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Vestweber D., Blanks J.E. Mechanisms that regulate the function of the selectins and their ligands. Physiol Rev. 79:1999;181-213.
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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
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x bound to P- and E-selectin and of an amino-terminal glycosulfopeptide of PSGL-1 bound to P-selectin.
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x bound to P- and E-selectin and of an amino-terminal glycosulfopeptide of PSGL-1 bound to P-selectin.
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Somers, W.S.1
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0034910611
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The α(1,3)fucosyltransferases FucT-IV and FucT-VII exert collaborative control over selectin-dependent leukocyte recruitment and lymphocyte homing
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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.
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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.
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Immunity
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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
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5
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0035801605
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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
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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.
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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.
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J Exp Med
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Smithson, G.1
Rogers, C.E.2
Smith, P.L.3
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Petryniak, B.5
Myers, J.T.6
Kim, D.S.L.7
Homeister, J.W.8
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Varki A. Selectin ligands: will the real ones please stand up? J Clin Invest. 99:1997;158-162.
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McEver R.P., Cummings R.D. Role of PSGL-1 binding to selectins in leukocyte recruitment. J Clin Invest. 100:1997;485-492.
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McEver, R.P.1
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A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin
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Leppänen A., Mehta P., Ouyang Y.-B., Ju T., Helin J., Moore K.L., van Die I., Canfield W.M., McEver R.P., Cummings R.D. A novel glycosulfopeptide binds to P-selectin and inhibits leukocyte adhesion to P-selectin. J Biol Chem. 274:1999;24838-24848.
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Leppänen, A.1
Mehta, P.2
Ouyang, Y.-B.3
Ju, T.4
Helin, J.5
Moore, K.L.6
Van Die, I.7
Canfield, W.M.8
McEver, R.P.9
Cummings, R.D.10
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9
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0034671746
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Binding of glycosulfopeptides to P-selectin requires stereospecific contributions of individual tyrosine sulfate and sugar residues
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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.
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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.
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J Biol Chem
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Leppänen, A.1
White, S.P.2
Helin, J.3
McEver, R.P.4
Cummings, R.D.5
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10
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0029763034
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Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
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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.
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Wilkins, P.P.1
McEver, R.P.2
Cummings, R.D.3
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11
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0032428668
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Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands essential for leukocyte homing and inflammation
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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.
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Ellies, L.G.1
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Lowe, J.B.4
Fukuda, M.5
Marth, J.D.6
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12
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0035877986
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Severe impairment of leukocyte rolling in venules of core 2 glucosaminyltransferase-deficient mice
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This work demonstrates that Core2GlcNAcT-I is required for construction of P-selectin ligands and some E-selectin ligands in vivo.
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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.
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Sperandio, M.1
Thatte, A.2
Foy, D.3
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Hemmerich S., Rosen S.D. Carbohydrate sulfotransferases in lymphocyte homing. Glycobiology. 10:2000;849-856.
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14
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0035930560
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Carbohydrate-modifying sulfotransferases: Structure, function and pathophysiology
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Fukuda M., Hiraoka N., Akama T.O., Fukuda M.N. Carbohydrate-modifying sulfotransferases: structure, function and pathophysiology. J Biol Chem. 276:2001;47747-47750.
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Fukuda, M.1
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Akama, T.O.3
Fukuda, M.N.4
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15
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0033523721
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Sulfation of a high endothelial venule-expressed ligand for L-selectin: Effects on tethering and rolling of lymphocytes
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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.
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Tangemann, K.1
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16
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0033577873
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Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin
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Bistrup A., Bhakta S., Lee J.K., Belov Y.Y., Gunn M.D., Zuo F.R., Huang C.C., Kannagi R., Rosen S.D., Hemmerich S. Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin. J Cell Biol. 145:1999;899-910.
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Bistrup, A.1
Bhakta, S.2
Lee, J.K.3
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Zuo, F.R.6
Huang, C.C.7
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Rosen, S.D.9
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x, an L-selectin ligand displayed by CD34
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x, an L-selectin ligand displayed by CD34. Immunity. 11:1999;79-89.
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Hiraoka, N.1
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Tsuboi, S.4
Suzuki, M.5
Yeh, J.C.6
Izawa, D.7
Tanaka, T.8
Miyasaka, M.9
Lowe, J.B.10
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18
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17944382137
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Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes
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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.
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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.
