메뉴 건너뛰기




Volumn 147, Issue 3, 1999, Pages 467-470

C-type lectins and Sialyl Lewis X oligosaccharides: Versatile roles in cell-cell interaction

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; LECTIN; OLIGOSACCHARIDE; SIALIC ACID DERIVATIVE;

EID: 0033229717     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.3.467     Document Type: Short Survey
Times cited : (113)

References (36)
  • 2
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell, G., and J. Harford. 1982. Carbohydrate-specific receptors of the liver. Ann. Rev. Biochem. 51:531-554.
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 3
    • 0030963839 scopus 로고    scopus 로고
    • The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, hind tenascin-R by protein-protein interactions independent of carbohydrate moiety
    • Aspberg, A., R. Miura, S. Bourdoulous, M. Shimonaka, D. Heinegard, M. Schachner, E. Ruoslahti, and Y. Yamaguchi. 1997. The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, hind tenascin-R by protein-protein interactions independent of carbohydrate moiety. Proc. Natl. Acad. Sci. USA. 94:10116-10121.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10116-10121
    • Aspberg, A.1    Miura, R.2    Bourdoulous, S.3    Shimonaka, M.4    Heinegard, D.5    Schachner, M.6    Ruoslahti, E.7    Yamaguchi, Y.8
  • 4
    • 0028863975 scopus 로고
    • Sulfated disaccharide inhibitors of L-selectin: Deriving structural leads from a physiological selectin ligand
    • Bertozzi, C.R., S. Fukuda, and S.D. Rosen. 1995. Sulfated disaccharide inhibitors of L-selectin: deriving structural leads from a physiological selectin ligand. Biochemistry. 34:14271-14278.
    • (1995) Biochemistry , vol.34 , pp. 14271-14278
    • Bertozzi, C.R.1    Fukuda, S.2    Rosen, S.D.3
  • 5
    • 0026662007 scopus 로고
    • Expression cloning of a cDNA encoding UDP-GlcNAc:Galβ1-3-GalNAc-R (GlcNAc to GalNAc) β1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen
    • Bierhuizen, M.F., and M. Fukuda. 1992. Expression cloning of a cDNA encoding UDP-GlcNAc:Galβ1-3-GalNAc-R (GlcNAc to GalNAc) β1-6GlcNAc transferase by gene transfer into CHO cells expressing polyoma large tumor antigen. Proc. Natl. Acad. Sci. USA. 89:9326-9330.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9326-9330
    • Bierhuizen, M.F.1    Fukuda, M.2
  • 7
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher, E.C., and L.J. Picker. 1996. Lymphocyte homing and homeostasis. Science. 272:60-66.
    • (1996) Science , vol.272 , pp. 60-66
    • Butcher, E.C.1    Picker, L.J.2
  • 8
    • 0032498546 scopus 로고    scopus 로고
    • L-selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules
    • Clark, R.A., R.C. Fuhlbrigge, and T.A. Springer. 1998. L-Selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules. J. Cell Biol. 140:721-731.
    • (1998) J. Cell Biol. , vol.140 , pp. 721-731
    • Clark, R.A.1    Fuhlbrigge, R.C.2    Springer, T.A.3
  • 9
    • 0002535419 scopus 로고
    • Molecular structure of animal lectins
    • M. Fukuda and O. Hindsgaul, editors. Oxford University Press, Oxford, U.K.
    • Drickamer, K. 1994. Molecular structure of animal lectins. In Molecular Glycobiology. M. Fukuda and O. Hindsgaul, editors. Oxford University Press, Oxford, U.K. 53-87.
    • (1994) Molecular Glycobiology , pp. 53-87
    • Drickamer, K.1
  • 10
    • 0032428668 scopus 로고    scopus 로고
    • Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands participating in leukocyte homing and inflammation
    • Ellies, L.G., S. Tsuboi, B. Petryniak, J.B. Lowe, M. Fukuda, and J.D. Marth. 1998. Core 2 oligosaccharide biosynthesis distinguishes between selectin ligands participating in leukocyte homing and inflammation. Immunity. 9:881-890.
    • (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
  • 11
    • 0021999503 scopus 로고
    • Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens
    • Feizi, T. 1985. Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens. Nature. 314:53-57.
    • (1985) Nature , vol.314 , pp. 53-57
