Abstract
Angiogenesis is the first regulatory step of tumor progression. Herein, we report on some findings that show that beta1,6-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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Catalytic Domain
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Cell Division
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Cells, Cultured
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Chick Embryo
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Chorion / metabolism
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Culture Media, Conditioned / pharmacology
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Dose-Response Relationship, Drug
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Endothelium, Vascular / cytology
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Extracellular Matrix / metabolism
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Fibroblast Growth Factor 2 / metabolism
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Glycosylation*
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Heparan Sulfate Proteoglycans / metabolism
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Humans
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Mice
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Mice, Nude
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Models, Biological
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Molecular Sequence Data
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N-Acetylglucosaminyltransferases / metabolism*
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N-Acetylglucosaminyltransferases / physiology*
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Neoplasm Metastasis
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Neoplasm Transplantation
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Neovascularization, Pathologic*
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Peptides / chemistry
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Transfection
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Tumor Cells, Cultured
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Umbilical Veins / cytology
Substances
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Culture Media, Conditioned
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Heparan Sulfate Proteoglycans
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Peptides
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Recombinant Proteins
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Fibroblast Growth Factor 2
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N-Acetylglucosaminyltransferases
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alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase