Evidence for glycosylation-dependent activities of polypeptide N-acetylgalactosaminyltransferases rGalNAc-T2 and -T4 on mucin glycopeptides

Glycobiology

Volumn 11, Issue 9, 2001, Pages 731-740

  Hanisch, Franz Georg ^a   Reis, Celso A ^b   Clausen, Henrik ^b   Paulsen, Hans ^c  

^a Medical Faculty   (Germany)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Glycoproteins; Glycosyltransferases; Mucins; O glycosylation; Polypeptide N acetylgalactos aminyltransferases

Indexed keywords

GLYCAN; GLYCOPEPTIDE; MUCIN; N ACETYLGALACTOSAMINYLTRANSFERASE; RECOMBINANT ENZYME; SERINE; THREONINE;

ARTICLE; CARBOHYDRATE ANALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME INDUCTION; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN MOTIF; TANDEM REPEAT;

EID: 0034780414     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/11.9.731     Document Type: Article

References (22)

1. Cloning and expression of a proteoglycan UDP-galactose: β-xylose β1-galactosyltransferase I. A seventh member of the human β4-galactosyltransferase gene family
2. Cloning and characterization of a close homologue of human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy
3. A novel human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates
4. Cloning of a human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat
5. A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases control the initiation of mucin-type O-linked glycosylation
6. The acceptor specificity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases
7. MUC1: The polymorphic appearance of a human mucin
8. Dynamic epigenetic regulation of initial O-glycosylation by UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases
9. Structures of neutral O-linked polylactosaminoglycans on human skim milk mucins
10. The lectin domain of UDP-GalNAc: N-acetylgalactosaminyltransferase T4 directs its glycopeptide specificities
11. The (QxW)3 domain: A flexible lectin scaffold
12. Incorporation of N-acetylgalactosamine into consecutive threonine residues in MUC2 tandem repeat recombinant human N-acetylgalactosaminyltransferase-T1, -T2, and -T3
13. Synthesis and characterization of highly glycosylated glycopeptides with Tn-antigenic structures corresponding to human glycophorin AN
14. Synthesis of glycopeptide sequences of repeating units of the mucins MUC2 and MUC3 containing oligosaccharide side-chains with core 1, core 2, core 3, core 4 and core 6 structure
15. Partial vapor-phase hydrolysis of peptide bonds: A method for mass spectrometric determination of O-glycosylated sites in glycopeptides
16. High density O-glycosylation on tandem repeat peptide from secretory MUC1 of T47D breast cancer cells
17. Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1
18. Isoform-specific O-glycosylation by murine UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase-T3, in vivo
19. Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase from milk ormammary carcinoma cells
20. Cloning and expression of a novel, tissue-specifically expressed member of the UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase family
21. Substrate specificities of three members of the human UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3
22. Identification of glycosylation sites in mucin peptides