메뉴 건너뛰기




Volumn 14, Issue 5, 2002, Pages 581-586

Selectins: Lectins that initiate cell adhesion under flow

Author keywords

[No Author keywords available]

Indexed keywords

LECTIN; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE 1; RAF PROTEIN; RAS PROTEIN; SELECTIN;

EID: 0036775765     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00367-8     Document Type: Review
Times cited : (370)

References (50)
  • 1
    • 0032904627 scopus 로고    scopus 로고
    • Mechanisms that regulate the function of the selectins and their ligands
    • Vestweber D., Blanks J.E. Mechanisms that regulate the function of the selectins and their ligands. Physiol Rev. 79:1999;181-213.
    • (1999) Physiol Rev , vol.79 , pp. 181-213
    • Vestweber, D.1    Blanks, J.E.2
  • 2
    • 0034846702 scopus 로고    scopus 로고
    • Adhesive interactions of leukocytes, platelets, and the vessel wall during hemostasis and inflammation
    • McEver R.P. Adhesive interactions of leukocytes, platelets, and the vessel wall during hemostasis and inflammation. Thromb Haemost. 86:2001;746-756.
    • (2001) Thromb Haemost , vol.86 , pp. 746-756
    • McEver, R.P.1
  • 3
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to sLe(X) and PSGL-1
    • x bound to P- and E-selectin and of an amino-terminal glycosulfopeptide of PSGL-1 bound to P-selectin.
    • x bound to P- and E-selectin and of an amino-terminal glycosulfopeptide of PSGL-1 bound to P-selectin.
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 4
    • 0034910611 scopus 로고    scopus 로고
    • The α(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative control over selectin-dependent leukocyte recruitment and lymphocyte homing
    • This is a very careful study of the relative contributions of two α1,3-fucosyltransferases to leukocyte trafficking in vivo. Fuc-TVII is the dominant enzyme for constructing fucosylated selectin ligands, but Fuc-TIV also contributes.
    • Homeister J.W., Thall A.D., Petryniak B., Maly P., Rogers C.E., Smith P.L., Kelly R.J., Gersten K.M., Askari S.W., Cheng G.Y., et al. The α(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative control over selectin-dependent leukocyte recruitment and lymphocyte homing. Immunity. 15:2001;115-126. This is a very careful study of the relative contributions of two α1,3-fucosyltransferases to leukocyte trafficking in vivo. Fuc-TVII is the dominant enzyme for constructing fucosylated selectin ligands, but Fuc-TIV also contributes.
    • (2001) Immunity , vol.15 , pp. 115-126
    • Homeister, J.W.1    Thall, A.D.2    Petryniak, B.3    Maly, P.4    Rogers, C.E.5    Smith, P.L.6    Kelly, R.J.7    Gersten, K.M.8    Askari, S.W.9    Cheng, G.Y.10
  • 5
    • 0035801605 scopus 로고    scopus 로고
    • Fuc-TVII is required for T helper 1 and T cytotoxic 1 lymphocyte selectin ligand expression and recruitment in inflammation, and together with Fuc-TIV regulates naïve T cell trafficking to lymph nodes
    • This is similar in scope to Homeister et al. (2001) [4••], but focuses on the contributions of Fuc-TVII and Fuc-TIV to trafficking of naïve and effector T cells. Here too, Fuc-TVII has the dominant role.
    • Smithson G., Rogers C.E., Smith P.L., Scheidegger E.P., Petryniak B., Myers J.T., Kim D.S.L., Homeister J.W., Lowe J.B. Fuc-TVII is required for T helper 1 and T cytotoxic 1 lymphocyte selectin ligand expression and recruitment in inflammation, and together with Fuc-TIV regulates naïve T cell trafficking to lymph nodes. J Exp Med. 194:2001;601-614. This is similar in scope to Homeister et al. (2001) [4••], but focuses on the contributions of Fuc-TVII and Fuc-TIV to trafficking of naïve and effector T cells. Here too, Fuc-TVII has the dominant role.
    • (2001) J Exp Med , vol.194 , pp. 601-614
    • Smithson, G.1    Rogers, C.E.2    Smith, P.L.3    Scheidegger, E.P.4    Petryniak, B.5    Myers, J.T.6    Kim, D.S.L.7    Homeister, J.W.8    Lowe, J.B.9
  • 6
    • 0031029280 scopus 로고    scopus 로고
    • Selectin ligands: Will the real ones please stand up?
