메뉴 건너뛰기




Volumn 62, Issue 1, 2003, Pages 34-41

Characterization of an O-glycosylated plaque-associated protein from Alzheimer disease brain

Author keywords

Alzheimer disease; Amaranthus leucocarpus lectin (ALL); O glycosylated proteins; Proteome analysis; T specific lectin; Tn specific lectin

Indexed keywords

GLYCAN DERIVATIVE; N ACETYLGALACTOSAMINE; TRYPSIN;

EID: 0037226444     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1093/jnen/62.1.34     Document Type: Article
Times cited : (16)

References (44)
  • 2
    • 0023708239 scopus 로고
    • Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease
    • Ihara Y. Massive somatodendritic sprouting of cortical neurons in Alzheimer's disease. Brain Res 1988;459:138-44
    • (1988) Brain Res , vol.459 , pp. 138-144
    • Ihara, Y.1
  • 3
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP, et al. Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment. Ann Neurol 1991;30:572-80
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3
  • 4
    • 0027229615 scopus 로고
    • Quantitative assessment of the synaptophysin immunoreactivity of the cortical neuropil in various neurodegenerative disorders with dementia
    • Zhan SS, Beyreuther K, Schmitt HP. Quantitative assessment of the synaptophysin immunoreactivity of the cortical neuropil in various neurodegenerative disorders with dementia. Dementia 1993;4:66-74
    • (1993) Dementia , vol.4 , pp. 66-74
    • Zhan, S.S.1    Beyreuther, K.2    Schmitt, H.P.3
  • 5
    • 0030513943 scopus 로고    scopus 로고
    • Structural correlates of cognition in dementia: Quantification and assessment of synapse change
    • DeKosky ST, Scheff SW, Styren SD. Structural correlates of cognition in dementia: Quantification and assessment of synapse change. Neurodegeneration 1996;5:417-21
    • (1996) Neurodegeneration , vol.5 , pp. 417-421
    • DeKosky, S.T.1    Scheff, S.W.2    Styren, S.D.3
  • 7
    • 78651158156 scopus 로고
    • Ultrastructural studies in Alzheimer's preneuritic dementia
    • Terry RD, Gonatas NK, Weiss M. Ultrastructural studies in Alzheimer's preneuritic dementia. Am J Pathol 1964;44:269-97
    • (1964) Am J Pathol , vol.44 , pp. 269-297
    • Terry, R.D.1    Gonatas, N.K.2    Weiss, M.3
  • 8
    • 0002942063 scopus 로고
    • Ultrastructure of neuritic dementia and of experimental analogs. Aging and the brain
    • Gaitz CM, ed. New York: Plenum Press
    • Terry RD, Wisniewski HM. Ultrastructure of neuritic dementia and of experimental analogs. Aging and the brain. In: Gaitz CM, ed. Advances in behavioral biology. New York: Plenum Press, vol. 3. 1972;89-116
    • (1972) Advances in Behavioral Biology , vol.3 , pp. 89-116
    • Terry, R.D.1    Wisniewski, H.M.2
  • 9
    • 0023105114 scopus 로고
    • The precursor of Alzheimer disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire HG, Unterbeck A, et al. The precursor of Alzheimer disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987;325:733-36
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3
  • 10
    • 0023987430 scopus 로고
    • Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease
    • Dyrks T, Weidemann A, Multhaup G, et al. Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease. EMBO J 1988;7:949-57
    • (1988) EMBO J , vol.7 , pp. 949-957
    • Dyrks, T.1    Weidemann, A.2    Multhaup, G.3
  • 11
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • Weidermann A, Koning G, Bunke D, et al. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell 1989;57:115-26
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidermann, A.1    Koning, G.2    Bunke, D.3
  • 12
    • 0035843950 scopus 로고    scopus 로고
    • Analysis of N-glycans of pathological tau: Possible occurrence of aberrant processing of tau in Alzheimer's disease
    • Sato Y, Naito Y, Grundke-Iqbal I, Iqbal K, Endo T. Analysis of N-glycans of pathological tau: Possible occurrence of aberrant processing of tau in Alzheimer's disease. FEBS Lett 2001;496:152-60
    • (2001) FEBS Lett , vol.496 , pp. 152-160
    • Sato, Y.1    Naito, Y.2    Grundke-Iqbal, I.3    Iqbal, K.4    Endo, T.5
  • 13
    • 0031755183 scopus 로고    scopus 로고
    • Altered glycosylation patterns of proteins in Alzheimer disease
    • Guevara J, Espinosa B, Zenteno E, et al. Altered glycosylation patterns of proteins in Alzheimer disease. J Neuropathol Exp Neurol 1998;57:905-14
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 905-914
    • Guevara, J.1    Espinosa, B.2    Zenteno, E.3
  • 14
    • 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 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 1998;273:6277-84
    • (1998) J Biol Chem , vol.273 , pp. 6277-6284
    • Tomita, S.1    Kirino, Y.2    Suzuki, T.3
  • 15
    • 0035395790 scopus 로고    scopus 로고
    • Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides
    • Tetaert D, Ten Hagen KG, Richet C, Boersma A, Gagnon J, Degand P. Glycopeptide N-acetylgalactosaminyltransferase specificities for O-glycosylated sites on MUC5AC mucin motif peptides. Biochem J 2001;357(Pt. 1):313-20
    • (2001) Biochem J , vol.357 , Issue.PART 1 , pp. 313-320
    • Tetaert, D.1    Ten Hagen, K.G.2    Richet, C.3    Boersma, A.4    Gagnon, J.5    Degand, P.6
  • 16
    • 0001127772 scopus 로고    scopus 로고
    • Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles
    • Van Damme EJ, Peumans WJ, Barre A, Rouge P. Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles. Crit Rev Biochem Mol Biol 1998;33:209-58
    • (1998) Crit Rev Biochem Mol Biol , vol.33 , pp. 209-258
    • Van Damme, E.J.1    Peumans, W.J.2    Barre, A.3    Rouge, P.4
  • 18
    • 0344348837 scopus 로고    scopus 로고
    • A comparative study on the purification of the Amaranthus leucocarpus syn. hypocondriacus lectin
    • Hernandez P, Bacilio M, Porras F, et al. A comparative study on the purification of the Amaranthus leucocarpus syn. hypocondriacus lectin. Prep Biochem Biotech 1999;29:219-34
    • (1999) Prep Biochem Biotech , vol.29 , pp. 219-234
    • Hernandez, P.1    Bacilio, M.2    Porras, F.3
  • 20
    • 0001392899 scopus 로고
    • Mitogenic immunosuppressive and phagocityc activity of Macharocerus eruca and Amaranthus leucocarpus lectin
    • Bög-Hansen TC, Breborowicz J, eds. Walter de Gruyter
    • Zenteno E, Ochoa JL, Parra C, et al. Mitogenic immunosuppressive and phagocityc activity of Macharocerus eruca and Amaranthus leucocarpus lectin. In: Bög-Hansen TC, Breborowicz J, eds. Lectins-biology, biochemistry, clinical biochemistry. Walter de Gruyter 1985;4:537-46
    • (1985) Lectins-biology, Biochemistry, Clinical Biochemistry , vol.4 , pp. 537-546
    • Zenteno, E.1    Ochoa, J.L.2    Parra, C.3
  • 21
    • 0025908356 scopus 로고
    • The consortium to establish a registry for Alzheimer's disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, et al. The consortium to establish a registry for Alzheimer's disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991;41:479-86
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3
  • 22
    • 0022414054 scopus 로고
    • Diagnosis of Alzheimer's disease
    • Khachaturian ZS. Diagnosis of Alzheimer's disease. Arch Neurol 1985;42:1097-1105
    • (1985) Arch Neurol , vol.42 , pp. 1097-1105
    • Khachaturian, Z.S.1
  • 24
    • 0040299037 scopus 로고    scopus 로고
    • AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease
