The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins

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 wit...

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Autores principales: Salomonsson, Emma, Thijssen, Victor L., Griffioen, Arjan W., Nilsson, Ulf J., Leffler, Hakon
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2011
Materias:
Reports
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077580/
https://www.ncbi.nlm.nih.gov/pubmed/21372130
http://dx.doi.org/10.1074/jbc.C111.229096
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author Salomonsson, Emma
Thijssen, Victor L.
Griffioen, Arjan W.
Nilsson, Ulf J.
Leffler, Hakon
author_facet Salomonsson, Emma
Thijssen, Victor L.
Griffioen, Arjan W.
Nilsson, Ulf J.
Leffler, Hakon
author_sort Salomonsson, Emma
collection PubMed
description 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.
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spelling pubmed-30775802011-05-02 The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins Salomonsson, Emma Thijssen, Victor L. Griffioen, Arjan W. Nilsson, Ulf J. Leffler, Hakon J Biol Chem Reports 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. American Society for Biochemistry and Molecular Biology 2011-04-22 2011-03-03 /pmc/articles/PMC3077580/ /pubmed/21372130 http://dx.doi.org/10.1074/jbc.C111.229096 Text en © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version full access. Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles
spellingShingle Reports
Salomonsson, Emma
Thijssen, Victor L.
Griffioen, Arjan W.
Nilsson, Ulf J.
Leffler, Hakon
The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title_full The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title_fullStr The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title_full_unstemmed The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title_short The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for Glycoproteins
title_sort anti-angiogenic peptide anginex greatly enhances galectin-1 binding affinity for glycoproteins
topic Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3077580/
https://www.ncbi.nlm.nih.gov/pubmed/21372130
http://dx.doi.org/10.1074/jbc.C111.229096
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