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Caspases: evolutionary aspects of their functions in vertebrates

Caspases (cysteine-dependent aspartyl-specific protease) belong to a family of cysteine proteases that mediate proteolytic events indispensable for biological phenomena such as cell death and inflammation. The first caspase was identified as an executioner of apoptotic cell death in the worm Caenorh...

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Detalles Bibliográficos
Autores principales: Sakamaki, K, Satou, Y
Formato: Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2779465/
https://www.ncbi.nlm.nih.gov/pubmed/20735596
http://dx.doi.org/10.1111/j.1095-8649.2009.02184.x
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author Sakamaki, K
Satou, Y
author_facet Sakamaki, K
Satou, Y
author_sort Sakamaki, K
collection PubMed
description Caspases (cysteine-dependent aspartyl-specific protease) belong to a family of cysteine proteases that mediate proteolytic events indispensable for biological phenomena such as cell death and inflammation. The first caspase was identified as an executioner of apoptotic cell death in the worm Caenorhabditis elegans. Additionally, a large number of caspases have been identified in various animals from sponges to vertebrates. Caspases are thought to play a pivotal role in apoptosis as an evolutionarily conserved function; however, the number of caspases that can be identified is distinct for each species. This indicates that species-specific functions or diversification of physiological roles has been cultivated through caspase evolution. Furthermore, recent studies suggest that caspases are also involved in inflammation and cellular differentiation in mammals. This review highlights vertebrate caspases in their universal and divergent functions and provides insight into the physiological roles of these molecules in animals.
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spelling pubmed-27794652009-11-24 Caspases: evolutionary aspects of their functions in vertebrates Sakamaki, K Satou, Y J Fish Biol Review Paper Caspases (cysteine-dependent aspartyl-specific protease) belong to a family of cysteine proteases that mediate proteolytic events indispensable for biological phenomena such as cell death and inflammation. The first caspase was identified as an executioner of apoptotic cell death in the worm Caenorhabditis elegans. Additionally, a large number of caspases have been identified in various animals from sponges to vertebrates. Caspases are thought to play a pivotal role in apoptosis as an evolutionarily conserved function; however, the number of caspases that can be identified is distinct for each species. This indicates that species-specific functions or diversification of physiological roles has been cultivated through caspase evolution. Furthermore, recent studies suggest that caspases are also involved in inflammation and cellular differentiation in mammals. This review highlights vertebrate caspases in their universal and divergent functions and provides insight into the physiological roles of these molecules in animals. Blackwell Publishing Ltd 2009-03 /pmc/articles/PMC2779465/ /pubmed/20735596 http://dx.doi.org/10.1111/j.1095-8649.2009.02184.x Text en Journal compilation © 2009 The Fisheries Society of the British Isles http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.
spellingShingle Review Paper
Sakamaki, K
Satou, Y
Caspases: evolutionary aspects of their functions in vertebrates
title Caspases: evolutionary aspects of their functions in vertebrates
title_full Caspases: evolutionary aspects of their functions in vertebrates
title_fullStr Caspases: evolutionary aspects of their functions in vertebrates
title_full_unstemmed Caspases: evolutionary aspects of their functions in vertebrates
title_short Caspases: evolutionary aspects of their functions in vertebrates
title_sort caspases: evolutionary aspects of their functions in vertebrates
topic Review Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2779465/
https://www.ncbi.nlm.nih.gov/pubmed/20735596
http://dx.doi.org/10.1111/j.1095-8649.2009.02184.x
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