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Cheng, A. J., Allodi, I., Chaillou, T., Schlittler, M., Ivarsson, N., Lanner, J. T., . . . Andersson, D. C. (2019). Intact single muscle fibres from SOD1(G93A) amyotrophic lateral sclerosis mice display preserved specific force, fatigue resistance and training-like adaptations. Journal of Physiology, 597(12), 3133-3146
Open this publication in new window or tab >>Intact single muscle fibres from SOD1(G93A) amyotrophic lateral sclerosis mice display preserved specific force, fatigue resistance and training-like adaptations
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2019 (English)In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 597, no 12, p. 3133-3146Article in journal (Refereed) Published
Abstract [en]

Key points:

  • How defects in muscle contractile function contribute to weakness in amyotrophic lateral sclerosis (ALS) were systematically investigated.
  • Weakness in whole muscles from late stage SOD1G93A mice was explained by muscle atrophy as seen by reduced mass and maximal force.
  • On the other hand, surviving single muscle fibres in late stage SOD1G93A have preserved intracellular Ca2+ handling, normal force-generating capacity and increased fatigue resistance.
  • These intriguing findings provide a substrate for therapeutic interventions to potentiate muscular capacity and delay the progression of the ALS phenotype.

Amyotrophic lateral sclerosis (ALS) is a motor neuron disease characterized by degeneration and loss of motor neurons, leading to severe muscle weakness and paralysis. The SOD1G93A mouse model of ALS displays motor neuron degeneration and a phenotype consistent with human ALS. The purpose of this study was to determine whether muscle weakness in ALS can be attributed to impaired intrinsic force generation in skeletal muscles. In the current study, motor neuron loss and decreased force were evident in whole flexor digitorum brevis (FDB) muscles of mice in the late stage of disease (125–150 days of age). However, in intact single muscle fibres, specific force, tetanic myoplasmic free [Ca2+] ([Ca2+]i), and resting [Ca2+]i remained unchanged with disease. Fibre-type distribution was maintained in late-stage SOD1G93A FDB muscles, but remaining muscle fibres displayed greater fatigue resistance compared to control and showed increased expression of myoglobin and mitochondrial respiratory chain proteins that are important determinants of fatigue resistance. Expression of genes central to both mitochondrial biogenesis and muscle atrophy where increased, suggesting that atrophic and compensatory adaptive signalling occurs simultaneously within the muscle tissue. These results support the hypothesis that muscle weakness in SOD1G93A is primarily attributed to neuromuscular degeneration and not intrinsic muscle fibre defects. In fact, surviving muscle fibres displayed maintained adaptive capacity with an exercise training-like phenotype, which suggests that compensatory mechanisms are activated that can function to delay disease progression.

Place, publisher, year, edition, pages
Cambridge University Press, 2019
Keywords
Amyotrophic lateral sclerosis, Muscle fatigue, Cytosolic calcium, Force, Muscle adaptation
National Category
Physiology
Identifiers
urn:nbn:se:oru:diva-74237 (URN)10.1113/JP277456 (DOI)000474245500011 ()31074054 (PubMedID)2-s2.0-85066899665 (Scopus ID)
Funder
Swedish Research Council, 2016-02112Swedish Society for Medical Research (SSMF), S16-0159Swedish Heart Lung Foundation, 20160741 20180803Wenner-Gren Foundations
Note

Funding Agencies:

Swedish Research Council for Sports Science  FO2018-0019 

Lars Hierta Minne Foundation  FO2015-0510 

Jeansson Foundation  

Stockholm County Council (ALF) 

Available from: 2019-05-14 Created: 2019-05-14 Last updated: 2019-07-29Bibliographically approved
Vechetti, I. J., Wen, Y., Chaillou, T., Murach, K. A., Alimov, A. P., Figueiredo, V. C., . . . McCarthy, J. J. (2019). Life-long reduction in myomiR expression does not adversely affect skeletal muscle morphology. Scientific Reports, 9(1), Article ID 5483.
Open this publication in new window or tab >>Life-long reduction in myomiR expression does not adversely affect skeletal muscle morphology
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2019 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, no 1, article id 5483Article in journal (Refereed) Published
Abstract [en]