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Immunity
, vol.15
, pp. 237-247
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Hemmerich, S.1
Bistrup, A.2
Singer, M.S.3
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Lee, J.K.5
Tsay, D.6
Peters, M.7
Carminati, J.L.8
Brennan, T.J.9
Carver-Moore, K.10
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19
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0035967869
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Novel sulfated lymphocyte homing receptors and their control by a core 1 extension beta 1,3-N-acetylglucosaminyltransferase
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x on extended core-1 O-glycans, which bind L-selectin.
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x on extended core-1 O-glycans, which bind L-selectin.
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(2001)
Cell
, vol.105
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Yeh, J.C.1
Hiraoka, N.2
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Hindsgaul, O.7
Marth, J.D.8
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20
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0035881534
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Differential requirements for core 2 glucosaminyltransferase for endothelial L-selectin ligand function in vivo
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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.
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Sperandio, M.1
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Ellies, L.G.4
Marth, J.D.5
Ley, K.6
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22
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0035844880
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CD44 is a major E-selectin ligand on human hematopoietic progenitor cells
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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.
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J Cell Biol
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Dimitroff, C.J.1
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Rafii, S.3
Fuhlbrigge, R.C.4
Sackstein, R.5
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23
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0036218902
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P-selectin glycoprotein ligand-1-deficient mice have impaired leukocyte tethering to E-selectin under flow
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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.
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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.
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(2002)
J Clin Invest
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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
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24
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0035853111
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Heparin and cancer revisited: Mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis
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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.
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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.
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(2001)
Proc Natl Acad Sci USA
, vol.98
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Borsig, L.1
Wong, R.2
Feramisco, J.3
Nadeau, D.R.4
Varki, N.M.5
Varki, A.6
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25
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0037133173
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Synergistic effects of L- and P-selectin in facilitating tumor metastasis can involve non-mucin ligands and implicate leukocytes as enhancers of metastasis
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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.
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Borsig, L.1
Wong, R.2
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Varki, N.M.4
Varki, A.5
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26
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0035885941
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P-selectin mediates the adhesion of sickle erythrocytes to the endothelium
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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.
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Matsui, N.M.1
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Varki, A.5
Embury, S.H.6
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27
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0037022684
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Primary role for adherent leukocytes in sickle cell vascular occlusion: A new paradigm
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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.
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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.
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Proc Natl Acad Sci USA
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Turhan, A.1
Weiss, L.A.2
Mohandas, N.3
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28
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0034665671
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Synergism of multiple adhesion molecules in mediating cytoadherence of Plasmodium falciparum-infected erythrocytes to microvascular endothelial cells under flow
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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.
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Blood
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Yipp, B.G.1
Anand, S.2
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Looareesuwan, S.5
Ho, M.6
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29
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0034595997
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Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1
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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.
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Affinity and kinetic analysis of P-selectin binding to P-selectin glycoprotein ligand-1
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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.
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Mehta, P.1
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31
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0031975762
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Affinity and kinetic analysis of L-selectin (CD62L) binding to glycosylation-dependent cell-adhesion molecule-1
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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.
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32
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0035943656
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Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1
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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.
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Wild, M.K.1
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0033545206
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An automatic braking system that stabilizes leukocyte rolling by an increase in selectin bond number with shear
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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.
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Chen, S.Q.1
Springer, T.A.2
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Influence of cell deformation on leukocyte rolling adhesion in shear flow
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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.
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35
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0034192454
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Direct observation of membrane tethers formed during neutrophil attachment to platelets or P-selectin under physiological flow
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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.
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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.
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J Cell Biol
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Schmidtke, D.W.1
Diamond, S.L.2
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36
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0035964311
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Dimerization of a selectin and its ligand stabilizes cell rolling and enhances tether strength in shear flow
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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.
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(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 10166-10171
-
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Ramachandran, V.1
Yago, T.2
Epperson, T.K.3
Kobzdej, M.M.A.4
Nollert, M.U.5
Cummings, R.D.6
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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.
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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.
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The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via α-actinin: Receptor positioning in microvilli does not require interaction with α-actinin
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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.
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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•].
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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.
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Endothelial chemokines destabilize L-selectin-mediated lymphocyte rolling without inducing selectin shedding
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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.
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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.
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Integration of inflammatory signals by rolling neutrophils
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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.
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Ley, K.1
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0035964340
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Cell adhesion regulates gene expression at translational checkpoints in human myeloid leukocytes
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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.
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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.
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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.
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50
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Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow
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Yago T, Leppänen A, Qiu H, Marcus WD, Nollert MU, Zhu C, Cummings RD, McEver RP: Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow. J Cell Biol 2002, in press.
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