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Autophagy in farm animals: current knowledge and future challenges.

Autophagy

Tesseraud S, Avril P, Bonnet M, Bonnieu A, Cassar-Malek I, Chabi B, Dessauge F, Gabillard JC, Perruchot MH, Seiliez I.
PMID: 32686564
Autophagy. 2021 Aug;17(8):1809-1827. doi: 10.1080/15548627.2020.1798064. Epub 2020 Jul 30.

Autophagy (a process of cellular self-eating) is a conserved cellular degradative process that plays important roles in maintaining homeostasis and preventing nutritional, metabolic, and infection-mediated stresses. Surprisingly, little attention has been paid to the role of this cellular function...

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Tesseraud S, Avril P, Bonnet M, et al. Autophagy in farm animals: current knowledge and future challenges. Autophagy. 2020;17(8):1809-1827doi: 10.1080/15548627.2020.1798064.
Tesseraud, S., Avril, P., Bonnet, M., Bonnieu, A., Cassar-Malek, I., Chabi, B., Dessauge, F., Gabillard, J. C., Perruchot, M. H., & Seiliez, I. (2021). Autophagy in farm animals: current knowledge and future challenges. Autophagy, 17(8), 1809-1827. https://doi.org/10.1080/15548627.2020.1798064
Tesseraud, Sophie, et al. "Autophagy in farm animals: current knowledge and future challenges." Autophagy vol. 17,8 (2021): 1809-1827. doi: https://doi.org/10.1080/15548627.2020.1798064
Tesseraud S, Avril P, Bonnet M, Bonnieu A, Cassar-Malek I, Chabi B, Dessauge F, Gabillard JC, Perruchot MH, Seiliez I. Autophagy in farm animals: current knowledge and future challenges. Autophagy. 2021 Aug;17(8):1809-1827. doi: 10.1080/15548627.2020.1798064. Epub 2020 Jul 30. PMID: 32686564; PMCID: PMC8386602.
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Distribution of H3K27me3, H3K9me3, and H3K4me3 along autophagy-related genes highly expressed in starved zebrafish myotubes.

Biology open

Biga PR, Latimer MN, Froehlich JM, Gabillard JC, Seiliez I.
PMID: 29025701
Biol Open. 2017 Nov 15;6(11):1720-1725. doi: 10.1242/bio.029090.

The zebrafish (

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Biga PR, Latimer MN, Froehlich JM, et al. Distribution of H3K27me3, H3K9me3, and H3K4me3 along autophagy-related genes highly expressed in starved zebrafish myotubes. Biol Open. 2017;6(11):1720-1725doi: 10.1242/bio.029090.
Biga, P. R., Latimer, M. N., Froehlich, J. M., Gabillard, J. C., & Seiliez, I. (2017). Distribution of H3K27me3, H3K9me3, and H3K4me3 along autophagy-related genes highly expressed in starved zebrafish myotubes. Biology open, 6(11), 1720-1725. https://doi.org/10.1242/bio.029090
Biga, Peggy R, et al. "Distribution of H3K27me3, H3K9me3, and H3K4me3 along autophagy-related genes highly expressed in starved zebrafish myotubes." Biology open vol. 6,11 (2017): 1720-1725. doi: https://doi.org/10.1242/bio.029090
Biga PR, Latimer MN, Froehlich JM, Gabillard JC, Seiliez I. Distribution of H3K27me3, H3K9me3, and H3K4me3 along autophagy-related genes highly expressed in starved zebrafish myotubes. Biol Open. 2017 Nov 15;6(11):1720-1725. doi: 10.1242/bio.029090. PMID: 29025701; PMCID: PMC5703616.
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The Autophagic Flux Inhibitor Bafilomycine A1 Affects the Expression of Intermediary Metabolism-Related Genes in Trout Hepatocytes.

Frontiers in physiology

Séité S, Pioche T, Ory N, Plagnes-Juan E, Panserat S, Seiliez I.
PMID: 30936838
Front Physiol. 2019 Mar 18;10:263. doi: 10.3389/fphys.2019.00263. eCollection 2019.

Autophagy is an evolutionarily conserved process of cellular self-eating which emerged these last years as a major adaptive metabolic response to various stresses such as fasting, hypoxia, or environmental pollutants. However, surprisingly very few data is currently available on...