We generated an inducible, skeletal muscle-specific Dicer knockout mouse to deplete microRNAs in adult skeletal muscle. Following tamoxifen treatment, Dicer mRNA expression was significantly decreased by 87%. Wild-type (WT) and Dicer knockout (KO) mice were subjected to either synergist ablation or hind limb suspension for two weeks. There was no difference in muscle weight with hypertrophy or atrophy between WT and KO groups; however, even with the significant loss of Dicer expression, myomiR (miR-1, -133a and -206) expression was only reduced by 38% on average. We next aged WT and KO mice for ~22 months following Dicer inactivation to determine if myomiR expression would be further reduced over a prolonged timeframe and assess the effects of myomiR depletion on skeletal muscle phenotype. Skeletal muscle Dicer mRNA expression remained significantly decreased by 80% in old KO mice and sequencing of cloned Dicer mRNA revealed the complete absence of the floxed exons in KO skeletal muscle. Despite a further reduction of myomiR expression to ~50% of WT, no change was observed in muscle morphology between WT and KO groups. These results indicate the life-long reduction in myomiR levels did not adversely affect skeletal muscle phenotype and suggest the possibility that microRNA expression is uniquely regulated in skeletal muscle.

Place, publisher, year, edition, pages
Nature Publishing Group, 2019
National Category
Physiology
Identifiers
urn:nbn:se:oru:diva-73536 (URN)10.1038/s41598-019-41476-8 (DOI)000462990000025 ()30940834 (PubMedID)2-s2.0-85063882282 (Scopus ID)
Note

Funding Agencies:

Sao Paulo Research Foundation, Brazil (FAPESP)  2014/24327-1  2015/19193-9 

NIH  AR061939  AR071753 

Available from: 2019-04-08 Created: 2019-04-08 Last updated: 2019-06-19Bibliographically approved
Chaillou, T. & Cheng, A. J. (2019). Mechanisms of prolonged low-frequency force depression: in-vivo studies get us closer to the truth [Letter to the editor]. American Journal of Physiology. Regulatory Integrative and Comparative Physiology, 316(5), R502-R503
Open this publication in new window or tab >>Mechanisms of prolonged low-frequency force depression: in-vivo studies get us closer to the truth
2019 (English)In: American Journal of Physiology. Regulatory Integrative and Comparative Physiology, ISSN 0363-6119, E-ISSN 1522-1490, Vol. 316, no 5, p. R502-R503Article in journal, Letter (Refereed) Published
Place, publisher, year, edition, pages
American Physiological Society, 2019
Keywords
PLFFD, antioxidant, calcium, fatigue, skeletal muscle
National Category
Psychiatry Physiology
Identifiers
urn:nbn:se:oru:diva-73277 (URN)10.1152/ajpregu.00063.2019 (DOI)000466488100008 ()30892917 (PubMedID)2-s2.0-85065345597 (Scopus ID)
Available from: 2019-03-22 Created: 2019-03-22 Last updated: 2019-06-19Bibliographically approved
Rantala, R. & Chaillou, T. (2019). Mild hypothermia affects the morphology and impairs glutamine-induced anabolic response in human primary myotubes. American Journal of Physiology - Cell Physiology, 317(1), C101-C110
Open this publication in new window or tab >>Mild hypothermia affects the morphology and impairs glutamine-induced anabolic response in human primary myotubes
2019 (English)In: American Journal of Physiology - Cell Physiology, ISSN 0363-6143, E-ISSN 1522-1563, Vol. 317, no 1, p. C101-C110Article in journal (Refereed) Published
Abstract [en]

The specific impact of reduced temperature on skeletal muscle adaptation has been poorly investigated. Cold water immersion, one situation leading to decreased skeletal muscle temperature, is commonly proposed to reduce the perception of fatigue and muscle soreness after strenuous exercise. In contrast, it may impair long-term benefits of resistance exercise training on muscle strength and hypertrophy. To date, the physiological factors responsible for this blunted muscle adaptation remain unclear. Here, we used a cell culture model of human primary myotubes to specifically investigate the intrinsic behavior of muscle cells during mild hypothermia (MH). Newly formed myotubes were exposed to either 37°C or 32°C to evaluate the effect of MH on myotube size and morphology, protein synthesis and anabolic signaling. We also compared the glutamine (GLUT)-induced hypertrophic response between myotubes incubated at 32°C or 37°C. We showed that 48 h exposure to MH altered the cellular morphology (greater myotube area, shorter myosegments, myotubes with irregular shape), and impaired GLUT-induced myotube hypertrophy. Moreover, MH specifically reduced protein synthesis at 8 h. This result may be explained by an altered regulation of ribosome biogenesis, as evidenced by a lower expression of 45S pre-rRNA and MYC protein, and a lower total RNA concentration. Furthermore, MH blunted GLUT-induced increase in protein synthesis at 8 h, a finding consistent with an impaired activation of the mechanistic target of rapamycin (mTOR) pathway. In conclusion, this study demonstrates that MH impairs the morphology of human myotubes and alters the hypertrophic response to GLUT.

