha 4 beta 7/alpha 4 beta P in lymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering J. Cell Biol 117 1992 179 189
    • (1992) J. Cell Biol , vol.117 , pp. 179-189
    • Ruegg, C.1    Postigo, A.A.2    Sikorski, E.E.3    Butcher, E.C.4    Pytela, R.5    Erle, D.J.6
  • 207
    • 0026644782 scopus 로고
    • Adhesion to vascular cell adhesion molecule 1 and fibronecin: Comparison of α4β1 (VLA-4) and α4gb7 on the human B cell line JY
    • B.M.C. Chan M.J. Elices E. Murphy M.E. Hemler Adhesion to vascular cell adhesion molecule 1 and fibronecin: Comparison of α4β1 (VLA-4) and α4gb7 on the human B cell line JY J. Biol. Chem 267 1992 8366 8370
    • (1992) J. Biol. Chem , vol.267 , pp. 8366-8370
    • Chan, B.M.C.1    Elices, M.J.2    Murphy, E.3    Hemler, M.E.4
  • 208
    • 0026642672 scopus 로고
    • Activated endothelium binds lymphocytes through novel binding site in the alternatively spliced domain of vascular cell adhesion molecule-1
    • L. Osborn C. Vassalo C.D. Benjamin Activated endothelium binds lymphocytes through novel binding site in the alternatively spliced domain of vascular cell adhesion molecule-1 J. Exp. Med 176 1992 99 107
    • (1992) J. Exp. Med , vol.176 , pp. 99-107
    • Osborn, L.1    Vassalo, C.2    Benjamin, C.D.3
  • 209
    • 0026504051 scopus 로고
    • Lymphocyte adhesion through VLA-4: Evidence for a novel binding site in the alternatively spliced domain of VCAM-1 and an additional α4 integrin counter receptor on stimulated endothelium
    • R.H. Vonderheide T.A. Springer Lymphocyte adhesion through VLA-4: Evidence for a novel binding site in the alternatively spliced domain of VCAM-1 and an additional α4 integrin counter receptor on stimulated endothelium J. Exp. Med 175 1992 1433 1442
    • (1992) J. Exp. Med , vol.175 , pp. 1433-1442
    • Vonderheide, R.H.1    Springer, T.A.2
  • 210
    • 0027537638 scopus 로고
    • Cloning of an inflammation-specific phosphatidyl inositol-linked form of murine vascular cell adhesion molecule-1
    • P. Moy R. Lobb R. Tizard D. Olson C. Hession Cloning of an inflammation-specific phosphatidyl inositol-linked form of murine vascular cell adhesion molecule-1 J. Biol. Chem 268 1993 8835 8841
    • (1993) J. Biol. Chem , vol.268 , pp. 8835-8841
    • Moy, P.1    Lobb, R.2    Tizard, R.3    Olson, D.4    Hession, C.5
  • 211
    • 0028088954 scopus 로고
    • A novel soluble form of mouse VCAM-1 is generated from a glycolipid-anchored splicing variant
    • M. Hahne M. Lenter U. Jäger D. Vestweber A novel soluble form of mouse VCAM-1 is generated from a glycolipid-anchored splicing variant Eur. J. Immunol 24 1993 421 428
    • (1993) Eur. J. Immunol , vol.24 , pp. 421-428
    • Hahne, M.1    Lenter, M.2    Jäger, U.3    Vestweber, D.4
  • 213
    • 0027299404 scopus 로고
    • Cytokine induction of an alternatively spliced murine vascular cell adhesion molecule (VCAM) mRNA encoding a glycosylphosphatidylinositol-anchored VCAM protein
    • R.W. Terry L. Kwee J.F. Levine M.A. Labow Cytokine induction of an alternatively spliced murine vascular cell adhesion molecule (VCAM) mRNA encoding a glycosylphosphatidylinositol-anchored VCAM protein Proc. Natl. Acad. Sci. USA 90 1993 5919 5923
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5919-5923
    • Terry, R.W.1    Kwee, L.2    Levine, J.F.3    Labow, M.A.4
  • 214
    • 0026787155 scopus 로고
    • Soluble forms of E-selectin, ICAM-1 and VCAM-1 are present in the supernatants of cytokine activated cultured endothelial cells
    • R. Pigott L.P. Dillon I.H. Hemingway A.J.H. Gearing Soluble forms of E-selectin, ICAM-1 and VCAM-1 are present in the supernatants of cytokine activated cultured endothelial cells Biochem. Biophys. Res. Commun 187 1992 584 589
    • (1992) Biochem. Biophys. Res. Commun , vol.187 , pp. 584-589
    • Pigott, R.1    Dillon, L.P.2    Hemingway, I.H.3    Gearing, A.J.H.4
  • 215
    • 0027311976 scopus 로고
    • Detection of a circulating form of vascular cell adhesion molecule-1: Raised levels in rheumatoid arthritis and systemic lupus erythematosus
    • R.L. Wellicome P. Kapahi J.C. Mason Y. Lebranchu H. Yarwood D.O. Haskard Detection of a circulating form of vascular cell adhesion molecule-1: Raised levels in rheumatoid arthritis and systemic lupus erythematosus Clin. Exp. Immunol 92 1993 412 418
    • (1993) Clin. Exp. Immunol , vol.92 , pp. 412-418
    • Wellicome, R.L.1    Kapahi, P.2    Mason, J.C.3    Lebranchu, Y.4    Yarwood, H.5    Haskard, D.O.6
  • 216
    • 0025152076 scopus 로고
    • IL-4 acts synergistically with IL-1β to promote lymphocyte adhesion to microvascular endothelium by induction of vascular cell adhesion molecule-1
    • B. Masinovsky D. Urdal W.M. Gallatin IL-4 acts synergistically with IL-1β to promote lymphocyte adhesion to microvascular endothelium by induction of vascular cell adhesion molecule-1 J. Immunol 145 1990 2886 2895
    • (1990) J. Immunol , vol.145 , pp. 2886-2895
    • Masinovsky, B.1    Urdal, D.2    Gallatin, W.M.3
  • 217
    • 0026693954 scopus 로고
    • Regulation of vascular cell adhesion molecule 1 on human dermal microvascular endothelial cells
