메뉴 건너뛰기




Volumn 10, Issue 8, 1999, Pages 1763-1771

Analysis of IgA1 O-glycans in IgA nephropathy by fluorophore-assisted carbohydrate electrophoresis

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE; GALACTOSE; GLYCAN; GLYCOSIDASE; IMMUNOGLOBULIN A1; LECTIN; N ACETYLGALACTOSAMINE; PROTEIN;

EID: 0032840295     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1681/asn.v1081763     Document Type: Article
Times cited : (110)

References (32)
  • 1
    • 0028934504 scopus 로고
    • IgA nephropathy
    • Galla JH: IgA nephropathy. Kidney Int 47: 377-387, 1995
    • (1995) Kidney Int , vol.47 , pp. 377-387
    • Galla, J.H.1
  • 2
    • 0029001438 scopus 로고
    • Galactosylation of N-and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy
    • Allen AC, Harper SJ, Feehally J: Galactosylation of N-and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy. Clin Exp Immunol 100: 470-474, 1995
    • (1995) Clin Exp Immunol , vol.100 , pp. 470-474
    • Allen, A.C.1    Harper, S.J.2    Feehally, J.3
  • 3
    • 0025639888 scopus 로고
    • Impairment of jacalin binding to serum IgA in IgA nephropathy
    • Andre PM, le Pogamp P, Chevet D: Impairment of jacalin binding to serum IgA in IgA nephropathy. J Clin Lab Anal 4: 115-119, 1990
    • (1990) J Clin Lab Anal , vol.4 , pp. 115-119
    • Andre, P.M.1    Le Pogamp, P.2    Chevet, D.3
  • 4
    • 0027356490 scopus 로고
    • Serum IgA and macromolecular IgA reacting with mesangial matrix components
    • Coppo R, Amore A, Gianoglio B: Serum IgA and macromolecular IgA reacting with mesangial matrix components. Contrib Nephrol 104: 162-171, 1993
    • (1993) Contrib Nephrol , vol.104 , pp. 162-171
    • Coppo, R.1    Amore, A.2    Gianoglio, B.3
  • 5
    • 0027355459 scopus 로고
    • Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy
    • Mestecky J, Tomana M, Crowley-Nowick PA: Defective galactosylation and clearance of IgA1 molecules as a possible etiopathogenic factor in IgA nephropathy. Contrib Nephrol 104: 172-182, 1993
    • (1993) Contrib Nephrol , vol.104 , pp. 172-182
    • Mestecky, J.1    Tomana, M.2    Crowley-Nowick, P.A.3
  • 6
    • 0030046183 scopus 로고    scopus 로고
    • Reactivity of glomerular and serum IgA1 to jacalin in IgA nephropathy
    • Hiki Y, Iwase H, Saitoh M: Reactivity of glomerular and serum IgA1 to jacalin in IgA nephropathy. Nephron 72: 429-435, 1996
    • (1996) Nephron , vol.72 , pp. 429-435
    • Hiki, Y.1    Iwase, H.2    Saitoh, M.3
  • 7
    • 0030836018 scopus 로고    scopus 로고
    • Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG
    • Tomana M, Matousovic K, Julian BA, Radl J, Konecny K, Mestecky J: Galactose-deficient IgA1 in sera of IgA nephropathy patients is present in complexes with IgG. Kidney Int 52: 509-516, 1997
    • (1997) Kidney Int , vol.52 , pp. 509-516
    • Tomana, M.1    Matousovic, K.2    Julian, B.A.3    Radl, J.4    Konecny, K.5    Mestecky, J.6
  • 8
    • 0031944497 scopus 로고    scopus 로고
    • Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry
    • Hiki Y, Tanaka A, Kokubo T: Analyses of IgA1 hinge glycopeptides in IgA nephropathy by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry. J Am Soc Nephrol 9: 577-582, 1998
    • (1998) J Am Soc Nephrol , vol.9 , pp. 577-582
    • Hiki, Y.1    Tanaka, A.2    Kokubo, T.3
  • 9
    • 0025007135 scopus 로고
    • The structure and function of human IgA
    • Kerr MA: The structure and function of human IgA. Biochem J 271: 285-296, 1990
    • (1990) Biochem J , vol.271 , pp. 285-296
    • Kerr, M.A.1
  • 10
    • 0031915973 scopus 로고    scopus 로고
    • The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fca receptor interactions