Place, publisher, year, edition, pages
HighWire Press, 2019
Keywords
mTOR signaling pathway, protein synthesis, reduced temperature, ribosome biogenesis, skeletal muscle hypertrophy
National Category
Physiology
Identifiers
urn:nbn:se:oru:diva-73428 (URN)10.1152/ajpcell.00008.2019 (DOI)000475698300002 ()30917033 (PubMedID)2-s2.0-85068886077 (Scopus ID)
Available from: 2019-04-04 Created: 2019-04-04 Last updated: 2019-08-12Bibliographically approved
Chaillou, T. (2019). Ribosome specialization and its potential role in the control of protein translation and skeletal muscle size. Journal of applied physiology, 127(2), 599-607
Open this publication in new window or tab >>Ribosome specialization and its potential role in the control of protein translation and skeletal muscle size
2019 (English)In: Journal of applied physiology, ISSN 8750-7587, E-ISSN 1522-1601, Vol. 127, no 2, p. 599-607Article, review/survey (Refereed) Published
Abstract [en]

The ribosome is typically viewed as a supramolecular complex with constitutive and invariant capacity in mediating translation of mRNA into protein. This view has been challenged by recent research revealing that ribosome composition could be heterogeneous, and this heterogeneity leads to functional ribosome specialization. This review presents the idea that ribosome heterogeneity results from changes in its various components, including variations in ribosomal protein (RP) composition, post-translational modifications of RPs, changes in ribosomal-associated proteins, alternative forms of rRNA and post-transcriptional modifications of rRNAs. Ribosome heterogeneity could be orchestrated at several levels and may depend on numerous factors, such as the subcellular location, cell type and tissue specificity, the development state, cell state, ribosome biogenesis, RP turnover, physiological stimuli and circadian rhythm. Ribosome specialization represents a completely new concept for the regulation of gene expression. Specialized ribosomes could modulate several aspects of translational control, such as mRNA translation selectivity, translation initiation, translational fidelity and translation elongation. Recent research indicates that the expression of Rpl3 is markedly increased, while that of Rpl3l is highly reduced during mouse skeletal muscle hypertrophy. Moreover, Rpl3l overexpression impairs the growth and myogenic fusion of myotubes. Although the function of Rpl3 and Rpl3l in the ribosome remains to be clarified, these findings suggest that ribosome specialization may be potentially involved in the control of protein translation and skeletal muscle size. Limited data concerning ribosome specialization are currently available in skeletal muscle. Future investigations have the potential to delineate the function of specialized ribosomes in skeletal muscle.

Place, publisher, year, edition, pages
American Physiological Society, 2019
Keywords
Control of muscle mass, Functional specialization, Ribosome heterogeneity, Skeletal muscle hypertrophy
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Physiology
Identifiers
urn:nbn:se:oru:diva-71179 (URN)10.1152/japplphysiol.00946.2018 (DOI)000482199900032 ()30605395 (PubMedID)2-s2.0-85071496985 (Scopus ID)
Available from: 2019-01-09 Created: 2019-01-09 Last updated: 2019-09-16Bibliographically approved
Rantala, R., Kadi, F. & Chaillou, T. (2018). Low temperature affects the morphology and impairs glutamine-induced hypertrophic response in human primary myotubes. In: : . Paper presented at Europhysiology, London, UK, September 14-16, 2018.
Open this publication in new window or tab >>Low temperature affects the morphology and impairs glutamine-induced hypertrophic response in human primary myotubes
2018 (English)Conference paper, Poster (with or without abstract) (Refereed)
Abstract [en]

