Volume 8 / Number 6 / December 2017

 

     Page 857–863

John E. Morley, Stefan D. Anker

Myopenia and precision (P4) medicinePrecision (P4) medicine represents a new medical paradigm that focuses on Personalized, Predictive, Preventive and Participatory approaches. The P4 paradigm is particularly appropriate for moving the care of persons with myopenia forward. Muscular dystrophies are clearly a set of genetically different diseases where genomics are the basis of diagnosis, and genetic modulation via DNA, oligonucleotides and clustered regularly interspaced short palendronic repeats hold great potential for a cure. The utility of personalized genomics for sarcopenia coupled with utilizing a predictive approach for the diagnosis with early preventive strategies is a key to improving sarcopenic outcomes. The importance of understanding different levels of patient enthusiasm and different responses to exercise should guide the participatory phase of sarcopenic treatment. In the case of cachexia, understanding the effects of the different therapies now available through the P4 approach on muscle wasting is a key to management strategies.

 

Morley, J. E., and Anker, S. D. (2017) Myopenia and precision (P4) medicine. Journal of Cachexia, Sarcopenia and Muscle, 8: 954–973 doi: 10.1002/jcsm.12231.

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     Page 853–854

Srinivasan Dasarathy

Myostatin and beyond in cirrhosis: all roads lead to sarcopeniano abstract

 

Dasarathy, S. (2017) Myostatin and beyond in cirrhosis: all roads lead to sarcopenia. Journal of Cachexia, Sarcopenia and Muscle, 8: 853–854. doi: 10.1002/jcsm.12262.

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     Page 870–880

Stephan von Haehling

Casting the net broader to confirm our imaginations: the long road to treating wasting disordersWasting embraces muscle and tissue wasting in sarcopenia and cachexia. This article describes recent advances in the field published in the Journal of Cachexia, Sarcopenia and Muscle concerning diagnostic tools, biomarker development, pathophysiology, and treatment. Studies discussed herein embrace those on sarcopenia and cachexia in heart failure, chronic obstructive pulmonary disease, and cancer including also animal models.

 

von Haehling, S. (2017) Casting the net broader to confirm our imaginations: the long road to treating wasting disorders. Journal of Cachexia, Sarcopenia and Muscle, 8: 870–880. doi: 10.1002/jcsm.12256.

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     Page 881–906

Giorgos K. Sakellariou, Adam P. Lightfoot, Kate E. Earl, Martin Stofanko, Brian McDonagh

Redox homeostasis and age-related deficits in neuromuscular integrity and functionSkeletal muscle is a major site of metabolic activity and is the most abundant tissue in the human body. Age-related muscle atrophy (sarcopenia) and weakness, characterized by progressive loss of lean muscle mass and function, is a major contributor to morbidity and has a profound effect on the quality of life of older people. With a continuously growing older population (estimated 2 billion of people aged >60 by 2050), demand for medical and social care due to functional deficits, associated with neuromuscular ageing, will inevitably increase. Despite the importance of this ‘epidemic’ problem, the primary biochemical and molecular mechanisms underlying age-related deficits in neuromuscular integrity and function have not been fully determined. Skeletal muscle generates reactive oxygen and nitrogen species (RONS) from a variety of subcellular sources, and age-associated oxidative damage has been suggested to be a major factor contributing to the initiation and progression of muscle atrophy inherent with ageing. RONS can modulate a variety of intracellular signal transduction processes, and disruption of these events over time due to altered redox control has been proposed as an underlying mechanism of ageing. The role of oxidants in ageing has been extensively examined in different model organisms that have undergone genetic manipulations with inconsistent findings. Transgenic and knockout rodent studies have provided insight into the function of RONS regulatory systems in neuromuscular ageing. This review summarizes almost 30 years of research in the field of redox homeostasis and muscle ageing, providing a detailed discussion of the experimental approaches that have been undertaken in murine models to examine the role of redox regulation in age-related muscle atrophy and weakness.

