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Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases

The identification of specific target proteins for any diseased condition involves extensive characterization of the potentially involved proteins. Members of a protein family demonstrating comparable features may show certain unusual features when implicated in a pathological condition. Advancement...

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Autores principales: Jaiswal, Astha, Chhabra, Aastha, Malhotra, Umang, Kohli, Shrey, Rani, Vibha
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064848/
https://www.ncbi.nlm.nih.gov/pubmed/21464841
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author Jaiswal, Astha
Chhabra, Aastha
Malhotra, Umang
Kohli, Shrey
Rani, Vibha
author_facet Jaiswal, Astha
Chhabra, Aastha
Malhotra, Umang
Kohli, Shrey
Rani, Vibha
author_sort Jaiswal, Astha
collection PubMed
description The identification of specific target proteins for any diseased condition involves extensive characterization of the potentially involved proteins. Members of a protein family demonstrating comparable features may show certain unusual features when implicated in a pathological condition. Advancements in the field of computational biology and the use of various bioinformatics tools for analysis can aid researchers to comprehend their system of work in primary stages of research. This initial screening can help to reduce time and cost of testing and experimentation in laboratory. Human matrix metalloproteinase (MMP) family of endopeptidases is one such family of 23 members responsible for the remodeling of extracellular matrix (ECM) by degradation of the ECM proteins. Though their role has been implicated in various pathological conditions such as arthritis, atherosclerosis, cancer, liver fibrosis, cardio-vascular and neurodegenerative disorders, little is known about the specific involvement of members of the large MMP family in diseases. A comparative in silico characterization of the MMP protein family has been carried out to analyze their physico-chemical, secondary structural and functional properties. Based on the observed patterns of occurrence of atypical features, we hypothesize that cysteine rich and highly thermostable MMPs might be key players in diseased conditions. Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done. This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns.
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spelling pubmed-30648482011-04-04 Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases Jaiswal, Astha Chhabra, Aastha Malhotra, Umang Kohli, Shrey Rani, Vibha Bioinformation Hypothesis The identification of specific target proteins for any diseased condition involves extensive characterization of the potentially involved proteins. Members of a protein family demonstrating comparable features may show certain unusual features when implicated in a pathological condition. Advancements in the field of computational biology and the use of various bioinformatics tools for analysis can aid researchers to comprehend their system of work in primary stages of research. This initial screening can help to reduce time and cost of testing and experimentation in laboratory. Human matrix metalloproteinase (MMP) family of endopeptidases is one such family of 23 members responsible for the remodeling of extracellular matrix (ECM) by degradation of the ECM proteins. Though their role has been implicated in various pathological conditions such as arthritis, atherosclerosis, cancer, liver fibrosis, cardio-vascular and neurodegenerative disorders, little is known about the specific involvement of members of the large MMP family in diseases. A comparative in silico characterization of the MMP protein family has been carried out to analyze their physico-chemical, secondary structural and functional properties. Based on the observed patterns of occurrence of atypical features, we hypothesize that cysteine rich and highly thermostable MMPs might be key players in diseased conditions. Thus, a plausible grouping of disease responsive MMPs that might be considered as promising clinical targets may be done. This study can be used as a fundamental approach to characterize, analyze and screen large protein families for the identification of signature patterns. Biomedical Informatics 2011-03-02 /pmc/articles/PMC3064848/ /pubmed/21464841 Text en © 2011 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Jaiswal, Astha
Chhabra, Aastha
Malhotra, Umang
Kohli, Shrey
Rani, Vibha
Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title_full Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title_fullStr Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title_full_unstemmed Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title_short Comparative analysis of human matrix metalloproteinases: Emerging therapeutic targets in diseases
title_sort comparative analysis of human matrix metalloproteinases: emerging therapeutic targets in diseases
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064848/
https://www.ncbi.nlm.nih.gov/pubmed/21464841
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