    • Varki A. Selectin ligands: will the real ones please stand up? J Clin Invest. 99:1997;158-162.
    • (1997) J Clin Invest , vol.99 , pp. 158-162
    • Varki, A.1
  • 7
    • 0030854107 scopus 로고    scopus 로고
    • Role of PSGL-1 binding to selectins in leukocyte recruitment
    • McEver R.P., Cummings R.D. Role of PSGL-1 binding to selectins in leukocyte recruitment. J Clin Invest. 100:1997;485-492.
    • (1997) J Clin Invest , vol.100 , pp. 485-492
    • McEver, R.P.1    Cummings, R.D.2
  • 9
    • 0034671746 scopus 로고    scopus 로고
    • Binding of glycosulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues
    • As in Leppänen et al. (2000), these authors use synthetic glycosulfopeptides modeled after the amino-terminal region of human PSGL-1. This approach circumvents the problems of heterogeneous post-translational modifications of glycoproteins expressed in cells and allows functional analysis of defined structures. Stereospecific placement of each tyrosine sulfate, peptide components and the sialic acid and fucose of a core-2 O-glycan are required for optimal binding to P-selectin.
    • Leppänen A., White S.P., Helin J., McEver R.P., Cummings R.D. Binding of glycosulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues. J Biol Chem. 275:2000;39569-39578. As in Leppänen et al. (2000) [8], these authors use synthetic glycosulfopeptides modeled after the amino-terminal region of human PSGL-1. This approach circumvents the problems of heterogeneous post-translational modifications of glycoproteins expressed in cells and allows functional analysis of defined structures. Stereospecific placement of each tyrosine sulfate, peptide components and the sialic acid and fucose of a core-2 O-glycan are required for optimal binding to P-selectin.
    • (2000) J Biol Chem , vol.275 , pp. 39569-39578
    • Leppänen, A.1    White, S.P.2    Helin, J.3    McEver, R.P.4    Cummings, R.D.5
  • 10
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins P.P., McEver R.P., Cummings R.D. Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J Biol Chem. 271:1996;18732-18742.
    • (1996) J Biol Chem , vol.271 , pp. 18732-18742
    • Wilkins, P.P.1    McEver, R.P.2    Cummings, R.D.3
  • 11
    • 0032428668 scopus 로고    scopus 로고
    • Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation
    • Ellies L.G., Tsuboi S., Petryniak B., Lowe J.B., Fukuda M., Marth J.D. Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation. Immunity. 9:1998;881-890.
    • (1998) Immunity , vol.9 , pp. 881-890
    • Ellies, L.G.1    Tsuboi, S.2    Petryniak, B.3    Lowe, J.B.4    Fukuda, M.5    Marth, J.D.6
  • 12
    • 0035877986 scopus 로고    scopus 로고
    • Severe impairment of leukocyte rolling in venules of core 2 glucosaminyltransferase-deficient mice
    • This work demonstrates that Core2GlcNAcT-I is required for construction of P-selectin ligands and some E-selectin ligands in vivo.
    • Sperandio M., Thatte A., Foy D., Ellies L.G., Marth J.D., Ley K. Severe impairment of leukocyte rolling in venules of core 2 glucosaminyltransferase-deficient mice. Blood. 97:2001;3812-3819. This work demonstrates that Core2GlcNAcT-I is required for construction of P-selectin ligands and some E-selectin ligands in vivo.
    • (2001) Blood , vol.97 , pp. 3812-3819
    • Sperandio, M.1    Thatte, A.2    Foy, D.3    Ellies, L.G.4    Marth, J.D.5    Ley, K.6
  • 13
    • 0033847258 scopus 로고    scopus 로고
    • Carbohydrate sulfotransferases in lymphocyte homing
    • Hemmerich S., Rosen S.D. Carbohydrate sulfotransferases in lymphocyte homing. Glycobiology. 10:2000;849-856.
