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Volumn 8, Issue 9, 1998, Pages 947-953

The extent of polylactosamine glycosylation of MDCK LAMP-2 is determined by its Golgi residence time

Author keywords

Epithelial cells; Golgi apparatus; LAMP; MDCK; Polylactosamine

Indexed keywords

GLYCOPROTEIN; GLYCOSYLTRANSFERASE; NOCODAZOLE; POLYLACTOSAMINE; UNCLASSIFIED DRUG;

EID: 0031656594     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/8.9.947     Document Type: Article
Times cited : (36)

References (30)
  • 1
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium
    • Bacallao, R., Antony, C., Dotti, C., Karsenti, E., Stelzer, E. and Simons, K. (1989) The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol., 109, 2817-2832.
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.5    Simons, K.6
  • 2
    • 0025005502 scopus 로고
    • Transient expression of p58 protein kinase cDNA enhances mammalian glycosyltransferase activity
    • Bunnell, B.A., Adams, D.E. and Kidd, V.J. (1990) Transient expression of p58 protein kinase cDNA enhances mammalian glycosyltransferase activity. Biochem. Biophys. Res. Commun., 171, 196-203.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 196-203
    • Bunnell, B.A.1    Adams, D.E.2    Kidd, V.J.3
  • 3
    • 0024245391 scopus 로고
    • Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2
    • Carlsson, S.R., Roth, J., Piller, F. and Fukuda, M. (1988) Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. J Biol. Chem., 263, 18911-18919.
    • (1988) J Biol. Chem. , vol.263 , pp. 18911-18919
    • Carlsson, S.R.1    Roth, J.2    Piller, F.3    Fukuda, M.4
  • 4
    • 0028360655 scopus 로고
    • Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAcs
    • Chou, C.-F. and Omary, M.B. (1994) Mitotic arrest with anti-microtubule agents or okadaic acid is associated with increased glycoprotein terminal GlcNAcs. J. Cell Sci., 107, 1833-1843.
    • (1994) J. Cell Sci. , vol.107 , pp. 1833-1843
    • Chou, C.-F.1    Omary, M.B.2
  • 5
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum sites
    • Cole, N.B., Sciaky, N., Marotta, A., Song, J. and Lippincott-Schwartz, J. (1996) Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum sites. Mol. Biol. Cell, 7, 631-650.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 6
    • 0023255440 scopus 로고
    • β1,6 branching of Asn-linked oligosaccharides is directly associated with metastasis
    • Dennis, J.W., Laferté, S., Waghorne, C., Breitman, M.L. and Kerbel, R. (1987) β1,6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science, 236, 582-585.
    • (1987) Science , vol.236 , pp. 582-585
    • Dennis, J.W.1    Laferté, S.2    Waghorne, C.3    Breitman, M.L.4    Kerbel, R.5
  • 7
    • 0021601136 scopus 로고
    • Cell surface glycoconjugates as onco-differentiation markers in hematopoietic cells
    • Fukuda, M. (1985) Cell surface glycoconjugates as onco-differentiation markers in hematopoietic cells. Biochim. Biophys. Acta, 780, 119-150.
    • (1985) Biochim. Biophys. Acta , vol.780 , pp. 119-150
    • Fukuda, M.1
  • 8
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cistema of the Golgi complex to the plasma membrane
    • Griffiths, G., Pfeiffer, S., Simons, K. and Matlin, K. (1985) Exit of newly synthesized membrane proteins from the trans cistema of the Golgi complex to the plasma membrane. J. Cell Biol., 101, 949-964.
    • (1985) J. Cell Biol. , vol.101 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 9
    • 0030961453 scopus 로고    scopus 로고
    • Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamme and accumulation of incompletely processed N-glycans on proteins from H129 cells
    • Haltiwanger, R.S. and Philipsberg, G.A. (1997) Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamme and accumulation of incompletely processed N-glycans on proteins from H129 cells J. Biol. Chem., 272, 8752-8758.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8752-8758
    • Haltiwanger, R.S.1    Philipsberg, G.A.2
  • 10
    • 0024462177 scopus 로고
    • Molecular characterization of P2B/LAMP-1, a major protein target of a metastasis-associated oligosaccharide structure
    • Heffernan, M., Yousefi, S. and Dennis, J.W. (1989) Molecular characterization of P2B/LAMP-1, a major protein target of a metastasis-associated oligosaccharide structure. Cancer Res., 49, 6077-6084.