    • R.A. Swerlick K.H. Lee L.J. Li N.T. Sepp S.W. Caughman T.J. Lawley Regulation of vascular cell adhesion molecule 1 on human dermal microvascular endothelial cells J. Immunol 149 1992 698 705
    • (1992) J. Immunol , vol.149 , pp. 698-705
    • Swerlick, R.A.1    Lee, K.H.2    Li, L.J.3    Sepp, N.T.4    Caughman, S.W.5    Lawley, T.J.6
  • 218
    • 0026490278 scopus 로고
    • Functional analysis of the human vascular cell adhesion molecule 1 promoter
    • A.S. Neish A.J. Williams H.J. Palmer M.Z. Whitley T. Collins Functional analysis of the human vascular cell adhesion molecule 1 promoter J. Exp. Med 176 1992 1583 1593
    • (1992) J. Exp. Med , vol.176 , pp. 1583-1593
    • Neish, A.S.1    Williams, A.J.2    Palmer, H.J.3    Whitley, M.Z.4    Collins, T.5
  • 219
    • 0025861825 scopus 로고
    • A VCAM-like adhesion molecule on murine bone marrow stromal cells mediates binding of lymphocyte precursors in culture
    • K. Miyake K. Median K. Ishihara M. Kimoto R. Auerback P.W. Kincade A VCAM-like adhesion molecule on murine bone marrow stromal cells mediates binding of lymphocyte precursors in culture J. Cell Biol 114 1991 557 565
    • (1991) J. Cell Biol , vol.114 , pp. 557-565
    • Miyake, K.1    Median, K.2    Ishihara, K.3    Kimoto, M.4    Auerback, R.5    Kincade, P.W.6
  • 221
    • 0025940034 scopus 로고
    • Vascular cell adhesion molecule-1 and the integrin VLA-4 mediate adhesion of human B cell precursors to cultured bone marrow adherent cells
    • D.H. Ryan B.L. Nuccie C.N. Abboud J.M. Winslow Vascular cell adhesion molecule-1 and the integrin VLA-4 mediate adhesion of human B cell precursors to cultured bone marrow adherent cells J. Clin. Invest 88 1991 995 1004
    • (1991) J. Clin. Invest , vol.88 , pp. 995-1004
    • Ryan, D.H.1    Nuccie, B.L.2    Abboud, C.N.3    Winslow, J.M.4
  • 222
  • 223
    • 0025215305 scopus 로고
    • EndoCAM: A novel endothelial cell—cell adhesion molecule
    • S.M. Albelda P.D. Oliver L.H. Romer C.A. Buck EndoCAM: A novel endothelial cell—cell adhesion molecule J. Cell Biol 110 1990 1227 1237
    • (1990) J. Cell Biol , vol.110 , pp. 1227-1237
    • Albelda, S.M.1    Oliver, P.D.2    Romer, L.H.3    Buck, C.A.4
  • 224
    • 0027157686 scopus 로고
    • Molecular cloning and adhesive properties of murine platelet/endothelial cell adhesion molecule-1 (PECAM-1)
    • Y. Xie W.A. Muller Molecular cloning and adhesive properties of murine platelet/endothelial cell adhesion molecule-1 (PECAM-1) Proc. Natl. Acad. Sci. USA 90 1993 5569 5573
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5569-5573
    • Xie, Y.1    Muller, W.A.2
  • 225
    • 0027248750 scopus 로고
    • PECAM-1 is required for transendothelial migration of leukocytes
    • W.A. Muller S.A. Weigl X. Deng D.M. Phillips PECAM-1 is required for transendothelial migration of leukocytes J. Exp. Med 178 1993 449 460
    • (1993) J. Exp. Med , vol.178 , pp. 449-460
    • Muller, W.A.1    Weigl, S.A.2    Deng, X.3    Phillips, D.M.4
  • 226
    • 0026672879 scopus 로고
    • Platelet endothelial cell adhesion molecule, PECAM-1, modulates cell migration
    • L.A. Schimmenti H.C. Yan J.A. Madri S.M. Albelda Platelet endothelial cell adhesion molecule, PECAM-1, modulates cell migration J. Cell Physiol 153 1992 417 428
    • (1992) J. Cell Physiol , vol.153 , pp. 417-428
    • Schimmenti, L.A.1    Yan, H.C.2    Madri, J.A.3    Albelda, S.M.4
  • 231
    • 0026514985 scopus 로고
    • A heterophilic adhesion mechanism for platelet/endothelial cell adhesion molecule 1 (CD31)
    • W.A. Muller M.E. Berman P.J. Newman H.M. DeLisser S.M. Albelda A heterophilic adhesion mechanism for platelet/endothelial cell adhesion molecule 1 (CD31) J. Exp. Med 175 1992 1401 1404
    • (1992) J. Exp. Med , vol.175 , pp. 1401-1404
    • Muller, W.A.1    Berman, M.E.2    Newman, P.J.3    DeLisser, H.M.4    Albelda, S.M.5
  • 232
    • 0026049319 scopus 로고
    • Different epitopes of the CD31 antigen identified by monoclonal antibodies: Cell type-specific pattern of expressions
    • L.K. Ashman G.W. Aylett A.C. Cambareri S.R. Cole Different epitopes of the CD31 antigen identified by monoclonal antibodies: Cell type-specific pattern of expressions Tissue Antigens 38 1991 199 207
    • (1991) Tissue Antigens , vol.38 , pp. 199-207
    • Ashman, L.K.1    Aylett, G.W.2    Cambareri, A.C.3    Cole, S.R.4
  • 233
    • 0025873304 scopus 로고
    • Molecular and cellular properties of PECAM-1 (endoCAM/CD31): A novel vascular cell—cell adhesion molecule
    • S.M. Albelda W.A. Muller C.A. Buck J.J. Newman Molecular and cellular properties of PECAM-1 (endoCAM/CD31): A novel vascular cell—cell adhesion molecule J. Cell Biol 114 1991 1059 1068
    • (1991) J. Cell Biol , vol.114 , pp. 1059-1068
    • Albelda, S.M.1    Muller, W.A.2    Buck, C.A.3    Newman, J.J.4
  • 234
    • 0027953008 scopus 로고
    • Deletions in the cytoplasmic domain of platelet-endothelial cell adhesion molecule-1 (PECAM-1, CD31) result in changes in ligand binding properties
    • H.M. DeLisser J. Chilkotowsky H.C. Yan M.L. Daise C.A. Buck S.M. Albelda Deletions in the cytoplasmic domain of platelet-endothelial cell adhesion molecule-1 (PECAM-1, CD31) result in changes in ligand binding properties J. Cell Biol 124 1994 195 203
    • (1994) J. Cell Biol , vol.124 , pp. 195-203