    • (2000) Glycobiology , vol.10 , pp. 849-856
    • Hemmerich, S.1    Rosen, S.D.2
  • 14
    • 0035930560 scopus 로고    scopus 로고
    • Carbohydrate-modifying sulfotransferases: Structure, function and pathophysiology
    • Fukuda M., Hiraoka N., Akama T.O., Fukuda M.N. Carbohydrate-modifying sulfotransferases: structure, function and pathophysiology. J Biol Chem. 276:2001;47747-47750.
    • (2001) J Biol Chem , vol.276 , pp. 47747-47750
    • Fukuda, M.1    Hiraoka, N.2    Akama, T.O.3    Fukuda, M.N.4
  • 15
    • 0033523721 scopus 로고    scopus 로고
    • Sulfation of a high endothelial venule-expressed ligand for L-selectin: Effects on tethering and rolling of lymphocytes
    • Tangemann K., Bistrup A., Hemmerich S., Rosen S.D. Sulfation of a high endothelial venule-expressed ligand for L-selectin: effects on tethering and rolling of lymphocytes. J Exp Med. 190:1999;935-941.
    • (1999) J Exp Med , vol.190 , pp. 935-941
    • Tangemann, K.1    Bistrup, A.2    Hemmerich, S.3    Rosen, S.D.4
  • 18
    • 17944382137 scopus 로고    scopus 로고
    • Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes
    • Genetic deletion of an high endothelial venule (HEV)-restricted N-acetylglucosamine-6-O-sulfotransferase markedly reduces homing of lymphocytes to lymph nodes. Residual L-selectin ligands on the lumenal and ablumenal aspects of HEV in the sulfotransferase-deficient mice are revealed.
    • Hemmerich S., Bistrup A., Singer M.S., van Zante A., Lee J.K., Tsay D., Peters M., Carminati J.L., Brennan T.J., Carver-Moore K., et al. Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes. Immunity. 15:2001;237-247. Genetic deletion of an high endothelial venule (HEV)-restricted N-acetylglucosamine-6-O-sulfotransferase markedly reduces homing of lymphocytes to lymph nodes. Residual L-selectin ligands on the lumenal and ablumenal aspects of HEV in the sulfotransferase-deficient mice are revealed.
    • (2001) Immunity , vol.15 , pp. 237-247
    • Hemmerich, S.1    Bistrup, A.2    Singer, M.S.3    Van Zante, A.4    Lee, J.K.5    Tsay, D.6    Peters, M.7    Carminati, J.L.8    Brennan, T.J.9    Carver-Moore, K.10
  • 20
    • 0035881534 scopus 로고    scopus 로고
    • Differential requirements for core 2 glucosaminyltransferase for endothelial L-selectin ligand function in vivo
    • Sperandio M., Forlow S.B., Thatte J., Ellies L.G., Marth J.D., Ley K. Differential requirements for core 2 glucosaminyltransferase for endothelial L-selectin ligand function in vivo. J Immunol. 167:2001;2268-2274.
    • (2001) J Immunol , vol.167 , pp. 2268-2274
    • Sperandio, M.1    Forlow, S.B.2    Thatte, J.3    Ellies, L.G.4    Marth, J.D.5    Ley, K.6
  • 21
    • 0034610327 scopus 로고    scopus 로고
    • A distinct glycoform of CD44 is an L-selectin ligand on human hematopoietic cells
    • Dimitroff C.J., Lee J.Y., Fuhlbrigge R.C., Sackstein R. A distinct glycoform of CD44 is an L-selectin ligand on human hematopoietic cells. Proc Natl Acad Sci USA. 97:2000;13841-13846.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13841-13846
    • Dimitroff, C.J.1    Lee, J.Y.2    Fuhlbrigge, R.C.3    Sackstein, R.4
  • 22
    • 0035844880 scopus 로고    scopus 로고
    • CD44 is a major E-selectin ligand on human hematopoietic progenitor cells
    • Dimitroff C.J., Lee J.Y., Rafii S., Fuhlbrigge R.C., Sackstein R. CD44 is a major E-selectin ligand on human hematopoietic progenitor cells. J Cell Biol. 153:2001;1277-1286.
    • (2001) J Cell Biol , vol.153 , pp. 1277-1286
    • Dimitroff, C.J.1    Lee, J.Y.2    Rafii, S.3    Fuhlbrigge, R.C.4    Sackstein, R.5
  • 23
    • 0036218902 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1-deficient mice have impaired leukocyte tethering to E-selectin under flow
    • PSGL1deficient leukocytes tether poorly to E-selectin. The residual cells that do tether roll normally, revealing separable functions for E-selectin ligands in tethering and rolling. This is the first demonstration of a glycoprotein ligand that mediates physiologically relevant interactions with E-selectin.