 

Sakellariou, G. K., Lightfoot, A. P., Earl, K. E., Stofanko, M., and McDonagh, B. (2017) Redox homeostasis and age-related deficits in neuromuscular integrity and function. Journal of Cachexia, Sarcopenia and Muscle, 8: 881–906 doi: 10.1002/jcsm.12223.

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     Page 907–914

Anna Maria Martone, Lara Bianchi, Pasquale Abete, Giuseppe Bellelli, Mario Bo, Antonio Cherubini, Francesco Corica, Mauro Di Bari, Marcello Maggio, Giovanna Maria Manca, Emanuele Marzetti, Maria Rosaria Rizzo, Andrea Rossi, Stefano Volpato, Francesco Landi the GLISTEN Group Investigators

The incidence of sarcopenia among hospitalized older patients: results from the Glisten studyBackground
New evidence is emerging on the importance of lean body mass during periods of illness and recovery. The preservation of lean body mass during such periods of intense stress impacts both patient and treatment outcomes. However, data concerning the incidence of sarcopenia among older people during hospitalization are scarce. The objective of this study was to evaluate the development of sarcopenia in a sample of hospitalized older subjects.
Methods
We used data of 394 participants from the multicentre Italian Study conducted by the Gruppo Lavoro Italiano Sarcopenia—Trattamento e Nutrizione (GLISTEN) in 12 Acute Care Wards (Internal Medicine and Geriatrics) of University Hospitals across Italy. This study was designed to determine the prevalence of sarcopenia at hospital admission and the change in muscle mass and strength during hospitalization. Sarcopenia was defined as low skeletal mass index (kg/m2) along with either low handgrip strength or slow walking speed [European Working Groups on Sarcopenia in Older People (EWGSOP) criteria]. Estimation of skeletal muscle mass was performed by bioelectrical impedance analysis (BIA).
Results
The mean age of the 394 enrolled patients (including 211 females who accounted for 53% of the sample) was 79.6 ± 6.4 years. Among those without sarcopenia at hospital admission, 14.7% of the study sample met the EWGSOP sarcopenia diagnostic criteria at discharge. The incidence of sarcopenia during hospitalization was significantly associated with the number of days spent in bed but was not correlated with the total length of hospital stay. In particular, patients who developed sarcopenia spent an average of 5.1 days in bed compared with 3.2 days for those with no sarcopenia at discharge (P = 0.02). Patients with sarcopenia showed a significantly lower body mass index compared with non-sarcopenic peers (25.0 ± 3.8 kg/m2 vs. 27.6 ± 4.9 kg/m2, respectively; P < 0.001). Similarly, the skeletal mass index at admission was significantly lower among patients who developed sarcopenia during hospital stay.
Conclusions
Incident sarcopenia during hospital stay is relatively common and is associated with nutritional status and the number of days of bed rest.

 

Martone, A. M., Bianchi, L., Abete, P., Bellelli, G., Bo, M., Cherubini, A., Corica, F., Di Bari, M., Maggio, M., Manca, G. M., Marzetti, E., Rizzo, M. R., Rossi, A., Volpato, S., and Landi, F. (2017) The incidence of sarcopenia among hospitalized older patients: results from the Glisten study. Journal of Cachexia, Sarcopenia and Muscle, 8: 907–914 doi: 10.1002/jcsm.12224.

