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Volumn 100, Issue 3, 1997, Pages 485-492

Role of PSGL-1 binding to selectins in leukocyte recruitment

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GLYCOPROTEIN; L SELECTIN; MEMBRANE PROTEIN; PADGEM PROTEIN; SIALOMUCIN; CELL ADHESION MOLECULE; P SELECTIN LIGAND PROTEIN; P-SELECTIN LIGAND PROTEIN; SELECTIN;

EID: 0030854107     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/jci119556     Document Type: Review
Times cited : (391)

References (70)
  • 1
    • 0030587922 scopus 로고    scopus 로고
    • Adhesion and signaling in vascular cell-cell interactions
    • Zimmerman, G.A., T.M. McIntyre, and S.M. Prescott. 1996. Adhesion and signaling in vascular cell-cell interactions. J. Clin. Invest. 98:1699-1702.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1699-1702
    • Zimmerman, G.A.1    McIntyre, T.M.2    Prescott, S.M.3
  • 2
    • 0030482482 scopus 로고    scopus 로고
    • Effects of fluid dynamic forces on vascular cell adhesion
    • Konstantopoulos, K., and L.V. McIntire. 1997. Effects of fluid dynamic forces on vascular cell adhesion. J. Clin. Invest. 98:2661-2665.
    • (1997) J. Clin. Invest. , vol.98 , pp. 2661-2665
    • Konstantopoulos, K.1    McIntire, L.V.2
  • 3
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • Springer, T.A. 1995. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Annu. Rev. Physiol. 57:827-872.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 4
    • 0029070815 scopus 로고
    • Leukocyte trafficking mediated by selectin-carbohydrate interactions
    • McEver, R.P., K.L. Moore, and R.D. Cummings. 1995. Leukocyte trafficking mediated by selectin-carbohydrate interactions. J. Biol. Chem. 270: 11025-11028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11025-11028
    • McEver, R.P.1    Moore, K.L.2    Cummings, R.D.3
  • 5
    • 0029858031 scopus 로고    scopus 로고
    • Selectins and their ligands: Current concepts and controversies
    • Kansas, G.S. 1996. Selectins and their ligands: current concepts and controversies. Blood. 88:3259-3287.
    • (1996) Blood , vol.88 , pp. 3259-3287
    • Kansas, G.S.1
  • 6
    • 0030907870 scopus 로고    scopus 로고
    • Therapeutic inhibition of carbohydrate-protein interactions in vivo
    • Lowe, J.B., and P.A. Ward. 1997. Therapeutic inhibition of carbohydrate-protein interactions in vivo. J. Clin. Invest. 99:822-826.
    • (1997) J. Clin. Invest. , vol.99 , pp. 822-826
    • Lowe, J.B.1    Ward, P.A.2
  • 7
    • 0031029280 scopus 로고    scopus 로고
    • Selectin ligands: Will the real ones please stand up?
    • Varki, A. 1997. Selectin ligands: will the real ones please stand up? J. Clin. Invest. 99:158-162.
    • (1997) J. Clin. Invest. , vol.99 , pp. 158-162
    • Varki, A.1
  • 9
    • 0027216123 scopus 로고
    • Characterization of a specific ligand for P-selectin on myeloid cells. A minor glycoprotein with sialylated O-linked oligosaccharides
    • Norgard, K.E., K.L. Moore, S. Diaz, N.L. Stults, S. Ushiyama, R.P. McEver, R.D. Cummings, and A. Varki. 1993. Characterization of a specific ligand for P-selectin on myeloid cells. A minor glycoprotein with sialylated O-linked oligosaccharides. J. Biol. Chem. 268:12764-12774.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12764-12774
    • Norgard, K.E.1    Moore, K.L.2    Diaz, S.3    Stults, N.L.4    Ushiyama, S.5    McEver, R.P.6    Cummings, R.D.7    Varki, A.8
  • 10
    • 0027218496 scopus 로고
    • Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin
    • Ushiyama, S., T.M. Laue, K.L. Moore, H.P. Erickson, and R.P. McEver. 1993. Structural and functional characterization of monomeric soluble P-selectin and comparison with membrane P-selectin. J. Biol. Chem. 268:15229-15237.