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Séité S, Pioche T, Ory N, et al. The Autophagic Flux Inhibitor Bafilomycine A1 Affects the Expression of Intermediary Metabolism-Related Genes in Trout Hepatocytes. Front Physiol. 2019;10:263doi: 10.3389/fphys.2019.00263.
Séité, S., Pioche, T., Ory, N., Plagnes-Juan, E., Panserat, S., & Seiliez, I. (2019). The Autophagic Flux Inhibitor Bafilomycine A1 Affects the Expression of Intermediary Metabolism-Related Genes in Trout Hepatocytes. Frontiers in physiology, 10263. https://doi.org/10.3389/fphys.2019.00263
Séité, Sarah, et al. "The Autophagic Flux Inhibitor Bafilomycine A1 Affects the Expression of Intermediary Metabolism-Related Genes in Trout Hepatocytes." Frontiers in physiology vol. 10 (2019): 263. doi: https://doi.org/10.3389/fphys.2019.00263
Séité S, Pioche T, Ory N, Plagnes-Juan E, Panserat S, Seiliez I. The Autophagic Flux Inhibitor Bafilomycine A1 Affects the Expression of Intermediary Metabolism-Related Genes in Trout Hepatocytes. Front Physiol. 2019 Mar 18;10:263. doi: 10.3389/fphys.2019.00263. eCollection 2019. PMID: 30936838; PMCID: PMC6431650.
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A Randomized Porcine Study in Low Cardiac Output of Vasoactive and Inotropic Drug Effects on the Gastrointestinal Tract.

Shock (Augusta, Ga.)

Seilitz J, Grafver I, Kiszakiewicz L, Oikonomakis I, Jansson K, Axelsson B, Nilsson KF.
PMID: 33443363
Shock. 2021 Aug 01;56(2):308-317. doi: 10.1097/SHK.0000000000001726.

BACKGROUND: Splanchnic vasodilation by inodilators is an argument for their use in critical cardiac dysfunction. To isolate peripheral vasoactivity from inotropy, such drugs were investigated, and contrasted to vasopressors, in a fixed low cardiac output (CO) model resembling acute...

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Seilitz J, Grafver I, Kiszakiewicz L, et al. A Randomized Porcine Study in Low Cardiac Output of Vasoactive and Inotropic Drug Effects on the Gastrointestinal Tract. Shock. 2021;56(2):308-317doi: 10.1097/SHK.0000000000001726.
Seilitz, J., Grafver, I., Kiszakiewicz, L., Oikonomakis, I., Jansson, K., Axelsson, B., & Nilsson, K. F. (2021). A Randomized Porcine Study in Low Cardiac Output of Vasoactive and Inotropic Drug Effects on the Gastrointestinal Tract. Shock (Augusta, Ga.), 56(2), 308-317. https://doi.org/10.1097/SHK.0000000000001726
Seilitz, Jenny, et al. "A Randomized Porcine Study in Low Cardiac Output of Vasoactive and Inotropic Drug Effects on the Gastrointestinal Tract." Shock (Augusta, Ga.) vol. 56,2 (2021): 308-317. doi: https://doi.org/10.1097/SHK.0000000000001726
Seilitz J, Grafver I, Kiszakiewicz L, Oikonomakis I, Jansson K, Axelsson B, Nilsson KF. A Randomized Porcine Study in Low Cardiac Output of Vasoactive and Inotropic Drug Effects on the Gastrointestinal Tract. Shock. 2021 Aug 01;56(2):308-317. doi: 10.1097/SHK.0000000000001726. PMID: 33443363; PMCID: PMC8529897.
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Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice.

Meat science

Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A.
PMID: 34973590
Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24.

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

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Nassar R, Vernus B, Carnac G, et al. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021;185:108726doi: 10.1016/j.meatsci.2021.108726.
Nassar, R., Vernus, B., Carnac, G., Fouret, G., Goustard, B., Casas, F., Tintignac, L., Cassar-Malek, I., Picard, B., Seiliez, I., Brioche, T., Koechlin-Ramonatxo, C., Bertrand-Gaday, C., Hamade, A., Najjar, F., Chabi, B., & Bonnieu, A. (2021). Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat science, 185108726. https://doi.org/10.1016/j.meatsci.2021.108726
Nassar, Rim, et al. "Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice." Meat science vol. 185 (2021): 108726. doi: https://doi.org/10.1016/j.meatsci.2021.108726
Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24. PMID: 34973590.
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An Orbitrap-based laser desorption/ablation mass spectrometer designed for spaceflight.