    • Mattu TS, Pleass RJ, Willis AC: The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fca receptor interactions. J Biol Chem 273: 2260-2272, 1998
    • (1998) J Biol Chem , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3
  • 11
    • 0016270014 scopus 로고
    • Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the o-glycosidically linked oligosaccharide units
    • Baenziger J, Kornfeld S: Structure of the carbohydrate units of IgA1 immunoglobulin. II. Structure of the O-glycosidically linked oligosaccharide units. J Biol Chem 249: 7270-7281, 1974
    • (1974) J Biol Chem , vol.249 , pp. 7270-7281
    • Baenziger, J.1    Kornfeld, S.2
  • 13
    • 0024540743 scopus 로고
    • Expression of Tn, sialosyl-Tn, and T antigens in human colon cancer
    • Itzkowitz SH, Yuan M, Montgomery CK: Expression of Tn, sialosyl-Tn, and T antigens in human colon cancer. Cancer Res 49: 197-204, 1989
    • (1989) Cancer Res , vol.49 , pp. 197-204
    • Itzkowitz, S.H.1    Yuan, M.2    Montgomery, C.K.3
  • 14
    • 0029681114 scopus 로고    scopus 로고
    • Estimation of the number of o-linked oligosaccharides per heavy chain of human serum Iga1 by matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of the hinge glycopeptide
    • Iwase H, Tanaka A, Hiki Y: Estimation of the number of O-linked oligosaccharides per heavy chain of human serum IgA1 by matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of the hinge glycopeptide. J Biochem 120: 393-397, 1996
    • (1996) J Biochem , vol.120 , pp. 393-397
    • Iwase, H.1    Tanaka, A.2    Hiki, Y.3
  • 15
    • 0026785503 scopus 로고
    • Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides
    • Iwase H, Ishii-Karakasa I, Fujii E, Hotta K, Hiki Y, Kobayashi Y: Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides. Anal Biochem 206: 202-205, 1992
    • (1992) Anal Biochem , vol.206 , pp. 202-205
    • Iwase, H.1    Ishii-Karakasa, I.2    Fujii, E.3    Hotta, K.4    Hiki, Y.5    Kobayashi, Y.6
  • 16
    • 0030358020 scopus 로고    scopus 로고
    • Association of asialo-galactosylβ1-3 N-acetyl galactosamine on the hinge with a conformational instability of jacalin reactive immunoglobulin A1 in immunoglobulin A nephropathy
    • Hiki Y, Iwase H, Kokubo T: Association of asialo-galactosylβ1-3 N-acetyl galactosamine on the hinge with a conformational instability of jacalin reactive immunoglobulin A1 in immunoglobulin A nephropathy. J Am Soc Nephrol 7: 955-960, 1996
    • (1996) J Am Soc Nephrol , vol.7 , pp. 955-960
    • Hiki, Y.1    Iwase, H.2    Kokubo, T.3
  • 17
    • 0025708306 scopus 로고
    • The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid
    • Jackson P: The use of polyacrylamide-gel electrophoresis for the high-resolution separation of reducing saccharides labelled with the fluorophore 8-aminonaphthalene-1,3,6-trisulfonic acid. Biochem J 210: 705-713, 1990
    • (1990) Biochem J , vol.210 , pp. 705-713
    • Jackson, P.1
  • 18
    • 0029072698 scopus 로고
    • Fluorophore assisted carbohydrate electrophoresis: Technology and applications
    • Hu G-F: Fluorophore assisted carbohydrate electrophoresis: Technology and applications. J Chromatogr A 705: 89-103, 1995
    • (1995) J Chromatogr A , vol.705 , pp. 89-103
    • Hu, G.-F.1
  • 19
    • 0031616486 scopus 로고    scopus 로고
    • Polyacrylamide gel electrophoresis of fluorophore-labeled carbohydrates from glycoproteins
    • Glycoanalysis Protocols, 2nd Ed., edited by Hounsell EF, Totowa, NJ, Humana Press
    • Klock JC, Starr CM: Polyacrylamide gel electrophoresis of fluorophore-labeled carbohydrates from glycoproteins. Methods in Molecular Biology, Vol 76. In: Glycoanalysis Protocols, 2nd Ed., edited by Hounsell EF, Totowa, NJ, Humana Press, 1998, pp 115-129
    • (1998) Methods in Molecular Biology , vol.76 , pp. 115-129
