Calpain II expression is increased by changes in mechanical loading of muscle in vivo

Spencer, Melissa J.; Lu, Bo; Tidball, James G.

doi:10.1002/(sici)1097-4644(199701)64:1<55::aid-jcb9>3.0.co;2-z

Cited by 31 publications

(30 citation statements)

References 61 publications

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“…Tissue sections were processed using procedures described by Spencer et al [36]. Positive control sections of young mouse thymus were treated in parallel with soleus sections.…”

Section: Tissue Preparation and Immunohistochemistrycontrasting

confidence: 44%

Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use

Pizza

Hernandez

Tidball

1998

Journal of Leukocyte Biology

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The objective of this study was to determine the role of nitric oxide in muscle inflammation, fiber necrosis, and apoptosis of inflammatory cells in vivo. The effects of nitric oxide synthase (NOS) inhibition on the concentrations of neutrophils, ED1 ؉ and ED2 ؉ macrophages, apoptotic inflammatory cells, and necrotic muscle fibers in rats subjected to 10 days of hindlimb unloading and 2 days of reloading were determined. Administration of NOS inhibitor N -nitro-L-arginine methyl ester (L-NAME) significantly reduced the concentrations of neutrophils, ED1 ؉ and ED2 ؉ macrophages, and necrotic fibers in soleus muscle relative to water-treated controls. The concentration of apoptotic inflammatory cells was also significantly lower for L-NAME-treated animals compared with watertreated controls. However, the proportion of the inflammatory cell population that was apoptotic did not differ between L-NAME-treated and control animals, suggesting that L-NAME treatment did not decrease inflammatory cell populations by increasing the frequency of apoptosis. Thus, nitric oxide or one of its intermediates promotes muscle inflammation and fiber necrosis during modified muscle use and plays no more than a minor role in the resolution of muscle inflammation by inducing apoptosis of inflammatory cells.

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“…Tissue sections were processed using procedures described by Spencer et al [36]. Positive control sections of young mouse thymus were treated in parallel with soleus sections.…”

Section: Tissue Preparation and Immunohistochemistrycontrasting

confidence: 44%

Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use

Pizza

Hernandez

Tidball

1998

Journal of Leukocyte Biology

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“…Little is known regarding the role of calpains in response to exercise; however, they are generally thought to play a pivotal role in the muscle remodeling process after muscle-damaging exercise (1). In support of this, calpain-2 mRNA abundance is elevated 2 days after exhaustive jumping exercise (28), 1 day after eccentric exercise (14), and in response to muscle reloading following hindlimb suspension (46). Our data reveal that calpain-2 mRNA is elevated in the immediate hours following cycling exercise, which is not typically associated with muscle damage.…”

