Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Blotting, Northern
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Cloning, Molecular
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DNA, Complementary / metabolism
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Glycosylation
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Humans
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Isoenzymes
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Kinetics
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Molecular Sequence Data
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N-Acetylgalactosaminyltransferases / isolation & purification
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N-Acetylgalactosaminyltransferases / metabolism*
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Peptides / chemistry
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Peptides / metabolism*
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Rats
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Substrate Specificity
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Tissue Distribution
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Uridine Diphosphate / chemistry
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Uridine Diphosphate / metabolism*
Substances
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DNA, Complementary
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Isoenzymes
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Peptides
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Recombinant Proteins
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Uridine Diphosphate
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N-Acetylgalactosaminyltransferases
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UDP-N-acetylgalactosamine--polypeptide N-acetylgalactosaminyltransferase 7