    • Klock, J.C.1    Starr, C.M.2
  • 20
    • 0019605113 scopus 로고
    • The release of N-acetyl-and N-glycolloyl-neuraminic acid from soluble complex carbohydrates and erythrocytes by bacterial, viral and mammalian sialydases
    • Corfield AP, Veh RW, Wember M, Michalski J-C, Schauer R: The release of N-acetyl-and N-glycolloyl-neuraminic acid from soluble complex carbohydrates and erythrocytes by bacterial, viral and mammalian sialydases. Biochem J 197: 293-299, 1981
    • (1981) Biochem J , vol.197 , pp. 293-299
    • Corfield, A.P.1    Veh, R.W.2    Wember, M.3    Michalski, J.-C.4    Schauer, R.5
  • 21
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins
    • Patel T, Bruce J, Merry A: Use of hydrazine to release in intact and unreduced form both N-and O-linked oligosaccharides from glycoproteins. Biochem 32: 679-693, 1993
    • (1993) Biochem , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3
  • 22
    • 0017182324 scopus 로고
    • Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of diplococcus pneumoniae
    • Endo Y, Kobata A: Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Diplococcus pneumoniae. J Biochem 80: 1-8, 1976
    • (1976) J Biochem , vol.80 , pp. 1-8
    • Endo, Y.1    Kobata, A.2
  • 23
    • 0023802135 scopus 로고
    • Monoclonal antibodies directed to the blood group A associated structure, galactosyl-A: Specificity and relation to the Thomsen-Friedenreich antigen
    • Clausen H, Stroud M, Parker J, Springer G, Hakomori S-I: Monoclonal antibodies directed to the blood group A associated structure, galactosyl-A: Specificity and relation to the Thomsen-Friedenreich antigen. Mol Immunol 25: 199-204, 1988
    • (1988) Mol Immunol , vol.25 , pp. 199-204
    • Clausen, H.1    Stroud, M.2    Parker, J.3    Springer, G.4    Hakomori, S.-I.5
  • 24
    • 0029153494 scopus 로고
    • Abnormal glycosylation of IgA: Is it related to the pathogenesis of IgA nephropathy?
    • Allen AC: Abnormal glycosylation of IgA: Is it related to the pathogenesis of IgA nephropathy? Nephrol Dial Transplant 10: 1121-1124, 1995
    • (1995) Nephrol Dial Transplant , vol.10 , pp. 1121-1124
    • Allen, A.C.1
  • 25
    • 0021111871 scopus 로고
    • Isolation and characterisation of lectins from Vicia villosa: Two distinct carbohydrate binding activities are present in seed extracts
    • Tollefsen SE, Kornfeld R: Isolation and characterisation of lectins from Vicia villosa: Two distinct carbohydrate binding activities are present in seed extracts. J Biol Chem 258: 5165-5171, 1983
    • (1983) J Biol Chem , vol.258 , pp. 5165-5171
    • Tollefsen, S.E.1    Kornfeld, R.2
  • 26
    • 0031925983 scopus 로고    scopus 로고
    • Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis
    • Allen AC, Willis FR, Beattie TJ, Feehally J: Abnormal IgA glycosylation in Henoch-Schönlein purpura restricted to patients with clinical nephritis. Nephrol Dial Transplant 13: 930-934, 1998
    • (1998) Nephrol Dial Transplant , vol.13 , pp. 930-934
    • Allen, A.C.1    Willis, F.R.2    Beattie, T.J.3    Feehally, J.4
  • 31
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft N: Why are proteins O-glycosylated? Trends Biochem Sci 15: 291-294, 1990
    • (1990) Trends Biochem Sci , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 32
    • 0030882005 scopus 로고    scopus 로고
    • Evidence for involvement of IgA1 hinge glycopeptide in the IgA1-IgA1 interaction in IgA nephropathy
    • Kokubo T, Hiki Y, Iwase H: Evidence for involvement of IgA1 hinge glycopeptide in the IgA1-IgA1 interaction in IgA nephropathy. J Am Soc Nephrol 8: 915-919, 1997
    • (1997) J Am Soc Nephrol , vol.8 , pp. 915-919
    • Kokubo, T.1    Hiki, Y.2    Iwase, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.