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     Page 915–925

Hiroki Nishikawa, Hirayuki Enomoto, Akio Ishii, Yoshinori Iwata, Yuho Miyamoto, Noriko Ishii, Yukihisa Yuri, Kunihiro Hasegawa, Chikage Nakano, Takashi Nishimura, Kazunori Yoh, Nobuhiro Aizawa, Yoshiyuki Sakai, Naoto Ikeda, Tomoyuki Takashima, Ryo Takata, Hiroko Iijima, Shuhei Nishiguchi

Elevated serum myostatin level is associated with worse survival in patients with liver cirrhosisBackground
We aimed to elucidate the relationship between serum myostatin levels and other markers including skeletal muscle mass and to investigate the influence of serum myostatin levels on survival for patients with liver cirrhosis (LC).
Methods
A total of 198 LC subjects were analysed in this study. Myostatin levels were measured using stored sera. We retrospectively investigated the relationship between myostatin level and other markers, and the influence of myostatin level on overall survival (OS). Assessment of skeletal muscle mass was performed using the psoas muscle index (PMI) on computed tomography images at baseline. PMI indicates the sum of bilateral psoas muscle mass calculated by hand tracing at the lumber three level on computed tomography images divided by height squared (cm2/m2). The study cohort was divided into two groups based on the median myostatin value in each gender.
Results
Our study cohort included 108 male and 90 female patients with a median age of 67.5 years. The median (range) myostatin level for male patients was 3419.6 pg/mL (578.4–12897.7 pg/mL), whereas that for female patients was 2662.4 pg/mL (710.4–8782.0 pg/mL) (P = 0.0024). Median (range) serum myostatin level for Child–Pugh A patients (n = 123) was 2726.0 pg/mL (578.4–12667.2 pg/mL), whereas that for Child–Pugh B or C patients (n = 75) was 3615.2 pg/mL (663.3–12897.7 pg/mL) (P = 0.0011). For the entire cohort, the 1-, 3-, 5-, and 7-year cumulative OS rates were 93.94%, 72.71%, 50.37%, and 38.47%, respectively, in the high-myostatin group and 96.97%, 83.27%, 73.60%, and 69.95%, respectively, in the low-myostatin group (P = 0.0001). After excluding hepatocellular carcinoma patients (at baseline) from our analysis (n = 158), the 1-, 3-, 5-, and 7-year cumulative OS rates were 96.0%, 77.93%, 52.97%, and 39.08%, respectively, in the high-myostatin group and 96.39%, 87.58%, 77.63%, and 73.24%, respectively, in the low-myostatin group (P = 0.0005). Higher age (P = 0.0111) and lower PMI (P < 0.0001) were identified as significant predictors of poorer OS in our multivariate analysis, while higher serum myostatin (P = 0.0855) tended to be a significant adverse predictor. In both genders, PMI, serum albumin, prothrombin time, and branched-chain amino acid to tyrosine ratio showed a significantly inverse correlation with myostatin levels, and serum ammonia levels showed a significantly positive correlation with myostatin levels.
Conclusions
Higher serum myostatin levels correlated with muscle mass loss, hyperammonemia, and impaired protein synthesis, as reflected by lower serum albumin levels and lower branched-chain amino acid to tyrosine ratio levels. High serum myostatin levels were also associated with a reduced OS rate in LC patients.

 

Nishikawa, H., Enomoto, H., Ishii, A., Iwata, Y., Miyamoto, Y., Ishii, N., Yuri, Y., Hasegawa, K., Nakano, C., Nishimura, T., Yoh, K., Aizawa, N., Sakai, Y., Ikeda, N., Takashima, T., Takata, R., Iijima, H., and Nishiguchi, S. (2017) Elevated serum myostatin level is associated with worse survival in patients with liver cirrhosis. Journal of Cachexia, Sarcopenia and Muscle, 8: 915–925 doi: 10.1002/jcsm.12212.

