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Papers In Press, published online ahead of print February 6, 2001
National Institute of Dental and Craniofacial Research, 31 Center Drive MSC 2290, Bethesda, MD 20892-2290
Corresponding Author: Lawrence.Tabak{at}nih.gov
We have cloned, expressed and characterized the gene encoding a ninth member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family, termed ppGaNTase-T9. This type II membrane protein consists of a 9 amino acid N-terminal cytoplasmic region, a 20 amino acid hydrophobic/transmembrane region, a 94 amino acid stem region and a 480 amino acid conserved region. Northern blot analysis revealed that the gene encoding this enzyme is expressed in a broadly distributed manner across many adult tissues. Significant levels of 5 kb and 4.2 kb transcripts were found in rat sublingual gland, testis, small intestine, colon and ovary, with lesser amounts in heart, brain, spleen, lung, stomach, cervix and uterus. In situ hybridization to mouse embryos (E14.5) revealed significant hybridization in the developing mandible, maxilla, intestine and mesencephalic ventricle. Constructs expressing this gene transiently in COS7 cells resulted in no detectable transferase activity in vitro against a panel of unmodified peptides, including MUC5AC (GTTPSPVPTTSTTSAP) and EA2 (PTTDSTTPAPTTK). However, when incubated with MUC5AC and EA2 glycopeptides (obtained by the prior action of ppGaNTase-T1), additional incorporation of GalNAc was achieved, resulting in new hydroxyamino acid modification. The activity of this glycopeptide transferase is distinguished from that of ppGaNTase-T7 in that it forms a tetra-glycopeptide species from the MUC5AC tri-glycopeptide substrate whereas ppGaNTase-T7 forms a hexa-glycopeptide species. This isoform thus represents the second example of a glycopeptide transferase and is distinct from the previously identified form in enzymatic activity as well as expression in embryonic and adult tissues. These findings lend further support to the existence of a hierarchical network of differential enzymatic activity within the diversely regulated ppGaNTase family which may play a role in the various processes governing development.
J. Biol. Chem, 10.1074/jbc.M009638200
Submitted on October 23, 2000
Revised on February 6, 2001
Accepted on February 6, 2001
Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9
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