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Originally published In Press as doi:10.1074/jbc.M009638200 on February 6, 2001

J. Biol. Chem., Vol. 276, Issue 20, 17395-17404, May 18, 2001
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Cloning and Characterization of a Ninth Member of the UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase Family, ppGaNTase-T9*

Kelly G. Ten HagenDagger , Gurrinder S. BediDagger , Daniel Tetaert§, Paul D. KingsleyDagger , Fred K. HagenDagger , Marlene M. BalysDagger , Thomas M. BeresDagger , Pierre Degand§, and Lawrence A. TabakDagger

From the Dagger  Center for Oral Biology, Aab Institute for Biomedical Sciences, University of Rochester, Rochester, New York 14642 and § INSERM Unite 377, Biologie et Physiopathologie de Cellules Mucipares, Place de Verdun, 59045 Lille Cedex, France

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- and 4.2-kilobase 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 (embryonic day 14.5) 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.

* This work was supported in part by National Institutes of Health Grant DE-08108 (to L. A. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF241241 (rat ppGaNTase-T9).

To whom correspondence should be addressed. Current address: NIDCR, National Institutes of Health, 31 Center Dr., MSC 2290, Bldg. 31, Rm. 2C39, Bethesda, MD 20892-2290. Tel.: 301-496-3571; Fax: 301-402-2185; E-mail: lawrence.tabak@nih.gov.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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