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     Page 926–938

Jacob L. Brown, Megan E. Rosa-Caldwell, David E. Lee1, Thomas A. Blackwell, Lemuel A. Brown, Richard A. Perry, Wesley S. Haynie, Justin P. Hardee, James A. Carson, Michael P. Wiggs, Tyrone A. Washington, Nicholas P. Greenearks

Mitochondrial degeneration precedes the development of muscle atrophy in progression of cancer cachexia in tumour-bearing miceBackground
Cancer cachexia is largely irreversible, at least via nutritional means, and responsible for 20–40% of cancer-related deaths. Therefore, preventive measures are of primary importance; however, little is known about muscle perturbations prior to onset of cachexia. Cancer cachexia is associated with mitochondrial degeneration; yet, it remains to be determined if mitochondrial degeneration precedes muscle wasting in cancer cachexia. Therefore, our purpose was to determine if mitochondrial degeneration precedes cancer-induced muscle wasting in tumour-bearing mice.
Methods
First, weight-stable (MinStable) and cachectic (MinCC) ApcMin/+ mice were compared with C57Bl6/J controls for mRNA contents of mitochondrial quality regulators in quadriceps muscle. Next, Lewis lung carcinoma (LLC) cells or PBS (control) were injected into the hind flank of C57Bl6/J mice at 8 week age, and tumour allowed to develop for 1, 2, 3, or 4 weeks to examine time course of cachectic development. Succinate dehydrogenase stain was used to measure oxidative phenotype in tibialis anterior muscle. Mitochondrial quality and function were assessed using the reporter MitoTimer by transfection to flexor digitorum brevis and mitochondrial function/ROS emission in permeabilized adult myofibres from plantaris. RT-qPCR and immunoblot measured the expression of mitochondrial quality control and antioxidant proteins. Data were analysed by one-way ANOVA with Student–Newman–Kuels post hoc test.
Results
MinStable mice displayed ~50% lower Pgc-1α, Pparα, and Mfn2 compared with C57Bl6/J controls, whereas MinCC exhibited 10-fold greater Bnip3 content compared with C57Bl6/J controls. In LLC, cachectic muscle loss was evident only at 4 weeks post-tumour implantation. Oxidative capacity and mitochondrial content decreased by ~40% 4 weeks post-tumour implantation. Mitochondrial function decreased by ~25% by 3 weeks after tumour implantation. Mitochondrial degeneration was evident by 2 week LLC compared with PBS control, indicated by MitoTimer red/green ratio and number of pure red puncta. Mitochondrial ROS production was elevated by ~50 to ~100% when compared with PBS at 1–3 weeks post-tumour implantation. Mitochondrial quality control was dysregulated throughout the progression of cancer cachexia in tumour-bearing mice. In contrast, antioxidant proteins were not altered in cachectic muscle wasting.
Conclusions
Functional mitochondrial degeneration is evident in LLC tumour-bearing mice prior to muscle atrophy. Contents of mitochondrial quality regulators across ApcMin/+ and LLC mice suggest impaired mitochondrial quality control as a commonality among pre-clinical models of cancer cachexia. Our data provide novel evidence for impaired mitochondrial health prior to cachectic muscle loss and provide a potential therapeutic target to prevent cancer cachexia.

 

Brown, J. L., Rosa-Caldwell, M. E., Lee, D. E., Blackwell, T. A., Brown, L. A., Perry, R. A., Haynie, W. S., Hardee, J. P., Carson, J. A., Wiggs, M. P., Washington, T. A., and Greene, N. P. (2017) Mitochondrial degeneration precedes the development of muscle atrophy in progression of cancer cachexia in tumour-bearing mice. Journal of Cachexia, Sarcopenia and Muscle, 8: 926–938 doi: 10.1002/jcsm.12232.

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     Page 939–953

Thomas Scott Bowen, Volker Adams, Sarah Werner, Tina Fischer, Paulien Vinke, Maria Noel Brogger, Norman Mangner, Axel Linke, Peter Sehr, Joe Lewis, Dittmar Labeit, Alexander Gasch, Siegfried Labeit