    • (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
  • 12
    • 0026039789 scopus 로고
    • The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and nonmyeloid cells
    • Zhou, Q., K.L. Moore, D.F. Smith, A. Varki, R.P. McEver, and R.D. Cummings. 1991. The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and nonmyeloid cells. J. Cell Biol. 115:557-564.
    • (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
  • 13
    • 0029937859 scopus 로고    scopus 로고
    • Mouse P-selectin glycoprotein ligand-1: Molecular cloning, chromosomal localization, and expression of a functional P-selectin receptor
    • Yang, J., J. Galipeau, C.A. Kozak, B.C. Furie, and B. Furie. 1996. Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal localization, and expression of a functional P-selectin receptor. Blood. 87:4176-4186.
    • (1996) Blood , vol.87 , pp. 4176-4186
    • Yang, J.1    Galipeau, J.2    Kozak, C.A.3    Furie, B.C.4    Furie, B.5
  • 14
    • 0029057305 scopus 로고
    • Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand
    • Veldman, G.M., K.M. Bean, D.A. Cumming, R.L. Eddy, S.N.J. Sait, and T.B. Shows. 1995. Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand. J. Biol. Chem. 270:16470-16475.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16470-16475
    • Veldman, G.M.1    Bean, K.M.2    Cumming, D.A.3    Eddy, R.L.4    Sait, S.N.J.5    Shows, T.B.6
  • 16
    • 0027992114 scopus 로고
    • The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated. O-linked poly-N-acetyllactosamine
    • Moore, K.L., S.F. Eaton, D.E. Lyons, H.S. Lichenstein, R.D. Cummings, and R.P. McEver. 1994. The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated. O-linked poly-N-acetyllactosamine. J. Biol. Chem. 269:23318-23327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23318-23327
    • Moore, K.L.1    Eaton, S.F.2    Lyons, D.E.3    Lichenstein, H.S.4    Cummings, R.D.5    McEver, R.P.6
  • 18
    • 0023645520 scopus 로고
    • Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA
    • Sasaki, H., B. Bothner, A. Dell, and M. Fukuda. 1987. Carbohydrate structure of erythropoietin expressed in Chinese hamster ovary cells by a human erythropoietin cDNA. J. Biol. Chem. 262:12059-12076.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12059-12076
    • Sasaki, H.1    Bothner, B.2    Dell, A.3    Fukuda, M.4
  • 19
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin
    • Li, F., P.P. Wilkins, S. Crawley, J. Weinstein, R.D. Cummings, and R.P. McEver. 1996. Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. J. Biol. Chem. 271: 3255-3264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3255-3264
    • Li, F.1    Wilkins, P.P.2    Crawley, S.3    Weinstein, J.4    Cummings, R.D.5    McEver, R.P.6
  • 20
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins, P.P., R.P. McEver, and R.D. Cummings. 1996. Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J. Biol. Chem. 271:18732-18742.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18732-18742
    • Wilkins, P.P.1    McEver, R.P.2    Cummings, R.D.3
  • 21
    • 0025955701 scopus 로고
    • Molecular cloning of a human fucosyltransferase gene that determines expression of the Lewis x and VIM-2 epitopes but not ELAM-1-dependent cell adhesion
    • Lowe, J.B., J.F. Kukowska-Latallo, R.P. Nair, R.D. Larsen, R.M. Marks, B.A. Macher, R.J. Kelly, and L.K. Ernst. 1991. Molecular cloning of a human fucosyltransferase gene that determines expression of the Lewis x and VIM-2 epitopes but not ELAM-1-dependent cell adhesion. J. Biol. Chem. 266: 17467-17477.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17467-17477
    • Lowe, J.B.1    Kukowska-Latallo, J.F.2    Nair, R.P.3    Larsen, R.D.4    Marks, R.M.5    Macher, B.A.6    Kelly, R.J.7    Ernst, L.K.8
  • 22
    • 0028292790 scopus 로고
    • Molecular cloning of a cDNA encoding a novel human leukocyte α1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant
    • Natsuka, S., K.M. Gersten, K. Zenitas, R. Kannagi, and J.B. Lowe. 1994. Molecular cloning of a cDNA encoding a novel human leukocyte α1,3-fucosyltransferase capable of synthesizing the sialyl Lewis x determinant. J. Biol. Chem. 269:16789-16794.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16789-16794
    • Natsuka, S.1    Gersten, K.M.2    Zenitas, K.3    Kannagi, R.4    Lowe, J.B.5
  • 23
    • 16044363014 scopus 로고    scopus 로고
    • The α(1,3)Fucosyltransferase Fuc-TVII controls leukocyte trafficking through an essential role in L-, E-, and P-selectin ligand biosynthesis
    • Maly, P., A.D. Thall, B. Petryniak, G.E. Rogers, P.L. Smith, R.M. Marks, R.J. Kelly, K.M. Gersten, G.Y. Cheng, T.L. Saunders, et al. 1996. The α(1,3)Fucosyltransferase Fuc-TVII controls leukocyte trafficking through an essential role in L-, E-, and P-selectin ligand biosynthesis. Cell. 86:643-653.
    • (1996) Cell , vol.86 , pp. 643-653
    • Maly, P.1    Thall, A.D.2    Petryniak, B.3    Rogers, G.E.4    Smith, P.L.5    Marks, R.M.6    Kelly, R.J.7    Gersten, K.M.8    Cheng, G.Y.9    Saunders, T.L.10
  • 24
    • 0029865762 scopus 로고    scopus 로고
    • Visualization of P-selectin glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies
    • Li, F., H.P. Erickson, J.A. James, K.L. Moore, R.D. Cummings, and R.P. McEver. 1996. Visualization of P-selectin glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies. J. Biol. Chem. 271:6342-6348.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6342-6348
    • Li, F.1    Erickson, H.P.2    James, J.A.3    Moore, K.L.4    Cummings, R.D.5    McEver, R.P.6
  • 25
    • 0029132217 scopus 로고
    • Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin
    • Wilkins, P.P., K.L. Moore, R.P. McEver, and R.D. Cummings. 1995. Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin. J. Biol. Chem. 270:22677-22680.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22677-22680
    • Wilkins, P.P.1    Moore, K.L.2    McEver, R.P.3    Cummings, R.D.4
  • 26
    • 0028863479 scopus 로고
    • PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus
    • Pouyani, T., and B. Seed. 1995. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Cell. 83:333-343.
    • (1995) Cell , vol.83 , pp. 333-343
    • Pouyani, T.1    Seed, B.2
  • 27
    • 0028885684 scopus 로고
    • A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding
    • Sako, D., K.M. Comess, K.M. Barone, R.T. Camphausen, D.A. Cumming, and G.D. Shaw. 1995. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell. 83:323-331.
    • (1995) Cell , vol.83 , pp. 323-331
    • Sako, D.1    Comess, K.M.2    Barone, K.M.3    Camphausen, R.T.4    Cumming, D.A.5    Shaw, G.D.6
  • 28
    • 0028807440 scopus 로고
    • A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature n terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding
    • De Luca, M., L.C. Dunlop, R.K. Andrews, J.V. Flannery, Jr., R. Ettling, D.A. Cumming, G.M. Veldman, and M.C. Berndt. 1995. A novel cobra venom metalloproteinase, mocarhagin, cleaves a 10-amino acid peptide from the mature n terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding. J. Biol. Chem. 270:26734-26737.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26734-26737
    • De Luca, M.1    Dunlop, L.C.2    Andrews, R.K.3    Flannery Jr., J.V.4    Ettling, R.5    Cumming, D.A.6    Veldman, G.M.7    Berndt, M.C.8
  • 29
    • 0031054445 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 (PSGL-1) on T helper 1 but not on T helper 2 cells binds to P-selectin and supports migration into inflamed skin
    • Borges, E., W. Tietz, M. Steegmaier, T. Moll, R. Hallmann, A. Hamann, and D. Vestweber. 1997. P-selectin glycoprotein ligand-1 (PSGL-1) on T helper 1 but not on T helper 2 cells binds to P-selectin and supports migration into inflamed skin. J. Exp. Med. 185:573-578.