    • Xia L., Sperandio M., Yago T., McDaniel J.M., Cummings R.D., Pearson-White S., Ley K., McEver R.P. P-selectin glycoprotein ligand-1-deficient mice have impaired leukocyte tethering to E-selectin under flow. J Clin Invest. 109:2002;939-950. PSGL1deficient leukocytes tether poorly to E-selectin. The residual cells that do tether roll normally, revealing separable functions for E-selectin ligands in tethering and rolling. This is the first demonstration of a glycoprotein ligand that mediates physiologically relevant interactions with E-selectin.
    • (2002) J Clin Invest , vol.109 , pp. 939-950
    • Xia, L.1    Sperandio, M.2    Yago, T.3    McDaniel, J.M.4    Cummings, R.D.5    Pearson-White, S.6    Ley, K.7    McEver, R.P.8
  • 24
    • 0035853111 scopus 로고    scopus 로고
    • Heparin and cancer revisited: Mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis
    • Demonstrates that P-selectin on platelets promotes experimental tumor metastasis to lung by binding to mucins on the tumor cell surface. Integrates these data with diverse previous observations suggesting that platelets and mucins contribute to tumor metastasis in humans.
    • Borsig L., Wong R., Feramisco J., Nadeau D.R., Varki N.M., Varki A. Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis. Proc Natl Acad Sci USA. 98:2001;3352-3357. Demonstrates that P-selectin on platelets promotes experimental tumor metastasis to lung by binding to mucins on the tumor cell surface. Integrates these data with diverse previous observations suggesting that platelets and mucins contribute to tumor metastasis in humans.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3352-3357
    • Borsig, L.1    Wong, R.2    Feramisco, J.3    Nadeau, D.R.4    Varki, N.M.5    Varki, A.6
  • 25
    • 0037133173 scopus 로고    scopus 로고
    • Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis
    • Borsig L., Wong R., Hynes R.O., Varki N.M., Varki A. Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis. Proc Natl Acad Sci USA. 99:2002;2193-2198.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2193-2198
    • Borsig, L.1    Wong, R.2    Hynes, R.O.3    Varki, N.M.4    Varki, A.5
  • 26
    • 0035885941 scopus 로고    scopus 로고
    • P-selectin mediates the adhesion of sickle erythrocytes to the endothelium
    • Matsui N.M., Borsig L., Rosen S.D., Yaghmai M., Varki A., Embury S.H. P-selectin mediates the adhesion of sickle erythrocytes to the endothelium. Blood. 98:2001;1955-1962.
    • (2001) Blood , vol.98 , pp. 1955-1962
    • Matsui, N.M.1    Borsig, L.2    Rosen, S.D.3    Yaghmai, M.4    Varki, A.5    Embury, S.H.6
  • 27
    • 0037022684 scopus 로고    scopus 로고
    • Primary role for adherent leukocytes in sickle cell vascular occlusion: A new paradigm
    • Using a murine model of sickle cell anemia, the authors show that vaso-occlusive episodes involve interactions of sickle erythrocytes with leukocytes that adhere to inflamed endothelial cells through selectins.
    • Turhan A., Weiss L.A., Mohandas N., Coller B.S., Frenette P.S. Primary role for adherent leukocytes in sickle cell vascular occlusion: a new paradigm. Proc Natl Acad Sci USA. 99:2002;3047-3051. Using a murine model of sickle cell anemia, the authors show that vaso-occlusive episodes involve interactions of sickle erythrocytes with leukocytes that adhere to inflamed endothelial cells through selectins.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3047-3051
    • Turhan, A.1    Weiss, L.A.2    Mohandas, N.3    Coller, B.S.4    Frenette, P.S.5
  • 28
    • 0034665671 scopus 로고    scopus 로고
    • Synergism of multiple adhesion molecules in mediating cytoadherence of Plasmodium falciparum-infected erythrocytes to microvascular endothelial cells under flow
    • Yipp B.G., Anand S., Schollaardt T., Patel K.D., Looareesuwan S., Ho M. Synergism of multiple adhesion molecules in mediating cytoadherence of Plasmodium falciparum-infected erythrocytes to microvascular endothelial cells under flow. Blood. 96:2000;2292-2298.
