메뉴 건너뛰기




Volumn 20, Issue 1, 2010, Pages 99-106

Protective effect of N-glycan bisecting GlcNAc residues on β-amyloid production in Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid precursor protein; Bisecting GlcNAc; N glycan

Indexed keywords

ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; GLYCOSYLTRANSFERASE; MEMBRANE PROTEIN; MESSENGER RNA; N ACETYGLUCOSAMINE; N GLYCAN; UNCLASSIFIED DRUG;

EID: 70849108548     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwp152     Document Type: Article
Times cited : (85)

References (50)
  • 1
    • 53849139399 scopus 로고    scopus 로고
    • Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins
    • Akasaka-Manya K, Manya H, Sakurai Y, Wojczyk BS, Spitalnik SL, Endo T. 2008. Increased bisecting and core-fucosylated N-glycans on mutant human amyloid precursor proteins. Glycoconj J. 25:775-786.
    • (2008) Glycoconj J , vol.25 , pp. 775-786
    • Akasaka-Manya, K.1    Manya, H.2    Sakurai, Y.3    Wojczyk, B.S.4    Spitalnik, S.L.5    Endo, T.6
  • 2
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production
    • Benjannet S, Elagoz A, Wickham L, Mamarbachi M, Munzer JS, Basak A, Lazure C, Cromlish JA, Sisodia S, Checler F, et al. 2001. Post-translational processing of β-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production. J Biol Chem. 276:10879-10887.
    • (2001) J Biol Chem , vol.276 , pp. 10879-10887
    • Benjannet, S.1    Elagoz, A.2    Wickham, L.3    Mamarbachi, M.4    Munzer, J.S.5    Basak, A.6    Lazure, C.7    Cromlish, J.A.8    Sisodia, S.9    Checler, F.10
  • 3
    • 0037135585 scopus 로고    scopus 로고
    • Truncated, inactive N-acetylglucosaminyltransferase III (GlcNAc-TIII) induces neurological and other traits absent in mice that lack GlcNAc-TIII
    • Bhattacharyya R, Bhaumik M, Raju TS, Stanley P. 2002. Truncated, inactive N-acetylglucosaminyltransferase III (GlcNAc-TIII) induces neurological and other traits absent in mice that lack GlcNAc-TIII. J Biol Chem. 277:26300-26309.
    • (2002) J Biol Chem , vol.277 , pp. 26300-26309
    • Bhattacharyya, R.1    Bhaumik, M.2    Raju, T.S.3    Stanley, P.4
  • 6
    • 0025981417 scopus 로고
    • Glycosylation of recombinant protein therapeutics: Control and functional implications
    • Cumming DA. 1991. Glycosylation of recombinant protein therapeutics: Control and functional implications. Glycobiology. 1:115-130.
    • (1991) Glycobiology , vol.1 , pp. 115-130
    • Cumming, D.A.1
  • 7
    • 43149108354 scopus 로고    scopus 로고
    • Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme
    • Escrevente C, Morais VA, Keller S, Soares CM, Altevogt P, Costa J. 2008. Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme. Biochim Biophys Acta. 1780:905-913.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 905-913
    • Escrevente, C.1    Morais, V.A.2    Keller, S.3    Soares, C.M.4    Altevogt, P.5    Costa, J.6
  • 11
    • 5444266511 scopus 로고    scopus 로고
    • Regulation of integrin functions by N glycans
    • Gu J, Taniguchi N. 2004. Regulation of integrin functions by N glycans. Glycoconj J. 21:9-15.
    • (2004) Glycoconj J , vol.21 , pp. 9-15
    • Gu, J.1    Taniguchi, N.2
  • 12
    • 0037444574 scopus 로고    scopus 로고
    • γ-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation
    • Herreman A, Van Gassen G, Bentahir M, Nyabi O, Craessaerts K, Mueller U, Annaert W, De Strooper B. 2003. γ-Secretase activity requires the presenilin-dependent trafficking of nicastrin through the Golgi apparatus but not its complex glycosylation. J Cell Sci. 116:1127-1136.
    • (2003) J Cell Sci , vol.116 , pp. 1127-1136
    • Herreman, A.1    Van Gassen, G.2    Bentahir, M.3    Nyabi, O.4    Craessaerts, K.5    Mueller, U.6    Annaert, W.7    De Strooper, B.8
  • 14
    • 0024207853 scopus 로고
    • Comparative study of the asparagine-linked sugar chains of natural human interferon-β 1 and recombinant human interferon-β 1 produced by three different mammalian cells
    • Kagawa Y, Takasaki S, Utsumi J, Hosoi K, Shimizu H, Kochibe N, Kobata A. 1988. Comparative study of the asparagine-linked sugar chains of natural human interferon-β 1 and recombinant human interferon-β 1 produced by three different mammalian cells. J Biol Chem. 263:17508-17515.