    • (1997) J. Exp. Med. , vol.185 , pp. 573-578
    • Borges, E.1    Tietz, W.2    Steegmaier, M.3    Moll, T.4    Hallmann, R.5    Hamann, A.6    Vestweber, D.7
  • 30
    • 0030883312 scopus 로고    scopus 로고
    • The P-selectin glycoprotein ligand-1 is important for recruitment of neutrophils into inflamed mouse peritoneum
    • In press
    • Borges, E., R. Eytner, T. Moll, M. Steegmaier, M.A. Campbell, K. Ley, H. Mossman, and D. Vestweber. 1997. The P-selectin glycoprotein ligand-1 is important for recruitment of neutrophils into inflamed mouse peritoneum. Blood. In press.
    • (1997) Blood
    • Borges, E.1    Eytner, R.2    Moll, T.3    Steegmaier, M.4    Campbell, M.A.5    Ley, K.6    Mossman, H.7    Vestweber, D.8
  • 31
    • 0029758146 scopus 로고    scopus 로고
    • Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1: A mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro
    • Walcheck, B., K.L. Moore, R.P. McEver, and T.K. Kishimoto. 1996. Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1: a mechanism that amplifies initial leukocyte accumulation on P-selectin in vitro. J. Clin. Invest. 98:1081-1087.
    • (1996) J. Clin. Invest. , vol.98 , pp. 1081-1087
    • Walcheck, B.1    Moore, K.L.2    McEver, R.P.3    Kishimoto, T.K.4
  • 32
    • 0030294239 scopus 로고    scopus 로고
    • L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes. Interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity
    • Tu, L.L., A.J. Chen, M.D. Delahunty, K.L. Moore, S.R. Watson, R.P. McEver, and T.F. Tedder. 1996. L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes. Interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity. J. Immunol. 157:3995-4004.
    • (1996) J. Immunol. , vol.157 , pp. 3995-4004
    • Tu, L.L.1    Chen, A.J.2    Delahunty, M.D.3    Moore, K.L.4    Watson, S.R.5    McEver, R.P.6    Tedder, T.F.7
  • 34
    • 0029076738 scopus 로고
    • The P-selectin glycoprotein ligand functions as a common human leukocyte ligand for P- and E-selectins
    • Asa, D., L. Raycroft, L. Ma, P.A. Aeed, P.S. Kaytes, Å.P. Elhammer, and J.-G. Geng. 1995. The P-selectin glycoprotein ligand functions as a common human leukocyte ligand for P- and E-selectins. J. Biol. Chem. 270:11662-11670.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11662-11670
    • Asa, D.1    Raycroft, L.2    Ma, L.3    Aeed, P.A.4    Kaytes, P.S.5    Elhammer, Å.P.6    Geng, J.-G.7
  • 35
    • 0028197560 scopus 로고
    • Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells
    • Lenter, M., A. Levinovitz, S. Isenmann, and D. Vestweber. 1994. Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells. J. Cell Biol. 125:471-481.
    • (1994) J. Cell Biol. , vol.125 , pp. 471-481
    • Lenter, M.1    Levinovitz, A.2    Isenmann, S.3    Vestweber, D.4
  • 36
    • 0029793468 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation
    • Guyer, D.A., K.L. Moore, E. Lynam, C.M.G. Schammel, S. Rogelj, R.P. McEver, and L.A. Sklar. 1996. P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. Blood. 88:2415-2421.
