Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice

Myostatin deficiency leads to extensive skeletal muscle hypertrophy, but its consequence on post-mortem muscle proteolysis is unknown. Here, we compared muscle myofibrillar protein degradation, and autophagy, ubiquitin-proteasome and Ca2+-dependent proteolysis relative to the energetic and redox sta...

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Published inMeat science Vol. 185; p. 108726
Main Authors Nassar, Rim, Vernus, Barbara, Carnac, Gilles, Fouret, Gilles, Goustard, Bénédicte, Casas, François, Tintignac, Lionel, Cassar-Malek, Isabelle, Picard, Brigitte, Seiliez, Iban, Brioche, Thomas, Koechlin-Ramonatxo, Christelle, Bertrand-Gaday, Christelle, Hamade, Aline, Najjar, Fadia, Chabi, Béatrice, Bonnieu, Anne
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.03.2022
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Abstract Myostatin deficiency leads to extensive skeletal muscle hypertrophy, but its consequence on post-mortem muscle proteolysis is unknown. Here, we compared muscle myofibrillar protein degradation, and autophagy, ubiquitin-proteasome and Ca2+-dependent proteolysis relative to the energetic and redox status in wild-type (WT) and myostatin knock-out mice (KO) during early post-mortem storage. KO muscles showed higher degradation of myofibrillar proteins in the first 24 h after death, associated with preserved antioxidant status, compared with WT muscles. Analysis of key autophagy and ubiquitin-proteasome system markers indicated that these two pathways were not upregulated in post-mortem muscle (both genotypes), but basal autophagic flux and ATP content were lower in KO muscles. Proteasome and caspase activities were not different between WT and KO mice. Conversely, calpain activity was higher in KO muscles, concomitantly with higher troponin T and desmin degradation. Altogether, these results suggest that calpains but not the autophagy, proteasome and caspase systems, explain the difference in post-mortem muscle protein proteolysis between both genotypes. •Specific proteolytic changes in post-mortem skeletal muscle are observed upon myostatin deletion (Mstn KO).•Loss of myostatin increases protein breakdown in post-mortem skeletal muscle.•Autophagy and proteasome are active in post-mortem skeletal muscle.•The increased post-mortem proteolysis in Mstn KO mice might be attributed to the calpain system.
AbstractList Myostatin deficiency leads to extensive skeletal muscle hypertrophy, but its consequence on post-mortem muscle proteolysis is unknown. Here, we compared muscle myofibrillar protein degradation, and autophagy, ubiquitin-proteasome and Ca2+-dependent proteolysis relative to the energetic and redox status in wild-type (WT) and myostatin knock-out mice (KO) during early post-mortem storage. KO muscles showed higher degradation of myofibrillar proteins in the first 24 h after death, associated with preserved antioxidant status, compared with WT muscles. Analysis of key autophagy and ubiquitin-proteasome system markers indicated that these two pathways were not upregulated in post-mortem muscle (both genotypes), but basal autophagic flux and ATP content were lower in KO muscles. Proteasome and caspase activities were not different between WT and KO mice. Conversely, calpain activity was higher in KO muscles, concomitantly with higher troponin T and desmin degradation. Altogether, these results suggest that calpains but not the autophagy, proteasome and caspase systems, explain the difference in post-mortem muscle protein proteolysis between both genotypes. •Specific proteolytic changes in post-mortem skeletal muscle are observed upon myostatin deletion (Mstn KO).•Loss of myostatin increases protein breakdown in post-mortem skeletal muscle.•Autophagy and proteasome are active in post-mortem skeletal muscle.•The increased post-mortem proteolysis in Mstn KO mice might be attributed to the calpain system.
Myostatin deficiency leads to extensive skeletal muscle hypertrophy, but its consequence on post-mortem muscle proteolysis is unknown. Here, we compared muscle myofibrillar protein degradation, and autophagy, ubiquitin-proteasome and Ca -dependent proteolysis relative to the energetic and redox status in wild-type (WT) and myostatin knock-out mice (KO) during early post-mortem storage. KO muscles showed higher degradation of myofibrillar proteins in the first 24 h after death, associated with preserved antioxidant status, compared with WT muscles. Analysis of key autophagy and ubiquitin-proteasome system markers indicated that these two pathways were not upregulated in post-mortem muscle (both genotypes), but basal autophagic flux and ATP content were lower in KO muscles. Proteasome and caspase activities were not different between WT and KO mice. Conversely, calpain activity was higher in KO muscles, concomitantly with higher troponin T and desmin degradation. Altogether, these results suggest that calpains but not the autophagy, proteasome and caspase systems, explain the difference in post-mortem muscle protein proteolysis between both genotypes.
ArticleNumber 108726
Author Vernus, Barbara
Brioche, Thomas
Casas, François
Bertrand-Gaday, Christelle
Tintignac, Lionel
Fouret, Gilles
Hamade, Aline
Koechlin-Ramonatxo, Christelle
Chabi, Béatrice
Nassar, Rim
Seiliez, Iban
Najjar, Fadia
Cassar-Malek, Isabelle
Carnac, Gilles
Picard, Brigitte
Goustard, Bénédicte
Bonnieu, Anne
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Keywords Oxidative stress
Myofibrillar protein
Post-mortem
Proteolysis
Skeletal muscle
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Snippet Myostatin deficiency leads to extensive skeletal muscle hypertrophy, but its consequence on post-mortem muscle proteolysis is unknown. Here, we compared muscle...
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StartPage 108726
SubjectTerms Animals
Calpain - genetics
Calpain - metabolism
Gene Silencing
Mice
Muscle, Skeletal - metabolism
Myofibrillar protein
Myostatin - genetics
Oxidative stress
Post-mortem
Proteolysis
Skeletal muscle
Title Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice
URI https://dx.doi.org/10.1016/j.meatsci.2021.108726
https://www.ncbi.nlm.nih.gov/pubmed/34973590
https://search.proquest.com/docview/2615919696
Volume 185
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