Cellular adaptations in soleus muscle during recovery after hindlimb unloading. 2008

Y Oishi, and T Ogata, and K-i Yamamoto, and M Terada, and T Ohira, and Y Ohira, and K Taniguchi, and R R Roy
Laboratory of Muscle Physiology, Faculty of Education, Kumamoto University, Kumamoto, Japan. oishi@gpo.kumamoto-u.ac.jp

OBJECTIVE We used a model of chronic unloading followed by reloading to examine the apoptotic responses associated with soleus muscle atrophy and subsequent recovery. METHODS Male Wistar rats were subjected to hindlimb unloading (HU) for 2 weeks and subsequent reloading for 0, 3, 7 and 14 days. One-half of the HU-reloaded rats were administered cyclosporine A (CsA), a calcineurin (CaN) inhibitor. RESULTS There was fibre atrophy (73%) and a decrease in slow type I fibre/myosin heavy chain (MyHC) composition in the soleus muscle after 2 weeks of HU. Fibre size and type I MyHC composition recovered to near the age-matched control levels by recovery day 14 in non-treated, but not in CsA-treated, rats. Myonuclear number was lower and the number of apoptotic nuclei higher in 2-week HU than control rats. These values returned to control levels after 7 and 14 days of recovery, respectively, in both HU-recovery groups. After 2 weeks of HU, the levels of heat shock proteins (Hsp) 60 and 72, mitochondrial cytochrome c oxidase subunit IV (Cox IV), and peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1) proteins were lower than control. The levels of all of these proteins gradually increased to or above the control levels during cage recovery in both groups. CONCLUSIONS Our results indicate that apoptotic mechanisms are involved in the modulation of myonuclear number during chronic unloading and subsequent reloading. Furthermore, it appears that CaN is related to fibre size and phenotype adaptations, but not to apoptotic responses.

UI MeSH Term Description Entries
D008297 Male Males
D008931 Mitochondria, Muscle Mitochondria of skeletal and smooth muscle. It does not include myocardial mitochondria for which MITOCHONDRIA, HEART is available. Sarcosomes,Mitochondrion, Muscle,Muscle Mitochondria,Muscle Mitochondrion,Sarcosome
D009133 Muscular Atrophy Derangement in size and number of muscle fibers occurring with aging, reduction in blood supply, or following immobilization, prolonged weightlessness, malnutrition, and particularly in denervation. Atrophy, Muscle,Neurogenic Muscular Atrophy,Neurotrophic Muscular Atrophy,Atrophies, Muscle,Atrophies, Muscular,Atrophies, Neurogenic Muscular,Atrophies, Neurotrophic Muscular,Atrophy, Muscular,Atrophy, Neurogenic Muscular,Atrophy, Neurotrophic Muscular,Muscle Atrophies,Muscle Atrophy,Muscular Atrophies,Muscular Atrophies, Neurogenic,Muscular Atrophies, Neurotrophic,Muscular Atrophy, Neurogenic,Muscular Atrophy, Neurotrophic,Neurogenic Muscular Atrophies,Neurotrophic Muscular Atrophies
D002467 Cell Nucleus Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed) Cell Nuclei,Nuclei, Cell,Nucleus, Cell
D003576 Electron Transport Complex IV A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane. Cytochrome Oxidase,Cytochrome aa3,Cytochrome-c Oxidase,Cytochrome Oxidase Subunit III,Cytochrome a,a3,Cytochrome c Oxidase Subunit VIa,Cytochrome-c Oxidase (Complex IV),Cytochrome-c Oxidase Subunit III,Cytochrome-c Oxidase Subunit IV,Ferrocytochrome c Oxygen Oxidoreductase,Heme aa3 Cytochrome Oxidase,Pre-CTOX p25,Signal Peptide p25-Subunit IV Cytochrome Oxidase,Subunit III, Cytochrome Oxidase,p25 Presequence Peptide-Cytochrome Oxidase,Cytochrome c Oxidase,Cytochrome c Oxidase Subunit III,Cytochrome c Oxidase Subunit IV,Oxidase, Cytochrome,Oxidase, Cytochrome-c,Signal Peptide p25 Subunit IV Cytochrome Oxidase,p25 Presequence Peptide Cytochrome Oxidase
D004791 Enzyme Inhibitors Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction. Enzyme Inhibitor,Inhibitor, Enzyme,Inhibitors, Enzyme
D000071248 Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha A transcriptional co-activator for NUCLEAR RECEPTORS. It is characterized by an N-terminal LxxLL sequence, a region that interacts with PPAR GAMMA, and a C-terminal RNA RECOGNITION MOTIF. It increases expression of MITOCHONDRIAL UNCOUPLING PROTEIN to regulate genes involved in metabolic reprogramming in response to dietary restriction and the integration of CIRCADIAN RHYTHMS with ENERGY METABOLISM. PGC-1-alpha Protein,PPARGC-1-alpha Protein,PPARGC1a Protein,PGC 1 alpha Protein,PPARGC 1 alpha Protein,Peroxisome Proliferator Activated Receptor Gamma Coactivator 1 alpha
D000220 Adaptation, Biological Changes in biological features that help an organism cope with its ENVIRONMENT. These changes include physiological (ADAPTATION, PHYSIOLOGICAL), phenotypic and genetic changes. Adaptation, Biologic,Biological Adaptation,Biologic Adaptation
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014157 Transcription Factors Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. Transcription Factor,Factor, Transcription,Factors, Transcription

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