Autophagic response to strenuous exercise in mouse skeletal muscle fibers

Salminen, Antero; Vihko, V.

doi:10.1007/bf02889856

Cited by 85 publications

(56 citation statements)

References 18 publications

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“…Many of the affected tissues in LAMP-2-deficient mice are those that have a high degree of autophagy in normal animals. Using mainly rat tissues, active autophagy has been described at least in liver (Pfeifer and Strauss, 1981;Kovacs et al, 1982;de Waal et al, 1986), pancreas (Kovacs et al, 1988), muscle (Salminen and Vihko, 1984;Bahro et al, 1992), heart (Pfeifer and Strauss, 1981;Dammrich and Pfeifer, 1983), and kidney (Pfeifer and Scheller, 1975;Bahro et al, 1988). This suggests that active ongoing autophagy in normal conditions may be the prerequisite for the observed phenotype of autophagic vacuole accumulation in LAMP-2-deficient tissues.…”

Section: Discussionmentioning

confidence: 98%

Role of LAMP-2 in Lysosome Biogenesis and Autophagy

Eskelinen

Illert²,

Tanaka

et al. 2002

MBoC

310

260

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In LAMP-2–deficient mice autophagic vacuoles accumulate in many tissues, including liver, pancreas, muscle, and heart. Here we extend the phenotype analysis using cultured hepatocytes. In LAMP-2–deficient hepatocytes the half-life of both early and late autophagic vacuoles was prolonged as evaluated by quantitative electron microscopy. However, an endocytic tracer reached the autophagic vacuoles, indicating delivery of endo/lysosomal constituents to autophagic vacuoles. Enzyme activity measurements showed that the trafficking of some lysosomal enzymes to lysosomes was impaired. Immunoprecipitation of metabolically labeled cathepsin D indicated reduced intracellular retention and processing in the knockout cells. The steady-state level of 300-kDa mannose 6-phosphate receptor was slightly lower in LAMP-2–deficient hepatocytes, whereas that of 46-kDa mannose 6-phosphate receptor was decreased to 30% of controls due to a shorter half-life. Less receptor was found in the Golgi region and in vesicles and tubules surrounding multivesicular endosomes, suggesting impaired recycling from endosomes to the Golgi. More receptor was found in autophagic vacuoles, which may explain its shorter half-life. Our data indicate that in hepatocytes LAMP-2 deficiency either directly or indirectly leads to impaired recycling of 46-kDa mannose 6-phosphate receptors and partial mistargeting of a subset of lysosomal enzymes. Autophagic vacuoles may accumulate due to impaired capacity for lysosomal degradation

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Section: Discussionmentioning

confidence: 98%

Role of LAMP-2 in Lysosome Biogenesis and Autophagy

Eskelinen

Illert²,

Tanaka

et al. 2002

MBoC

310

260

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“…176 In these older studies, strenuous physical exercise associated with the appearance of necrotic fibers in skeletal muscle results in the most pronounced changes in autophagy levels between 2 and 7 d after exercise and returns to baseline within 2 wk after exertion. Recently these results were confirmed in mice performing a short but more strenuous exercise.…”

Section: Exercise Modulates Autophagy In Animalsmentioning

confidence: 96%

Heat shock response and autophagy—cooperation and control

2015

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Abbreviations: AKT, v-akt murine thymoma viral oncogene homolog 1; AMPK, adenosine monophosphate-activated protein kinase; ATG, autophagy-related; BECN1, Beclin 1, autophagy related; EIF4EBP1, eukaryotic translation initiation factor 4E binding protein 1; ER, endoplasmic reticulum; FOXO, forkhead box O; HSF1, heat shock transcription factor 1; HSP, heat shock protein; HSPA8/ HSC70, heat shock 70kDa protein 8; IL, interleukin; LC3, MAP1LC3, microtubule-associated protein 1 light chain 3; MTMR14/ hJumpy, myotubularin related protein 14; MTOR, mechanistic target of rapamycin; NR1D1/Rev-Erb-a, nuclear receptor subfamily 1, group D, member 1; PBMC, peripheral blood mononuclear cell; PPARGC1A/PGC-1a, peroxisome proliferator-activated receptor, gamma, coactivator 1 a; RHEB, Ras homolog enriched in brain; SOD, superoxide dismutase; SQSTM1/p62, sequestosome 1; TPR, translocated promoter region, nuclear basket protein; TSC, tuberous sclerosis complex; ULK1, unc-51 like autophagy activating kinase 1.Protein quality control (proteostasis) depends on constant protein degradation and resynthesis, and is essential for proper homeostasis in systems from single cells to whole organisms. Cells possess several mechanisms and processes to maintain proteostasis. At one end of the spectrum, the heat shock proteins modulate protein folding and repair. At the other end, the proteasome and autophagy as well as other lysosome-dependent systems, function in the degradation of dysfunctional proteins. In this review, we examine how these systems interact to maintain proteostasis. Both the direct cellular data on heat shock control over autophagy and the time course of exercise-associated changes in humans support the model that heat shock response and autophagy are tightly linked. Studying the links between exercise stress and molecular control of proteostasis provides evidence that the heat shock response and autophagy coordinate and undergo sequential activation and downregulation, and that this is essential for proper proteostasis in eukaryotic systems.

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“…These three situations can be triggered by exercise (de Lange et al 2007;Kim et al 2011;Sahlin et al 2010). While increased lysosomal enzyme activities and elevated number of autophagic vacuoles have been reported during the repair of exercise injuries due to strenuous endurance exercise in rodents (Salminen 1985;Salminen and Vihko 1984), no data are available concerning the possible regulation of ATG in response to an acute form of strenuous endurance exercise in human. There is evidence that autophagy-related as well as autophagy-regulatory genes are regulated during ALP activation (Mammucari et al 2007).…”

Section: Introductionmentioning

confidence: 96%

Autophagy-related and autophagy-regulatory genes are induced in human muscle after ultraendurance exercise

et al. 2011

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The purpose of this study was to evaluate whether ultra endurance exercise changes the mRNA levels of the autophagy-related and autophagy-regulatory genes. Eight men (44 ± 1 years, range: 38-50 years) took part in a 200-km running race. The average running time was 28 h 03 min ± 2 h 01 min (range: 22 h 15 min-35 h 04 min). A muscle sample was taken from the vastus lateralis 2 weeks prior to the race and 3 h after arrival. Gene expression was assessed by RT-qPCR. Transcript levels of autophagy-related genes were increased by 49% for ATG4b (P = 0.025), 57% for ATG12 (P = 0.013), 286% for Gabarapl1 (P = 0.008) and 103% for LC3b (P = 0.011). The lysosomal enzyme cathepsin L mRNA was upregulated by 123% (P = 0.003). Similarly, transcript levels of the autophagy-regulatory genes BNIP3 and BNIP3l were both increased by 113% (P = 0.031 and P = 0.007, respectively). Since upregulation of these genes has been related with an increased autophagic flux in various models, our results strongly suggest that autophagy is activated in response to ultra endurance exercise.

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Autophagic response to strenuous exercise in mouse skeletal muscle fibers

Cited by 85 publications

References 18 publications

Role of LAMP-2 in Lysosome Biogenesis and Autophagy

Role of LAMP-2 in Lysosome Biogenesis and Autophagy

Heat shock response and autophagy—cooperation and control

Autophagy-related and autophagy-regulatory genes are induced in human muscle after ultraendurance exercise

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