    • Buée-Scherrer V, Condamines O, Mourton-Gilles C, et al. AD2, a phosphorylation-dependent monoclonal antibody directed against tau proteins found in Alzheimer's disease. Mol Brain Res 1996;39:79-88
    • (1996) Mol Brain Res , vol.39 , pp. 79-88
    • Buée-Scherrer, V.1    Condamines, O.2    Mourton-Gilles, C.3
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing the principle of protein dye-binding
    • Bradford MM. A rapid and sensitive method for quantitation of microgram quantities of proteins utilizing the principle of protein dye-binding. Anal Biochem 1976;37:157-223
    • (1976) Anal Biochem , vol.37 , pp. 157-223
    • Bradford, M.M.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during assembly of the bacteriophage T4. Nature 1970;227:680-85
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0028983813 scopus 로고
    • Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman U, Wernstedt C, Gonez J, Heldin CH. Improvement of an "In-Gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal Biochem 1995; 224:451-55
    • (1995) Anal Biochem , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 29
    • 0030250714 scopus 로고    scopus 로고
    • Glycation and microglial reaction in lesions of Alzheimer's disease
    • Dickson DW, Sinicropi S, Yen HS, et al. Glycation and microglial reaction in lesions of Alzheimer's disease. Neurobiol Aging 1996;17:733-43
    • (1996) Neurobiol Aging , vol.17 , pp. 733-743
    • Dickson, D.W.1    Sinicropi, S.2    Yen, H.S.3
  • 30
  • 31
    • 0031592838 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro
    • Ishikawa K, Nagase T, Nakajima DS. Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res 1997; 4:307-13
    • (1997) DNA Res , vol.4 , pp. 307-313
    • Ishikawa, K.1    Nagase, T.2    Nakajima, D.S.3
  • 32
    • 0030959841 scopus 로고    scopus 로고
    • Developmentally regulated expression of peanut agglutinin (PNA)-specific glycans on murine thymocytes
    • Wenyu W, Punt JA, Granger L, Sharrow SO, Kearse KP. Developmentally regulated expression of peanut agglutinin (PNA)-specific glycans on murine thymocytes. Glycobiology 1997;7: 349-56
    • (1997) Glycobiology , vol.7 , pp. 349-356
    • Wenyu, W.1    Punt, J.A.2    Granger, L.3    Sharrow, S.O.4    Kearse, K.P.5
  • 33
    • 0030894597 scopus 로고    scopus 로고
    • Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide: Galnac transferase peptide binding site
    • Gerken AT, Owens LC, Pasumarthy M. Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide. Model proposed for the polypeptide: galnac transferase peptide binding site. J Biol Chem 1997;272: 9709-19
    • (1997) J Biol Chem , vol.272 , pp. 9709-9719
    • Gerken, A.T.1    Owens, L.C.2    Pasumarthy, M.3
  • 34
    • 0025961689 scopus 로고
    • Use of the lectin from Amaranthus caudatus as a histochemical probe of proliferating colonic epithelial cells
    • Boland CR, Chen YF, Rinderle SJ, et al. Use of the lectin from Amaranthus caudatus as a histochemical probe of proliferating colonic epithelial cells. Cancer Res 1991;51:657-65
    • (1991) Cancer Res , vol.51 , pp. 657-665
    • Boland, C.R.1    Chen, Y.F.2    Rinderle, S.J.3
  • 35
  • 36
    • 0031588904 scopus 로고    scopus 로고
    • Analysis of carbohydrate recognition by legume lectin: Size of the combining site loops and their primary specificity
    • Sharma V, Surolia A. Analysis of carbohydrate recognition by legume lectin: Size of the combining site loops and their primary specificity. J Mol Biol 1997;267:433-45
    • (1997) J Mol Biol , vol.267 , pp. 433-445
    • Sharma, V.1    Surolia, A.2
  • 37
    • 0035707742 scopus 로고    scopus 로고
    • Chemical characterization of the lectin from Amaranthus leucocarpus syn. hypocondriacus by 2-D proteome analysis
