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J Biol Chem, Vol. 273, Issue 13, 7375-7381, March 27, 1998
From the Enzymatic elimination of heparan sulfate (HS)
causes abnormal mesodermal and neural formation in Xenopus
embryos, and HS plays an indispensable role in establishing the
embryogenesis and tissue morphogenesis during early Xenopus
development (Furuya, S., Sera, M., Tohno-oka, R., Sugahara, K.,
Shiokawa, K., and Hirabayashi, Y. (1995) Dev. Growth
Differ. 37, 337-346). In this study, HS was purified from
Xenopus embryos to investigate its disaccharide composition
and binding ability to basic fibroblast growth factor (bFGF) and
follistatin (FS), the latter being provided in two isoforms with core
sequences of 315 and 288 amino acids (designated FS-315 and FS-288)
originating from alternative mRNA splicing. Disaccharide
composition analysis of the purified Xenopus HS showed the
preponderance of a disulfated disaccharide unit with uronic acid
2-O-sulfate and glucosamine 2-N-sulfate, which
has been implicated in the interactions with bFGF. Specific binding of
the HS to bFGF and FS-288, the COOH-terminal truncated form, was
observed in the filter binding assay, whereas HS did not bind to
FS-315, indicating that the acidic Glu-rich domain of FS-315 precluded
the binding. The binding of the HS to bFGF or FS-288 was markedly
inhibited by heparin (HP) and various HS preparations, but not by
chondroitin sulfate, supporting the binding specificity of HS. The
binding specificity was further investigated using FS-288 and bovine
intestinal [3H]HS. Competitive inhibition assays of the
HS binding to FS-288 using size-defined HP oligosaccharides revealed
that the minimum size required for significant inhibition was a
dodecasaccharide, which is larger than the pentasaccharide required for
bFGF binding. The binding affinity of FS to HS increased in the
presence of activin, a growth/differentiation factor, which could be
inactivated by direct binding to FS. These results, taken together,
indicate that the structural requirement for binding of HS to bFGF and FS is different. HS may undergo dynamic changes in its structure during
early Xenopus embryogenesis in response to the temporal and
spatial expression of various growth/differentiation factors.
Molecular Characterization of Xenopus Embryo Heparan
Sulfate
DIFFERENTIAL STRUCTURAL REQUIREMENTS FOR THE SPECIFIC BINDING TO
BASIC FIBROBLAST GROWTH FACTOR AND FOLLISTATIN
,,,
, and
Department of Biochemistry, Kobe
Pharmaceutical University, Higashinada-ku, Kobe 658, the
§ Laboratory for Cellular Glycobiology, Frontier Research
Program, Institute of Physical and Chemical Research (RIKEN), Wako,
Saitama 351-01, the ¶ Laboratory for Molecular Embryology,
Zoological Institute, Faculty of Science, University of Tokyo, Hongo,
Tokyo 113, and the Institute for Enzyme Research, University of
Tokushima, Kuramoto, Tokushima 770, Japan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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