Unknown

Dataset Information

0

The anti-angiogenic peptide anginex greatly enhances galectin-1 binding affinity for glycoproteins.


ABSTRACT: Angiogenesis is a key event in cancer progression and therefore a promising target in cancer treatment. Galectin-1, a ?-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.

SUBMITTER: Salomonsson E 

PROVIDER: S-EPMC3077580 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

The anti-angiogenic peptide anginex greatly enhances galectin-1 binding affinity for glycoproteins.

Salomonsson Emma E   Thijssen Victor L VL   Griffioen Arjan W AW   Nilsson Ulf J UJ   Leffler Hakon H  

The Journal of biological chemistry 20110303 16


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,  ...[more]

Similar Datasets

| S-EPMC3305883 | biostudies-literature
| S-EPMC4788467 | biostudies-literature
| S-EPMC4598770 | biostudies-literature
| S-EPMC2783032 | biostudies-literature
| S-EPMC5431226 | biostudies-literature
| S-EPMC6311502 | biostudies-literature
| S-EPMC5914451 | biostudies-literature
| S-EPMC2785595 | biostudies-literature
| S-EPMC3553736 | biostudies-literature
| S-EPMC8148638 | biostudies-literature