Determination of UDP-N-acetylglucosamine:β-D-mannoside-1,4-N- acetylglucosaminyltransferase-III in patients sera with chronic hepatitis and liver cirrhosis using a monoclonal antibody

Glycoconjugate Journal

Volumn 19, Issue 6, 2002, Pages 415-421

  Song, Eun Young ^a,g   Kim, Kyung Sook ^b,c   Kim, Kyoung A ^d   Kim, Yung Dai ^d   Kwon, Dur Han ^a   Byun, Si Myung ^e   Kim, Hee Jung ^f   Chung, Tae Wook ^b,c   Choe, Yong Kyung ^a   Chung, Tai Wha ^d   Kim, Cheorl Ho ^b,c  

^a Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^b Ministry of Science and Technology   (South Korea)

^c Dongguk University   (South Korea)

^d Research Laboratory   (South Korea)

^e Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^f Daejeon St Mary's Hospital   (South Korea)

^g NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

Enzyme linked immunosorbent assay; Human N acetylglucosaminyltransferase III; Liver disease; Monoclonal antibody

Indexed keywords

MONOCLONAL ANTIBODY; N ACETYLGLUCOSAMINYLTRANSFERASE; RECOMBINANT ENZYME; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

ARTICLE; CHRONIC HEPATITIS; CHRONIC LIVER DISEASE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; LIVER CIRRHOSIS; LIVER DISEASE; MAJOR CLINICAL STUDY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; SERUM;

ANTIBODIES, MONOCLONAL; BLOTTING, WESTERN; DOSE-RESPONSE RELATIONSHIP, DRUG; HEPATITIS, CHRONIC; HUMANS; IMMUNOASSAY; LIVER CIRRHOSIS; MANNOSIDES; N-ACETYLGLUCOSAMINYLTRANSFERASES; URIDINE DIPHOSPHATE N-ACETYLGLUCOSAMINE;

EID: 0347504718     PISSN: 02820080     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:GLYC.0000004013.36690.78     Document Type: Article

References (24)

1. Nishikawa A, Ihara Y, Hatakeyama M, Kangawa K, Taniguchi N, Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4N-acetylglucosaminyltransferase III from rat kidney, J Biol Chem 267, 18199-204 (1992).
2. Narasimhan S, Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides, J Biol Chem 257, 10235-42 (1982).
3. Nishikawa N, Fujii S, Sugiyama T, Taniguchi N, A method for the determination of N-acetylglucosaminyltransferase III activity in rat tissues involving HPLC, Anal Biochem 170, 349-54 (1988).
4. Nishikawa A, Gu J, Fujii S, Taniguchi N, Determination of N-acetylglucosaminyltransferases III, IV and V in normal and hepatoma tissues of rats, Biochim Biophys Acta 1035, 313-8 (1990).
5. Pascale R, Narasimhan S, Rajalakshmi S, Expression of N-acetylglucosaminyltransferase III in hepatic nodules generated by different models of rat liver carcinogenesis, Carcinogenesis 10, 961-4 (1989).
6. Koenderman AHL, Koppen PL, Koeleman CAM, Van den Eijnden DH, N-acetylglucosaminyltransferase III, IV and V activities in Novikoff ascites tumour cells, mouse lymphoma cells and hen oviduct. Application of a sensitive and specific assay by use of high-performance liquid chromatography, Eur J Biochem 181, 651-5 (1989).
7. Narasimhan S, Lee JWW, Cheung RK, Gelfand EW, Schachter H, Beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase III activity in human B and T lymphocyte lines and in tonsillar B and T lymphocytes, Biochem Cell Biol 66, 889-900 (1988).
8. Brockhausen I, Romero PA, Herscovics A, Glycosyltransferase changes upon differentiation of CaCo-2 human colonic adenocarcinoma cells, Cancer Res 51, 3136-42 (1991).
9. Ohno M, Nishikawa A, Koketsu M, Taga H, Endo Y, Hada T, Taniguchi N, Enzymatic basis of sugar structures of alpha-fetoprotein in hepatoma and hepatoblastoma cell lines: correlation with activities of alpha 1-6 fucosyltransferase and N-acetylglucosaminyltransferases III and V, Int J Cancer 51, 315-7 (1992).
10. Koenderman AHL, Wijermans PW, Van den Eijnden DH, Changes in the expression of N-acetylglucosaminyltransferase III, IV, V associated with the differentiation of HL-60 cells, FEBS Lett 222, 42-6 (1987).
11. Song EY, Park C, Chung TH, Kwon DH, Byun SM, Kim CH, Expression of bisecting N-acetylglucosaminyltransferase-III in human hepatocarcinoma tissues, fetal liver tissues, and hepatoma cell lines of Hep3B and HepG2, Cancer investigation 19(8), 797-805 (2001).
12. Ishibashi K, Nishikawa A, Hayashi N, Kasahara A, Sato N, Fujii S, Kamada T, Taniguchi N, N-acetylglucosaminyltransferase III in human serum, and liver and hepatoma tissues: increased activity in liver cirrhosis and hepatoma patients, Clin Chim Acta 185, 325-32 (1989).
13. Mori S, Aoyagi Y, Yanagi M, Suzuki Y, Asakura H, Serum N-acetylglucosaminyltransferase III activities in hepatocellular carcinoma, J Gastroenterology and Hepatology 13, 610-9 (1998).
14. Ihara Y, Nishikawa A, Tohma T, Soejima H, Nikawa N, Taniguchi N, cDNA cloning, expression, and chromosomal localization of human N- acetylglucosaminyltransferase III (GnT-III), J Biochem 113, 692-8 (1993).
15. Kim YJ, Ko JH, Chung DH, Chung TW, Choe IS, Kim CH, Sequence analysis of the 5′-flanking region of the gene encoding human N- acetylglucosaminyltransferase III, Gene 170, 281-3 (1996).
16. Song EY, Kim KA, Kim YD, Kwon DH, Lee HS, Kim CH, Chung TW, Byun SM, A simplified procedure for the purification of human N- acetylglucosaminyltransferase-III from human hepatocellular carcinoma tissues, Biotech Letters 22(3), 201-4 (2000).
17. Harlow E, Lane DP, Antibodies, A Laboratory Mannual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1988).
18. Bokhout BA, Van Asten-Noordijk JJ, Divergent results in radial immunodiffusion. III. Isolation and specificity test of class-specific antibodies, J Immunol Methods 27, 101-9 (1979).
19. Feizi T, Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens, Nature 314, 53-7 (1985).
20. Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A, Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis, J Biol Chem 259, 10834-40 (1984).
21. Pierce M, Arango J, Rous sarcoma virus-transformed baby hamster kidney cells express higher levels of asparagine-linked tri-and tetraantennary glycopeptides containing [GlcNAc-beta (1,6)Man-alpha (1,6)Man] and poly-N-acetyllactosamine sequences than baby hamster kidney cells, J Biol Chem 261, 10772-7 (1986).
22. Hubbard SC, Differential effects of oncogenic transformation on N-linked oligosaccharide processing at individual glycosylation sites of viral glycoproteins, J Biol Chem 262, 16403-11 (1987).
23. Warren L, Fuhrer JP, Buck CA, Surface glycoproteins of normal and transformed cells: a difference determined by sialic acid and a growth-dependent sialyl transferase, Proc Natl Acad Sci USA 69, 1838-42 (1972).
24. Paulson JC, Colley KJ, Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation, J Biol Chem 264, 17615-8 (1989).