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Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells

Calpains are a family of Ca(2+)-dependent intracellular cysteine proteases, including the ubiquitously expressed μ-calpain (CANP1) and m-calpain (CANP2). The CANP1 has been found to play a central role in postmortem proteolysis and meat tenderization. However, the physiological roles of CANP1 in cat...

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Autores principales: Van Ba, Hoa, Inho, Hwang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3825316/
https://www.ncbi.nlm.nih.gov/pubmed/23943438
http://dx.doi.org/10.1007/s11626-013-9666-5
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author Van Ba, Hoa
Inho, Hwang
author_facet Van Ba, Hoa
Inho, Hwang
author_sort Van Ba, Hoa
collection PubMed
description Calpains are a family of Ca(2+)-dependent intracellular cysteine proteases, including the ubiquitously expressed μ-calpain (CANP1) and m-calpain (CANP2). The CANP1 has been found to play a central role in postmortem proteolysis and meat tenderization. However, the physiological roles of CANP1 in cattle skeletal satellite cells remain unclear. In this study, three small interference RNA sequences (siRNAs) targeting CANP1 gene were designed and ligated into pSilencer plasmid vector to construct shRNA expression constructs. Suppression of CANP1 in satellite cells was evaluated using these shRNA expressing constructs. Our results revealed that all three siRNAs could downregulate the expression of CANP1. Suppression of CANP1 significantly reduced cell viability in cell proliferation when compared with control cells. We found a crosstalk between CANP1 and caspase systems, particularly suppression of CANP1 resulted in an increase in the expressions of apoptotic caspases such as caspase-3, caspase-6, caspase-7, caspase-8, and caspase-9, as well as heat-shock protein (HSP) systems. Additionally, suppression of CANP1 led to the upregulation of other apoptosis and DNA damage-regulating genes whilst at the same time downregulating proliferation, migration, and differentiation-regulating genes. The results of our findings report for the first time that suppression of CANP1 resulted in the activation of caspase and HSP systems which might in turn regulate apoptosis through the caspase-dependent cell death pathway. This clearly demonstrates the key roles of CANP1 in regulation of cell proliferation and survival. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s11626-013-9666-5) contains supplementary material, which is available to authorized users.
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spelling pubmed-38253162013-11-21 Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells Van Ba, Hoa Inho, Hwang In Vitro Cell Dev Biol Anim Article Calpains are a family of Ca(2+)-dependent intracellular cysteine proteases, including the ubiquitously expressed μ-calpain (CANP1) and m-calpain (CANP2). The CANP1 has been found to play a central role in postmortem proteolysis and meat tenderization. However, the physiological roles of CANP1 in cattle skeletal satellite cells remain unclear. In this study, three small interference RNA sequences (siRNAs) targeting CANP1 gene were designed and ligated into pSilencer plasmid vector to construct shRNA expression constructs. Suppression of CANP1 in satellite cells was evaluated using these shRNA expressing constructs. Our results revealed that all three siRNAs could downregulate the expression of CANP1. Suppression of CANP1 significantly reduced cell viability in cell proliferation when compared with control cells. We found a crosstalk between CANP1 and caspase systems, particularly suppression of CANP1 resulted in an increase in the expressions of apoptotic caspases such as caspase-3, caspase-6, caspase-7, caspase-8, and caspase-9, as well as heat-shock protein (HSP) systems. Additionally, suppression of CANP1 led to the upregulation of other apoptosis and DNA damage-regulating genes whilst at the same time downregulating proliferation, migration, and differentiation-regulating genes. The results of our findings report for the first time that suppression of CANP1 resulted in the activation of caspase and HSP systems which might in turn regulate apoptosis through the caspase-dependent cell death pathway. This clearly demonstrates the key roles of CANP1 in regulation of cell proliferation and survival. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s11626-013-9666-5) contains supplementary material, which is available to authorized users. Springer US 2013-08-13 2013 /pmc/articles/PMC3825316/ /pubmed/23943438 http://dx.doi.org/10.1007/s11626-013-9666-5 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by-nc/2.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Article
Van Ba, Hoa
Inho, Hwang
Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title_full Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title_fullStr Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title_full_unstemmed Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title_short Significant role of μ-calpain (CANP1) in proliferation/survival of bovine skeletal muscle satellite cells
title_sort significant role of μ-calpain (canp1) in proliferation/survival of bovine skeletal muscle satellite cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3825316/
https://www.ncbi.nlm.nih.gov/pubmed/23943438
http://dx.doi.org/10.1007/s11626-013-9666-5
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