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En bleu, les références de l’équipe des porteurs du projet TRANS-BEAR

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4.      Morley, J. E. et al. Sarcopenia With Limited Mobility: An International Consensus. J. Am. Med. Dir. Assoc. 12, 403–409 (2011).

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6.      Peris-Moreno, D., Taillandier, D. & Polge, C. MuRF1/TRIM63, Master regulator of muscle mass. Int. J. Mol. Sci. 21, 6663 (2020).

7.      Peris-Moreno, D., Cussonneau, L. & Combaret, L. Ubiquitin Ligases at the Heart of Skeletal Muscle Atrophy Control. 26, (2021).

8.      Taillandier, D. & Polge, C. Skeletal muscle atrogenes: From rodent models to human pathologies. Biochimie 166, 251–269 (2019).

9.      Polge, C. et al. Recent progress in elucidating signalling proteolytic pathways in muscle wasting: Potential clinical implications. Nutr Metab Cardiovasc Dis 23 Suppl 1, S1-5 (2013).

10.    Combaret, L. et al. A leucine-supplemented diet restores the defective postprandial inhibition of proteasome-dependent proteolysis in aged rat skeletal muscle. J. Physiol.-Lond. 569, 489–499 (2005).

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12.    B’Chir, W. et al. The eIF2alpha/ATF4 pathway is essential for stress-induced autophagy gene expression. Nucleic Acids Res 41, 7683–99 (2013).

13.    Maurin, A.-C. et al. GCN2 upregulates autophagy in response to short-term deprivation of a single essential amino acid. Autophagy Rep. 1, 119–142 (2022).

14.    Polge, C. et al. Muscle actin is polyubiquitinylated in vitro and in vivo and targeted for breakdown by the E3 ligase MuRF1. FASEB J 25, 3790–802 (2011).

15.    Aniort, J. et al. Upregulation of MuRF1 and MAFbx participates to muscle wasting upon gentamicin-induced acute kidney injury. Int J Biochem Cell Biol https://doi.org/10.1016/j.biocel.2016.04.006 (2016) doi:10.1016/j.biocel.2016.04.006.

16.    Claustre, A. et al. Structure predictions of MuRF1-UBE2 complexes identify amino acid residues governing interaction selectivity for each MuRF1-E2 pair. FEBS J. 292, 2559–2577 (2025).

17.    Polge, C., Cabantous, S. & Taillandier, D. Tripartite Split-GFP for High Throughput Screening of Small Molecules: A Powerful Strategy for Targeting Transient/Labile Interactors like E2-E3 Ubiquitination Enzymes. ChemBioChem 25, (2024).

18.    Peris-Moreno, D. et al. UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin. Cells 10, 1974 (2021).

19.    Aniort, J. et al. Muscle wasting in patients with end-stage renal disease or early-stage lung cancer: common mechanisms at work. 10, 323–337 (2019).

20.    Polge, C. et al. Erratum: Polge, C., et al. UBE2E1 Is Preferentially Expressed in the Cytoplasm of Slow-Twitch Fibers and Protects Skeletal Muscles from Exacerbated Atrophy upon Dexamethasone Treatment. Cells 2018, 7, 214. Cells 7, 242 (2018).

21.    Polge, C. et al. A muscle-specific MuRF1-E2 network requires stabilization of MuRF1-E2 complexes by telethonin, a newly identified substrate. J. Cachexia Sarcopenia Muscle 9, 129–145 (2018).

22.    Polge, C. et al. UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes. J. Cachexia Sarcopenia Muscle 7, 377–387 (2016).

23.    Vazeille, E. et al. The ubiquitin-proteasome and the mitochondria-associated apoptotic pathways are sequentially downregulated during recovery after immobilization-induced muscle atrophy. Am. J. Physiol.-Endocrinol. Metab. 295, E1181–E1190 (2008).

24.    Capel, F. et al. Lysosomal and proteasome-dependent proteolysis are differentially regulated by insulin and/or amino acids following feeding in young, mature and old rats. J Nutr Biochem 20, 570–6 (2009).

25.    Slimani, L. et al. The worsening of tibialis anterior muscle atrophy during recovery post-immobilization correlates with enhanced connective tissue area, proteolysis, and apoptosis. Am J Physiol Endocrinol Metab 303, E1335-47 (2012).

26.    Deval, C. et al. Docosahexaenoic acid-supplementation prior to fasting prevents muscle atrophy in mice. J Cachexia Sarcopenia Muscle 7, 587–603 (2016).

27.    Salles, J. et al. TNFalpha gene knockout differentially affects lipid deposition in liver and skeletal muscle of high-fat-diet mice. J Nutr Biochem 23, 1685–93 (2012).

28.    Cussonneau, L. et al. Induction of ATF4-Regulated Atrogenes Is Uncoupled from Muscle Atrophy during Disuse in Halofuginone-Treated Mice and in Hibernating Brown Bears. Int. J. Mol. Sci. 24, 621 (2023).

29.    Slimani, L. et al. The delayed recovery of the remobilized rat tibialis anterior muscle reflects a defect in proliferative and terminal differentiation that impairs early regenerative processes. J. Cachexia Sarcopenia Muscle https://doi.org/10.1002/jcsm.12011 (2015) doi:10.1002/jcsm.12011.