    • (2000) Blood , vol.96 , pp. 2292-2298
    • Yipp, B.G.1    Anand, S.2    Schollaardt, T.3    Patel, K.D.4    Looareesuwan, S.5    Ho, M.6
  • 29
    • 0034595997 scopus 로고    scopus 로고
    • Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1
    • Herron M.J., Nelson C.M., Larson J., Snapp K.R., Kansas G.S., Goodman J.L. Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1. Science. 288:2000;1653-1656.
    • (2000) Science , vol.288 , pp. 1653-1656
    • Herron, M.J.1    Nelson, C.M.2    Larson, J.3    Snapp, K.R.4    Kansas, G.S.5    Goodman, J.L.6
  • 30
    • 0032483992 scopus 로고    scopus 로고
    • Affinity and kinetic analysis of P-selectin binding to P-selectin glycoprotein ligand-1
    • Mehta P., Cummings R.D., McEver R.P. Affinity and kinetic analysis of P-selectin binding to P-selectin glycoprotein ligand-1. J Biol Chem. 273:1998;32506-32513.
    • (1998) J Biol Chem , vol.273 , pp. 32506-32513
    • Mehta, P.1    Cummings, R.D.2    McEver, R.P.3
  • 31
    • 0031975762 scopus 로고    scopus 로고
    • Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1
    • Nicholson M.W., Barclay A.N., Singer M.S., Rosen S.D., Van der Merwe P.A. Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1. J Biol Chem. 273:1998;763-770.
    • (1998) J Biol Chem , vol.273 , pp. 763-770
    • Nicholson, M.W.1    Barclay, A.N.2    Singer, M.S.3    Rosen, S.D.4    Van der Merwe, P.A.5
  • 32
    • 0035943656 scopus 로고    scopus 로고
    • Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1
    • Wild M.K., Huang M.C., Schulze-Horsel U., van Der Merwe P.A., Vestweber D. Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1. J Biol Chem. 276:2001;31602-31612.
    • (2001) J Biol Chem , vol.276 , pp. 31602-31612
    • Wild, M.K.1    Huang, M.C.2    Schulze-Horsel, U.3    Van Der Merwe, P.A.4    Vestweber, D.5
  • 33
    • 0033545206 scopus 로고    scopus 로고
    • An automatic braking system that stabilizes leukocyte rolling by an increase in selectin bond number with shear
    • Chen S.Q., Springer T.A. An automatic braking system that stabilizes leukocyte rolling by an increase in selectin bond number with shear. J Cell Biol. 144:1999;185-200.
    • (1999) J Cell Biol , vol.144 , pp. 185-200
    • Chen, S.Q.1    Springer, T.A.2
  • 34
    • 0033457348 scopus 로고    scopus 로고
    • Influence of cell deformation on leukocyte rolling adhesion in shear flow
    • Lei X., Lawrence M.B., Dong C. Influence of cell deformation on leukocyte rolling adhesion in shear flow. J Biomech Eng. 121:1999;636-643.
    • (1999) J Biomech Eng , vol.121 , pp. 636-643
    • Lei, X.1    Lawrence, M.B.2    Dong, C.3
  • 35
    • 0034192454 scopus 로고    scopus 로고
    • Direct observation of membrane tethers formed during neutrophil attachment to platelets or P-selectin under physiological flow
    • Using high-speed, high-resolution videomicroscopy, the authors visualized the rapid formation and breakage of long membrane tethers at adhesive contacts between rolling neutrophils and P-selectin. This may be an important mechanism to stabilize rolling by reducing the force applied to adhesive contacts.
    • Schmidtke D.W., Diamond S.L. Direct observation of membrane tethers formed during neutrophil attachment to platelets or P-selectin under physiological flow. J Cell Biol. 149:2000;719-729. Using high-speed, high-resolution videomicroscopy, the authors visualized the rapid formation and breakage of long membrane tethers at adhesive contacts between rolling neutrophils and P-selectin. This may be an important mechanism to stabilize rolling by reducing the force applied to adhesive contacts.
