Journal of the National Cancer Institute · 2015
Preclinical Investigation of the Novel Histone Deacetylase Inhibitor AR-42 in the Treatment of Cancer-Induced Cachexia.
СтатьяПоддержка исследования: вне правительства СШАНазвание и аннотация: Перевод в очереди
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Tseng Yu-Chou, Kulp Samuel K, Lai I-Lu, Hsu En-Chi, He Wei A, Frankhouser David E, Yan Pearlly S, Mo Xiaokui, Bloomston Mark, Lesinski Gregory B, Marcucci Guido, Guttridge Denis C, Bekaii-Saab Tanios, Chen Ching-Shih
Аннотация
BACKGROUND: Cancer cachexia is a debilitating condition that impacts patient morbidity, mortality, and quality of life and for which effective therapies are lacking. The anticachectic activity of the novel HDAC inhibitor AR-42 was investigated in murine models of cancer cachexia.
METHODS: The effects of AR-42 on classic features of cachexia were evaluated in the C-26 colon adenocarcinoma and Lewis lung carcinoma (LLC) models. Effects on survival in comparison with approved HDAC inhibitors (vorinostat, romidepsin) were determined. The muscle metabolome and transcriptome (by RNA-seq), as well as serum cytokine profile, were evaluated. Data were analyzed using mixed effects models, analysis of variance, or log-rank tests. All statistical tests were two-sided.
RESULTS: In the C-26 model, orally administered AR-42 preserved body weight (23.9±2.6 grams, AR-42-treated; 20.8±1.3 grams, vehicle-treated; P = .005), prolonged survival (P < .001), prevented reductions in muscle and adipose tissue mass, muscle fiber size, and muscle strength and restored intramuscular mRNA expression of the E3 ligases MuRF1 and Atrogin-1 to basal levels (n = 8). This anticachectic effect, confirmed in the LLC model, was not observed after treatment with vorinostat and romidepsin. AR-42 suppressed tumor-induced changes in inflammatory cytokine production and multiple procachexia drivers (IL-6, IL-6Rα, leukemia inhibitory factor, Foxo1, Atrogin-1, MuRF1, adipose triglyceride lipase, uncoupling protein 3, and myocyte enhancer factor 2c). Metabolomic analysis revealed cachexia-associated changes in glycolysis, glycogen synthesis, and protein degradation in muscle, which were restored by AR-42 to a state characteristic of tumor-free mice.
CONCLUSIONS: These findings support further investigation of AR-42 as part of a comprehensive therapeutic strategy for cancer cachexia.
METHODS: The effects of AR-42 on classic features of cachexia were evaluated in the C-26 colon adenocarcinoma and Lewis lung carcinoma (LLC) models. Effects on survival in comparison with approved HDAC inhibitors (vorinostat, romidepsin) were determined. The muscle metabolome and transcriptome (by RNA-seq), as well as serum cytokine profile, were evaluated. Data were analyzed using mixed effects models, analysis of variance, or log-rank tests. All statistical tests were two-sided.
RESULTS: In the C-26 model, orally administered AR-42 preserved body weight (23.9±2.6 grams, AR-42-treated; 20.8±1.3 grams, vehicle-treated; P = .005), prolonged survival (P < .001), prevented reductions in muscle and adipose tissue mass, muscle fiber size, and muscle strength and restored intramuscular mRNA expression of the E3 ligases MuRF1 and Atrogin-1 to basal levels (n = 8). This anticachectic effect, confirmed in the LLC model, was not observed after treatment with vorinostat and romidepsin. AR-42 suppressed tumor-induced changes in inflammatory cytokine production and multiple procachexia drivers (IL-6, IL-6Rα, leukemia inhibitory factor, Foxo1, Atrogin-1, MuRF1, adipose triglyceride lipase, uncoupling protein 3, and myocyte enhancer factor 2c). Metabolomic analysis revealed cachexia-associated changes in glycolysis, glycogen synthesis, and protein degradation in muscle, which were restored by AR-42 to a state characteristic of tumor-free mice.
CONCLUSIONS: These findings support further investigation of AR-42 as part of a comprehensive therapeutic strategy for cancer cachexia.
Предметные рубрики MeSH
AdenocarcinomaAdipose TissueAdministration, OralAnimalsCachexiaCarcinoma, Lewis LungColonic NeoplasmsCytokinesForkhead Box Protein O1Forkhead Transcription FactorsGene Expression RegulationHistone Deacetylase InhibitorsInterleukin-6Ion ChannelsLeukemia Inhibitory FactorLipaseMEF2 Transcription FactorsMiceMitochondrial ProteinsMuscle ProteinsMuscle StrengthMuscle, SkeletalNeoplasms, ExperimentalPhenylbutyratesReceptors, Interleukin-6SKP Cullin F-Box Protein LigasesSurvival AnalysisTripartite Motif ProteinsUbiquitin-Protein LigasesUncoupling Protein 3Weight LossAcyltransferases