Title

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

Authors

Astha Jaiswal, Aastha Chhabra, Umang Malhotra, Shrey Kohli, Vibha Rani* 

Affiliation

Department of Biotechnology, Jaypee Institute of Information Technology, A-10, Sector-62, NOIDA- 201307, Uttar Pradesh, India 

Email

vibha.rani@jiit.ac.in; *Corresponding author

Phone

+ (91)-120-2594210

Fax

+ (91)-120-2400986

Article Type

Hypothesis

Date

Received February 03, 2011; Accepted February 07, 2011; Published March 02, 2011

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.  

Citation

Jaiswal et al. Bioinformation 6(1): 23-30 (2011)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.