مؤتمر
Tibialis anterior atrophy after immobilization correlates with changes in extracellular matrix molecules Sparc and Tenascin-C, and in integrin scaffold proteins
العنوان: | Tibialis anterior atrophy after immobilization correlates with changes in extracellular matrix molecules Sparc and Tenascin-C, and in integrin scaffold proteins |
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المؤلفون: | Slimani, Lamia, Listrat, Anne, Amat, Julien, Deval, Christiane, Vazeille, Emilie, Micol, Didier, Meunier, Bruno, Dardevet, Dominique, Picard, Brigitte, Taillandier, Daniel, Attaix, Didier, Combaret, Lydie |
المساهمون: | Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Centre de Recherche en Nutrition Humaine, Unité Mixte de Recherche sur les Herbivores - UMR 1213 (UMRH), Institut National de la Recherche Agronomique (INRA)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA), Société Française de Biochimie et Biologie Moléculaire (SFBBM). FRA. |
المصدر: | 6. Colloque du Groupe Thématique "Protéolyse Cellulaire" de la Société Française de Biochimie et de Biologie Cellulaire https://hal.inrae.fr/hal-02746794Test 6. Colloque du Groupe Thématique "Protéolyse Cellulaire" de la Société Française de Biochimie et de Biologie Cellulaire, Nov 2012, Clermont-Ferrand, France. , 2012 http://www.auvergnesciences.com/?post_type=actualite&p=2389Test |
بيانات النشر: | HAL CCSD |
سنة النشر: | 2012 |
المجموعة: | HAL Clermont Auvergne (Université Blaise Pascal Clermont-Ferrand / Université d'Auvergne) |
مصطلحات موضوعية: | skeletal muscle atrophy, remobilization, outside-in signaling, extracellular matrix, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition |
جغرافية الموضوع: | Clermont-Ferrand, France |
الوصف: | National audience ; Sustained muscle loss leads to weakening and severe metabolic consequences. Immobilization-induced muscle atrophy worsened in the tibialis anterior (TA) muscle immediately after cast removal and was associated with connective tissue alterations and sustained activation of proteolysis, suggesting a cross-talk between extracellular matrix (ECM) and muscle fibres. We investigated ECM alterations and integrin signalling in the immobilized and remobilized TA. Adult rats were subjected to unilateral hindlimb casting for 8 days (I8). Casts were removed at I8 and animals were allowed to recover for 10 days (R1 to R10). The immobilization-induced connective tissue thickening in the TA resulted from an increase in perimysium at I8 and in endomysium after remobilization. These alterations correlated with additional ramifications in the ECM during early recovery and with a decrease of muscle fibre area associated with their deformation. Levels of mRNA encoding two matricellular proteins, i.e. tenascin-C and Sparc, increased immediately after cast removal, while mRNA and/or protein levels ILK, Parvin-α, integrin-α7 and -β1 increased during immobilization and early recovery. Finally, mRNA levels for MyoD and Myf5 increased during immobilization and returned to basal levels at R6. In conclusion, the TA muscle atrophy during remobilization was associated with pronounced structural changes of the endomysium, suggesting changes in the transmission of contractile forces from adjacent muscle fibres within fascicles. In addition, the up-regulation of integrin scaffold proteins and of some matricellular proteins that regulate myogenesis during immobilization and remobilization suggests that integrin signalling was enhanced and may influence skeletal muscle recovery |
نوع الوثيقة: | conference object still image |
اللغة: | English |
العلاقة: | hal-02746794; https://hal.inrae.fr/hal-02746794Test; PRODINRA: 368482 |
الإتاحة: | https://hal.inrae.fr/hal-02746794Test |
رقم الانضمام: | edsbas.20E1BD8C |
قاعدة البيانات: | BASE |
الوصف غير متاح. |