    • (1996) Blood , vol.88 , pp. 2415-2421
    • Guyer, D.A.1    Moore, K.L.2    Lynam, E.3    Schammel, C.M.G.4    Rogelj, S.5    McEver, R.P.6    Sklar, L.A.7
  • 38
    • 0028834456 scopus 로고
    • Neutrophils use both shared and distinct mechanisms to adhere to selectins under static and flow conditions
    • Patel, K.D., K.L. Moore, M.U. Nollert, and R.P. McEver. 1995. Neutrophils use both shared and distinct mechanisms to adhere to selectins under static and flow conditions. J. Clin. Invest. 96:1887-1896.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1887-1896
    • Patel, K.D.1    Moore, K.L.2    Nollert, M.U.3    McEver, R.P.4
  • 39
    • 0029859481 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 is broadly expressed in cells of myeloid, lymphoid, and dendritic lineage and in some nonhematopoietic cells
    • Laszik, Z., P.J. Jansen, R.D. Cummings, T.F. Tedder, R.P. McEver, and K.L. Moore. 1996. P-selectin glycoprotein ligand-1 is broadly expressed in cells of myeloid, lymphoid, and dendritic lineage and in some nonhematopoietic cells. Blood. 88:3010-3021.
    • (1996) Blood , vol.88 , pp. 3010-3021
    • Laszik, Z.1    Jansen, P.J.2    Cummings, R.D.3    Tedder, T.F.4    McEver, R.P.5    Moore, K.L.6
  • 40
    • 0029099304 scopus 로고
    • P-selectin glycoprotein ligand-1 is the major counter-receptor for P-selectin on stimulated T cells and is widely distributed in non-functional form on many lymphocytic cells
    • Vachino, G., X.-J. Chang, G.M. Veldman, R. Kumar, D. Sako, L.A. Fouser, M.C. Berndt, and D.A. Cumming. 1995. P-selectin glycoprotein ligand-1 is the major counter-receptor for P-selectin on stimulated T cells and is widely distributed in non-functional form on many lymphocytic cells. J. Biol. Chem. 270:21966-21974.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21966-21974
    • Vachino, G.1    Chang, X.-J.2    Veldman, G.M.3    Kumar, R.4    Sako, D.5    Fouser, L.A.6    Berndt, M.C.7    Cumming, D.A.8
  • 41
    • 0026758565 scopus 로고
    • P-selectin (CD62) binds to subpopulations of human memory T lymphocytes and natural killer cells
    • Moore, K.L., and L.F. Thompson. 1992. P-selectin (CD62) binds to subpopulations of human memory T lymphocytes and natural killer cells. Biochem. Biophys. Res. Commun. 186:173-181.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 173-181
    • Moore, K.L.1    Thompson, L.F.2
  • 42
    • 0029924114 scopus 로고    scopus 로고
    • Interactions of human α/β and γ/δ T lymphocyte subsets in shear flow with E-selectin and P-selectin
    • Diacovo, T.G., S.J. Roth, C.T. Morita, J.P. Rosat, M.B. Brenner, and T.A. Springer. 1996. Interactions of human α/β and γ/δ T lymphocyte subsets in shear flow with E-selectin and P-selectin. J. Exp. Med. 183:1193-1203.
    • (1996) J. Exp. Med. , vol.183 , pp. 1193-1203
    • Diacovo, T.G.1    Roth, S.J.2    Morita, C.T.3    Rosat, J.P.4    Brenner, M.B.5    Springer, T.A.6
  • 44
    • 0030919187 scopus 로고    scopus 로고
    • Expression of a P-selectin ligand in zona pellucida of porcine oocytes and P-selectin on acrosomal membrane of porcine sperm cells. Potential implications for their involvement in sperm-egg interactions
    • Geng, J.-G., T.J. Raub, C.A. Baker, G.A. Sawada, L. Ma, and A.P. Elhammer. 1997. Expression of a P-selectin ligand in zona pellucida of porcine oocytes and P-selectin on acrosomal membrane of porcine sperm cells. Potential implications for their involvement in sperm-egg interactions. J. Cell Biol. 137:743-754.
    • (1997) J. Cell Biol. , vol.137 , pp. 743-754
    • Geng, J.-G.1    Raub, T.J.2    Baker, C.A.3    Sawada, G.A.4    Ma, L.5    Elhammer, A.P.6
  • 45
    • 0028913968 scopus 로고
    • Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-α secretion
    • Weyrich, A.S., T.M. McIntyre, R.P. McEver, S.M. Prescott, and G.A. Zimmerman. 1995. Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-α secretion. J. Clin. Invest. 95: 2297-2303.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2297-2303
    • Weyrich, A.S.1    McIntyre, T.M.2    McEver, R.P.3    Prescott, S.M.4    Zimmerman, G.A.5
  • 47
    • 0029595303 scopus 로고
    • P-selectin must extend a sufficient length from the plasma membrane to mediate rolling of neutrophils
    • Patel, K.D., M.U. Nollert, and R.P. McEver. 1995. P-selectin must extend a sufficient length from the plasma membrane to mediate rolling of neutrophils. J. Cell Biol. 131:1893-1902.
    • (1995) J. Cell Biol. , vol.131 , pp. 1893-1902
    • Patel, K.D.1    Nollert, M.U.2    McEver, R.P.3
  • 49
    • 0029152811 scopus 로고
    • Activation of polymorphonuclear leukocytes reduces their adhesion to P-selectin and causes redistribution of ligands for P-selectin on their surfaces
    • Lorant, D.E., R.P. McEver, T.M. McIntyre, K.L. Moore, S.M. Prescott, and G. A. Zimmerman. 1995. Activation of polymorphonuclear leukocytes reduces their adhesion to P-selectin and causes redistribution of ligands for P-selectin on their surfaces. J. Clin. Invest. 96:171-182.
    • (1995) J. Clin. Invest. , vol.96 , pp. 171-182
    • Lorant, D.E.1    McEver, R.P.2    McIntyre, T.M.3    Moore, K.L.4    Prescott, S.M.5    Zimmerman, G.A.6
  • 50
    • 0030064894 scopus 로고    scopus 로고
    • Chemoattractant-induced changes in surface expression and redistribution of a functional ligand for P-selectin on neutrophils
    • Doré, M., A.R. Burns, B.J. Hughes, M.L. Entman, and C.W. Smith. 1996. Chemoattractant-induced changes in surface expression and redistribution of a functional ligand for P-selectin on neutrophils. Blood. 87:2029-2037.
    • (1996) Blood , vol.87 , pp. 2029-2037
    • Doré, M.1    Burns, A.R.2    Hughes, B.J.3    Entman, M.L.4    Smith, C.W.5
  • 51
    • 0025939215 scopus 로고
    • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140
    • Picker, L.J., R.A. Warnock, A.R. Burns, C.M. Doerschuk, E.L. Berg, and B.C. Butcher. 1991. The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. Cell. 66:921-933.
    • (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, B.C.6
  • 52
    • 0028143514 scopus 로고
    • Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells
    • Bargatze, R.F., S. Kurk, E.C. Butcher, and M.A. Jutila. 1994. Neutrophils roll on adherent neutrophils bound to cytokine-induced endothelial cells via L-selectin on the rolling cells. J. Exp. Med. 180:1785-1792.
    • (1994) J. Exp. Med. , vol.180 , pp. 1785-1792
    • Bargatze, R.F.1    Kurk, S.2    Butcher, E.C.3    Jutila, M.A.4
  • 53
    • 0027217949 scopus 로고
    • β2-Integrin and L-selectin are obligatory receptors in neutrophil aggregation
    • Simon, S.I., Y.P. Rochon, E.B. Lynam, C.W. Smith, D.C. Anderson, and L.A. Sklar. 1993. β2-Integrin and L-selectin are obligatory receptors in neutrophil aggregation. Blood. 82:1097-1106.