Section: Discussionmentioning

confidence: 99%

Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states

Harber

Konopka

Jemioło

et al. 2010

American Journal of Physiology-Regulatory, Integrative and Comp

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Harber MP, Konopka AR, Jemiolo B, Trappe SW, Trappe TA, Reidy PT. Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states. Am J Physiol Regul Integr Comp Physiol 299: R1254 -R1262, 2010. First published August 18, 2010 doi:10.1152/ajpregu.00348.2010.-The purpose of this investigation was to assess mixed-muscle fractional synthesis rate (FSR) and the expression of genes involved in skeletal muscle remodeling after aerobic exercise in the fasted and fed states. Eight recreationally active males (25 Ϯ 1 yr; V O2 max: 52 Ϯ 2 ml·kg Ϫ1 ·min Ϫ1 ) performed 60-min of cycle ergometry at 72 Ϯ 1% V O2 max on two occasions in a counter-balanced design. Subjects ingested a noncaloric placebo (EX-FAST) or a beverage containing (per kg body wt): 5 kcal, 0.83 g carbohydrate, 0.37 g protein, and 0.03 g fat (EX-FED) immediately and 1 h after exercise. FSR was assessed at rest and following exercise with the use of a L-[ring 2 H5]-phenylalanine infusion combined with muscle biopsies at 2 and 6 h postexercise. mRNA expression was assessed at 2 and 6 h postexercise via real-time RT-PCR. FSR was higher (P Ͻ 0.05) after exercise in both EX-FAST (0.112 Ϯ 0.010%·h Ϫ1 ) and EX-FED (0.129 Ϯ 0.014%·h Ϫ1 ) compared with rest (0.071 Ϯ 0.005%·h Ϫ1 ). Feeding attenuated the mRNA expression (P Ͻ 0.05) of proteolytic factors MuRF-1 (6 h) and calpain-2 (2 and 6 h) postexercise but did not alter FOXO3A, calpain-1, caspase3, or myostatin mRNA expression compared with EX-FAST. Myogenic regulatory factor (MRF4) mRNA was also attenuated (P Ͻ 0.05) at 2 and 6 h postexercise in EX-FED compared with EX-FAST. These data demonstrate that a nonexhaustive bout of aerobic exercise stimulates skeletal muscle FSR in the fasted state and that feeding does not measurably enhance FSR between 2 and 6 h after aerobic exercise. Additionally, postexercise nutrient intake attenuates the expression of factors involved in the ubiquitin-proteosome and Ca 2ϩ -dependent protein degradation pathways. These data provide insight into the role of feeding on muscle protein metabolism during recovery from aerobic exercise. protein turnover; endurance; proteolysis; muscle-specific RING finger protein-1; calpain AEROBIC EXERCISE ACUTELY (8, 44) and chronically (41, 45) alters skeletal muscle protein metabolism. The influence of nutrient supply (i.e., feeding) on skeletal muscle protein kinetics following exercise that is considered to be aerobic or endurancenatured remains relatively unexplored. Levenhagen et al. (29) initially showed that ingestion of minimal amounts of carbohydrate (8 g) combined with 10 g of protein creates a positive protein balance across the leg following aerobic exercise, apparently through promoting muscle protein synthesis with little influence on protein breakdown. Recently, it was reported that coingestion of protein and carbohydrate following aerobic exercise stimulates muscle protein synthesis greater than carbohydrate intake alone and yields a net positive whole-body protein balance (24). Whi...

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“…In situ reverse transcription polymerase chain reaction (RT-PCR) protocol was adapted from a previously published procedure (27), that was modified as described previously (28).…”

Section: Reagentsmentioning

confidence: 99%

Myonuclear apoptosis in dystrophic mdx muscle occurs by perforin-mediated cytotoxicity.

Spencer

Walsh²,

Dorshkind³

et al. 1997

J. Clin. Invest.

157

124

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Myonuclear apoptosis is an early event in the pathology of dystrophin-deficient muscular dystrophy in the mdx mouse. However, events that initiate apoptosis in muscular dystrophy are unknown, and whether elimination of apoptosis can ameliorate subsequent muscle wasting remains a major question. We have tested the hypothesis that cytotoxic T-lymphocytes initiate myonuclear apoptosis in dystrophic muscle, and examined whether perforin-mediated cytotoxicity plays a role in the pathophysiology of muscular dystrophy. Mdx mice showed muscle invasion by cytotoxic T cells and helper T cells at the onset of histologically detectable muscle fiber pathology. At this time, perforin-expressing cells were also present at elevated concentration. Mdx mice depleted of CD8 ϩ cells showed a significant reduction of apoptotic myonuclei concentration and a reduction in necrosis, judged by macrophage invasion of muscle fibers. Double-mutant mice, deficient in dystrophin and perforin, showed nearly complete absence of myonuclear apoptosis, and a significant reduction in the concentration of macrophages in the connective tissue surrounding muscle fibers. However, muscle fiber invasion by macrophages was not reduced significantly in double mutant mice. Thus, cytotoxic T-lymphocytes contribute significantly to apoptosis and necrosis in mdx dystrophy, and perforin-mediated killing is primarily responsible for myonuclear apoptosis. ( J. Clin. Invest. 1997. 99:2745-2751.)

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Calpain II expression is increased by changes in mechanical loading of muscle in vivo

Cited by 31 publications

References 61 publications

Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use

Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use

Muscle protein synthesis and gene expression during recovery from aerobic exercise in the fasted and fed states

Myonuclear apoptosis in dystrophic mdx muscle occurs by perforin-mediated cytotoxicity.

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