    • DeLisser, H.M.1    Chilkotowsky, J.2    Yan, H.C.3    Daise, M.L.4    Buck, C.A.5    Albelda, S.M.6
  • 236
    • 0025139119 scopus 로고
    • Functional cooperation between the neural adhesion molecules LI and N-CAM is carbohydrate dependent
    • G. Kadmon A. Kowitz P. Altevogt M. Schachner Functional cooperation between the neural adhesion molecules LI and N-CAM is carbohydrate dependent J. Cell Biol 110 1990 209 218
    • (1990) J. Cell Biol , vol.110 , pp. 209-218
    • Kadmon, G.1    Kowitz, A.2    Altevogt, P.3    Schachner, M.4
  • 237
    • 0025173903 scopus 로고
    • The neural cell adhesion molecule N-CAM enhances Ll-dependent cell-cell interactions
    • G. Kadmon A. Kowitz P. Altevogt M. Schachner The neural cell adhesion molecule N-CAM enhances Ll-dependent cell-cell interactions J. Cell Biol 110 1990 193 208
    • (1990) J. Cell Biol , vol.110 , pp. 193-208
    • Kadmon, G.1    Kowitz, A.2    Altevogt, P.3    Schachner, M.4
  • 238
    • 0027361672 scopus 로고
    • LI adhesion molecule on mouse leukocytes: Regulation and involvement in endothelial cell binding
    • M. Hubbe A. Kowitz V. Schirrmacher M. Schachner P. Altevogt LI adhesion molecule on mouse leukocytes: Regulation and involvement in endothelial cell binding Eur. J. Immunol 23 1993 2927 2931
    • (1993) Eur. J. Immunol , vol.23 , pp. 2927-2931
    • Hubbe, M.1    Kowitz, A.2    Schirrmacher, V.3    Schachner, M.4    Altevogt, P.5
  • 239
    • 0027491845 scopus 로고
    • CD44 and its interaction with extracellular matrix
    • J. Lesley R. Hyman P.W. Kincade CD44 and its interaction with extracellular matrix Adv. Immunol 54 1993 271 335
    • (1993) Adv. Immunol , vol.54 , pp. 271-335
    • Lesley, J.1    Hyman, R.2    Kincade, P.W.3
  • 240
    • 0027141396 scopus 로고
    • CD44: A multitude of isoforms with diverse functions
    • U. Günthert CD44: A multitude of isoforms with diverse functions Curr. Topics Microbiol. Immunol 184 1993 47 63
    • (1993) Curr. Topics Microbiol. Immunol , vol.184 , pp. 47-63
    • Günthert, U.1
  • 241
    • 0026019628 scopus 로고
    • The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate-bearing cells
    • I. Stamenkovic A. Aruffo M. Amiot B. Seed The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate-bearing cells EMBO J 10 1991 343 348
    • (1991) EMBO J , vol.10 , pp. 343-348
    • Stamenkovic, I.1    Aruffo, A.2    Amiot, M.3    Seed, B.4
  • 242
    • 0027065573 scopus 로고
    • Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons
    • G.R. Screaton M.V. Bell D.G. Jackson F.B. Cornelis U. Gerth J.I. Bell Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons Proc. Natl. Acad. Sci. USA 89 1992 12160 12164
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12160-12164
    • Screaton, G.R.1    Bell, M.V.2    Jackson, D.G.3    Cornelis, F.B.4    Gerth, U.5    Bell, J.I.6
  • 243
    • 0027269982 scopus 로고
    • Identification of hyaluronic acid binding sites in the extracellular domain of CD44
    • R.J. Peach D. Hollenbaugh I. Stamenkovic A. Aruffo Identification of hyaluronic acid binding sites in the extracellular domain of CD44 J. Cell Biol 122 1993 257 264
    • (1993) J. Cell Biol , vol.122 , pp. 257-264
    • Peach, R.J.1    Hollenbaugh, D.2    Stamenkovic, I.3    Aruffo, A.4
  • 244
    • 0026557413 scopus 로고
    • Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin
    • S. Jalkanen M. Jalkanen Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin J. Cell Biol 116 1992 817 825
    • (1992) J. Cell Biol , vol.116 , pp. 817-825
    • Jalkanen, S.1    Jalkanen, M.2
  • 245
    • 0023923181 scopus 로고
    • Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells
    • W.G. Carter E.A. Wayner Characterization of the class III collagen receptor, a phosphorylated, transmembrane glycoprotein expressed in nucleated human cells J. Biol. Chem 263 1988 4193 4201
    • (1988) J. Biol. Chem , vol.263 , pp. 4193-4201
    • Carter, W.G.1    Wayner, E.A.2
  • 246
    • 0026633256 scopus 로고
    • Shedding of the CD44 adhesion molecule from leukocytes induced by anti-CD44 monoclonal antibody simulating the effect of a natural receptor ligand
    • V. Bazil V. Horejsi Shedding of the CD44 adhesion molecule from leukocytes induced by anti-CD44 monoclonal antibody simulating the effect of a natural receptor ligand J. Immunol 149 1992 747 753
    • (1992) J. Immunol , vol.149 , pp. 747-753
    • Bazil, V.1    Horejsi, V.2
  • 247
    • 85113046855 scopus 로고
    • Selective triggering of CD44 receptor function for hyaluronate and nonhyaluronate endothelial ligands
    • H. Uhlig S. Rebstock J. Lesley D. Jablonski-Westrich A. Hamann Selective triggering of CD44 receptor function for hyaluronate and nonhyaluronate endothelial ligands 1994 Submitted for publication
    • (1994)
    • Uhlig, H.1    Rebstock, S.2    Lesley, J.3    Jablonski-Westrich, D.4    Hamann, A.5
  • 248
    • 0027377499 scopus 로고
    • Regulation of human CD44H and CD44I isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies
    • H.X. Liao M.C. Levesque K. Patton B. Bergamo D. Jones M.A. Moody M.J. Telen B.F. Haynes Regulation of human CD44H and CD44I isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies J. Immunol 151 1993 6490 6499