    • (2000) J Cell Biol , vol.149 , pp. 719-729
    • Schmidtke, D.W.1    Diamond, S.L.2
  • 36
    • 0035964311 scopus 로고    scopus 로고
    • Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow
    • Using dimeric and monomeric forms of P-selectin and PSGL-1, the authors show that dimerization of these molecules strengthens tethers of rolling cells. The data indicate that transient adhesive tethers may have more than one bond, suggesting that the mechanical strengths of single selectin-ligand bonds may be less than the initial estimates.
    • Ramachandran V., Yago T., Epperson T.K., Kobzdej M.M.A., Nollert M.U., Cummings R.D., Zhu C., McEver R.P. Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow. Proc Natl Acad Sci USA. 98:2001;10166-10171. Using dimeric and monomeric forms of P-selectin and PSGL-1, the authors show that dimerization of these molecules strengthens tethers of rolling cells. The data indicate that transient adhesive tethers may have more than one bond, suggesting that the mechanical strengths of single selectin-ligand bonds may be less than the initial estimates.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10166-10171
    • Ramachandran, V.1    Yago, T.2    Epperson, T.K.3    Kobzdej, M.M.A.4    Nollert, M.U.5    Cummings, R.D.6    Zhu, C.7    McEver, R.P.8
  • 38
    • 0034705388 scopus 로고    scopus 로고
    • An activated L-selectin mutant with conserved equilibrium binding properties but enhanced ligand recognition under shear flow
    • A very interesting study of a chimeric L-selectin protein, which suggests that subtle alterations in the orientation of the lectin domain of L-selectin affect the ability to interact with cell-surface ligands under flow.
    • Dwir O., Kansas G.S., Alon R. An activated L-selectin mutant with conserved equilibrium binding properties but enhanced ligand recognition under shear flow. J Biol Chem. 275:2000;18682-18691. A very interesting study of a chimeric L-selectin protein, which suggests that subtle alterations in the orientation of the lectin domain of L-selectin affect the ability to interact with cell-surface ligands under flow.
    • (2000) J Biol Chem , vol.275 , pp. 18682-18691
    • Dwir, O.1    Kansas, G.S.2    Alon, R.3
  • 39
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
    • Pavalko F.M., Walker D.M., Graham L., Goheen M., Doerschuk C.M., Kansas G.S. The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: receptor positioning in microvilli does not require interaction with α-actinin. J Cell Biol. 129:1995;1155-1164.
    • (1995) J Cell Biol , vol.129 , pp. 1155-1164
    • Pavalko, F.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 40
    • 0037127291 scopus 로고    scopus 로고
    • The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixin-moesin (ERM) family of proteins
    • Ivetic A., Deka J., Ridley A., Ager A. The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixin-moesin (ERM) family of proteins. J Biol Chem. 277:2002;2321-2329.
    • (2002) J Biol Chem , vol.277 , pp. 2321-2329
    • Ivetic, A.1    Deka, J.2    Ridley, A.3    Ager, A.4
  • 41
    • 0035494494 scopus 로고    scopus 로고
    • Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether
    • A very thorough study of the rolling of transfected cells expressing L-selectin with a partial truncation or a complete deletion of the cytoplasmic domain. Cytoplasmic anchorage strengthens adhesive tethers, probably by favoring bond clusters, which may also be favored by dimerization of a selectin or its ligand [36•].
    • Dwir O., Kansas G.S., Alon R. Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether. J Cell Biol. 155:2001;145-156. A very thorough study of the rolling of transfected cells expressing L-selectin with a partial truncation or a complete deletion of the cytoplasmic domain. Cytoplasmic anchorage strengthens adhesive tethers, probably by favoring bond clusters, which may also be favored by dimerization of a selectin or its ligand [36•] .
    • (2001) J Cell Biol , vol.155 , pp. 145-156
    • Dwir, O.1    Kansas, G.S.2    Alon, R.3
  • 42
    • 0027509819 scopus 로고
    • Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin
    • Kansas G.S., Ley K., Munro J.M., Tedder T.F. Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin. J Exp Med. 177:1993;833-838.
    • (1993) J Exp Med , vol.177 , pp. 833-838
    • Kansas, G.S.1    Ley, K.2    Munro, J.M.3    Tedder, T.F.4
  • 43
    • 0037097835 scopus 로고    scopus 로고
    • Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin
    • Snapp K.R., Heitzig C.E., Kansas G.S. Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Blood. 99:2002;4494-4502.