    • (1988) J Biol Chem , vol.263 , pp. 17508-17515
    • Kagawa, Y.1    Takasaki, S.2    Utsumi, J.3    Hosoi, K.4    Shimizu, H.5    Kochibe, N.6    Kobata, A.7
  • 16
    • 0035980062 scopus 로고    scopus 로고
    • Down-regulation of the α-Gal epitope expression in N-glycans of swine endothelial cells by transfection with the N acetylglucosaminyltransferase III gene. Modulation of the biosynthesis of terminal structures by a bisecting GlcNAc
    • Koyota S, Ikeda Y, Miyagawa S, Ihara H, Koma M, Honke K, Shirakura R, Taniguchi N. 2001. Down-regulation of the α-Gal epitope expression in N-glycans of swine endothelial cells by transfection with the N acetylglucosaminyltransferase III gene. Modulation of the biosynthesis of terminal structures by a bisecting GlcNAc. J Biol Chem. 276:32867-32874.
    • (2001) J Biol Chem , vol.276 , pp. 32867-32874
    • Koyota, S.1    Ikeda, Y.2    Miyagawa, S.3    Ihara, H.4    Koma, M.5    Honke, K.6    Shirakura, R.7    Taniguchi, N.8
  • 17
    • 0141733204 scopus 로고    scopus 로고
    • Differential glycosylation regulates processing of lipoprotein receptors by γ-secretase
    • May P, Bock HH, Nimpf J, Herz J. 2003. Differential glycosylation regulates processing of lipoprotein receptors by γ-secretase. J Biol Chem. 278:37386-37392.
    • (2003) J Biol Chem , vol.278 , pp. 37386-37392
    • May, P.1    Bock, H.H.2    Nimpf, J.3    Herz, J.4
  • 18
    • 0032974408 scopus 로고    scopus 로고
    • The role of the protein glycosylation state in the control of cellular transport of the amyloid β precursor protein
    • McFarlane I, Georgopoulou N, Coughlan CM, Gillian AM, Breen KC. 1999. The role of the protein glycosylation state in the control of cellular transport of the amyloid β precursor protein. Neuroscience. 90:15-25.
    • (1999) Neuroscience , vol.90 , pp. 15-25
    • McFarlane, I.1    Georgopoulou, N.2    Coughlan, C.M.3    Gillian, A.M.4    Breen, K.C.5
  • 21
    • 4644298126 scopus 로고    scopus 로고
    • Neuropathological diagnostic criteria for Alzheimer's disease
    • Murayama S, Saito Y. 2004. Neuropathological diagnostic criteria for Alzheimer's disease. Neuropathology. 24:254-260.
    • (2004) Neuropathology , vol.24 , pp. 254-260
    • Murayama, S.1    Saito, Y.2
  • 23
    • 0020373041 scopus 로고
    • Control of glycoprotein synthesis. UDP-GlcNAc: Glycopeptide β 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides
    • Narasimhan S. 1982. Control of glycoprotein synthesis. UDP-GlcNAc: glycopeptide β 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in β 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J Biol Chem. 257:10235-10242.
    • (1982) J Biol Chem , vol.257 , pp. 10235-10242
    • Narasimhan, S.1
  • 24
    • 0026705382 scopus 로고
    • Purification, cDNA cloning, and expression of UDP-N acetylglucosamine: β-D-mannoside β-1,4N acetylglucosaminyltransferase III from rat kidney
    • Nishikawa A, Ihara Y, Hatakeyama M, Kangawa K, Taniguchi N. 1992. Purification, cDNA cloning, and expression of UDP-N acetylglucosamine: β-D-mannoside β-1,4N acetylglucosaminyltransferase III from rat kidney. J Biol Chem. 267:18199-18204.
    • (1992) J Biol Chem , vol.267 , pp. 18199-18204
    • Nishikawa, A.1    Ihara, Y.2    Hatakeyama, M.3    Kangawa, K.4    Taniguchi, N.5
  • 25
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K, Marth JD. 2006. Glycosylation in cellular mechanisms of health and disease. Cell. 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 28
    • 0032491494 scopus 로고    scopus 로고
    • Genetic neurodegenerative diseases: The human illness and transgenic models
    • Price DL, Sisodia SS, Borchelt DR. 1998. Genetic neurodegenerative diseases: The human illness and transgenic models. Science. 282:1079-1083.
    • (1998) Science , vol.282 , pp. 1079-1083
    • Price, D.L.1    Sisodia, S.S.2    Borchelt, D.R.3
  • 29
    • 0030983084 scopus 로고    scopus 로고
    • Gene transfection-mediated overexpression of β 1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function
    • Rebbaa A, Yamamoto H, Saito T, Meuillet E, Kim P, Kersey DS, Bremer EG, Taniguchi N, Moskal JR. 1997. Gene transfection-mediated overexpression of β 1,4-N-acetylglucosamine bisecting oligosaccharides in glioma cell line U373 MG inhibits epidermal growth factor receptor function. J Biol Chem. 272:9275-9279.