Small-molecule inhibition of MuRF1 attenuates skeletal muscle atrophy and dysfunction in cardiac cachexiaBackground
Muscle ring finger 1 (MuRF1) is a muscle-specific ubiquitin E3 ligase activated during clinical conditions associated with skeletal muscle wasting. Yet, there remains a paucity of therapeutic interventions that directly inhibit MuRF1 function, particularly in vivo. The current study, therefore, developed a novel compound targeting the central coiled coil domain of MuRF1 to inhibit muscle wasting in cardiac cachexia.
Methods
We identified small molecules that interfere with the MuRF1–titin interaction from a 130 000 compound screen based on Alpha Technology. A subset of nine prioritized compounds were synthesized and administrated during conditions of muscle wasting, that is, to C2C12 muscle cells treated with dexamethasone and to mice treated with monocrotaline to induce cardiac cachexia.
Results
The nine selected compounds inhibited MuRF1–titin complexation with IC50 values <25 μM, of which three were found to also inhibit MuRF1 E3 ligase activity, with one further showing low toxicity on cultured myotubes. This last compound, EMBL chemical core ID#704946, also prevented atrophy in myotubes induced by dexamethasone and attenuated fibre atrophy and contractile dysfunction in mice during cardiac cachexia. Proteomic and western blot analyses showed that stress pathways were attenuated by ID#704946 treatment, including down-regulation of MuRF1 and normalization of proteins associated with apoptosis (BAX) and protein synthesis (elF2B-delta). Furthermore, actin ubiquitinylation and proteasome activity was attenuated.
Conclusions
We identified a novel compound directed to MuRF1's central myofibrillar protein recognition domain. This compound attenuated in vivo muscle wasting and contractile dysfunction in cardiac cachexia by protecting de novo protein synthesis and by down-regulating apoptosis and ubiquitin-proteasome-dependent proteolysis.

 

Bowen, T. S., Adams, V., Werner, S., Fischer, T., Vinke, P., Brogger, M. N., Mangner, N., Linke, A., Sehr, P., Lewis, J., Labeit, D., Gasch, A., and Labeit, S. (2017) Small-molecule inhibition of MuRF1 attenuates skeletal muscle atrophy and dysfunction in cardiac cachexia. Journal of Cachexia, Sarcopenia and Muscle, 8: 939–953 doi: 10.1002/jcsm.12233.

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     Page 926–938

Francesca Molinari, Fabrizio Pin, Stefania Gorini, Sergio Chiandotto, Laura Pontecorvo, Fabio Penna, Emanuele Rizzuto,
Simona Pisu, Antonio Musarò, Paola Costelli, Giuseppe Rosano, Elisabetta Ferraro

The mitochondrial metabolic reprogramming agent trimetazidine as an ‘exercise mimetic’ in cachectic C26-bearing miceBackground
Cancer cachexia is characterized by muscle depletion and exercise intolerance caused by an imbalance between protein synthesis and degradation and by impaired myogenesis. Myofibre metabolic efficiency is crucial so as to assure optimal muscle function. Some drugs are able to reprogram cell metabolism and, in some cases, to enhance metabolic efficiency. Based on these premises, we chose to investigate the ability of the metabolic modulator trimetazidine (TMZ) to counteract skeletal muscle dysfunctions and wasting occurring in cancer cachexia.
Methods
For this purpose, we used mice bearing the C26 colon carcinoma as a model of cancer cachexia. Mice received 5 mg/kg TMZ (i.p.) once a day for 12 consecutive days. A forelimb grip strength test was performed and tibialis anterior, and gastrocnemius muscles were excised for analysis. Ex vivo measurement of skeletal muscle contractile properties was also performed.
Results
Our data showed that TMZ induces some effects typically achieved through exercise, among which is grip strength increase, an enhanced fast-to slow myofibre phenotype shift, reduced glycaemia, PGC1a up-regulation, oxidative metabolism, and mitochondrial biogenesis. TMZ also partially restores the myofibre cross-sectional area in C26-bearing mice, while modulation of autophagy and apoptosis were excluded as mediators of TMZ effects.
Conclusions
In conclusion, our data show that TMZ acts like an ‘exercise mimetic’ and is able to enhance some mechanisms of adaptation to stress in cancer cachexia. This makes the modulation of the metabolism, and in particular TMZ, a suitable candidate for a therapeutic rehabilitative protocol design, particularly considering that TMZ has already been approved for clinical use.

