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.
Highlights
Anginex is a 33-mer cytokine-like artificial -peptide that inhibits endothelial cell growth by blocking adhesion and migration of activated endothelial cells leading to angiogenesis in vitro and in vivo [1, 2]
Galectin-1 consists of an ϳ135-amino acid canonical galectin carbohydrate recognition domain (CRD),2 which exists as a
We analyzed the effect of anginex on the carbohydrate binding activity of galectin-1, with the hypothesis that it would act as an inhibitor
Summary
Anginex is a 33-mer cytokine-like artificial -peptide (the sequence is given in supplemental Fig. S1) that inhibits endothelial cell growth by blocking adhesion and migration of activated endothelial cells leading to angiogenesis in vitro and in vivo [1, 2]. With a fixed concentration of a newly designed high affinity tdga-probe [8] (supplemental Fig. S2A) and increasing concentrations of galectin-1, the anisotropy rose from a value
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