    • (1989) Cancer Res. , vol.49 , pp. 6077-6084
    • Heffernan, M.1    Yousefi, S.2    Dennis, J.W.3
  • 12
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and non-polarized cells
    • Musch, A., Xu, H., Shields, D. and Rodriguez-Boulan, E. (1996) Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and non-polarized cells. J. Cell Biol., 133, 543-558.
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Musch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 13
    • 0027211772 scopus 로고
    • Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer
    • Nabi, I.R. and Rodriguez-Boulan, E. (1993) Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer. Mol. Biol. Cell, 4, 627-635.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 627-635
    • Nabi, I.R.1    Rodriguez-Boulan, E.2
  • 14
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes
    • Nabi, I.R., Le Bivic, A., Fambrough, D. and Rodriguez-Boulan, E. (1991) An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol., 115, 1573-1584.
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Le Bivic, A.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 16
    • 0027472941 scopus 로고
    • Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells
    • Nilsson, T., Pypaert, M., Hoe, M.H., Slusarewicz, P., Berger, E.G. and Warren, G. (1993) Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells. J. Cell Biol., 120, 5-13.
    • (1993) J. Cell Biol. , vol.120 , pp. 5-13
    • Nilsson, T.1    Pypaert, M.2    Hoe, M.H.3    Slusarewicz, P.4    Berger, E.G.5    Warren, G.6
  • 17
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer, S.R. and Rothman, J.E. (1987) Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem., 56, 829-832.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-832
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 18
    • 0031019168 scopus 로고    scopus 로고
    • Expression of human H-type alpha1,2-fucosyltransferase encoding for blood group H(O) antigen in Chinese hamster ovary cells. Evidence for preferential fucosylation and truncation ot polylactosamine sequences
    • Prieto, P., Larsen, R., Cho, M., Rivera, H., Shilatifard, A., Lowe, J., Cummings, R. and Smith, D. (1997) Expression of human H-type alpha1,2-fucosyltransferase encoding for blood group H(O) antigen in Chinese hamster ovary cells. Evidence for preferential fucosylation and truncation ot polylactosamine sequences. J. Biol. Chem., 272, 2089-2097.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2089-2097
    • Prieto, P.1    Larsen, R.2    Cho, M.3    Rivera, H.4    Shilatifard, A.5    Lowe, J.6    Cummings, R.7    Smith, D.8
  • 19
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille, C., Hui, N., Hunte, F., Kieckbusch, R., Berger, E.G., Warren, G. and Nilsson, T. (1995) Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci., 108, 1617-1627.
    • (1995) J. Cell Sci. , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6    Nilsson, T.7
  • 20
    • 0020037889 scopus 로고
    • Immunocytochemical localization of galactosyl-transferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cisternae
    • Roth, J. and Berger, E.G. (1982) Immunocytochemical localization of galactosyl-transferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. J. Cell Biol., 93, 223-229.
    • (1982) J. Cell Biol. , vol.93 , pp. 223-229
    • Roth, J.1    Berger, E.G.2
  • 21
    • 0026713211 scopus 로고
    • The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence ot brefeldin A
    • Sampath, D., Varki, A. and Freeze, H. (1992) The spectrum of incomplete N-linked oligosaccharides synthesized by endothelial cells in the presence ot brefeldin A. J. Biol. Chem., 267, 4440-4455.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4440-4455
    • Sampath, D.1    Varki, A.2    Freeze, H.3
  • 22
    • 0031930477 scopus 로고    scopus 로고
    • Molecular cloning of a human cDNA encoding β-1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase
    • Sato, T., Furukawa, K., Bakker, H., Van den Eijnden, D. and Van Die, I. (1997) Molecular cloning of a human cDNA encoding β-1,4-galactosyltransferase with 37% identity to mammalian UDP-Gal:GlcNAc β-1,4-galactosyltransferase. Proc. Natl. Acad. Sci. USA, 95, 472-477.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 472-477
