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Changes in calpains and calpastatin in the soleus muscle of Daurian ground squirrels during hibernation.

Abstract

We investigated changes in muscle mass, calpains, calpastatin and Z-disk ultrastructure in the soleus muscle (SOL) of Daurian ground squirrels (Spermophilus dauricus) after hibernation or hindlimb suspension to determine possible mechanisms by which muscle atrophy is prevented in hibernators. Squirrels (n=30) were divided into five groups: no hibernation group (PRE, n=6); hindlimb suspension group (HLS, n=6); two month hibernation group (HIB, n=6); two day group after 90±12 days of hibernation (POST, n=6); and forced exercise group (one time forced, moderate-intensity treadmill exercise) after arousal (FE, n=6). Activity and protein expression of calpains were determined by casein zymography and western blotting, and Z-disk ultrastructure was observed by transmission electron microscopy. The following results were found. Lower body mass and higher SOL muscle mass (mg) to total body mass (g) ratio were observed in HIB and POST; calpain-1 activity increased significantly by 176% (P=0.034) in HLS compared to the PRE group; no significant changes were observed in calpain-2 activity. Protein expression of calpain-1 and calpain-2 increased by 83% (P=0.041) and 208% (P=0.029) in HLS compared to the PRE group, respectively; calpastatin expression increased significantly by 180% (P<0.001) and 153% (P=0.007) in HIB and POST, respectively; the myofilaments were well-organized, and the width of the sarcomere and the Z-disk both appeared visually similar among the pre-hibernation, hibernating and post-hibernation animals. Inhibition of calpain activity and consequently calpain-mediated protein degradation by highly elevated calpastatin protein expression levels may be an important mechanism for preventing muscle protein loss during hibernation and ensuring that Z-lines remained ultrastructurally intact.

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  • Authors+Show Affiliations

    ,

    Key Laboratory of Resource Biology and Biotechnology in Western China, Northwest University, Ministry of Education, Xi'an 71069, China; College of Life Science and Technology, Longdong University, Qingyang, Gansu, 745000, China.

    ,

    Key Laboratory of Resource Biology and Biotechnology in Western China, Northwest University, Ministry of Education, Xi'an 71069, China.

    ,

    Key Laboratory of Resource Biology and Biotechnology in Western China, Northwest University, Ministry of Education, Xi'an 71069, China. Electronic address: gaoyunf@nwu.edu.cn.

    ,

    Key Laboratory of Resource Biology and Biotechnology in Western China, Northwest University, Ministry of Education, Xi'an 71069, China.

    Institute of Physiology, Center of Physiological Medicine, Medical University Graz, Austria.

    Source

    MeSH

    Animals
    Calcium-Binding Proteins
    Calpain
    Female
    Hibernation
    Hindlimb
    Male
    Muscle Proteins
    Muscle, Skeletal
    Muscular Atrophy
    Sciuridae

    Pub Type(s)

    Journal Article
    Research Support, Non-U.S. Gov't

    Language

    eng

    PubMed ID

    24937257

    Citation

    Yang, Chen-Xi, et al. "Changes in Calpains and Calpastatin in the Soleus Muscle of Daurian Ground Squirrels During Hibernation." Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, vol. 176, 2014, pp. 26-31.
    Yang CX, He Y, Gao YF, et al. Changes in calpains and calpastatin in the soleus muscle of Daurian ground squirrels during hibernation. Comp Biochem Physiol, Part A Mol Integr Physiol. 2014;176:26-31.
    Yang, C. X., He, Y., Gao, Y. F., Wang, H. P., & Goswami, N. (2014). Changes in calpains and calpastatin in the soleus muscle of Daurian ground squirrels during hibernation. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 176, pp. 26-31. doi:10.1016/j.cbpa.2014.05.022.
    Yang CX, et al. Changes in Calpains and Calpastatin in the Soleus Muscle of Daurian Ground Squirrels During Hibernation. Comp Biochem Physiol, Part A Mol Integr Physiol. 2014;176:26-31. PubMed PMID: 24937257.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Changes in calpains and calpastatin in the soleus muscle of Daurian ground squirrels during hibernation. AU - Yang,Chen-Xi, AU - He,Yue, AU - Gao,Yun-Fang, AU - Wang,Hui-Ping, AU - Goswami,Nandu, Y1 - 2014/06/14/ PY - 2014/02/12/received PY - 2014/05/03/revised PY - 2014/05/27/accepted PY - 2014/6/18/entrez PY - 2014/6/18/pubmed PY - 2015/4/17/medline KW - Disuse atrophy KW - Forced exercise KW - Hindlimb suspension KW - Reloading KW - Ultrastructural KW - Z-disk SP - 26 EP - 31 JF - Comparative biochemistry and physiology. Part A, Molecular & integrative physiology JO - Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. VL - 176 N2 - We investigated changes in muscle mass, calpains, calpastatin and Z-disk ultrastructure in the soleus muscle (SOL) of Daurian ground squirrels (Spermophilus dauricus) after hibernation or hindlimb suspension to determine possible mechanisms by which muscle atrophy is prevented in hibernators. Squirrels (n=30) were divided into five groups: no hibernation group (PRE, n=6); hindlimb suspension group (HLS, n=6); two month hibernation group (HIB, n=6); two day group after 90±12 days of hibernation (POST, n=6); and forced exercise group (one time forced, moderate-intensity treadmill exercise) after arousal (FE, n=6). Activity and protein expression of calpains were determined by casein zymography and western blotting, and Z-disk ultrastructure was observed by transmission electron microscopy. The following results were found. Lower body mass and higher SOL muscle mass (mg) to total body mass (g) ratio were observed in HIB and POST; calpain-1 activity increased significantly by 176% (P=0.034) in HLS compared to the PRE group; no significant changes were observed in calpain-2 activity. Protein expression of calpain-1 and calpain-2 increased by 83% (P=0.041) and 208% (P=0.029) in HLS compared to the PRE group, respectively; calpastatin expression increased significantly by 180% (P<0.001) and 153% (P=0.007) in HIB and POST, respectively; the myofilaments were well-organized, and the width of the sarcomere and the Z-disk both appeared visually similar among the pre-hibernation, hibernating and post-hibernation animals. Inhibition of calpain activity and consequently calpain-mediated protein degradation by highly elevated calpastatin protein expression levels may be an important mechanism for preventing muscle protein loss during hibernation and ensuring that Z-lines remained ultrastructurally intact. SN - 1531-4332 UR - https://www.unboundmedicine.com/medline/citation/24937257/Changes_in_calpains_and_calpastatin_in_the_soleus_muscle_of_Daurian_ground_squirrels_during_hibernation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1095-6433(14)00116-0 DB - PRIME DP - Unbound Medicine ER -