Abstract
Angiogenesis is a key event in cancer progression and therefore a promising target in cancer treatment. Galectin-1, a β-galactoside binding lectin, is up-regulated in the endothelium of tumors of different origin and has been shown to be the target for anginex, a powerful anti-angiogenic peptide with anti-tumor activity. Here we show that when bound to anginex, galectin-1 binds various glycoproteins with hundred- to thousand-fold higher affinity. Anginex also interacts with galectin-2, -7, -8N, and -9N but not with galectin-3, -4, or -9C.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Angiogenesis Inhibitors / chemistry
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Angiogenesis Inhibitors / pharmacology*
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Disaccharides / chemistry
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Fluorescence Polarization / methods
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Galectin 1 / biosynthesis*
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Galectins / chemistry
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Glycoconjugates / chemistry
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Glycoproteins / chemistry*
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Haptoglobins / chemistry
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Humans
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Kinetics
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Lectins / chemistry
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Microscopy, Fluorescence / methods
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Neoplasms / metabolism
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Peptides / chemistry
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Peptides / pharmacology*
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Protein Binding
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alpha-Fetoproteins / chemistry
Substances
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Angiogenesis Inhibitors
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Disaccharides
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Galectin 1
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Galectins
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Glycoconjugates
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Glycoproteins
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Haptoglobins
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Lectins
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Peptides
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alpha-Fetoproteins
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anginex peptide