    • (2002) Blood , vol.99 , pp. 4494-4502
    • Snapp, K.R.1    Heitzig, C.E.2    Kansas, G.S.3
  • 45
    • 0035478705 scopus 로고    scopus 로고
    • Immobilized IL-8 triggers progressive activation of neutrophils rolling in vitro on P-selectin and intercellular adhesion molecule-1
    • DiVietro J.A., Smith M.J., Smith B.R., Petruzzelli L., Larson R.S., Lawrence M.B. Immobilized IL-8 triggers progressive activation of neutrophils rolling in vitro on P-selectin and intercellular adhesion molecule-1. J Immunol. 167:2001;4017-4025.
    • (2001) J Immunol , vol.167 , pp. 4017-4025
    • DiVietro, J.A.1    Smith, M.J.2    Smith, B.R.3    Petruzzelli, L.4    Larson, R.S.5    Lawrence, M.B.6
  • 46
    • 0037036443 scopus 로고    scopus 로고
    • Endothelial chemokines destabilize L-selectin-mediated lymphocyte rolling without inducing selectin shedding
    • Lymphocytes roll less stably on L-selectin after encountering immobilized chemokine, suggesting that chemokine engagement subtly impairs the cell-surface presentation of L-selectin. This may be a mechanism to assist transition from selectin-dependent to integrin-dependent adhesion.
    • Grabovsky V., Dwir O., Alon R. Endothelial chemokines destabilize L-selectin-mediated lymphocyte rolling without inducing selectin shedding. J Biol Chem. 277:2002;20640-20650. Lymphocytes roll less stably on L-selectin after encountering immobilized chemokine, suggesting that chemokine engagement subtly impairs the cell-surface presentation of L-selectin. This may be a mechanism to assist transition from selectin-dependent to integrin-dependent adhesion.
    • (2002) J Biol Chem , vol.277 , pp. 20640-20650
    • Grabovsky, V.1    Dwir, O.2    Alon, R.3
  • 47
    • 85031383211 scopus 로고    scopus 로고
    • Integration of inflammatory signals by rolling neutrophils
    • in press
    • Ley K: Integration of inflammatory signals by rolling neutrophils. Immunol Rev, in press.A very thoughtful and comprehensive review of the available information on the conversion from rolling to firm adhesion of leukocytes on vascular surfaces. The author presents an interesting case for the importance of integration of signals through adhesion molecules and chemokine receptors as the cell rolls. This may be particularly important for neutrophils.
    • Immunol Rev
    • Ley, K.1
  • 48
    • 0035964340 scopus 로고    scopus 로고
    • Cell adhesion regulates gene expression at translational checkpoints in human myeloid leukocytes
    • Adhesion of myeloid cells to P-selectin initiates a novel signaling mechanism that involves translational control of protein synthesis from pre-formed mRNAs. This provides a rapid mechanism to alter protein expression on emigrating leukocytes.
    • Mahoney T.S., Weyrich A.S., Dixon D.A., McIntyre T., Prescott S.M., Zimmerman G.A. Cell adhesion regulates gene expression at translational checkpoints in human myeloid leukocytes. Proc Natl Acad Sci USA. 98:2001;10284-10289. Adhesion of myeloid cells to P-selectin initiates a novel signaling mechanism that involves translational control of protein synthesis from pre-formed mRNAs. This provides a rapid mechanism to alter protein expression on emigrating leukocytes.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10284-10289
    • Mahoney, T.S.1    Weyrich, A.S.2    Dixon, D.A.3    McIntyre, T.4    Prescott, S.M.5    Zimmerman, G.A.6
  • 49
    • 0035930591 scopus 로고    scopus 로고
    • Molecular events in transmembrane signaling via E-selectin-SHP2 association, adaptor protein complex formation and ERK1/2 activation
    • Hu Y.Y., Szente B., Kiely J.M., Gimbrone M.A. Jr. Molecular events in transmembrane signaling via E-selectin-SHP2 association, adaptor protein complex formation and ERK1/2 activation. J Biol Chem. 276:2001;48549-48553.
    • (2001) J Biol Chem , vol.276 , pp. 48549-48553
    • Hu, Y.Y.1    Szente, B.2    Kiely, J.M.3    Gimbrone M.A., Jr.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.