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Volumn 300, Issue 5, 2011, Pages

Alterations of serum protein N-glycosylation in two mouse models of chronic liver disease are hepatocyte and not B cell driven

Author keywords

B cells; CBDL; CCI4; DSA FACE; Glycomics

Indexed keywords

CARBON TETRACHLORIDE; GLYCAN; GLYCOSIDASE; IMMUNOGLOBULIN G; PLASMA PROTEIN;

EID: 79955551474     PISSN: 01931857     EISSN: 15221547     Source Type: Journal    
DOI: 10.1152/ajpgi.00228.2010     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0029778988 scopus 로고    scopus 로고
    • An algorithm for the grading of activity in chronic hepatitis C. The METAVIR Cooperative Study Group
    • Bedossa P, Poynard T. An algorithm for the grading of activity in chronic hepatitis C. The METAVIR Cooperative Study Group. Hepatology 24: 289-293, 1996.
    • (1996) Hepatology , vol.24 , pp. 289-293
    • Bedossa, P.1    Poynard, T.2
  • 3
    • 1942454310 scopus 로고    scopus 로고
    • Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics
    • Callewaert N, Van Vlierberghe H, Van Hecke A, Laroy W, Delanghe J, Contreras R. Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics. Nat Med 10: 429-434, 2004.
    • (2004) Nat Med , vol.10 , pp. 429-434
    • Callewaert, N.1    van Vlierberghe, H.2    van Hecke, A.3    Laroy, W.4    Delanghe, J.5    Contreras, R.6
  • 4
    • 45549094069 scopus 로고    scopus 로고
    • Glyco-WorkBench: A tool for the computer-assisted annotation of mass spectra of glycans
    • Ceroni A, Maass K, Geyer H, Geyer R, Dell A, Haslam SM. Glyco-WorkBench: a tool for the computer-assisted annotation of mass spectra of glycans. J Proteome Res 7: 1650-1659, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 1650-1659
    • Ceroni, A.1    Maass, K.2    Geyer, H.3    Geyer, R.4    Dell, A.5    Haslam, S.M.6
  • 5
    • 47649116115 scopus 로고    scopus 로고
    • Comparison of three research models of portal hypertension in mice: Macroscopic, histological and portal pressure evaluation
    • Geerts AM, Vanheule E, Praet M, Van Vlierberghe H, De Vos M, Colle I. Comparison of three research models of portal hypertension in mice: macroscopic, histological and portal pressure evaluation. Int J Exp Pathol 89: 251-263, 2008.
    • (2008) Int J Exp Pathol , vol.89 , pp. 251-263
    • Geerts, A.M.1    Vanheule, E.2    Praet, M.3    van Vlierberghe, H.4    de Vos, M.5    Colle, I.6
  • 6
    • 0034851008 scopus 로고    scopus 로고
    • Nucleotide sugar transporters: Biological and functional aspects
    • Gerardy-Schahn R, Oelmann S, Bakker H. Nucleotide sugar transporters: biological and functional aspects. Biochimie 83: 775-782, 2001.
    • (2001) Biochimie , vol.83 , pp. 775-782
    • Gerardy-Schahn, R.1    Oelmann, S.2    Bakker, H.3
  • 7
    • 0037717192 scopus 로고    scopus 로고
    • Optimization of the dose and route of injection, and characterisation of the time course of carbon tetrachloride-induced hepatotoxicity in the rat
    • Janakat S, Al-Merie H. Optimization of the dose and route of injection, and characterisation of the time course of carbon tetrachloride-induced hepatotoxicity in the rat. J Pharmacol Toxicol Methods 48: 41-44, 2002.
    • (2002) J Pharmacol Toxicol Methods , vol.48 , pp. 41-44
    • Janakat, S.1    Al-Merie, H.2
  • 9
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: Isotype and glycoform selection
    • Jefferis R. Antibody therapeutics: isotype and glycoform selection. Expert Opin Biol Ther 7: 1401-1413, 2007.
    • (2007) Expert Opin Biol Ther , vol.7 , pp. 1401-1413
    • Jefferis, R.1
  • 10
    • 0025852445 scopus 로고
    • A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin mu chain gene
    • Kitamura D, Roes J, Kuhn R, Rajewsky K. A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin mu chain gene. Nature 350: 423-426, 1991.
    • (1991) Nature , vol.350 , pp. 423-426
    • Kitamura, D.1    Roes, J.2    Kuhn, R.3    Rajewsky, K.4
  • 11
    • 77953715893 scopus 로고    scopus 로고
    • Immunoglobulins are the major glycoproteins involved in the modifications of total N-glycome in cirrhotic patients
    • Klein A, Carre Y, Louvet A, Michalski JC, Morelle W. Immunoglobulins are the major glycoproteins involved in the modifications of total N-glycome in cirrhotic patients. Proteomics Clin Appl 4: 379-393, 2010.
    • (2010) Proteomics Clin Appl , vol.4 , pp. 379-393
    • Klein, A.1    Carre, Y.2    Louvet, A.3    Michalski, J.C.4    Morelle, W.5
  • 12
    • 77953797887 scopus 로고    scopus 로고
    • Modifications of human total serum N-glycome during liver fibrosis-cirrhosis, it is all about immunoglobulins?