 

Molinari, F., Pin, F., Gorini, S., Chiandotto, S., Pontecorvo, L., Penna, F., Rizzuto, E., Pisu, S., Musarò, A., Costelli, P., Rosano, G., and Ferraro, E. (2017) The mitochondrial metabolic reprogramming agent trimetazidine as an ‘exercise mimetic’ in cachectic C26-bearing mice. Journal of Cachexia, Sarcopenia and Muscle, 8: 926–938. doi: 10.1002/jcsm.12226.
 

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     Page 974–990

Tania Cid-Díaz, Icía Santos-Zas, Jessica González-Sánchez, Uxía Gurriarán-Rodríguez, Carlos S. Mosteiro, Xesús Casabiell, Tomás García-Caballero, Vincent Mouly, Yolanda Pazos1, Jesús P. Camiña

Obestatin controls the ubiquitin–proteasome and autophagy–lysosome systems in glucocorticoid-induced muscle cell atrophyBackground
Many pathological states characterized by muscle atrophy are associated with an increase in circulating glucocorticoids and poor patient prognosis, making it an important target for treatment. The development of treatments for glucocorticoid-induced and wasting disorder-related skeletal muscle atrophy should be designed based on how the particular transcriptional program is orchestrated and how the balance of muscle protein synthesis and degradation is deregulated. Here, we investigated whether the obestatin/GPR39 system, an autocrine/paracrine signaling system acting on myogenesis and with anabolic effects on the skeletal muscle, could protect against glucocorticoid-induced muscle cell atrophy.
Methods
In the present study, we have utilized mouse C2C12 myotube cultures to examine whether the obestatin/GPR39 signaling pathways can affect the atrophy induced by the synthetic glucocorticoid dexamethasone. We have extended these findings to in vitro effects on human atrophy using human KM155C25 myotubes.
Results
The activation of the obestatin/GPR39 system protects from glucocorticoid-induced atrophy by regulation of Akt, PKD/PKCµ, CAMKII and AMPK signaling and its downstream targets in the control of protein synthesis, ubiquitin–proteasome system and autophagy–lysosome system in mouse cells. We compared mouse and human myotube cells in their response to glucocorticoid and identified differences in both the triggering of the atrophic program and the response to obestatin stimulation. Notably, we demonstrate that specific patterns of post-translational modifications of FoxO4 and FoxO1 play a key role in directing FoxO activity in response to obestatin in human myotubes.
Conclusions
Our findings emphasize the function of the obestatin/GPR39 system in coordinating a variety of pathways involved in the regulation of protein degradation during catabolic conditions.

 

Cid-Díaz, T., Santos-Zas, I., González-Sánchez, J., Gurriarán-Rodríguez, U., Mosteiro, C. S., Casabiell, X., García-Caballero, T., Mouly, V., Pazos, Y., and Camiña, J. P. (2017) Obestatin controls the ubiquitin–proteasome and autophagy–lysosome systems in glucocorticoid-induced muscle cell atrophy. Journal of Cachexia, Sarcopenia and Muscle, 8: 974–990 doi: 10.1002/jcsm.12222.

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     Page 991–998

Rocco Barazzoni, Gianluca Gortan Cappellari, Sandra Palus, Pierandrea Vinci, Giulia Ruozi, Michela Zanetti, Annamaria Semolic, Nicole Ebner, Stephan von Heahling, Gianfranco Sinagra, Mauro Giacca, Jochen Springer