    • Hernández P, Debray H, Jaekel H, et al. Chemical characterization of the lectin from Amaranthus leucocarpus syn. hypocondriacus by 2-D proteome analysis. Glycocon J 2001;18:321-29
    • (2001) Glycocon J , vol.18 , pp. 321-329
    • Hernández, P.1    Debray, H.2    Jaekel, H.3
  • 38
    • 0002942063 scopus 로고
    • Ultrastructure of neuritic dementia and of experimental analogs. Aging and the brain
    • Gaitz CM, ed., New York: Plenum Press
    • Terry RD, Wisniewski HM. Ultrastructure of neuritic dementia and of experimental analogs. Aging and the brain. In: Gaitz CM, ed. Advances in behavioral biology, New York: Plenum Press, vol. 3. 1972;89-116
    • (1972) Advances in Behavioral Biology , vol.3 , pp. 89-116
    • Terry, R.D.1    Wisniewski, H.M.2
  • 39
    • 0033836217 scopus 로고    scopus 로고
    • Phagocytic clearance of apoptotic neurons by microglia/brain macrophages in vitro: Involvement of lectin-, integrin-, and phosphatidylserine-mediated recognition
    • Witting A, Muller P, Herrmann A, Kettenmann H, Nolte C. Phagocytic clearance of apoptotic neurons by microglia/brain macrophages in vitro: Involvement of lectin-, integrin-, and phosphatidylserine-mediated recognition. J Neurochem 2000;75:1060-70
    • (2000) J Neurochem , vol.75 , pp. 1060-1070
    • Witting, A.1    Muller, P.2    Herrmann, A.3    Kettenmann, H.4    Nolte, C.5
  • 40
    • 0031983986 scopus 로고    scopus 로고
    • Glial-neuronal interactions in Alzheimer's disease: The potential role of a "cytokine cycle" in disease progression
    • Griffin WS, Sheng JG, Royston MC, et al. Glial-neuronal interactions in Alzheimer's disease: The potential role of a "cytokine cycle" in disease progression. Brain Pathol 1998;8:65-72
    • (1998) Brain Pathol , vol.8 , pp. 65-72
    • Griffin, W.S.1    Sheng, J.G.2    Royston, M.C.3
  • 41
    • 0032563098 scopus 로고    scopus 로고
    • A basic amino acid in the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein (APP) is essential for cleavage of APP at the alpha-site
    • Tomita S, Kirino Y, Suzuki T. A basic amino acid in the cytoplasmic domain of Alzheimer's beta-amyloid precursor protein (APP) is essential for cleavage of APP at the alpha-site. J Biol Chem 1998; 273:19304-10
    • (1998) J Biol Chem , vol.273 , pp. 19304-19310
    • Tomita, S.1    Kirino, Y.2    Suzuki, T.3
  • 42
    • 0033582159 scopus 로고    scopus 로고
    • Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer beta-amyloid peptides
    • Greenfield JP, Tsai J, Gouras GK, et al. Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer beta-amyloid peptides. Proc Natl Acad Sci USA 1999;96: 742-47
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 742-747
    • Greenfield, J.P.1    Tsai, J.2    Gouras, G.K.3
  • 43
    • 0031863688 scopus 로고    scopus 로고
    • Building a secretory apparatus: Role of ARF1/COPI in Golgi biogenesis and maintenance
    • Lippincott-Schwartz J, Cole NB, Donaldson JG. Building a secretory apparatus: Role of ARF1/COPI in Golgi biogenesis and maintenance. Histochem Cell Biol 1998;109:449-62
    • (1998) Histochem Cell Biol , vol.109 , pp. 449-462
    • Lippincott-Schwartz, J.1    Cole, N.B.2    Donaldson, J.G.3
  • 44
    • 0031966903 scopus 로고    scopus 로고
    • Retrograde trafficking of both Golgi complex and TGN markers to the ER induced by nordihydroguaiaretic acid and cyclofenil diphenol
    • Drecktrah D, de Figueiredo P, Mason RM, Brown WJ. Retrograde trafficking of both Golgi complex and TGN markers to the ER induced by nordihydroguaiaretic acid and cyclofenil diphenol. J Cell Sci 1998;111(Pt. 7):951-65
    • (1998) J Cell Sci , vol.111 , Issue.PART 7 , pp. 951-965
    • Drecktrah, D.1    De Figueiredo, P.2    Mason, R.M.3    Brown, W.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.