    • (1993) J. Immunol , vol.151 , pp. 6490-6499
    • Liao, H.X.1    Levesque, M.C.2    Patton, K.3    Bergamo, B.4    Jones, D.5    Moody, M.A.6    Telen, M.J.7    Haynes, B.F.8
  • 249
    • 0028345088 scopus 로고
    • Inducible binding of human lymphocytes to hyaluronate via CD44 does not require cytoskeleton association but does require new protein synthesis
    • S. Murakami Y. Shimabukuro Y. Miki T. Saho E. Hino D. Kasai T. Nozaki Y. Kusumoto H. Okada Inducible binding of human lymphocytes to hyaluronate via CD44 does not require cytoskeleton association but does require new protein synthesis J. Immunol 152 1994 467 477
    • (1994) J. Immunol , vol.152 , pp. 467-477
    • Murakami, S.1    Shimabukuro, Y.2    Miki, Y.3    Saho, T.4    Hino, E.5    Kasai, D.6    Nozaki, T.7    Kusumoto, Y.8    Okada, H.9
  • 250
    • 0023574615 scopus 로고
    • Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85–95 kD glycoprotein antigen differentially inhibit lymphocyte binding to lymphnode, mucosal or synovial endothelial cells
    • S. Jalkanen R.F. Bargatze J. del los Toyos E.C. Butcher Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85–95 kD glycoprotein antigen differentially inhibit lymphocyte binding to lymphnode, mucosal or synovial endothelial cells J. Cell Biol 105 1987 983 990
    • (1987) J. Cell Biol , vol.105 , pp. 983-990
    • Jalkanen, S.1    Bargatze, R.F.2    del los Toyos, J.3    Butcher, E.C.4
  • 251
    • 0025641883 scopus 로고
    • The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins
    • M. Culty K. Miyake P.W. Kincade E. Sikorski E.C. Butcher C. Underhill The hyaluronate receptor is a member of the CD44 (H-CAM) family of cell surface glycoproteins J. Cell Biol 111 1990 2765 2774
    • (1990) J. Cell Biol , vol.111 , pp. 2765-2774
    • Culty, M.1    Miyake, K.2    Kincade, P.W.3    Sikorski, E.4    Butcher, E.C.5    Underhill, C.6
  • 252
    • 0028273202 scopus 로고
    • A novel ligand for CD44 is sulfated proteoglycan
    • N. Toyama-Sorimachi M. Miyasaka A novel ligand for CD44 is sulfated proteoglycan Int. Immunol 6 1994 655 660
    • (1994) Int. Immunol , vol.6 , pp. 655-660
    • Toyama-Sorimachi, N.1    Miyasaka, M.2
  • 253
    • 0027184738 scopus 로고
    • CD44 is necessary for optimal contact allergic responses but is not required for normal leukocyte extravasation
    • R.L. Camp A. Scheynius C. Johansson E. Pure CD44 is necessary for optimal contact allergic responses but is not required for normal leukocyte extravasation J. Exp. Med 178 1993 497 507
    • (1993) J. Exp. Med , vol.178 , pp. 497-507
    • Camp, R.L.1    Scheynius, A.2    Johansson, C.3    Pure, E.4
  • 254
    • 0025137103 scopus 로고
    • Monoclonal antibodies to Pgp-1/CD44 block lympho-hemopoiesis in long-term bone marrow cultures
    • K. Miyake K.L. Medina S.-I. Hayashi S. Ono T. Hamaoka P.W. Kincade Monoclonal antibodies to Pgp-1/CD44 block lympho-hemopoiesis in long-term bone marrow cultures J. Exp. Med 171 1990 477 488
    • (1990) J. Exp. Med , vol.171 , pp. 477-488
    • Miyake, K.1    Medina, K.L.2    Hayashi, S.-I.3    Ono, S.4    Hamaoka, T.5    Kincade, P.W.6
  • 255
    • 0023649591 scopus 로고
    • A subset of T cell receptors associated with L3T4 molecules mediates C6VL leukemia cell binding of its cognate retrovirus
    • H.C. O'Neill M.S. McGrath J.P. Allison I.L. Weissman A subset of T cell receptors associated with L3T4 molecules mediates C6VL leukemia cell binding of its cognate retrovirus Cell 49 1987 143 151
    • (1987) Cell , vol.49 , pp. 143-151
    • O'Neill, H.C.1    McGrath, M.S.2    Allison, J.P.3    Weissman, I.L.4
  • 256
    • 0027282460 scopus 로고
    • The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44
    • M.F. Naujokas M. Morin M.S. Anderson M. Peterson J. Miller The chondroitin sulfate form of invariant chain can enhance stimulation of T cell responses through interaction with CD44 Cell 74 1993 257 258
    • (1993) Cell , vol.74 , pp. 257-258
    • Naujokas, M.F.1    Morin, M.2    Anderson, M.S.3    Peterson, M.4    Miller, J.5
  • 258
    • 0026757630 scopus 로고
    • A 90 kilodalton endothelial molecule mediating lymphocyte binding in humans
    • M. Salmi S. Jalkanen A 90 kilodalton endothelial molecule mediating lymphocyte binding in humans Science 257 1992 1407 1409
    • (1992) Science , vol.257 , pp. 1407-1409
    • Salmi, M.1    Jalkanen, S.2
  • 259
    • 0027368071 scopus 로고
    • Induction and function of vascular adhesion protein-1 at sites of inflammation
    • M. Salmi K. Kalimo S. Jalkanen Induction and function of vascular adhesion protein-1 at sites of inflammation J. Exp. Med 178 1993 2255 2260
    • (1993) J. Exp. Med , vol.178 , pp. 2255-2260
    • Salmi, M.1    Kalimo, K.2    Jalkanen, S.3
  • 260
    • 0027440443 scopus 로고
    • Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium
    • L. Airas M. Salmi S. Jalkanen Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium J. Immunol 151 1993 4228 4238
    • (1993) J. Immunol , vol.151 , pp. 4228-4238
    • Airas, L.1    Salmi, M.2    Jalkanen, S.3
  • 262
    • 0010617993 scopus 로고
    • Chemokines link the two steps of leukocyte adhesion to endothelium