Acylated ghrelin treatment normalizes skeletal muscle mitochondrial oxidative capacity and AKT phosphorylation in rat chronic heart failureBackground
Chronic heart failure (CHF) is associated with skeletal muscle abnormalities contributing to exercise intolerance, muscle loss, and negative impact on patient prognosis. A primary role has been proposed for mitochondrial dysfunction, which may be induced by systemic and tissue inflammation and further contribute to low insulin signalling. The acylated form of the gastric hormone ghrelin (AG) may improve mitochondrial oxidative capacity and insulin signalling in both healthy and diseased rodent models.
Methods
We investigated the impact of AG continuous subcutaneous administration (AG) by osmotic minipump (50 nmol/kg/day for 28 days) compared with placebo (P) on skeletal muscle mitochondrial enzyme activities, mitochondrial biogenesis regulators transcriptional expression and insulin signalling in a rodent post-myocardial infarction CHF model.
Results
No statistically significant differences (NS) were observed among the three group in cumulative food intake. Compared with sham-operated, P had low mitochondrial enzyme activities, mitochondrial biogenesis regulators transcripts, and insulin signalling activation at AKT level (P < 0.05), associated with activating nuclear translocation of pro-inflammatory transcription factor nuclear factor-?B. AG completely normalized all alterations (P < 0.05 vs P, P = NS vs sham-operated). Direct AG activities were strongly supported by in vitro C2C12 myotubes experiments showing AG-dependent stimulation of mitochondrial enzyme activities. No changes in mitochondrial parameters and insulin signalling were observed in the liver in any group.
Conclusions
Sustained peripheral AG treatment with preserved food intake normalizes a CHF-induced tissue-specific cluster of skeletal muscle mitochondrial dysfunction, pro-inflammatory changes, and reduced insulin signalling. AG is therefore a potential treatment for CHF-associated muscle catabolic alterations, with potential positive impact on patient outcome.

 

 

Barazzoni, R., Gortan Cappellari, G., Palus, S., Vinci, P., Ruozi, G., Zanetti, M., Semolic, A., Ebner, N., von Heahling, S., Sinagra, G., Giacca, M., and Springer, J. (2017) Acylated ghrelin treatment normalizes skeletal muscle mitochondrial oxidative capacity and AKT phosphorylation in rat chronic heart failure. Journal of Cachexia, Sarcopenia and Muscle, 8: 991–998 doi: 10.1002/jcsm.12254.

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     Page 999–1080

Abstracts of the 10th International Conference on Cachexia, Sarcopenia and Muscle Wasting, Rome, Italy, 8–10 December 2017 (Part 1)Abstracts of the 10th International Conference on Cachexia, Sarcopenia and Muscle Wasting, Rome, Italy, 8–10 December 2017 (Part 1)

 

(2017), Abstracts of the 10th International Conference on Cachexia, Sarcopenia and Muscle Wasting, Rome, Italy, 8–10 December 2017 (Part 1). Journal of Cachexia, Sarcopenia and Muscle, 8: 999–1080. doi: 10.1002/jcsm.12255
 

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     Page 1081–1083

Stephan von Haehling, John E. Morley, Andrew J.S. Coats, Stefan D. Anker

Ethical guidelines for publishing in the journal of cachexia, sarcopenia and muscle: update 2017This article details an updated version of the principles of ethical authorship and publishing in the Journal of Cachexia, Sarcopenia and Muscle (JCSM). At the time of submission to JCSM, the corresponding author, on behalf of all co-authors, needs to certify adherence to these principles. The principles are as follows:

 

von Haehling, S., Morley, J. E., Coats, A. J. S., and Anker, S. D. (2017) Ethical guidelines for publishing in the journal of cachexia, sarcopenia and muscle: update 2017. Journal of Cachexia, Sarcopenia and Muscle, 8: 1081–1083. doi: 10.1002/jcsm.12261.

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Thank You to Reviewers     Page 1084–1085

John E. Morley, Stefan D. Anker

With Appreciationno abstract

 

(2017), With Appreciation. Journal of Cachexia, Sarcopenia and Muscle, 8: 1084–1085. doi: 10.1002/jcsm.12263

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