    • (1997) J Biol Chem , vol.272 , pp. 9275-9279
    • Rebbaa, A.1    Yamamoto, H.2    Saito, T.3    Meuillet, E.4    Kim, P.5    Kersey, D.S.6    Bremer, E.G.7    Taniguchi, N.8    Moskal, J.R.9
  • 31
    • 0028991306 scopus 로고
    • N-Linked oligosaccharide of β-amyloid precursor protein (β APP) of C6 glioma cells: Putative regulatory role in β APP processing
    • Saito F, Tani A, Miyatake T, Yanagisawa K. 1995. N-Linked oligosaccharide of β-amyloid precursor protein (β APP) of C6 glioma cells: Putative regulatory role in β APP processing. Biochem Biophys Res Commun. 210:703-710.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 703-710
    • Saito, F.1    Tani, A.2    Miyatake, T.3    Yanagisawa, K.4
  • 32
    • 0032825983 scopus 로고    scopus 로고
    • Study of the sugar chains of recombinant human amyloid precursor protein produced by Chinese hamster ovary cells
    • Sato Y, Liu C, Wojczyk BS, Kobata A, Spitalnik SL, Endo T. 1999. Study of the sugar chains of recombinant human amyloid precursor protein produced by Chinese hamster ovary cells. Biochim Biophys Acta. 1472:344-358.
    • (1999) Biochim Biophys Acta , vol.1472 , pp. 344-358
    • Sato, Y.1    Liu, C.2    Wojczyk, B.S.3    Kobata, A.4    Spitalnik, S.L.5    Endo, T.6
  • 33
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter H. 1986. Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem Cell Biol. 64:163-181.
    • (1986) Biochem Cell Biol , vol.64 , pp. 163-181
    • Schachter, H.1
  • 34
    • 0021014033 scopus 로고
    • Control of branching during the biosynthesis of asparagine-linked oligosaccharides
    • Schachter H, Narasimhan S, Gleeson P, Vella G. 1983. Control of branching during the biosynthesis of asparagine-linked oligosaccharides. Can J Biochem Cell Biol. 61:1049-1066.
    • (1983) Can J Biochem Cell Biol , vol.61 , pp. 1049-1066
    • Schachter, H.1    Narasimhan, S.2    Gleeson, P.3    Vella, G.4
  • 35
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE)
    • Schlondorff J, Becherer JD, Blobel CP. 2000. Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE). Biochem J. 347(Pt 1):131-138.
    • (2000) Biochem J , vol.347 , Issue.PART 1 , pp. 131-138
    • Schlondorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 37
    • 33646880044 scopus 로고    scopus 로고
    • β 1,4- N-acetylglucosaminyltransferase III potentiates β1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells
    • Shigeta M, Shibukawa Y, Ihara H, Miyoshi E, Taniguchi N, Gu J. 2006. β 1,4- N-acetylglucosaminyltransferase III potentiates β1 integrin-mediated neuritogenesis induced by serum deprivation in Neuro2a cells. Glycobiology. 16:564-571.
    • (2006) Glycobiology , vol.16 , pp. 564-571
    • Shigeta, M.1    Shibukawa, Y.2    Ihara, H.3    Miyoshi, E.4    Taniguchi, N.5    Gu, J.6
  • 38
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of β-amyloid production and secretion
    • Sinha S, Lieberburg I. 1999. Cellular mechanisms of β-amyloid production and secretion. Proc Natl Acad Sci USA. 96:11049-11053.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 39
    • 0034741796 scopus 로고    scopus 로고
    • Neuronal localization of the TNFα converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques
    • Skovrons ky DM, Fath S, Lee VM, Milla ME. 2001. Neuronal localization of the TNFα converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques. J Neurobiol. 49:40-46.
    • (2001) J Neurobiol , vol.49 , pp. 40-46
    • Skovrons ky, D.M.1    Fath, S.2    Lee, V.M.3    Milla, M.E.4
  • 40
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the trans-Golgi network
    • Skovronsky DM, Moore DB, Milla ME, Doms RW, Lee VM. 2000. Protein kinase C-dependent α-secretase competes with β-secretase for cleavage of amyloid-β precursor protein in the trans-Golgi network. J Biol Chem 275:2568-2575.
    • (2000) J Biol Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 41
    • 0028322017 scopus 로고
    • An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β APP717) mutants
    • Suzuki N, Cheung TT, Cai XD, Odaka A, Otvos L Jr, Eckman C, Golde TE, Younkin SG. 1994. An increased percentage of long amyloid β protein secreted by familial amyloid β protein precursor (β APP717) mutants. Science. 264:1336-1340.
