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Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment

Members of the lysyl oxidase (LOX) family are secreted copper-dependent amine oxidases that catalyze the covalent crosslinking of collagens and elastin in the extracellular matrix (ECM), an essential process for the structural integrity of all tissues. LOX enzymes can also remodel the tumor microenv...

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Detalles Bibliográficos
Autores principales: Amendola, Pier Giorgio, Reuten, Raphael, Erler, Janine Terra
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6562985/
https://www.ncbi.nlm.nih.gov/pubmed/31130685
http://dx.doi.org/10.3390/cancers11050729
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author Amendola, Pier Giorgio
Reuten, Raphael
Erler, Janine Terra
author_facet Amendola, Pier Giorgio
Reuten, Raphael
Erler, Janine Terra
author_sort Amendola, Pier Giorgio
collection PubMed
description Members of the lysyl oxidase (LOX) family are secreted copper-dependent amine oxidases that catalyze the covalent crosslinking of collagens and elastin in the extracellular matrix (ECM), an essential process for the structural integrity of all tissues. LOX enzymes can also remodel the tumor microenvironment and have been implicated in all stages of tumor initiation and progression of many cancer types. Changes in the ECM can influence several cancer cell phenotypes. Integrin adhesion complexes (IACs) physically connect cells with their microenvironment. This review article summarizes the main findings on the role of LOX proteins in modulating the tumor microenvironment, with a particular focus on how ECM changes are integrated by IACs to modulate cells behavior. Finally, we discuss how the development of selective LOX inhibitors may lead to novel and effective therapies in cancer treatment.
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spelling pubmed-65629852019-06-17 Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment Amendola, Pier Giorgio Reuten, Raphael Erler, Janine Terra Cancers (Basel) Review Members of the lysyl oxidase (LOX) family are secreted copper-dependent amine oxidases that catalyze the covalent crosslinking of collagens and elastin in the extracellular matrix (ECM), an essential process for the structural integrity of all tissues. LOX enzymes can also remodel the tumor microenvironment and have been implicated in all stages of tumor initiation and progression of many cancer types. Changes in the ECM can influence several cancer cell phenotypes. Integrin adhesion complexes (IACs) physically connect cells with their microenvironment. This review article summarizes the main findings on the role of LOX proteins in modulating the tumor microenvironment, with a particular focus on how ECM changes are integrated by IACs to modulate cells behavior. Finally, we discuss how the development of selective LOX inhibitors may lead to novel and effective therapies in cancer treatment. MDPI 2019-05-26 /pmc/articles/PMC6562985/ /pubmed/31130685 http://dx.doi.org/10.3390/cancers11050729 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Amendola, Pier Giorgio
Reuten, Raphael
Erler, Janine Terra
Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title_full Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title_fullStr Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title_full_unstemmed Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title_short Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
title_sort interplay between lox enzymes and integrins in the tumor microenvironment
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6562985/
https://www.ncbi.nlm.nih.gov/pubmed/31130685
http://dx.doi.org/10.3390/cancers11050729
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