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Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis

Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be responsible for cleaving procaspase-12, a caspase localized in the ER, to generate active caspase-12. In addition, calpain may be responsibl...

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Detalles Bibliográficos
Autores principales: Nakagawa, Toshiyuki, Yuan, Junying
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175271/
https://www.ncbi.nlm.nih.gov/pubmed/10953012
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author Nakagawa, Toshiyuki
Yuan, Junying
author_facet Nakagawa, Toshiyuki
Yuan, Junying
author_sort Nakagawa, Toshiyuki
collection PubMed
description Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be responsible for cleaving procaspase-12, a caspase localized in the ER, to generate active caspase-12. In addition, calpain may be responsible for cleaving the loop region in Bcl-xL and, therefore, turning an antiapoptotic molecule into a proapoptotic molecule. We propose that disturbance to intracellular calcium storage as a result of ischemic injury or amyloid β peptide cytotoxicity may induce apoptosis through calpain- mediated caspase-12 activation and Bcl-xL inactivation. These data suggest a novel apoptotic pathway involving calcium-mediated calpain activation and cross-talks between calpain and caspase families.
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spelling pubmed-21752712008-05-01 Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis Nakagawa, Toshiyuki Yuan, Junying J Cell Biol Report Calpains and caspases are two cysteine protease families that play important roles in regulating pathological cell death. Here, we report that m-calpain may be responsible for cleaving procaspase-12, a caspase localized in the ER, to generate active caspase-12. In addition, calpain may be responsible for cleaving the loop region in Bcl-xL and, therefore, turning an antiapoptotic molecule into a proapoptotic molecule. We propose that disturbance to intracellular calcium storage as a result of ischemic injury or amyloid β peptide cytotoxicity may induce apoptosis through calpain- mediated caspase-12 activation and Bcl-xL inactivation. These data suggest a novel apoptotic pathway involving calcium-mediated calpain activation and cross-talks between calpain and caspase families. The Rockefeller University Press 2000-08-21 /pmc/articles/PMC2175271/ /pubmed/10953012 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Report
Nakagawa, Toshiyuki
Yuan, Junying
Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title_full Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title_fullStr Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title_full_unstemmed Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title_short Cross-Talk between Two Cysteine Protease Families: Activation of Caspase-12 by Calpain in Apoptosis
title_sort cross-talk between two cysteine protease families: activation of caspase-12 by calpain in apoptosis
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175271/
https://www.ncbi.nlm.nih.gov/pubmed/10953012
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