    • (1994) Science , vol.264 , pp. 1336-1340
    • Suzuki, N.1    Cheung, T.T.2    Cai, X.D.3    Odaka, A.4    Otvos Jr, L.5    Eckman, C.6    Golde, T.E.7    Younkin, S.G.8
  • 42
    • 0024840851 scopus 로고    scopus 로고
    • Taniguchi N, Nishikawa A, Fujii S, Gu JG. 1989. Glycosyltransferase assays using pyridylaminated acceptors: N acetylglucosaminyltransferase III, IV, and V. Methods Enzymol. 179:397-408.
    • Taniguchi N, Nishikawa A, Fujii S, Gu JG. 1989. Glycosyltransferase assays using pyridylaminated acceptors: N acetylglucosaminyltransferase III, IV, and V. Methods Enzymol. 179:397-408.
  • 44
    • 0032513060 scopus 로고    scopus 로고
    • Cleavage of Alzheimer's amyloid precursor protein (APP) by secretases occurs after O-glycosylation of APP in the protein secretory pathway. Identification of intracellular compartments in which APP cleavage occurs without using toxic agents that interfere with protein metabolism
    • Tomita S, Kirino Y, Suzuki T. 1998. Cleavage of Alzheimer's amyloid precursor protein (APP) by secretases occurs after O-glycosylation of APP in the protein secretory pathway. Identification of intracellular compartments in which APP cleavage occurs without using toxic agents that interfere with protein metabolism. J Biol Chem. 273:6277-6284.
    • (1998) J Biol Chem , vol.273 , pp. 6277-6284
    • Tomita, S.1    Kirino, Y.2    Suzuki, T.3
  • 45
    • 27644439090 scopus 로고    scopus 로고
    • Dysregulation of TGF-β1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice
    • Wang X, Inoue S, Gu J, Miyoshi E, Noda K, Li W, Mizuno-Horikawa Y, Nakano M, Asahi M, Takahashi M, et al. 2005. Dysregulation of TGF-β1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice. Proc Natl Acad Sci USA. 102:15791-15796.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15791-15796
    • Wang, X.1    Inoue, S.2    Gu, J.3    Miyoshi, E.4    Noda, K.5    Li, W.6    Mizuno-Horikawa, Y.7    Nakano, M.8    Asahi, M.9    Takahashi, M.10
  • 46
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidemann A, Konig G, Bunke D, Fischer P, Salbaum JM, Masters CL, Beyreuther K. 1989. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell. 57:115-126.
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    Konig, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 47
    • 0017193878 scopus 로고
    • The control of glycoprotein synthesis: N-acetylglucosamine linkage to a mannose residue as a signal for the attachment of L-fucose to the asparagine-linked N acetylglucosamine residue of glycopeptide from α1-acid glycoprotein
    • Wilson JR, Williams D, Schachter H. 1976. The control of glycoprotein synthesis: N-acetylglucosamine linkage to a mannose residue as a signal for the attachment of L-fucose to the asparagine-linked N acetylglucosamine residue of glycopeptide from α1-acid glycoprotein. Biochem Biophys Res Commun. 72:909-916.
    • (1976) Biochem Biophys Res Commun , vol.72 , pp. 909-916
    • Wilson, J.R.1    Williams, D.2    Schachter, H.3
  • 48
    • 0021112907 scopus 로고
    • Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides
    • Yamashita K, Hitoi A, Kobata A. 1983. Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides. J Biol Chem. 258:14753-14755.
    • (1983) J Biol Chem , vol.258 , pp. 14753-14755
    • Yamashita, K.1    Hitoi, A.2    Kobata, A.3
  • 49
    • 0030604231 scopus 로고    scopus 로고
    • Mutation of potential N-linked glycosylation sites in the Alzheimer's disease amyloid precursor protein (APP)
    • Yazaki M, Tagawa K, Maruyama K, Sorimachi H, Tsuchiya T, Ishiura S, Suzuki K. 1996. Mutation of potential N-linked glycosylation sites in the Alzheimer's disease amyloid precursor protein (APP). Neurosci Lett. 221:57-60.
    • (1996) Neurosci Lett , vol.221 , pp. 57-60
    • Yazaki, M.1    Tagawa, K.2    Maruyama, K.3    Sorimachi, H.4    Tsuchiya, T.5    Ishiura, S.6    Suzuki, K.7
  • 50
    • 0029933659 scopus 로고    scopus 로고
    • Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis
    • Yoshimura M, Ihara Y, Matsuzawa Y, Taniguchi N. 1996. Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis. J Biol Chem. 271:13811-13815.
    • (1996) J Biol Chem , vol.271 , pp. 13811-13815
    • Yoshimura, M.1    Ihara, Y.2    Matsuzawa, Y.3    Taniguchi, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.