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J. Biol. Chem., Vol. 276, Issue 31, 29134-29140, August 3, 2001
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From the Syndecan-1, present on the surfaces of normal
murine mammary gland epithelial cells, is a transmembrane hybrid
proteoglycan, which bears glycosaminoglycan (GAG) side chains of
heparan sulfate (HS) and chondroitin sulfate (CS). Purified syndecan-1
ectodomains were analyzed for disaccharide composition and the
GAG-protein linkage region after digestion with bacterial lyases. The
HS chains contained predominantly a nonsulfated unit with smaller
proportions of two monosulfated, two disulfated, and a trisulfated
unit, whereas CS chains were demonstrated for the first time to bear
GlcUA-GalNAc(4-O-sulfate) as a major component as well as
GlcUA-GalNAc, GlcUA-GalNAc(6-O-sulfate), and an E
disaccharide unit GlcUA-GalNAc(4,6-O-disulfate) as minor yet appreciable components. Two kinds of linkage region
tetrasaccharides, GlcUA-Gal-Gal-Xyl and
GlcUA-Gal-Gal-Xyl(2-O-phosphate), were found for
the HS chains in a molar ratio of 55:45. In marked contrast, an
additional sulfated tetrasaccharide,
GlcUA-Gal(4-O-sulfate)-Gal-Xyl, was demonstrated only for
the CS chains, and the unmodified phosphorylated and sulfated
components were present at a molar ratio of 55:26:19. The present study
thus provided conclusive evidence for the hypothesis that
4-O-sulfation of Gal is peculiar to CS chains in contrast to the phosphorylation of Xyl, which is common to both HS and CS
chains. These modifications may be required for biosynthetic maturation
of the linkage region tetrasaccharide sequence, which is a prerequisite
for creating the repeating disaccharide region of GAG chains and/or
biosynthetic selective chain assembly of CS and HS chains.
Structural Characterization of Heparan Sulfate and Chondroitin
Sulfate of Syndecan-1 Purified from Normal Murine Mammary Gland
Epithelial Cells
COMMON PHOSPHORYLATION OF XYLOSE AND DIFFERENTIAL SULFATION OF
GALACTOSE IN THE PROTEIN LINKAGE REGION TETRASACCHARIDE SEQUENCE*
,,¶
Department of Biochemistry, Kobe
Pharmaceutical University, Higashinada-ku, Kobe 658-8558, Japan and the
§ Departments of Pediatrics and Cell Biology, Harvard
Medical School, Children's Hospital, Boston, Massachusetts 02115
*
This work was supported in part by the Science
Research Promotion Fund from Japan Private School Promotion Foundation,
and Grants-in-aid for Encouragement of Young Scientists 11771474 (to S. Y.), Scientific Research 13470493 (to K. S.), and Scientific Research on Priority Areas 10178102 (to K. S.) from the Ministry of
Education, Science, Culture, and Sports of Japan, as well as grants
CA28734 and HD06763 from the National Institutes of Health (to M. B.).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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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