    • Klein A, Michalski JC, Morelle W. Modifications of human total serum N-glycome during liver fibrosis-cirrhosis, it is all about immunoglobulins? Proteomics Clin Appl 4: 372-378, 2010.
    • (2010) Proteomics Clin Appl , vol.4 , pp. 372-378
    • Klein, A.1    Michalski, J.C.2    Morelle, W.3
  • 13
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles
    • Kobata A. The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles. Biochim Biophys Acta 1780: 472-478, 2008.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 472-478
    • Kobata, A.1
  • 15
    • 0021238490 scopus 로고
    • Prolonged bile duct obstruction: A new experimental model for cirrhosis in the rat
    • Kountouras J, Billing BH, Scheuer PJ. Prolonged bile duct obstruction: a new experimental model for cirrhosis in the rat. Br J Exp Pathol 65: 305-311, 1984.
    • (1984) Br J Exp Pathol , vol.65 , pp. 305-311
    • Kountouras, J.1    Billing, B.H.2    Scheuer, P.J.3
  • 16
    • 0029983426 scopus 로고    scopus 로고
    • Immunoglobulin G galactosylation deficiency determined by isoelectric focusing and lectin affinoblotting in differential diagnosis of rheumatoid arthritis
    • Kotz K, Hansler M, Sauer H, Kaltenhauser S, Hantzschel H. Immunoglobulin G galactosylation deficiency determined by isoelectric focusing and lectin affinoblotting in differential diagnosis of rheumatoid arthritis. Electrophoresis 17: 533-534, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 533-534
    • Kotz, K.1    Hansler, M.2    Sauer, H.3    Kaltenhauser, S.4    Hantzschel, H.5
  • 17
    • 34247616380 scopus 로고    scopus 로고
    • Glycome mapping on DNA sequencing equipment
    • Laroy W, Contreras R, Callewaert N. Glycome mapping on DNA sequencing equipment. Nat Protoc 1: 397-405, 2006.
    • (2006) Nat Protoc , vol.1 , pp. 397-405
    • Laroy, W.1    Contreras, R.2    Callewaert, N.3
  • 19
    • 58149400525 scopus 로고    scopus 로고
    • Fucosylated glycoproteins as markers of liver disease
    • Mehta A, Block TM. Fucosylated glycoproteins as markers of liver disease. Dis Markers 25: 259-265, 2008.
    • (2008) Dis Markers , vol.25 , pp. 259-265
    • Mehta, A.1    Block, T.M.2
  • 20
    • 0025038766 scopus 로고
    • Structural changes in the oligosaccharide chains of IgG in autoimmune MRL/Mp-lpr/lpr mice
    • Mizuochi T, Hamako J, Nose M, Titani K. Structural changes in the oligosaccharide chains of IgG in autoimmune MRL/Mp-lpr/lpr mice. J Immunol 145: 1794-1798, 1990.
    • (1990) J Immunol , vol.145 , pp. 1794-1798
    • Mizuochi, T.1    Hamako, J.2    Nose, M.3    Titani, K.4
  • 21
    • 0023414234 scopus 로고
    • Structures of the sugar chains of mouse immunoglobulin G
    • Mizuochi T, Hamako J, Titani K. Structures of the sugar chains of mouse immunoglobulin G. Arch Biochem Biophys 257: 387-394, 1987.
    • (1987) Arch Biochem Biophys , vol.257 , pp. 387-394
    • Mizuochi, T.1    Hamako, J.2    Titani, K.3
  • 24
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: Evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju TS, Briggs JB, Borge SM, Jones AJ. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 10: 477-486, 2000.
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 25
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju TS. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr Opin Immunol 20: 471-478, 2008.
    • (2008) Curr Opin Immunol , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 26
    • 0036233290 scopus 로고    scopus 로고
    • UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: Regulation based on the kinetic properties of N-acetylglucosaminyltransferase V
    • Sasai K, Ikeda Y, Fujii T, Tsuda T, Taniguchi N. UDP-GlcNAc concentration is an important factor in the biosynthesis of β1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V. Glycobiology 12: 119-127, 2002.
    • (2002) Glycobiology , vol.12 , pp. 119-127
    • Sasai, K.1    Ikeda, Y.2    Fujii, T.3    Tsuda, T.4    Taniguchi, N.5
  • 30
    • 0344412943 scopus 로고    scopus 로고
    • Reduced hepatocyte proliferation is the basis of retarded liver tumor progression and liver regeneration in mice lacking N-acetylglucosaminyltransferase III
    • Yang X, Tang J, Rogler C, Stanley P. Reduced hepatocyte proliferation is the basis of retarded liver tumor progression and liver regeneration in mice lacking N-acetylglucosaminyltransferase III. Cancer Res 63: 7753-7759.
    • Cancer Res , vol.63 , pp. 7753-7759
    • Yang, X.1    Tang, J.2    Rogler, C.3    Stanley, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.