A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

A novel human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

A novel member of the human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive sp...

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Veröffentlicht in:FEBS letters 1999-10, Vol.460 (2), p.226-230
Hauptverfasser: Bennett, Eric Paul, Hassan, Helle, Hollingsworth, Michael A., Clausen, Henrik
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Animals
Blotting, Northern
Cloning, Molecular
DNA, Complementary - metabolism
EST, expressed sequence tags
GalNAc, N-acetylgalactosamine
GalNAc-transferase
GalNAc-transferase, UDP-GalNAc:polypeptide αGalNAc-transferase (EC 2.4.1.41)
Glycosylation
Glycosyltransferase
Humans
Isoenzymes
Kinetics
Molecular Sequence Data
Mucin
N-Acetylgalactosaminyltransferases - isolation & purification
N-Acetylgalactosaminyltransferases - metabolism
O-Glycosylation
Peptides - chemistry
Peptides - metabolism
RACE, rapid amplification of cDNA ends
Rats
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Substrate Specificity
Tissue Distribution
Uridine Diphosphate - chemistry
Uridine Diphosphate - metabolism
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Zusammenfassung:A novel member of the human UDP- N-acetyl- D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)01268-5