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Falconi, J.

Publications and source records attributed to Falconi, J..

4 recordsLinked to original sources

Furan fatty acid supplementation protects against muscle atrophy during cancer cachexia

Background: Cachexia is a multifactorial syndrome frequently observed in cancer patients, characterized by progressive weight loss, muscle atrophy, and systemic inflammation. We recently demonstrated that supplementation with FuFA-F2, a naturally occurring lipid found in various foods, increases muscle mass in different metabolic contexts. Here, we investigated whether FuFA-F2 supplementation could prevent tumor-induced muscle wasting and preserve skeletal muscle integrity during cancer cachexia. Methods: In vitro, C2C12 myotubes were exposed to TNF and IFN{gamma} to mimic cachectic conditions, and the effects of FuFA-F2 on myotube morphology were assessed. In vivo, cancer cachexia was induced by subcutaneous injection of C26 adenocarcinoma cells into male CD2F1 mice. Three groups were compared: non-grafted control mice, untreated C26 tumor-bearing mice, and C26 tumor-bearing mice orally supplemented with FuFA-F2 (13 mg/kg/day) for 14 days. Results: In C2C12 myotubes, TNF and IFN{gamma} exposure reduced myotube area by 17% (p < 0.05), whereas FuFA-F2 treatment prevented this atrophy and restored myotube area to control levels (p < 0.05). In vivo, FuFA-F2 supplementation prevented muscle wasting in C26 tumor-bearing mice without affecting tumor growth or the loss of white adipose tissue. After 14 days, hindlimb muscle weight was reduced by 22% in C26 mice compared with controls (0.706 vs. 0.903 g, p < 0.05), whereas muscle weight in FuFA-F2-treated mice (0.835 g) was not significantly different from controls. Consistently, spontaneous wheel activity was markedly reduced in C26 mice during the final four days (-79%; 3.4 vs. 16.5 km, p < 0.05), whereas FuFA-F2-treated mice maintained activity levels closer to those of controls (11.2 km). RNA-seq analysis revealed extensive transcriptional reprogramming of skeletal muscle in response to C26 tumor growth, with 5,465 differentially expressed genes (DEGs; 32% of detected genes) between Control and C26 mice. Notably, FuFA-F2 substantially attenuated this response, with only 366 DEGs (2%) between Control and C26 + FuFA-F2 mice, and principal component analysis (PCA) showed a transcriptomic profile closer to controls. Tumor-induced alterations involved pathways related to proteostasis, inflammation, and tissue remodeling, which were largely prevented or attenuated by FuFA-F2. Consistent with these findings, FuFA-F2 prevented the induction of Myostatin, Activin A, MAFbx and MuRF1, and attenuated muscle fibrosis and local inflammation. Conclusions: These findings demonstrate that FuFA-F2 preserves skeletal muscle mass and function in the C26 model of cancer cachexia, despite ongoing tumor progression. FuFA-F2 markedly attenuates tumor-induced transcriptional reprogramming and associated catabolic, inflammatory and fibrotic responses, supporting its potential as a therapeutic strategy to preserve skeletal muscle during cancer cachexia.

cancer biology↗

E(spl)m4 Directly Antagonizes Traf4 to Inhibit JNK Signaling in Drosophila

TRAF proteins are adaptor proteins that participate in signal transduction downstream of the Toll or TNF receptors and could elicit E3-Ubiquitin Ligase activity. They have been implicated in multiple processes during signal transduction, inflammation, and morphogenesis. In Drosophila, Traf4 has been implicated in the regulation of JNK signaling and cell death as well as Adherens Junctions regulation. Using overexpression approaches, we show here that Traf4 promotes JNK and caspase activation, as well as junctional E-Cadherin/ {beta}-Catenin depletion, resulting in epithelial cell delamination. Using biochemical, modelling, and functional genetics approaches, we further show that the Bearded-type small protein E(spl)m4 binds to Traf4, and inhibits its downstream signaling towards JNK activation and cell delamination, without affecting the effects of Traf4 on Adherens Junctions. Thus, this study identifies an endogenous peptide inhibiting Traf4 signaling, potentially by blocking Traf4 trimerization.

developmental biology↗

Tumour-derived Ilp8 and Upd3 control intestinal progenitor cells depletion during cachexia in Drosophila larvae

In animals, tumour development triggers systemic effects, impacting the physiology of distant organs. In Drosophila larvae, wing disc neoplastic tumours result in developmental delay and organ wasting reminiscent of cachexia. This paraneoplastic syndrome affects many organs, but its effects on the intestine, a key organ in the regulation of nutrient and energy homeostasis, remain understudied. We describe here that neoplastic tumours also affect the development of the larval midgut, leading to altered cell type numbers, with a depletion of the stem-cell-like Adult Midgut Precursors (AMPs), and a disorganisation of the niche cells which enter precocious differentiation. Importantly, these intestinal cell type alterations are initiated before the onset of reduced food intake, and of muscle and adipose tissue atrophies, and thus represent a new paraneoplastic phenotype. Screening for mediators, we show that tumour derived Ilp8 and Upd3 control AMPs number and niche specification respectively.

developmental biology↗

Fat body glycolysis defects inhibit mTOR and promote distant muscle disorganization through TNF-α/egr and ImpL2 signaling in Drosophila larvae

The fat body in Drosophila larvae serves as a reserve tissue and participates, through its endocrine function, in the regulation of organismal growth and homeostasis. To better understand its role in growth coordination, we induced severe fat body atrophy by knocking down in adipose cells several key enzymes of the glycolytic pathway. Our results show that impairing the last steps of glycolysis led to a drastic shrinkage in adipose cell size and lipid droplets content, and a downregulation of the mTOR pathway. Strikingly, fat body atrophy resulted in the distant disorganization of body wall muscles and the release of muscle-specific proteins in the hemolymph. Molecularly we showed that REPTOR activity was required for fat body atrophy downstream of glycolysis inhibition, and that the effect of fat body atrophy on muscles did not require upd3 secretion, but depended the production of egr/TNF- and of the insulin pathway inhibitor ImpL2.

physiology↗