    • Feizi, T.1
  • 12
    • 0021611610 scopus 로고
    • Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes
    • Fukuda, M., E. Spooncer, J.E. Oates, A. Dell, and J.C. Klock. 1984. Structure of sialylated fucosyl lactosaminoglycan isolated from human granulocytes. J. Biol. Chem. 259:10925-10935.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10925-10935
    • Fukuda, M.1    Spooncer, E.2    Oates, J.E.3    Dell, A.4    Klock, J.C.5
  • 13
    • 0023008168 scopus 로고
    • Structures of O-linked oligosaccharides isolated from normal granulocytes, chronic myelogenous leukemia cells, and acute myelogenous leukemia cells
    • Fukuda, M., S.R. Carlsson, J.C. Klock, and A. Dell. 1986. Structures of O-linked oligosaccharides isolated from normal granulocytes, chronic myelogenous leukemia cells, and acute myelogenous leukemia cells. J. Biol. Chem. 261:12796-12806.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12796-12806
    • Fukuda, M.1    Carlsson, S.R.2    Klock, J.C.3    Dell, A.4
  • 14
    • 0022262016 scopus 로고
    • Aberrant glycosylation in cancer cell membranes as focused on glycolipids: Overview and perspectives
    • Hakomori, S. 1985. Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives. Cancer Res. 45:2405-2414.
    • (1985) Cancer Res. , vol.45 , pp. 2405-2414
    • Hakomori, S.1
  • 15
    • 0027941762 scopus 로고
    • Sulfation-dependent recognition of high endothelial venules (HEV)-ligands by L-selectin and MECA 79, an adhesion-blocking monoclonal antibody
    • Hemmerich, S., E.C. Butcher, and S.D. Rosen. 1994. Sulfation-dependent recognition of high endothelial venules (HEV)-ligands by L-selectin and MECA 79, an adhesion-blocking monoclonal antibody. J. Exp. Med. 180: 2219-2226.
    • (1994) J. Exp. Med. , vol.180 , pp. 2219-2226
    • Hemmerich, S.1    Butcher, E.C.2    Rosen, S.D.3
  • 16
    • 0029016563 scopus 로고
    • Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin
    • Hemmerich, S., H. Leffler, and S.D. Rosen. 1995. Structure of the O-glycans in GlyCAM-1, an endothelial-derived ligand for L-selectin. J. Biol. Chem. 270: 12035-12047.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12035-12047
    • Hemmerich, S.1    Leffler, H.2    Rosen, S.D.3
  • 17
    • 0033166088 scopus 로고    scopus 로고
    • A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewis X, an L-selectin ligand displayed by CD34
    • Hiraoka, N., B. Petryniak, J. Nakayama, S. Tsuboi, M. Suzuki, J.C. Yeh, T. Tanaka, M. Miyasaka, J.B. Lowe, and M. Fukuda. 1999. A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewis X, an L-selectin ligand displayed by CD34. Immunity. 11:79-89.
    • (1999) Immunity , vol.11 , pp. 79-89
    • Hiraoka, N.1    Petryniak, B.2    Nakayama, J.3    Tsuboi, S.4    Suzuki, M.5    Yeh, J.C.6    Tanaka, T.7    Miyasaka, M.8    Lowe, J.B.9    Fukuda, M.10
  • 18
    • 0027473659 scopus 로고
    • Sulphation requirement for GlyCAM-1, an endothelial ligand for l-selectin
    • Imai, Y., L.A. Lasky, and S.D. Rosen. 1993. Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin. Nature. 361:555-557.
    • (1993) Nature , vol.361 , pp. 555-557
    • Imai, Y.1    Lasky, L.A.2    Rosen, S.D.3
  • 19
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn, J., B. Walcheck, G.I. Migaki, M.A. Jutila, and T.K. Kishimoto. 1998. Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell. 92:809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 20
    • 0025018353 scopus 로고
    • ELAM-1-dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA
    • Lowe, J.B., L.M. Stoolman, R.P. Nair, R.D. Larsen, T.L. Berhend, and R.M. Marks. 1990. ELAM-1-dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA. Cell. 63:475-484.
    • (1990) Cell , vol.63 , pp. 475-484
    • Lowe, J.B.1    Stoolman, L.M.2    Nair, R.P.3    Larsen, R.D.4    Berhend, T.L.5    Marks, R.M.6
  • 21
    • 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. Thall, B. Petryniak, C.E. Rogers, P.L. Smith, R.M. Marks, R.J. Kelly, K.M. Gersten, G. 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.2    Petryniak, B.3    Rogers, C.E.4    Smith, P.L.5    Marks, R.M.6    Kelly, R.J.7    Gersten, K.M.8    Cheng, G.9    Saunders, T.L.10