    • A. Rot Chemokines link the two steps of leukocyte adhesion to endothelium Immunologist 1 1993 145 149
    • (1993) Immunologist , vol.1 , pp. 145-149
    • Rot, A.1
  • 264
    • 0024573776 scopus 로고
    • The neutrophil-activating protein (NAP-1) is also chemotactic for T lymphocytes
    • C.G. Larsen A.O. Anderson E. Apella J.J. Oppenheim K. Matsushima The neutrophil-activating protein (NAP-1) is also chemotactic for T lymphocytes Science 243 1989 1464 1467
    • (1989) Science , vol.243 , pp. 1464-1467
    • Larsen, C.G.1    Anderson, A.O.2    Apella, E.3    Oppenheim, J.J.4    Matsushima, K.5
  • 266
    • 0025873068 scopus 로고
    • Inflammatory properties of neutrophil-activating protein-1/interleukin 8 (NAP-1/IL-8) in human skin: A light- and electronmicroscopic study
    • O. Swensson C. Schubert E. Christophers J.M. Schröder Inflammatory properties of neutrophil-activating protein-1/interleukin 8 (NAP-1/IL-8) in human skin: A light- and electronmicroscopic study J. Invest. Dermatol 96 1991 682 689
    • (1991) J. Invest. Dermatol , vol.96 , pp. 682-689
    • Swensson, O.1    Schubert, C.2    Christophers, E.3    Schröder, J.M.4
  • 267
    • 0025038599 scopus 로고
    • Selective attraction of monocytes and T lymphocytes of the memory phenotype by cytokine RANTES
    • T.J. Schall K. Bacon K.J. Toy D.V. Goeddel Selective attraction of monocytes and T lymphocytes of the memory phenotype by cytokine RANTES Nature 347 1990 669 671
    • (1990) Nature , vol.347 , pp. 669-671
    • Schall, T.J.1    Bacon, K.2    Toy, K.J.3    Goeddel, D.V.4
  • 268
    • 0026161899 scopus 로고
    • Biology of the RANTES/SIS cytokine family
    • T.J. Schall Biology of the RANTES/SIS cytokine family Cytokine 3 1991 165 183
    • (1991) Cytokine , vol.3 , pp. 165-183
    • Schall, T.J.1
  • 269
    • 0027322567 scopus 로고
    • Human macrophage inflammatory protein a (MIP-1α) and MIP-1β chemokines attract distinct populations of lymphocytes
    • T.J. Schall K. Bacon D.R. Camp J.W. Kaspari D.V. Goeddel Human macrophage inflammatory protein a (MIP-1α) and MIP-1β chemokines attract distinct populations of lymphocytes J. Exp. Med 177 1993 1821 1825
    • (1993) J. Exp. Med , vol.177 , pp. 1821-1825
    • Schall, T.J.1    Bacon, K.2    Camp, D.R.3    Kaspari, J.W.4    Goeddel, D.V.5
  • 272
    • 0027462365 scopus 로고
    • Molecular cloning, functional expression, and signaling characteristics of a C—C chemokine receptor
    • K. Neote D. DiGregorio J.Y. Mak R. Horuk T.J. Schall Molecular cloning, functional expression, and signaling characteristics of a C—C chemokine receptor Cell 72 1993 415 425
    • (1993) Cell , vol.72 , pp. 415-425
    • Neote, K.1    DiGregorio, D.2    Mak, J.Y.3    Horuk, R.4    Schall, T.J.5
  • 273
    • 0026095795 scopus 로고
    • Structure and functional expression of a human interleukin-8 receptor
    • W.E. Holmes J. Lee W.J. Kuang G.C. Rice W.I. Wood Structure and functional expression of a human interleukin-8 receptor Science 253 1991 1278 1280
    • (1991) Science , vol.253 , pp. 1278-1280
    • Holmes, W.E.1    Lee, J.2    Kuang, W.J.3    Rice, G.C.4    Wood, W.I.5
  • 275
    • 43949153331 scopus 로고
    • CC chemokines in allergic inflammation
    • M. Baggiolini C.A. Dahinden CC chemokines in allergic inflammation Immunol. Today 15 1994 127 133
    • (1994) Immunol. Today , vol.15 , pp. 127-133
    • Baggiolini, M.1    Dahinden, C.A.2
  • 276
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • M.I. Simon M.P. Strathmann N. Gautam Diversity of G proteins in signal transduction Science 252 1991 802 808
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 277
    • 0027279671 scopus 로고
    • G protein-coupled signal transduction pathways for interleukin-8
    • D. Wu G.J. LaRosa M.I. Simon G protein-coupled signal transduction pathways for interleukin-8 Science 261 1993 101 103
    • (1993) Science , vol.261 , pp. 101-103
    • Wu, D.1    LaRosa, G.J.2    Simon, M.I.3
  • 278
    • 0027178531 scopus 로고
    • Rapid G protein-regulated activation event involved in lymphocyte binding to high endothelial venules
    • R.F. Bargatze E.C. Butcher Rapid G protein-regulated activation event involved in lymphocyte binding to high endothelial venules J. Exp. Med 178 1993 367 372
    • (1993) J. Exp. Med , vol.178 , pp. 367-372
    • Bargatze, R.F.1    Butcher, E.C.2
  • 279
    • 0028365273 scopus 로고
    • Hepatocyte growth factor and macrophage inflammatory protein-1β: Structurally distinct cytokines that induce rapid cytoskeletal changes and subset-preferential migration in T cells
    • D.H. Adams L. Harvath D.P. Bottaro R. Interrante G. Catalano Y. Tanaka A. Strain S.G. Hubscher S. Shaw Hepatocyte growth factor and macrophage inflammatory protein-1β: Structurally distinct cytokines that induce rapid cytoskeletal changes and subset-preferential migration in T cells Proc. Natl. Acad. Sci. USA 91 1994 7144 7148
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7144-7148
    • Adams, D.H.1    Harvath, L.2    Bottaro, D.P.3    Interrante, R.4    Catalano, G.5    Tanaka, Y.6    Strain, A.7    Hubscher, S.G.8    Shaw, S.9
  • 280
    • 0025351332 scopus 로고
    • Hepatocytes and scatter factor
    • E. Gherardi M. Stoker Hepatocytes and scatter factor Nature 346 1990 228
