Can Bioinformatic Methods Inform Us about the Molecular Evolution of Different Human Caspases?

ISSN: 2212-392X (Online)
ISSN: 1574-8936 (Print)


Volume 9, 5 Issues, 2014


Download PDF Flyer




Current Bioinformatics

Aims & ScopeAbstracted/Indexed in

Ranking and Category:
  • 20th of 52 in Mathematical & Computational Biology

Submit Abstracts Online Submit Manuscripts Online

Editor-in-Chief:
Alessandro Giuliani
Istituto Superiore di Sanitá (Italian NIH) Environment and Health Dept
Roma
Italy


View Full Editorial Board

Subscribe Purchase Articles Order Reprints

Current: 1.726
5 - Year: 1.577

Can Bioinformatic Methods Inform Us about the Molecular Evolution of Different Human Caspases?

Author(s): Jinny Tomar, Vishnu Kumar Gera and Chiranjib Chakraborty


Abstract

Caspases are very important molecule which are playing key role for apoptosis. Deregulation of apoptosis contributes to the pathogenesis of many human diseases. Therefore, the regulation of this protein can be controlled for the therapeutic purpose. To determine molecular evolution (in silico) of proteins is popular method for certain laboratories and biotechnology companies. It may help to detect mutations often occur far away from the active site of the protein. It can give us insight thinking about drug development. Using sequence analysis and phylogenetic approach, we have described about the different human caspases and about their origin in terms of ancestral relationship. It was envisaged using the tools of bioinformatics. Among the fourteen mammalian caspases defined, we are able to make use of twelve human caspases, whose data is publicly available. It is evident from the data studied that human caspase 4 and 5 shares the same origin in comparison to human caspase 1 and caspase 12, irrespective of the fact that both share quite high level of similarity. Although, human caspase related ancestral aspect had been studied earlier but the variation which seems to be quite peculiar in this study is that the executioner, caspase3 shares a remarkable high level of similarity with caspase 7 but this is not applicable to human caspase 6, the other member of executioner group. Human caspase 3 and 7 were seen to have similar substrate specificity but it was not evident in terms of origin. Our findings are assumed to play a significant role in the studies of programmed cell death, inflammatory responses and for scholarly studies in the near future.


Purchase Online Order Reprints Order Eprints Rights and Permissions

  
  



Article Details

Volume: 8
First Page:
Page Count:
DOI: 10.2174/15748936113089990008
Advertisement

Related Journals




Webmaster Contact: urooj@benthamscience.org Copyright © 2014 Bentham Science