  • 22
    • 0032006214 scopus 로고    scopus 로고
    • The lectin-like NK cell receptor Ly-49A recognizes a carbohydrate-independent epitope on its MHC class I ligand
    • Matsumoto, N., R.K. Ribaudo, J.P. Abastado, D.H. Margulies, and W.M. Yokoyama. 1998. The lectin-like NK cell receptor Ly-49A recognizes a carbohydrate-independent epitope on its MHC class I ligand. Immunity. 8:245-254.
    • (1998) Immunity , vol.8 , pp. 245-254
    • Matsumoto, N.1    Ribaudo, R.K.2    Abastado, J.P.3    Margulies, D.H.4    Yokoyama, W.M.5
  • 23
    • 0032079776 scopus 로고    scopus 로고
    • Identification of a major carbohydrate capping group of the L-selectin ligand on high endothelial venules in human lymph nodes as 6-sulfo sialyl Lewis x
    • Mitsuoka, C., M. Sawada-Kasugai, K. Ando-Furui, M. Izawa, H. Nakanishi, S. Nakamura, H. Ishiba, M. Kiso, and R. Kannagi. 1998. Identification of a major carbohydrate capping group of the L-selectin ligand on high endothelial venules in human lymph nodes as 6-sulfo sialyl Lewis x. J. Biol. Chem. 273: 11225-11233.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11225-11233
    • Mitsuoka, C.1    Sawada-Kasugai, M.2    Ando-Furui, K.3    Izawa, M.4    Nakanishi, H.5    Nakamura, S.6    Ishiba, H.7    Kiso, M.8    Kannagi, R.9
  • 25
    • 0021184795 scopus 로고
    • Changes in asparagine-linked sugar chains of human promyeiocytic leukemic cells (HL-60) during monocytoid differentiation and myeloid differentiation. Decrease of high-molecular-weight oligosaccharides in acidic fraction
    • Mizoguchi, A., S. Takasaki, S. Maeda, and A. Kobata. 1984. Changes in asparagine-linked sugar chains of human promyeiocytic leukemic cells (HL-60) during monocytoid differentiation and myeloid differentiation. Decrease of high-molecular-weight oligosaccharides in acidic fraction. J. Biol. Chem. 259: 11949-11957.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11949-11957
    • Mizoguchi, A.1    Takasaki, S.2    Maeda, S.3    Kobata, A.4
  • 26
    • 0033559260 scopus 로고    scopus 로고
    • Dual roles of sialyl Lewis X oligosaccharides in tumor metastasis and rejection by natural killer cells
    • Ohyama, C., S. Tsuboi, and M. Fukuda. 1999. Dual roles of sialyl Lewis X oligosaccharides in tumor metastasis and rejection by natural killer cells. EMBO (Eur. Mol. Biol. Organ.) J. 18:1516-1525.
    • (1999) EMBO (Eur. Mol. Biol. Organ.) J. , vol.18 , pp. 1516-1525
    • Ohyama, C.1    Tsuboi, S.2    Fukuda, M.3
  • 27
    • 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
  • 28
    • 0030091954 scopus 로고    scopus 로고
    • Leukocyte adhesion. Two selectins converge on sulphate
    • Rosen, S.D., and C.R. Bertozzi. 1996. Leukocyte adhesion. Two selectins converge on sulphate. Can. Biol. 261:261-264.
    • (1996) Can. Biol. , vol.261 , pp. 261-264
    • Rosen, S.D.1    Bertozzi, C.R.2
  • 29
    • 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
  • 30
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T.A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 31
    • 0024109988 scopus 로고
    • Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes
    • Streeter, P.R., B.T. Rouse, and B.C. Butcher. 1988. Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes. J. Cell Biol. 107:1853-1862.
    • (1988) J. Cell Biol. , vol.107 , pp. 1853-1862
    • Streeter, P.R.1    Rouse, B.T.2    Butcher, B.C.3
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0033613934 scopus 로고    scopus 로고
    • Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches
    • Yen, J.C., E. Ong, and M. Fukuda. 1999. Molecular cloning and expression of a novel β-1,6-N-acetylglucosaminyltransferase that forms core 2, core 4, and I branches. J Biol. Chem. 274:3215-3221.
    • (1999) J Biol. Chem. , vol.274 , pp. 3215-3221
    • Yen, J.C.1    Ong, E.2    Fukuda, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.