    • (1990) Nature , vol.346 , pp. 228
    • Gherardi, E.1    Stoker, M.2
  • 282
    • 0026485023 scopus 로고
    • A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis
    • G. Hartmann L. Naldini K.M. Weidner M. Sachs M. Vigna P.M. Comoglio W. Birchmeier A functional domain in the heavy chain of scatter factor/hepatocyte growth factor binds the c-Met receptor and induces cell dissociation but not mitogenesis Proc. Natl. Acad. Sci. USA 89 1992 11574 11578
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11574-11578
    • Hartmann, G.1    Naldini, L.2    Weidner, K.M.3    Sachs, M.4    Vigna, M.5    Comoglio, P.M.6    Birchmeier, W.7
  • 283
    • 0027410889 scopus 로고
    • The Met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/ hepatocyte growth factor in epithelial cells
    • K.M. Weidner M. Sachs W. Birchmeier The Met receptor tyrosine kinase transduces motility, proliferation, and morphogenic signals of scatter factor/ hepatocyte growth factor in epithelial cells J. Cell Biol 121 1993 145 154
    • (1993) J. Cell Biol , vol.121 , pp. 145-154
    • Weidner, K.M.1    Sachs, M.2    Birchmeier, W.3
  • 286
    • 0024588320 scopus 로고
    • Characterization of rat T cell precursors sorted by chemotactic migration toward thymotaxin
    • M.A. Deugnier B.A. Imhof B. Bauvois D. Dunon M. Denoyelle J.P. Thiery Characterization of rat T cell precursors sorted by chemotactic migration toward thymotaxin Cell 56 1989 1073 1083
    • (1989) Cell , vol.56 , pp. 1073-1083
    • Deugnier, M.A.1    Imhof, B.A.2    Bauvois, B.3    Dunon, D.4    Denoyelle, M.5    Thiery, J.P.6
  • 287
    • 0025146574 scopus 로고
    • T-cell precursor migration toward β2-microglobulin is involved in thymus colonization of chicken embryos
    • D. Dunon J. Kaufman J. Salomonsen K. Skjoedt O. Vainio J.P. Thiery B.A. Imhof T-cell precursor migration toward β2-microglobulin is involved in thymus colonization of chicken embryos EMBO J 9 1990 3315 3322
    • (1990) EMBO J , vol.9 , pp. 3315-3322
    • Dunon, D.1    Kaufman, J.2    Salomonsen, J.3    Skjoedt, K.4    Vainio, O.5    Thiery, J.P.6    Imhof, B.A.7
  • 288
    • 85113044397 scopus 로고
    • Inflammation
    • J.I. Gallin Inflammation W.E. Paul 3rd ed. Fundamental Immunology 1993 Raven Press New York 1015 1032
    • (1993) , pp. 1015-1032
    • Gallin, J.I.1
  • 290
    • 0027410996 scopus 로고
    • Human chemotaxis receptor genes cluster at 19q13.3–13.4. Characterization of the human C5a receptor gene
    • N.P. Gerard L. Bao H. Xiao-Ping R.L. Eddy T.B. Shows C. Gerard Human chemotaxis receptor genes cluster at 19q13.3–13.4. Characterization of the human C5a receptor gene Biochemistry 32 1993 1243 1250
    • (1993) Biochemistry , vol.32 , pp. 1243-1250
    • Gerard, N.P.1    Bao, L.2    Xiao-Ping, H.3    Eddy, R.L.4    Shows, T.B.5    Gerard, C.6
  • 291
    • 0026442285 scopus 로고
    • Cloning of the gene coding for a human receptor for formyl peptides. Characterization of a promoter region and evidence for a polymorphic expression
    • H.D. Perez R. Holmes E. Kelly J. McClary Q. Chou W.H. Andrews Cloning of the gene coding for a human receptor for formyl peptides. Characterization of a promoter region and evidence for a polymorphic expression Biochemistry 31 1992 11595 11599
    • (1992) Biochemistry , vol.31 , pp. 11595-11599
    • Perez, H.D.1    Holmes, R.2    Kelly, E.3    McClary, J.4    Chou, Q.5    Andrews, W.H.6
  • 292
    • 0026558365 scopus 로고
    • Quantitative and qualitative differences in guanine nucleotide binding protein activation by formyl peptide and leukotriene B4 receptors
    • T.M. Schepers M.E. Brier K.R. McLeish Quantitative and qualitative differences in guanine nucleotide binding protein activation by formyl peptide and leukotriene B4 receptors J. Biol. Chem 267 1992 159 165
    • (1992) J. Biol. Chem , vol.267 , pp. 159-165
    • Schepers, T.M.1    Brier, M.E.2    McLeish, K.R.3
  • 293
    • 0025854524 scopus 로고
    • Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins
    • M.B. Lawrence T.A. Springer Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins Cell 65 1991 859 873
    • (1991) Cell , vol.65 , pp. 859-873
    • Lawrence, M.B.1    Springer, T.A.2
  • 294
    • 0027408343 scopus 로고
    • Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes
    • Y. Tanaka D.H. Adams S. Shaw Proteoglycans on endothelial cells present adhesion-inducing cytokines to leukocytes Immunol. Today 14 1993 111 115
    • (1993) Immunol. Today , vol.14 , pp. 111-115
    • Tanaka, Y.1    Adams, D.H.2    Shaw, S.3
  • 295
    • 0027486922 scopus 로고
    • Circulating adhesion molecules in disease
    • J.H. Gearing W. Newman Circulating adhesion molecules in disease Immunol. Today 14 1993 506 512
    • (1993) Immunol. Today , vol.14 , pp. 506-512
    • Gearing, J.H.1    Newman, W.2
  • 297
    • 0027218496 scopus 로고
    • Structural and functional characterization of minomeric soluble P-selectin and comparison with membrane P-selectin
    • S. Ushiyama T.M. Laue K.L. Moore H.P. Erickson R.P. McEver Structural and functional characterization of minomeric soluble P-selectin and comparison with membrane P-selectin J. Biol. Chem 268 1993 15229 15237