    • Sato, T.1    Furukawa, K.2    Bakker, H.3    Van Den Eijnden, D.4    Van Die, I.5
  • 23
    • 0345009059 scopus 로고
    • Bovine galactosyltransferase: Identification by a clone of direct immunological screening of a cDNA library
    • Shaper, N., Shaper, J., Meuth, J., Fox, J., Chang, H., Kirsch, I. and Hollis, G. (1986) Bovine galactosyltransferase: identification by a clone of direct immunological screening of a cDNA library. Proc. Natl. Acad. Sci. USA, 83, 1573-577.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1573-1577
    • Shaper, N.1    Shaper, J.2    Meuth, J.3    Fox, J.4    Chang, H.5    Kirsch, I.6    Hollis, G.7
  • 24
    • 0030931796 scopus 로고    scopus 로고
    • Altered Golgi localization of core 2 beta-1,6-N-acetylglucosaminyltransferase leads to decreased synthesis of branched O-glycans
    • Skrincosky, D., Kain, R., El-Battari, A., Exner, M., Kerjaschki, D. and Fukuda, M. (1997) Altered Golgi localization of core 2 beta-1,6-N-acetylglucosaminyltransferase leads to decreased synthesis of branched O-glycans. J. Biol. Chem., 272, 22695-22702.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22695-22702
    • Skrincosky, D.1    Kain, R.2    El-Battari, A.3    Exner, M.4    Kerjaschki, D.5    Fukuda, M.6
  • 25
    • 0024357921 scopus 로고
    • Relationship between Golgi architecture and glycoprotein biosynthesis and transport in Chinese hamster ovary cells
    • Stults, N.L., Fechmeier, M. and Cummings, R.D. (1989) Relationship between Golgi architecture and glycoprotein biosynthesis and transport in Chinese hamster ovary cells. J. Biol. Chem., 264, 19956-19966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19956-19966
    • Stults, N.L.1    Fechmeier, M.2    Cummings, R.D.3
  • 26
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex
    • Thyberg, J. and Moskalewski, S. (1985) Microtubules and the organization of the Golgi complex. Exp. Cell Res., 159, 1-16.
    • (1985) Exp. Cell Res. , vol.159 , pp. 1-16
    • Thyberg, J.1    Moskalewski, S.2
  • 27
    • 0026333183 scopus 로고
    • The poly-N-acetyllactosamines attached to lysosomal membrane glycoproteins are increased by prolonged association with the Golgi complex
    • Wang, W.-C., Lee, N., Aoki, D., Fukuda, M. and Fukuda, M. (1991) The poly-N-acetyllactosamines attached to lysosomal membrane glycoproteins are increased by prolonged association with the Golgi complex. J. Biol. Chem., 266, 23185-23190.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23185-23190
    • Wang, W.-C.1    Lee, N.2    Aoki, D.3    Fukuda, M.4    Fukuda, M.5
  • 28
    • 0030905585 scopus 로고    scopus 로고
    • A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans
    • Whitehouse, C., Burchell, J., Gschmeissner, S., Brockhausen, I., Lloyd, K.O. and Taylor-Papadimitriou, J. (1997) A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans. J. Cell Biol., 137, 1229-1241.
    • (1997) J. Cell Biol. , vol.137 , pp. 1229-1241
    • Whitehouse, C.1    Burchell, J.2    Gschmeissner, S.3    Brockhausen, I.4    Lloyd, K.O.5    Taylor-Papadimitriou, J.6
  • 29
    • 0024826146 scopus 로고
    • Decrease in polylactosamines associated with lysosomal membrane glycoproteins during differentiation of CaCo-2 human colonie adenocarcinoma cells
    • Youakim, A., Romero, P.A., Yee, K., Carlsson, S.R., Fukuda, M. and Heiscovics, A. (1989) Decrease in polylactosamines associated with lysosomal membrane glycoproteins during differentiation of CaCo-2 human colonie adenocarcinoma cells. Cancer Res., 49, 6889-6895.
    • (1989) Cancer Res. , vol.49 , pp. 6889-6895
    • Youakim, A.1    Romero, P.A.2    Yee, K.3    Carlsson, S.R.4    Fukuda, M.5    Heiscovics, A.6
  • 30
    • 0026086828 scopus 로고
    • 1-3GalNAc-R (GlcNAc to GalNAc) β-1,6-N-acetylglucosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine synthesis
    • 1-3GalNAc-R (GlcNAc to GalNAc) β-1,6-N-acetylglucosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine synthesis. J. Biol. Chem., 266, 1772-1782.
    • (1992) J. Biol. Chem. , vol.266 , pp. 1772-1782
    • Yousefi, S.1    Higgins, E.2    Daoling, Z.3    Pollex-Kruger, A.4    Hindsgaul, O.5    Dennis, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.