    • (1993) Blood , vol.82 , pp. 1097-1106
    • Simon, S.I.1    Rochon, Y.P.2    Lynam, E.B.3    Smith, C.W.4    Anderson, D.C.5    Sklar, L.A.6
  • 54
    • 0029826160 scopus 로고    scopus 로고
    • Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow
    • Alon, R., R.C. Fuhlbrigge, E.B. Finger, and T.A. Springer. 1996. Interactions through L-selectin between leukocytes and adherent leukocytes nucleate rolling adhesions on selectins and VCAM-1 in shear flow. J. Cell Biol. 135: 849-865.
    • (1996) J. Cell Biol. , vol.135 , pp. 849-865
    • Alon, R.1    Fuhlbrigge, R.C.2    Finger, E.B.3    Springer, T.A.4
  • 55
    • 0029844407 scopus 로고    scopus 로고
    • Sialylated, fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions
    • Fuhlbrigge, R.C., R. Alon, K.D. Puri, J.B. Lowe, and T.A. Springer. 1996. Sialylated, fucosylated ligands for L-selectin expressed on leukocytes mediate tethering and rolling adhesions in physiologic flow conditions. J. Cell Biol. 135:837-848.
    • (1996) J. Cell Biol. , vol.135 , pp. 837-848
    • Fuhlbrigge, R.C.1    Alon, R.2    Puri, K.D.3    Lowe, J.B.4    Springer, T.A.5
  • 56
    • 0347303446 scopus 로고    scopus 로고
    • Myeloid cells roll on L-selectin: Evidence for mucin-like ligand activity on HL-60 cells distinct from P-selectin glycoprotein ligand-1
    • Abstr.
    • Ramos, C.L., B.B. Donell, K.S. Snapp, G.S. Kansas, K. Ley, and M.B. Lawrence. 1997. Myeloid cells roll on L-selectin: evidence for mucin-like ligand activity on HL-60 cells distinct from P-selectin glycoprotein ligand-1. FASEB (Fed. Am. Soc. Exp. Biol.) J. 11:A102. (Abstr.)
    • (1997) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.11
    • Ramos, C.L.1    Donell, B.B.2    Snapp, K.S.3    Kansas, G.S.4    Ley, K.5    Lawrence, M.B.6
  • 58
    • 0030894982 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 is essential for adhesion to P-selectin but not E-selectin in stably transfected hematopoietic cell lines
    • Snapp, K.R., A.J. Wagers, R. Craig, L.M. Stoolman, and G.S. Kansas. 1997. P-selectin glycoprotein ligand-1 is essential for adhesion to P-selectin but not E-selectin in stably transfected hematopoietic cell lines. Blood. 89:896-901.
    • (1997) Blood , vol.89 , pp. 896-901
    • Snapp, K.R.1    Wagers, A.J.2    Craig, R.3    Stoolman, L.M.4    Kansas, G.S.5
  • 59
    • 0030588551 scopus 로고    scopus 로고
    • E-selectin preferentially supports neutrophil but not eosinophil rolling under conditions of flow in vitro and in vivo
    • Sriramarao, P., C.R. Norton, P. Borgstrom, R.G. DiScipio, B.A. Wolitzky, and D.H. Broide. 1996. E-selectin preferentially supports neutrophil but not eosinophil rolling under conditions of flow in vitro and in vivo. J. Immunol. 157:4672-4680.
    • (1996) J. Immunol. , vol.157 , pp. 4672-4680
    • Sriramarao, P.1    Norton, C.R.2    Borgstrom, P.3    DiScipio, R.G.4    Wolitzky, B.A.5    Broide, D.H.6
  • 60
    • 0031148627 scopus 로고    scopus 로고
    • Cross-talk between cell adhesion molecules regulates the migration velocity of neutrophils
    • Rainger, G.E., C. Buckley, D.L. Simmons, and G.B. Nash. 1997. Cross-talk between cell adhesion molecules regulates the migration velocity of neutrophils. Curr. Biol. 7:316-325.