    • (1993) J. Biol. Chem , vol.268 , pp. 15229-15237
    • Ushiyama, S.1    Laue, T.M.2    Moore, K.L.3    Erickson, H.P.4    McEver, R.P.5
  • 299
    • 0344370136 scopus 로고
    • Transendothelial migration of T cells in chronic inflammation
    • N. Oppenheimer-Marks P.E. Lipsky Transendothelial migration of T cells in chronic inflammation Immunologist 2 1994 58 64
    • (1994) Immunologist , vol.2 , pp. 58-64
    • Oppenheimer-Marks, N.1    Lipsky, P.E.2
  • 300
    • 0021325825 scopus 로고
    • Molecular mechanisms of lymphocyte extravasation. I. Studies of two selective inhibitors of lymphocyte recirculation
    • G.J. Spangrude B.A. Braaten R.A. Daynes Molecular mechanisms of lymphocyte extravasation. I. Studies of two selective inhibitors of lymphocyte recirculation J. Immunol 132 1984 354 362
    • (1984) J. Immunol , vol.132 , pp. 354-362
    • Spangrude, G.J.1    Braaten, B.A.2    Daynes, R.A.3
  • 302
    • 0027299866 scopus 로고
    • Homing of naive, memory and effector lymphocytes
    • C.R. Mackay Homing of naive, memory and effector lymphocytes Curr. Opin. Immunol 5 1993 423 427
    • (1993) Curr. Opin. Immunol , vol.5 , pp. 423-427
    • Mackay, C.R.1
  • 304
    • 0025981454 scopus 로고
    • Molecular mechanisms underlying lymphocyte recirculation II. Differential regulation of LFA-1 in the interaction between lymphocytes and high endothelial cells
    • T. Tamatani M. Kotani T. Tanaka M. Miyasaka Molecular mechanisms underlying lymphocyte recirculation II. Differential regulation of LFA-1 in the interaction between lymphocytes and high endothelial cells Eur. J. Immunol 21 1991 855 858
    • (1991) Eur. J. Immunol , vol.21 , pp. 855-858
    • Tamatani, T.1    Kotani, M.2    Tanaka, T.3    Miyasaka, M.4
  • 305
    • 0027153196 scopus 로고
    • Triggering of L-selectin (gp90Mel–14) induces homotypic lymphocyte adhesion by a mechanism independent of LFA–1
    • U.G. Strauch B. Holzmann Triggering of L-selectin (gp90Mel–14) induces homotypic lymphocyte adhesion by a mechanism independent of LFA–1 Int. Immunol 5 1993 393 398
    • (1993) Int. Immunol , vol.5 , pp. 393-398
    • Strauch, U.G.1    Holzmann, B.2
  • 307
    • 0026642637 scopus 로고
    • Physiological and molecular mechanisms of lymphocyte homing
    • L.J. Picker E.C. Butcher Physiological and molecular mechanisms of lymphocyte homing Annu. Rev. Immunol 10 1992 561 591
    • (1992) Annu. Rev. Immunol , vol.10 , pp. 561-591
    • Picker, L.J.1    Butcher, E.C.2
  • 308
    • 0026343689 scopus 로고
    • Inhibition of in vivo migration to inflammation and homing to lymphoid tissues by the TA-2 monoclonal antibody. A likely role for VLA–4 in vivo
    • T.B. Issekutz Inhibition of in vivo migration to inflammation and homing to lymphoid tissues by the TA-2 monoclonal antibody. A likely role for VLA–4 in vivo J. Immunol 147 1991 4178 4184
    • (1991) J. Immunol , vol.147 , pp. 4178-4184
    • Issekutz, T.B.1
  • 309
    • 0026743048 scopus 로고
    • Altered patterns of T cell migration through lymph nodes and skin following antigen challenge
    • C.R. Mackay W. Marston L. Dudler Altered patterns of T cell migration through lymph nodes and skin following antigen challenge Eur. J. Immunol 22 1992 2205 2210
    • (1992) Eur. J. Immunol , vol.22 , pp. 2205-2210
    • Mackay, C.R.1    Marston, W.2    Dudler, L.3
  • 313
    • 0024446350 scopus 로고
    • Transforming growth factor β induces IgA production by lipopolysaccharide-stimulated murine B lymphocytes
    • R.L. Coffman D.A. Lebman B. Shrader Transforming growth factor β induces IgA production by lipopolysaccharide-stimulated murine B lymphocytes J. Exp. Med 170 1989 1039 1044
    • (1989) J. Exp. Med , vol.170 , pp. 1039-1044
    • Coffman, R.L.1    Lebman, D.A.2    Shrader, B.3
  • 314
    • 0026542346 scopus 로고
    • The CD56 adhesion molecules is the major determinant for detecting non-major histocompatibility complex-restricted cytotoxic mononuclear cells from the intestinal lamina propria
    • E.A.F. Van Tol H.W. Verspaget S. Pena C.V. Elzo Kraemer C.B.H.W. Lamers The CD56 adhesion molecules is the major determinant for detecting non-major histocompatibility complex-restricted cytotoxic mononuclear cells from the intestinal lamina propria Eur. J. Immunol 22 1992 23 29
    • (1992) Eur. J. Immunol , vol.22 , pp. 23-29
    • Van Tol, E.A.F.1    Verspaget, H.W.2    Pena, S.3    Elzo Kraemer, C.V.4    Lamers, C.B.H.W.5
  • 316
    • 0027278234 scopus 로고
    • Epiligrin, a component of epithelial basement membranes, is an adhesive ligand for α3β1 positive T lymphocytes
    • E.A. Wayner S.G. Gil G.F. Murphy M.S. Wilke W.G. Carter Epiligrin, a component of epithelial basement membranes, is an adhesive ligand for α3β1 positive T lymphocytes J. Cell. Biol 121 1993 1141 1152
    • (1993) J. Cell. Biol , vol.121 , pp. 1141-1152
    • Wayner, E.A.1    Gil, S.G.2    Murphy, G.F.3    Wilke, M.S.4    Carter, W.G.5
  • 317
    • 85113056300 scopus 로고
    • Cooperative role of α3β1 and E-cadherin in mediating T lymphocyte adhesion to keratinocytes
    • E.A. Wayner B. Hoffstrom M.R. Pittelkow Cooperative role of α 3 β 1 and E-cadherin in mediating T lymphocyte adhesion to keratinocytes 1994 Submitted for publication.