Rapid communications in mass spectrometry : RCM

Arevalo R, Selliez L, Briois C, Carrasco N, Thirkell L, Cherville B, Colin F, Gaubicher B, Farcy B, Li X, Makarov A.
PMID: 30048021
Rapid Commun Mass Spectrom. 2018 Nov 15;32(21):1875-1886. doi: 10.1002/rcm.8244.

RATIONALE: The investigation of cryogenic planetary environments as potential harbors for extant life and/or contemporary sites of organic synthesis represents an emerging focal point in planetary exploration. Next generation instruments need to be capable of unambiguously determining elemental and/or...

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Arevalo R, Selliez L, Briois C, et al. An Orbitrap-based laser desorption/ablation mass spectrometer designed for spaceflight. Rapid Commun Mass Spectrom. 2018;32(21):1875-1886doi: 10.1002/rcm.8244.
Arevalo, R., Selliez, L., Briois, C., Carrasco, N., Thirkell, L., Cherville, B., Colin, F., Gaubicher, B., Farcy, B., Li, X., & Makarov, A. (2018). An Orbitrap-based laser desorption/ablation mass spectrometer designed for spaceflight. Rapid communications in mass spectrometry : RCM, 32(21), 1875-1886. https://doi.org/10.1002/rcm.8244
Arevalo, Ricardo, et al. "An Orbitrap-based laser desorption/ablation mass spectrometer designed for spaceflight." Rapid communications in mass spectrometry : RCM vol. 32,21 (2018): 1875-1886. doi: https://doi.org/10.1002/rcm.8244
Arevalo R, Selliez L, Briois C, Carrasco N, Thirkell L, Cherville B, Colin F, Gaubicher B, Farcy B, Li X, Makarov A. An Orbitrap-based laser desorption/ablation mass spectrometer designed for spaceflight. Rapid Commun Mass Spectrom. 2018 Nov 15;32(21):1875-1886. doi: 10.1002/rcm.8244. PMID: 30048021.
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Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice.

Meat science

Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A.
PMID: 34973590
Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24.

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

Cite
Nassar R, Vernus B, Carnac G, et al. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021;185:108726doi: 10.1016/j.meatsci.2021.108726.
Nassar, R., Vernus, B., Carnac, G., Fouret, G., Goustard, B., Casas, F., Tintignac, L., Cassar-Malek, I., Picard, B., Seiliez, I., Brioche, T., Koechlin-Ramonatxo, C., Bertrand-Gaday, C., Hamade, A., Najjar, F., Chabi, B., & Bonnieu, A. (2021). Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat science, 185108726. https://doi.org/10.1016/j.meatsci.2021.108726
Nassar, Rim, et al. "Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice." Meat science vol. 185 (2021): 108726. doi: https://doi.org/10.1016/j.meatsci.2021.108726
Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24. PMID: 34973590.
Copy Download .nbib Format: NLM
Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice.

Meat science

Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A.
PMID: 34973590
Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24.

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

Cite
Nassar R, Vernus B, Carnac G, et al. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021;185:108726doi: 10.1016/j.meatsci.2021.108726.
Nassar, R., Vernus, B., Carnac, G., Fouret, G., Goustard, B., Casas, F., Tintignac, L., Cassar-Malek, I., Picard, B., Seiliez, I., Brioche, T., Koechlin-Ramonatxo, C., Bertrand-Gaday, C., Hamade, A., Najjar, F., Chabi, B., & Bonnieu, A. (2021). Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat science, 185108726. https://doi.org/10.1016/j.meatsci.2021.108726
Nassar, Rim, et al. "Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice." Meat science vol. 185 (2021): 108726. doi: https://doi.org/10.1016/j.meatsci.2021.108726
Nassar R, Vernus B, Carnac G, Fouret G, Goustard B, Casas F, Tintignac L, Cassar-Malek I, Picard B, Seiliez I, Brioche T, Koechlin-Ramonatxo C, Bertrand-Gaday C, Hamade A, Najjar F, Chabi B, Bonnieu A. Myostatin gene inactivation increases post-mortem calpain-dependent muscle proteolysis in mice. Meat Sci. 2021 Dec 24;185:108726. doi: 10.1016/j.meatsci.2021.108726. Epub 2021 Dec 24. PMID: 34973590.
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Showing 13 to 20 of 20 entries