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Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo
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| Zeitschriftentitel: | Muscle & Nerve |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , , , , , |
| In: | Muscle & Nerve, 42, 2010, 5, S. 778-787 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. |
|---|---|
| author |
Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. |
| spellingShingle |
Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. Muscle & Nerve Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo Physiology (medical) Cellular and Molecular Neuroscience Neurology (clinical) Physiology |
| author_sort |
miyabara, elen h. |
| spelling |
Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. 0148-639X 1097-4598 Wiley Physiology (medical) Cellular and Molecular Neuroscience Neurology (clinical) Physiology http://dx.doi.org/10.1002/mus.21754 <jats:title>Abstract</jats:title><jats:p>This work was undertaken to provide further insight into the role of mammalian target of rapamycin complex 1 (mTORC1) in skeletal muscle regeneration, focusing on myofiber size recovery. Rats were treated or not with rapamycin, an mTORC1 inhibitor. Soleus muscles were then subjected to cryolesion and analyzed 1, 10, and 21 days later. A decrease in soleus myofiber cross‐section area on post‐cryolesion days 10 and 21 was accentuated by rapamycin, which was also effective in reducing protein synthesis in these freeze‐injured muscles. The incidence of proliferating satellite cells during regeneration was unaltered by rapamycin, although immunolabeling for neonatal myosin heavy chain (MHC) was weaker in cryolesion+rapamycin muscles than in cryolesion‐only muscles. In addition, the decline in tetanic contraction of freeze‐injured muscles was accentuated by rapamycin. This study indicates that mTORC1 plays a key role in the recovery of muscle mass and the differentiation of regenerating myofibers, independently of necrosis and satellite cell proliferation mechanisms. Muscle Nerve 42: 778–787, 2010</jats:p> Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo Muscle & Nerve |
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| title |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_unstemmed |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_full |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_fullStr |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_full_unstemmed |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_short |
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_sort |
mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| topic |
Physiology (medical) Cellular and Molecular Neuroscience Neurology (clinical) Physiology |
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http://dx.doi.org/10.1002/mus.21754 |
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2010 |
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778-787 |
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<jats:title>Abstract</jats:title><jats:p>This work was undertaken to provide further insight into the role of mammalian target of rapamycin complex 1 (mTORC1) in skeletal muscle regeneration, focusing on myofiber size recovery. Rats were treated or not with rapamycin, an mTORC1 inhibitor. Soleus muscles were then subjected to cryolesion and analyzed 1, 10, and 21 days later. A decrease in soleus myofiber cross‐section area on post‐cryolesion days 10 and 21 was accentuated by rapamycin, which was also effective in reducing protein synthesis in these freeze‐injured muscles. The incidence of proliferating satellite cells during regeneration was unaltered by rapamycin, although immunolabeling for neonatal myosin heavy chain (MHC) was weaker in cryolesion+rapamycin muscles than in cryolesion‐only muscles. In addition, the decline in tetanic contraction of freeze‐injured muscles was accentuated by rapamycin. This study indicates that mTORC1 plays a key role in the recovery of muscle mass and the differentiation of regenerating myofibers, independently of necrosis and satellite cell proliferation mechanisms. Muscle Nerve 42: 778–787, 2010</jats:p> |
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| author | Miyabara, Elen H., Conte, Talita C., Silva, Meiricris T., Baptista, Igor L., Bueno, Carlos, Fiamoncini, Jarlei, Lambertucci, Rafael H., Serra, Carmen S., Brum, Patricia C., Pithon‐curi, Tania, Curi, Rui, Aoki, Marcelo S., Oliveira, Antonio C., Moriscot, Anselmo S. |
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| description | <jats:title>Abstract</jats:title><jats:p>This work was undertaken to provide further insight into the role of mammalian target of rapamycin complex 1 (mTORC1) in skeletal muscle regeneration, focusing on myofiber size recovery. Rats were treated or not with rapamycin, an mTORC1 inhibitor. Soleus muscles were then subjected to cryolesion and analyzed 1, 10, and 21 days later. A decrease in soleus myofiber cross‐section area on post‐cryolesion days 10 and 21 was accentuated by rapamycin, which was also effective in reducing protein synthesis in these freeze‐injured muscles. The incidence of proliferating satellite cells during regeneration was unaltered by rapamycin, although immunolabeling for neonatal myosin heavy chain (MHC) was weaker in cryolesion+rapamycin muscles than in cryolesion‐only muscles. In addition, the decline in tetanic contraction of freeze‐injured muscles was accentuated by rapamycin. This study indicates that mTORC1 plays a key role in the recovery of muscle mass and the differentiation of regenerating myofibers, independently of necrosis and satellite cell proliferation mechanisms. Muscle Nerve 42: 778–787, 2010</jats:p> |
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| spelling | Miyabara, Elen H. Conte, Talita C. Silva, Meiricris T. Baptista, Igor L. Bueno, Carlos Fiamoncini, Jarlei Lambertucci, Rafael H. Serra, Carmen S. Brum, Patricia C. Pithon‐curi, Tania Curi, Rui Aoki, Marcelo S. Oliveira, Antonio C. Moriscot, Anselmo S. 0148-639X 1097-4598 Wiley Physiology (medical) Cellular and Molecular Neuroscience Neurology (clinical) Physiology http://dx.doi.org/10.1002/mus.21754 <jats:title>Abstract</jats:title><jats:p>This work was undertaken to provide further insight into the role of mammalian target of rapamycin complex 1 (mTORC1) in skeletal muscle regeneration, focusing on myofiber size recovery. Rats were treated or not with rapamycin, an mTORC1 inhibitor. Soleus muscles were then subjected to cryolesion and analyzed 1, 10, and 21 days later. A decrease in soleus myofiber cross‐section area on post‐cryolesion days 10 and 21 was accentuated by rapamycin, which was also effective in reducing protein synthesis in these freeze‐injured muscles. The incidence of proliferating satellite cells during regeneration was unaltered by rapamycin, although immunolabeling for neonatal myosin heavy chain (MHC) was weaker in cryolesion+rapamycin muscles than in cryolesion‐only muscles. In addition, the decline in tetanic contraction of freeze‐injured muscles was accentuated by rapamycin. This study indicates that mTORC1 plays a key role in the recovery of muscle mass and the differentiation of regenerating myofibers, independently of necrosis and satellite cell proliferation mechanisms. Muscle Nerve 42: 778–787, 2010</jats:p> Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo Muscle & Nerve |
| spellingShingle | Miyabara, Elen H., Conte, Talita C., Silva, Meiricris T., Baptista, Igor L., Bueno, Carlos, Fiamoncini, Jarlei, Lambertucci, Rafael H., Serra, Carmen S., Brum, Patricia C., Pithon‐curi, Tania, Curi, Rui, Aoki, Marcelo S., Oliveira, Antonio C., Moriscot, Anselmo S., Muscle & Nerve, Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo, Physiology (medical), Cellular and Molecular Neuroscience, Neurology (clinical), Physiology |
| title | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_full | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_fullStr | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_full_unstemmed | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_short | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_sort | mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| title_unstemmed | Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo |
| topic | Physiology (medical), Cellular and Molecular Neuroscience, Neurology (clinical), Physiology |
| url | http://dx.doi.org/10.1002/mus.21754 |