    • (1994)
    • Wayner, E.A.1    Hoffstrom, B.2    Pittelkow, M.R.3
  • 318
    • 85113075249 scopus 로고
    • T lymphocyte precursors adhere to thymic endothelium
    • P. Ruiz D. Dunon B. Hesse B.A. Imhof T lymphocyte precursors adhere to thymic endothelium B.A. Imhof S. Berrih-Aknin S. Ezine Lymphocyte Reaction and in Vivo Immunology 1991 Dekker New York 953 957
    • (1991) , pp. 953-957
    • Ruiz, P.1    Dunon, D.2    Hesse, B.3    Imhof, B.A.4
  • 319
    • 0023201634 scopus 로고
    • Isolation of a thymus homing lyt-2-,L3T4- T-cell line from mouse spleen
    • H.C. O'Neill Isolation of a thymus homing lyt-2-,L3T4- T-cell line from mouse spleen Cell. Immunol 109 1987 222 230
    • (1987) Cell. Immunol , vol.109 , pp. 222-230
    • O'Neill, H.C.1
  • 320
    • 0024404442 scopus 로고
    • Antibody which defines a subset of bone marrow cells that can migrate to the thymus
    • H.C. O'Neill Antibody which defines a subset of bone marrow cells that can migrate to the thymus Immunology 68 1989 59 65
    • (1989) Immunology , vol.68 , pp. 59-65
    • O'Neill, H.C.1
  • 321
    • 0026699789 scopus 로고
    • Lymphoid precursor cell lines have capacity to migrate to multiple lymphoid sites
    • H.C. O'Neill K. Ni T.J. O'Neill Lymphoid precursor cell lines have capacity to migrate to multiple lymphoid sites Immunology 76 1992 631 635
    • (1992) Immunology , vol.76 , pp. 631-635
    • O'Neill, H.C.1    Ni, K.2    O'Neill, T.J.3
  • 322
    • 0025339160 scopus 로고
    • The ontogeny of human lymphocyte recirculation: High endothelial cell antigen (HECA-452) and CD44 homing receptor expression in the development of the immune system
    • E. Horst C.J.L.M. Meijer A.M. Duijvestjin N. Hartwig H.J. Van der Harten S. Pals The ontogeny of human lymphocyte recirculation: High endothelial cell antigen (HECA-452) and CD44 homing receptor expression in the development of the immune system Eur. J. Immunol 20 1990 1483 1489
    • (1990) Eur. J. Immunol , vol.20 , pp. 1483-1489
    • Horst, E.1    Meijer, C.J.L.M.2    Duijvestjin, A.M.3    Hartwig, N.4    Van der Harten, H.J.5    Pals, S.6
  • 323
    • 0026601077 scopus 로고
    • Flow cytometric assessment of human T-cell differentiation in thymus and bone marrow
    • L.W.M.M. Terstappen S. Huang L.J. Picker Flow cytometric assessment of human T-cell differentiation in thymus and bone marrow Blood 79 1992 666 677
    • (1992) Blood , vol.79 , pp. 666-677
    • Terstappen, L.W.M.M.1    Huang, S.2    Picker, L.J.3
  • 324
    • 0002882408 scopus 로고
    • Ontogeny of hematopoietic organs studied in avian embryo interspecific chimeras
    • N.M. Le Douarin Ontogeny of hematopoietic organs studied in avian embryo interspecific chimeras B. Clakson P.A. Marks J.E. Till Differentiation of Normal and Neoplastic Hematopoietic Cells 5 1978 Cold Spring Harbor Laboratory Press, Cold Spring Harbor New York. 5 31
    • (1978) , pp. 5-31
    • Le Douarin, N.M.1
  • 325
    • 0022453509 scopus 로고
    • The embryonic thymus produces chemotactic peptides involved in the homing of hemopoietic precursors
    • S. Champion B.A. Imhof P. Savagner J.P. Thiery The embryonic thymus produces chemotactic peptides involved in the homing of hemopoietic precursors Cell 44 1986 781 790
    • (1986) Cell , vol.44 , pp. 781-790
    • Champion, S.1    Imhof, B.A.2    Savagner, P.3    Thiery, J.P.4
  • 328
    • 0022913595 scopus 로고
    • Homing of hemopoietic precursor cells tothe embryonic thymus: Characterization of an invasive mechanism induced by chemotactic peptides
    • P. Savagner B.A. Imhof K.M. Yamada J.P. Thiery Homing of hemopoietic precursor cells tothe embryonic thymus: Characterization of an invasive mechanism induced by chemotactic peptides J. Cell Biol 103 1986 2715 2727
    • (1986) J. Cell Biol , vol.103 , pp. 2715-2727
    • Savagner, P.1    Imhof, B.A.2    Yamada, K.M.3    Thiery, J.P.4
  • 329
    • 85113043117 scopus 로고
    • Lymphocyte trafficking
    • A.O. Anderson S. Shaw Lymphocyte trafficking R.R. Rich T.A. Fleisher B.D. Schwartz W.T. Shearer W. Strober Clinical Immunology 1994 in press
    • (1994)
    • Anderson, A.O.1    Shaw, S.2
  • 330
    • 0027209421 scopus 로고
    • Leukocyte rolling and extravasation are severely compromized in P selectin deficient mice
    • T.N. Mayadas R.C. Johnson H. Rayburn R.O. Hynes D.D. Wagner Leukocyte rolling and extravasation are severely compromized in P selectin deficient mice Cell 74 1993 541 554
    • (1993) Cell , vol.74 , pp. 541-554
    • Mayadas, T.N.1    Johnson, R.C.2    Rayburn, H.3    Hynes, R.O.4    Wagner, D.D.5
  • 331
    • 0024815584 scopus 로고
    • An inducible endothelial cell surface glycoprotein mediates melanoma adhesion
    • G.E. Rice M.P. Bevilacqua An inducible endothelial cell surface glycoprotein mediates melanoma adhesion Science 246 1989 1303 1306
    • (1989) Science , vol.246 , pp. 1303-1306
    • Rice, G.E.1    Bevilacqua, M.P.2
  • 332
    • 0025805031 scopus 로고
    • Cell adhesion molecules of the immunoglobulin supergene family and their role in malignant transformation and progression to metastatic disease
    • J.P. Johnson Cell adhesion molecules of the immunoglobulin supergene family and their role in malignant transformation and progression to metastatic disease Cancer Metastasis Rev 10 1991 11 22
    • (1991) Cancer Metastasis Rev , vol.10 , pp. 11-22
    • Johnson, J.P.1
  • 335
    • 0028429944 scopus 로고
    • Neutrophil tethering to and rolling on E-selectin are separable by requirement for L-selectin
    • M.B. Lawrence D.F. Bainton T.A. Springer Neutrophil tethering to and rolling on E-selectin are separable by requirement for L-selectin Immunity 1 1994 137 145
    • (1994) Immunity , vol.1 , pp. 137-145
    • Lawrence, M.B.1    Bainton, D.F.2    Springer, T.A.3
  • 337
    • 0028362088 scopus 로고
    • The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent
    • A.M. Romanic J.A. Madti The induction of 72-kD gelatinase in T cells upon adhesion to endothelial cells is VCAM-1 dependent J. Cell Biol 125 1994 1165 1178
    • (1994) J. Cell Biol , vol.125 , pp. 1165-1178
    • Romanic, A.M.1    Madti, J.A.2


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