Cold water immersion and other strategies are extensively used by athletes to reduce muscle temperature (TEMP) and are believed to limit muscle soreness and improve recovery after strenuous exercise. However, it remains unclear whether low TEMP affects skeletal muscle hypertrophy and protein synthesis in response to anabolic stimuli. In this study, we used an in vitro model to investigate whether a reduced TEMP (32°C, TEMP in skeletal muscle during cold water immersion vs. 37°C, core TEMP) affects the growth and impairs glutamine (GLUT)-induced hypertrophic response in human myotubes. Myoblasts from human muscle biopsies (n=8) were first differentiated into myotubes during 48h at 37°C. Then, myotubes were treated with GLUT to induce hypertrophy and were incubated at either 37 or 32°C during 1h (T1), 8h (T8) or 48h (T48). Myotube area (a marker of myotube size) was assessed at T48 by using immunocytology. Protein synthesis (puromycin incorporation) and phosphorylation levels of two components of the mechanistic target of rapamycin (mTOR) pathway [P70 S6 kinase (P70S6K) and eukaryotic translation initiation factor 4E (4E-BP1] were assessed at T1 and T8 from western blot analysis. Ribosome biogenesis was evaluated at T8 by determining total RNA concentration, and by assessing the levels of 18S ribosomal RNA (18S rRNA), precursor 45S rRNA (pre-45S rRNA) and MYC mRNA from quantitative polymerase chain reaction. Data were analysed by a two-way ANOVA for repeated measures. A first major observation was that low TEMP induced morphological alterations (short myotube segments and larger myotube area). Importantly, GLUT-induced myotube hypertrophy was only observed at 37°C (+40%, P<0,01 at 37°C; +4%, NS at 32°C). Similarly, GLUT stimulated protein synthesis at T1 (main effect, P<0,01), with a 53% increase at 37°C (P<0,05) and a 23% increase at 32°C (NS). Protein synthesis was reduced at 32°C at T8 (main effect, P<0,01), while GLUT increased protein synthesis at 37°C (+17%, P<0,01) but not at 32°C (-7%, NS). GLUT-induced 4E-BP1 phosphorylation at T1 was found at 37°C (+16%, P<0,01) but not at 32°C (-1%, NS). Moreover, GLUT increased the phosphorylation of P70S6K at T8 by 50% at 37°C (P<0,01) and by 26% at 32°C (P<0,05). Overall, total RNA concentration, levels of MYC mRNA, 18S rRNA and pre-45S rRNA were reduced at 32°C. In conclusion, this study indicates that low TEMP affects myotube morphology. In addition, we demonstrate that low TEMP impairs GLUT-induced myotube hypertrophy and protein synthesis, a result accompanied by a minored activation of the mTOR pathway. The impaired ribosome biogenesis observed at 32°C at T8 may also contribute to the reduced protein synthesis at this time point. These findings suggest that reducing muscle TEMP after resistance exercise may be detrimental for muscle hypertrophy and training adaptations.

 

National Category
Medical and Health Sciences Physiology
Identifiers
urn:nbn:se:oru:diva-70158 (URN)
Conference
Europhysiology, London, UK, September 14-16, 2018
Available from: 2018-11-13 Created: 2018-11-13 Last updated: 2018-11-13Bibliographically approved
Mader, T., Kenne, E., Chaillou, T., Petkovic, M., Steinz, M., Liu, Z., . . . Lanner, J. (2018). Metabolic alteration and muscle dysfunction in mice with breast cancer. In: : . Paper presented at Europhysiology, London, UK, September 14-16, 2018.
Open this publication in new window or tab >>Metabolic alteration and muscle dysfunction in mice with breast cancer
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2018 (English)Conference paper, Poster (with or without abstract) (Refereed)
Abstract [en]

Breast cancer accounts for ~25% of diagnosed cancer types in woman [1]. Decreased physical fitness and muscle weakness are common complications in patients with breast cancer. In cancer, muscle weakness has traditionally been linked to muscle wasting and significant weight loss (cachexia) [2]. However, muscle weakness is present in non-cachectic, weight-stable patients with breast cancer [3]. In fact, cancer-induced muscle dysfunction is a broad clinical challenge that is not restricted to palliative or advanced stage patients, but also observed in newly diagnosed patients with low tumor burden [4]. Further, with the breast cancer treatment improving, it is important to take a look on the patients quality of life [5]. However, little is known about the features underlying breast cancer-induced muscle impairments and no drug preventing cancer-induced muscle weakness is clinically proven. Here we aim at characterizing the metabolic status and the muscle function in mice with breast cancer.

