Caspase-1 and IL-1β processing in a teleost fish.

Interleukine-1β (IL-1β) is the most studied pro-inflammatory cytokine, playing a central role in the generation of systemic and local responses to infection, injury, and immunological challenges. In mammals, IL-1β is synthesized as an inactive 31 kDa precursor that is cleaved by caspase-1 generating...

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Autores principales:	Marta I R Reis, Ana do Vale, Pedro J B Pereira, Jorge E Azevedo, Nuno M S Dos Santos
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a54b338533c143e7b7aa3d0d767b8813
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spelling	oai:doaj.org-article:a54b338533c143e7b7aa3d0d767b88132021-11-18T08:06:51ZCaspase-1 and IL-1β processing in a teleost fish.1932-620310.1371/journal.pone.0050450https://doaj.org/article/a54b338533c143e7b7aa3d0d767b88132012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23226286/?tool=EBIhttps://doaj.org/toc/1932-6203Interleukine-1β (IL-1β) is the most studied pro-inflammatory cytokine, playing a central role in the generation of systemic and local responses to infection, injury, and immunological challenges. In mammals, IL-1β is synthesized as an inactive 31 kDa precursor that is cleaved by caspase-1 generating a 17.5 kDa secreted active mature form. The caspase-1 cleavage site strictly conserved in all mammalian IL-1β sequences is absent in IL-1β sequences reported for non-mammalian vertebrates. Recently, fish caspase-1 orthologues have been identified in sea bass (Dicentrarchus labrax) and sea bream (Sparus aurata) but very little is known regarding their processing and activity. In this work it is shown that sea bass caspase-1 auto-processing is similar to that of the human enzyme, resulting in active p24/p10 and p20/p10 heterodimers. Moreover, the presence of alternatively spliced variants of caspase-1 in sea bass is reported. The existence of caspase-1 isoforms in fish and in mammals suggests that they have been evolutionarily maintained and therefore are likely to play a regulatory role in the inflammatory response, as shown for other caspases. Finally, it is shown that sea bass and avian IL-1β are specifically cleaved by caspase-1 at different but phylogenetically conserved aspartates, distinct from the cleavage site of mammalian IL-1β.Marta I R ReisAna do ValePedro J B PereiraJorge E AzevedoNuno M S Dos SantosPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 11, p e50450 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marta I R Reis Ana do Vale Pedro J B Pereira Jorge E Azevedo Nuno M S Dos Santos Caspase-1 and IL-1β processing in a teleost fish.
description	Interleukine-1β (IL-1β) is the most studied pro-inflammatory cytokine, playing a central role in the generation of systemic and local responses to infection, injury, and immunological challenges. In mammals, IL-1β is synthesized as an inactive 31 kDa precursor that is cleaved by caspase-1 generating a 17.5 kDa secreted active mature form. The caspase-1 cleavage site strictly conserved in all mammalian IL-1β sequences is absent in IL-1β sequences reported for non-mammalian vertebrates. Recently, fish caspase-1 orthologues have been identified in sea bass (Dicentrarchus labrax) and sea bream (Sparus aurata) but very little is known regarding their processing and activity. In this work it is shown that sea bass caspase-1 auto-processing is similar to that of the human enzyme, resulting in active p24/p10 and p20/p10 heterodimers. Moreover, the presence of alternatively spliced variants of caspase-1 in sea bass is reported. The existence of caspase-1 isoforms in fish and in mammals suggests that they have been evolutionarily maintained and therefore are likely to play a regulatory role in the inflammatory response, as shown for other caspases. Finally, it is shown that sea bass and avian IL-1β are specifically cleaved by caspase-1 at different but phylogenetically conserved aspartates, distinct from the cleavage site of mammalian IL-1β.
format	article
author	Marta I R Reis Ana do Vale Pedro J B Pereira Jorge E Azevedo Nuno M S Dos Santos
author_facet	Marta I R Reis Ana do Vale Pedro J B Pereira Jorge E Azevedo Nuno M S Dos Santos
author_sort	Marta I R Reis
title	Caspase-1 and IL-1β processing in a teleost fish.
title_short	Caspase-1 and IL-1β processing in a teleost fish.
title_full	Caspase-1 and IL-1β processing in a teleost fish.
title_fullStr	Caspase-1 and IL-1β processing in a teleost fish.
title_full_unstemmed	Caspase-1 and IL-1β processing in a teleost fish.
title_sort	caspase-1 and il-1β processing in a teleost fish.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/a54b338533c143e7b7aa3d0d767b8813
work_keys_str_mv	AT martairreis caspase1andil1bprocessinginateleostfish AT anadovale caspase1andil1bprocessinginateleostfish AT pedrojbpereira caspase1andil1bprocessinginateleostfish AT jorgeeazevedo caspase1andil1bprocessinginateleostfish AT nunomsdossantos caspase1andil1bprocessinginateleostfish
_version_	1718422248245690368

Caspase-1 and IL-1β processing in a teleost fish.

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