30.    Deval, C. et al. Mitophagy and Mitochondria Biogenesis Are Differentially Induced in Rat Skeletal Muscles during Immobilization and/or Remobilization. Int. J. Mol. Sci. 21, 3691 (2020).

31.    Vazeille, E. et al. Curcumin treatment prevents increased proteasome and apoptosome activities in rat skeletal muscle during reloading and improves subsequent recovery. J Nutr Biochem 23, 245–51 (2012).

32.    Verney, J. et al. Soluble Milk Proteins Improve Muscle Mass Recovery after Immobilization-Induced Muscle Atrophy in Old Rats but Do not Improve Muscle Functional Property Restoration. J. Nutr. Health Aging 21, 1133–1141 (2017).

33.    Magne, H. et al. Contrarily to whey and high protein diets, dietary free leucine supplementation cannot reverse the lack of recovery of muscle mass after prolonged immobilization during ageing. J Physiol 590, 2035–49 (2012).

34.    Magne, H. et al. Unilateral hindlimb casting induced a delayed generalized muscle atrophy during rehabilitation that is prevented by a whey or a high protein diet but not a free leucine-enriched diet. PLoS One 8, e70130 (2013).

35.    Martin, V. et al. Whey proteins are more efficient than casein in the recovery of muscle functional properties following a casting induced muscle atrophy. PLoS One 8, e75408 (2013).

36.    Carraro, V. et al. Activation of the eIF2α-ATF4 Pathway by Chronic Paracetamol Treatment Is Prevented by Dietary Supplementation with Cysteine. Int. J. Mol. Sci. 23, 7196 (2022).

37.    Savary-Auzeloux, I. et al. A dietary supplementation with leucine and antioxidants is capable to accelerate muscle mass recovery after immobilization in adult rats. PLoS One 8, e81495 (2013).

38.    Mosoni, L. et al. Antioxidant supplementation had positive effects in old rat muscle, but through better oxidative status in other organs. Nutrition 26, 1157–62 (2010).

39.    Plissonneau, C. et al. High-Intensity interval training and α-linolenic acid supplementation improve DHA conversion and increase the abundance of gut mucosa-associated oscillospira bacteria. Nutrients 13, 1–19 (2021).

40.    Tardif, N. et al. Oleate-enriched diet improves insulin sensitivity and restores muscle protein synthesis in old rats. Clin Nutr 30, 799–806 (2011).

41.    Chavanelle, V. et al. Effects of high-intensity interval training and moderate-intensity continuous training on glycaemic control and skeletal muscle mitochondrial function in db/db mice. Sci. Rep. 7, 204 (2017).

42.    Groussard, C. et al. Tissue-Specific Oxidative Stress Modulation by Exercise: A Comparison between MICT and HIIT in an Obese Rat Model. 2019, 1965364 (2019).

43.    Rieu, I. et al. Reduction of Low Grade Inflammation Restores Blunting of Postprandial Muscle Anabolism and Limits Sarcopenia in Old Rats. J. Physiol.-Lond. 587, 5483–5492 (2009).

44.    Cussonneau, L. et al. Concurrent BMP Signaling Maintenance and TGF-β Signaling Inhibition Is a Hallmark of Natural Resistance to Muscle Atrophy in the Hibernating Bear. Cells 10, 1873 (2021).

45.    Boyer, C. et al. Specific shifts in the endocannabinoid system in hibernating brown bears. Front. Zool. 17, 35 (2020).

46.    Chazarin, B. et al. Metabolic reprogramming involving glycolysis in the hibernating brown bear skeletal muscle. Front. Zool. 16, (2019).

47.    Chazarin, B. et al. Limited Oxidative Stress Favors Resistance to Skeletal Muscle Atrophy in Hibernating Brown Bears (Ursus Arctos). Antioxidants 8, (2019).

48.    Luu, B. E. et al. MicroRNAs facilitate skeletal muscle maintenance and metabolic suppression in hibernating brown bears. J. Cell. Physiol. https://doi.org/10.1002/jcp.29294 (2019) doi:10.1002/jcp.29294.

49.    Bergouignan, A. et al. The Preservation of Muscle Mitochondrial Machinery During Hypometabolic Hibernation in Scandinavian Brown Bears ( Ursus arctos ). Acta Physiol. Oxf. Engl. 242, e70177 (2026).

50.    De Napoli, C. et al. Reduced ATP turnover during hibernation in relaxed skeletal muscle. Nat. Commun. 16, 80 (2025).

51.    Giroud, S. et al. Lipidomics Reveals Seasonal Shifts in a Large-Bodied Hibernator, the Brown Bear. Front. Physiol. 10, (2019).

52.    Richard, C. et al. Hibernating brown bear serum modulates the balance of TGF-β and BMP pathways in human muscle cells. Int. J. Biochem. Cell Biol. 189, 106864 (2025).

53.    Chanon, S. et al. Proteolysis inhibition by hibernating bear serum leads to increased protein content in human muscle cells. Sci Rep 8, 5525 (2018).

54.    Givre, L. et al. Cardiomyocyte Protection by Hibernating Brown Bear Serum: Toward the Identification of New Protective Molecules Against Myocardial Infarction. Front. Cardiovasc. Med. 8, 687501 (2021).

55.    Sutter, J. et al. Hibernating bear serum triggers an anti-fibrotic signature in human fibroblasts, involving ECM remodeling and MAPK signaling activation. Sci. Rep. 16, 14434 (2026).