The breast cancer mouse-model MMTV-PyMT (PyMT) used here, is characterized by an early onset of mammary cancer (from 5 weeks of age) and follows a similar progression pattern as the one observed in human patients [6]. Soleus muscle from PyMT mice exhibited ~30% lower specific force (kN/m2) than soleus muscle from wildtype (WT) mice (n=28-29, p ≤ 0.05, mice were 12 week old at sacrifice). There were no significant differences in muscle mass, fiber size or fiber type distribution between PyMT and WT muscle. Furthermore, there were no differences in glycogen content (μg/g muscle) in soleus muscle from PyMT and WT mice. Simultaneous measurement of numerous parameters (e.g. oxygen consumption (VO2), carbon dioxide production (VCO2), and food and water intake) was carried out using comprehensive lab animal monitoring system (CLAMS) to gain insight into the metabolic status of the mice. The mice were monitored over a week and the average respiratory exchange ratio (RER = CO2production: O2 uptake) were significantly differed between PyMT and WT mice, with mean PyMT RER of 0.95±0.01 and WT RER of 1.0±0.01 (mean data +/-SEM, n=8, p<0.001). Thus, indicative that PyMT have an altered metabolism towards fatty acid utilization.

In summary, soleus muscles are weaker and the whole-body metabolism appears altered in mice with breast cancer as compared with healthy control mice. Gene and molecular analysis are currently being performed to further assess mitochondrial and glucose metabolism. Nevertheless, further studies are needed to gain insight into cancer-derived factors that contributes to skeletal muscle dysfunction and altered metabolism.

1. Jemal, A., et al., Cancer statistics, 2008. CA Cancer J Clin, 2008. 58(2): p. 71-96.

2. Johns, N., N.A. Stephens, and K.C. Fearon, Muscle wasting in cancer. Int J Biochem Cell Biol, 2013. 45(10): p. 2215-29.

3. Klassen, O., et al., Muscle strength in breast cancer patients receiving different treatment regimes. Journal of Cachexia, Sarcopenia and Muscle, 2017. 8(2): p. 305-316.

4. Villasenor, A., et al., Prevalence and prognostic effect of sarcopenia in breast cancer survivors: the HEAL Study. J Cancer Surviv, 2012. 6(4): p. 398-406.

5. Perry, S., T.L. Kowalski, and C.H. Chang, Quality of life assessment in women with breast cancer: benefits, acceptability and utilization. Health Qual Life Outcomes, 2007. 5: p. 24.

6. Fantozzi, A. and G. Christofori, Mouse models of breast cancer metastasis. Breast Cancer Res, 2006. 8(4): p. 212.

National Category
Medical and Health Sciences Cancer and Oncology Physiology
Identifiers
urn:nbn:se:oru:diva-70160 (URN)
Conference
Europhysiology, London, UK, September 14-16, 2018
Available from: 2018-11-13 Created: 2018-11-13 Last updated: 2018-11-14Bibliographically approved
Chaillou, T. (2018). Skeletal Muscle Fiber Type in Hypoxia: Adaptation to High-Altitude Exposure and Under Conditions of Pathological Hypoxia. Frontiers in Physiology, 9, Article ID 1450.
Open this publication in new window or tab >>Skeletal Muscle Fiber Type in Hypoxia: Adaptation to High-Altitude Exposure and Under Conditions of Pathological Hypoxia
2018 (English)In: Frontiers in Physiology, ISSN 1664-042X, E-ISSN 1664-042X, Vol. 9, article id 1450Article, review/survey (Refereed) Published
Abstract [en]

Skeletal muscle is able to modify its size, and its metabolic/contractile properties in response to a variety of stimuli, such as mechanical stress, neuronal activity, metabolic and hormonal influences, and environmental factors. A reduced oxygen availability, called hypoxia, has been proposed to inducemetabolic adaptations and loss ofmass in skeletal muscle. In addition, several evidences indicate that muscle fiber-type composition could be affected by hypoxia. The main purpose of this review is to explore the adaptation of skeletal muscle fiber-type composition to exposure to high altitude (ambient hypoxia) and under conditions of pathological hypoxia, including chronic obstructive pulmonary disease (COPD), chronic heart failure (CHF) and obstructive sleep apnea syndrome (OSAS). The muscle fiber-type composition of both adult animals and humans is not markedly altered during chronic exposure to high altitude. However, the fast-to-slow fiber-type transition observed in hind limb muscles during post-natal development is impaired in growing rats exposed to severe altitude. A slow-to-fast transition in fiber type is commonly found in lower limb muscles from patients with COPD and CHF, whereas a transition toward a slower fiber-type profile is often found in the diaphragm muscle in these two pathologies. A slow-to-fast transformation in fiber type is generally observed in the upper airway muscles in rodent models of OSAS. The factors potentially responsible for the adaptation of fiber type under these hypoxic conditions are also discussed in this review. The impaired locomotor activity most likely explains the changes in fiber type composition in growing rats exposed to severe altitude. Furthermore, chronic inactivity and muscle deconditioning could result in the slow-to-fast fiber-type conversion in lower limb muscles during COPD and CHF, while the factors responsible for the adaptation of muscle fiber type during OSAS remain hypothetical. Finally, the role played by cellular hypoxia, hypoxia-inducible factor-1 alpha (HIF-1 alpha), and other molecular regulators in the adaptation of muscle fiber-type composition is described in response to high altitude exposure and conditions of pathological hypoxia.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2018
Keywords
myosin heavy chain, oxygen, hypoxia-inducible factor-1 alpha, chronic obstructive pulmonary disease, chronic heart failure, obstructive sleep apnea syndrome, muscle plasticity
National Category
Physiology
Identifiers
urn:nbn:se:oru:diva-69862 (URN)10.3389/fphys.2018.01450 (DOI)000447145400001 ()30369887 (PubMedID)2-s2.0-85055123060 (Scopus ID)
Available from: 2018-10-26 Created: 2018-10-26 Last updated: 2018-11-14Bibliographically approved
Chaillou, T., McPeek, A. & Lanner, J. T. (2017). Docetaxel does not impair skeletal muscle force production in a murine model of cancer chemotherapy. Physiological Reports, 5(11), Article ID e13261.
Open this publication in new window or tab >>Docetaxel does not impair skeletal muscle force production in a murine model of cancer chemotherapy
2017 (English)In: Physiological Reports, E-ISSN 2051-817X, Vol. 5, no 11, article id e13261Article in journal (Refereed) Published
Abstract [en]

