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Originally published In Press as doi:10.1074/jbc.M111690200 on January 2, 2002

J. Biol. Chem., Vol. 277, Issue 10, 7736-7751, March 8, 2002
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Determination of the Site-specific Oligosaccharide Distribution of the O-Glycans Attached to the Porcine Submaxillary Mucin Tandem Repeat
FURTHER EVIDENCE FOR THE MODULATION OF O-GLYCAN SIDE CHAIN STRUCTURES BY PEPTIDE SEQUENCE*

Thomas A. GerkenDagger , Marc Gilmore, and Jiexin Zhang

From the Departments of Pediatrics and Biochemistry, W. A. Bernbaum Center for Cystic Fibrosis Research, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106

Little is known of the degree that polypeptide sequence and the local environment modulate the structures of O-linked glycans. Toward this understanding, the site-specific mono- (GalNAc-O-), di- (beta -Gal-1,3-alpha -GalNAc-O-), and trisaccharide (alpha -Fuc-1,2-beta -Gal-1,3-alpha -GalNAc-O-) distributions have been determined for 29 of the 31 O-glycosylated Ser/Thr residues in the tandem repeat domains of blood group A-negative porcine submaxillary gland mucin. The glycosylation patterns obtained from three individual animals are in agreement with earlier incomplete determinations on a pooled mucin (Gerken, T. A., Owens, C. L., and Pasumarthy, M. (1997) J. Biol. Chem. 272, 9709-9719; Gerken, T. A., Owens, C. L., and Pasumarthy, M. (1998) J. Biol. Chem. 273, 26580-26588), confirming that the addition of the peptide-linked GalNAc and its substitution by beta -1,3-Gal are sensitive to local peptide sequence in a highly reproducible manner in vivo. The present data further support earlier suggestions of an inverse correlation of the density of hydroxyamino acid residues (and by inference the density of peptide GalNAc) with the extent of substitution of the peptide-linked GalNAc by beta -1,3-Gal. This effect is highly correlated for Ser-linked glycans but not for Thr-linked glycans. A similar correlation is observed with respect to the in vivo peptide GalNAc glycosylation pattern. In contrast, the addition of alpha -1,2-Fuc to beta -Gal shows no apparent correlation with hydroxyamino acid density, although a marked elevation in the fucosylation of Ser-linked glycans compared with Thr-linked glycans is observed. The above effects may represent both steric and conformational factors acting to alter the relative accessibility and activity of the glycosyltransferases toward substrate. These results demonstrate that the porcine submaxillary gland core 1 beta 3-galactosyltransferase and alpha 2-fucosyltransferase exhibit unique peptide/glycopeptide sensitivities that may provide mechanisms for the modulation of O-linked side chain structures.

* This work was supported by NCI Grant RO1-CA-78834 from the National Institutes of Health and by the Cystic Fibrosis Foundation.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.

Dagger To whom correspondence should be addressed: Dept. of Pediatrics, Case Western Reserve University School of Medicine, BRB, 2109 Adelbert Rd., Cleveland, OH 44106-4948. Tel.: 216-368-4556; Fax: 216-368-4223; E-mail: txg2@po.cwru.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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