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J. Biol. Chem., Vol. 277, Issue 19, 17002-17008, May 10, 2002
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From the Department of Biochemistry, Osaka University Medical
School, Suita, Osaka 565-0871, Japan
Angiogenesis is the first regulatory
step of tumor progression. Herein, we report on some findings that show
that
A Secreted Type of
1,6-N-Acetylglucosaminyltransferase V (GnT-V) Induces
Tumor Angiogenesis without Mediation of Glycosylation
A NOVEL FUNCTION OF GnT-V DISTINCT FROM THE ORIGINAL
GLYCOSYLTRANSFERASE ACTIVITY*
1,6-N-acetylglucosaminyltransferase V (GnT-V)
functions as an inducer of angiogenesis that has a novel and completely
different function from the original function of glycosyltransferase. A
secreted type of GnT-V protein itself promoted angiogenesis in
vitro and in vivo at physiological concentrations. The highly basic domain of GnT-V induced the release of fibroblast growth factor-2 from heparan sulfate proteoglycan on the cell surface
and/or extracellular matrix, leading to angiogenesis. These findings
provide some novel information on the relationship between GnT-V and
tumor metastasis. The inhibition of GnT-V secretion or its expression
represents a novel potential strategy for the inhibition of tumor angiogenesis.
*
This work was supported by Grant-in-Aid for Scientific
Research (S) No. 13854010 from the Japan Society for the promotion of
Science.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.
To whom correspondence should be addressed. Tel.: 81-6-6879-3421;
Fax: 81-6-6879-3429; E-mail: proftani@biochem.med.osaka-u.ac.jp.
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