Chemotherapy drugs such as docetaxel are commonly used to treat cancer. Cancer patients treated with chemotherapy experience decreased physical fitness, muscle weakness and fatigue. To date, it is unclear whether these symptoms result only from cancer-derived factors or from the combination of cancer disease and cancer treatments, such as chemotherapy. In this study, we aimed at determining the impact of chemotherapy per se on force production of hind limb muscles from healthy mice treated with docetaxel. We hypothesized that docetaxel will decrease maximal force, exacerbate the force decline during repeated contractions and impair recovery after fatiguing stimulations. We examined the function of soleus and extensor digitorum longus (EDL) muscles 24h and 72h after a single injection of docetaxel (acute treatment), and 7days after the third weekly injection of docetaxel (repeated treatment). Docetaxel was administrated by intravenous injection (20mg/kg) in female FVB/NRj mice and control mice were injected with saline solution. Our results show that neither acute nor repeated docetaxel treatment significantly alters force production during maximal contractions, repeated contractions or recovery. Only a tendency to decreased peak specific force was observed in soleus muscles 24h after a single injection of docetaxel (-17%, P=0.13). In conclusion, docetaxel administered intravenously does not impair force production in hind limb muscles from healthy mice. It remains to be clarified whether docetaxel, or other chemotherapy drugs, affect muscle function in subjects with cancer and whether the side effects associated with chemotherapy (neurotoxicity, central fatigue, decreased physical activity, etc.) are responsible for the experienced muscle weakness and fatigue.

Place, publisher, year, edition, pages
American Physiological Society, 2017
Keywords
Acute and repeated treatments, disease, fatigue, muscle weakness, recovery
National Category
Physiology
Identifiers
urn:nbn:se:oru:diva-58956 (URN)10.14814/phy2.13261 (DOI)000403500600003 ()28583990 (PubMedID)2-s2.0-85020790483 (Scopus ID)
Funder
Swedish Research CouncilMagnus Bergvall FoundationWenner-Gren Foundations
Available from: 2017-08-18 Created: 2017-08-18 Last updated: 2018-01-13Bibliographically approved
Chaillou, T. (2017). Impaired ribosome biogenesis could contribute to anabolic resistance to strength exercise in the elderly. Journal of Physiology, 595(5), 1447-1448
Open this publication in new window or tab >>Impaired ribosome biogenesis could contribute to anabolic resistance to strength exercise in the elderly
2017 (English)In: Journal of Physiology, ISSN 0022-3751, E-ISSN 1469-7793, Vol. 595, no 5, p. 1447-1448Article, review/survey (Refereed) Published
Place, publisher, year, edition, pages
John Wiley & Sons, 2017
National Category
Physiology Neurology
Identifiers
urn:nbn:se:oru:diva-55273 (URN)10.1113/JP273773 (DOI)000398112300012 ()28105708 (PubMedID)2-s2.0-85016617790 (Scopus ID)
Available from: 2017-02-02 Created: 2017-02-02 Last updated: 2018-07-30Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-5322-4150

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