    • (1997) Curr. Biol. , vol.7 , pp. 316-325
    • Rainger, G.E.1    Buckley, C.2    Simmons, D.L.3    Nash, G.B.4
  • 62
  • 63
    • 0027933127 scopus 로고
    • Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule
    • Laudanna, C., G. Constantin, P. Baron, E. Scarpini, G. Scarlato, G. Cabrini, C. Dechecchi, F. Rossi, M.A. Cassatella, and G. Berton. 1994. Sulfatides trigger increase of cytosolic free calcium and enhanced expression of tumor necrosis factor-α and interleukin-8 mRNA in human neutrophils. Evidence for a role of L-selectin as a signaling molecule. J. Biol. Chem. 269:4021-4026.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4021-4026
    • Laudanna, C.1    Constantin, G.2    Baron, P.3    Scarpini, E.4    Scarlato, G.5    Cabrini, G.6    Dechecchi, C.7    Rossi, F.8    Cassatella, M.A.9    Berton, G.10
  • 64
    • 0028065619 scopus 로고
    • Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin
    • Waddell, T.K., L. Fialkow, C.K. Chan, T.K. Kishimoto, and G.P. Downey. 1994. Potentiation of the oxidative burst of human neutrophils. A signaling role for L-selectin. J. Biol. Chem. 269:18485-18491.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18485-18491
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 65
    • 0029904693 scopus 로고    scopus 로고
    • GlyCAM-1, a physiologic ligand for L-selectin, activates β2 integrins on naive peripheral lymphocytes
    • Hwang, S.T., M.S. Singer, P.A. Giblin, T.A. Yednock, K.B. Bacon, S.I. Simon, and S.D. Rosen. 1996. GlyCAM-1, a physiologic ligand for L-selectin, activates β2 integrins on naive peripheral lymphocytes. J. Exp. Med. 184:1343-1348.
    • (1996) J. Exp. Med. , vol.184 , pp. 1343-1348
    • Hwang, S.T.1    Singer, M.S.2    Giblin, P.A.3    Yednock, T.A.4    Bacon, K.B.5    Simon, S.I.6    Rosen, S.D.7
  • 67
    • 0029075155 scopus 로고
    • Signaling functions of L-selectin. Enhancement of tyrosine phosphorylation and activation of MAP kinase
    • Waddell, T.K., L. Fialkow, C.K. Chan, T.K. Kishimoto, and G.P. Downey. 1995. Signaling functions of L-selectin. Enhancement of tyrosine phosphorylation and activation of MAP kinase. J. Biol. Chem. 270:15403-15411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15403-15411
    • Waddell, T.K.1    Fialkow, L.2    Chan, C.K.3    Kishimoto, T.K.4    Downey, G.P.5
  • 69
    • 0028788963 scopus 로고
    • Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1
    • Norman, K.E., K.L. Moore, R.P. McEver, and K. Ley. 1995. Leukocyte rolling in vivo is mediated by P-selectin glycoprotein ligand-1. Blood. 86:4417-4421.
    • (1995) Blood , vol.86 , pp. 4417-4421
    • Norman, K.E.1    Moore, K.L.2    McEver, R.P.3    Ley, K.4
  • 70
    • 0030975020 scopus 로고    scopus 로고
    • The cytokine-adhesion molecule cascade in ischemia/reperfusion injury of the rat kidney. Inhibition by a soluble P-selectin ligand
    • Takada, M., K.C. Nadeau, G.D. Shaw, K.A. Marquette, and N.L. Tilney. 1997. The cytokine-adhesion molecule cascade in ischemia/reperfusion injury of the rat kidney. Inhibition by a soluble P-selectin ligand. J. Clin. Invest. 99:2682-2690.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2682-2690
    • Takada, M.1    Nadeau, K.C.2    Shaw, G.D.3    Marquette, K.A.4    Tilney, N.L.5


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