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Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation

The family of matrix metalloproteinases (MMPs) consists of a set of biological targets that are involved in a multitude of severe pathogenic events such as different forms of cancers or arthritis. Modulation of the target class with small molecule drugs has not led to the anticipated success until p...

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Detalles Bibliográficos
Autores principales: Fischer, Thomas, Riedl, Rainer
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6631688/
https://www.ncbi.nlm.nih.gov/pubmed/31216704
http://dx.doi.org/10.3390/molecules24122265
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author Fischer, Thomas
Riedl, Rainer
author_facet Fischer, Thomas
Riedl, Rainer
author_sort Fischer, Thomas
collection PubMed
description The family of matrix metalloproteinases (MMPs) consists of a set of biological targets that are involved in a multitude of severe pathogenic events such as different forms of cancers or arthritis. Modulation of the target class with small molecule drugs has not led to the anticipated success until present, as all clinical trials failed due to unacceptable side effects or a lack of therapeutic outcome. Monoclonal antibodies offer a tremendous therapeutic potential given their high target selectivity and good pharmacokinetic profiles. For the treatment of a variety of diseases there are already antibody therapies available and the number is increasing. Recently, several antibodies were developed for the selective inhibition of single MMPs that showed high potency and were therefore investigated in in vivo studies with promising results. In this review, we highlight the progress that has been achieved toward the design of inhibitory antibodies that successfully modulate MMP-9 and MMP-14.
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spelling pubmed-66316882019-08-19 Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation Fischer, Thomas Riedl, Rainer Molecules Review The family of matrix metalloproteinases (MMPs) consists of a set of biological targets that are involved in a multitude of severe pathogenic events such as different forms of cancers or arthritis. Modulation of the target class with small molecule drugs has not led to the anticipated success until present, as all clinical trials failed due to unacceptable side effects or a lack of therapeutic outcome. Monoclonal antibodies offer a tremendous therapeutic potential given their high target selectivity and good pharmacokinetic profiles. For the treatment of a variety of diseases there are already antibody therapies available and the number is increasing. Recently, several antibodies were developed for the selective inhibition of single MMPs that showed high potency and were therefore investigated in in vivo studies with promising results. In this review, we highlight the progress that has been achieved toward the design of inhibitory antibodies that successfully modulate MMP-9 and MMP-14. MDPI 2019-06-18 /pmc/articles/PMC6631688/ /pubmed/31216704 http://dx.doi.org/10.3390/molecules24122265 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
Fischer, Thomas
Riedl, Rainer
Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title_full Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title_fullStr Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title_full_unstemmed Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title_short Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
title_sort inhibitory antibodies designed for matrix metalloproteinase modulation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6631688/
https://www.ncbi.nlm.nih.gov/pubmed/31216704
http://dx.doi.org/10.3390/molecules24122265
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