Role of the ubiquitin-proteasome pathway in muscle atrophy in cachexia

Current Opinion in Supportive and Palliative Care

Volumn 2, Issue 4, 2008, Pages 262-266

  Attaix, Didier ^a,b   Combaret, Lydie ^a,b   Béchet, Daniel ^a,b   Taillandier, Daniel ^a,b  

^a CEMAGREF   (France)

^b INRA and University of Auvergne   (France)

Author keywords

Autophagy; Cachexia; Muscle wasting; Proteasome; Ubiquitin

Indexed keywords

PROTEASOME; UBIQUITIN;

ARTICLE; CACHEXIA; HUMAN; METABOLISM; MUSCLE ATROPHY; NEOPLASM; PHYSIOLOGY; SIGNAL TRANSDUCTION;

CACHEXIA; HUMANS; MUSCULAR ATROPHY; NEOPLASMS; PROTEASOME ENDOPEPTIDASE COMPLEX; SIGNAL TRANSDUCTION; UBIQUITIN;

EID: 61749088619     PISSN: 17514258     EISSN: 17514266     Source Type: Journal    
DOI: 10.1097/SPC.0b013e3283196ac2     Document Type: Article

References (40)

1. Evans WJ, Morley JE, Argiles J, et al. Cachexia: a new definition. Clin Nutr 2008. [Epub ahead of print.
2. Attaix D, Combaret L, Tilignac T, etal. Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia. Mol Biol Rep 1999; 26:77-82.
3. Attaix D, Ventadour S, Codran A, etal. The ubiquitin-proteasome system and skeletal muscle wasting. Essays Biochem 2005; 41:173-186.
4. Tisdale MJ. Molecular pathways leading to cancer cachexia. Physiology 2005; 20:340-348.
5. Smith IJ, Lecker SH, Hasselgren PO. Calpain activity and muscle wasting in sepsis. Am J Physiol Endocrinol Metab 2008. [Epub ahead of print.]
6. Rajan V, Mitch WE. Ubiquitin, proteasomes and proteolytic mechanisms activated by kidney disease. Biochim Biophys Acta 2008. [Epub ahead of print.]
7. Wing SS. Control of ubiquitination in skeletal muscle wasting. Int J Biochem Cell Biol 2005; 37:2075-2087.
8. Kwak KS, Zhou X, Solomon V, et al. Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia. Cancer Res 2004; 64:8193-8198.
9. Gomes MD, Lecker SH, Jagoe RT, et al. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci U S A 2001; 98:14440-14445.
10. Bodine SC, Latres E, Baumhueter S, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001; 294:1704-1708.
11. Lecker SH, Jagoe RT, GilbertA, etal. Multiple types ofskeletal muscle atrophy involve a common program of changes in gene expression. FASEB J 2004; 18:39 -51.
12. Glass DJ. Skeletal muscle hypertrophy and atrophy signaling pathways. Int J Biochem Cell Biol 2005; 37:1974-1984.
13. Fareed MU, Evenson AR, Wei W, et al. Treatment of rats with calpain inhibitors prevents sepsis-induced muscle proteolysis independent of atro- gin-1/MAFbx and MuRF1 expression. Am J Physiol Regul Integr Comp Physiol 2006; 290:R1589-R1597.
14. Tintignac LA, Lagirand J, Batonnet S, et al. Degradation ofMyoD mediated by the SCF (MAFbx) ubiquitin ligase. J Biol Chem 2005; 280:2847-2856.
15. Lagirand-Cantaloube J, Offner N, Csibi A, et al. The initiation factor eIF3-f is a major target for atrogin1/MAFbx function in skeletal muscle atrophy. EMBO J 2008; 27:1266 -1276.
16. Koyama S, Hata S, Witt CC, et al. Muscle RING-finger protein-1 (MuRFI) as a connector of muscle energy metabolism and protein synthesis. J Mol Biol 2008; 376:1224-1236.
17. Witt CC, Witt SH, LercheS, etal. Cooperative control of striated muscle mass and metabolism by MuRFI and MuRF2. EMBO J 2008; 27:350-360.
18. Cao PR, Kim HJ, Lecker SH. Ubiquitin-protein ligases in muscle wasting. Int J Biochem Cell Biol 2005; 37:2088-2097.
19. Combaret L, Adegoke OAJ, Bedard N, etal. USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states. Am J Physiol Endocrinol Metab 2005; 288:E693-E700.
20. Combaret L, Taillandier D, Dardevet D, etal. Glucocorticoids regulated mRNA levels for subunits of the 19S regulatory complex of the proteasome in fast- twitch rat muscles. Biochem J 2004; 378:239 -246.
21. Williams A, Sun X, Fischer JE, et al. The expression of genes in the ubiquitin- proteasome proteolytic pathway is increased in skeletal muscle from patients with cancer. Surgery 1999; 126:744-749.
22. Khal J, Hine AV, Fearon KC, et al. Increased expression of proteasome subunits in skeletal muscle of cancer patients with weight loss. Int J Biochem Cell Biol 2005; 37:2196 -2206.
23. Combaret L, Tilignac T, Claustre A, et al. Torbafylline (HWA 448) inhibits enhanced skeletal muscle ubiquitin-proteasome-dependent proteolysis in cancer and septic rats. Biochem J 2002; 361:185-192.
24. Heng AE, Ventadour S, Jarzaguet M, etal. Coordinate expression of the 19S regulatory complex and evidence for ubiquitin-dependent telethonin degradation in the unloaded soleus muscle. Int J Biochem Cell Biol 2008; 40:2544-2552.
25. Bossola M, Muscaritoli M, Costelli P, et al. Increased muscle proteasome activity correlates with disease severity in gastric cancer patients. Ann Surg 2003; 237:384-389.
26. Taillandier D, Aurousseau E, Combaret L, et al. Regulation of proteolysis during reloading of the unweighted soleus muscle. Int J Biochem Cell Biol 2003; 35:665-675.
27. Clarke BA, Drujan D, Willis MS, etal. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab 2007; 6:376-385.
28. Ventadour S, Jarzaguet M, Wing SS, et al. A new method of purification of proteasome substrates reveals polyubiquitination of 20 S proteasome sub- units. J Biol Chem 2007; 282:5302-5309.
29. Sandri M. Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda) 2008; 23:160-170.
30. Sandri M, Sandri C, Gilbert A, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004; 117:399 -412.
31. Jackman RW, Kandarian SC. The molecular basis ofskeletal muscle atrophy. Am J Physiol Cell Physiol 2004; 287:C834-C843.
32. Acharyya S, Butchbach ME, SahenkZ, etal. Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell 2005; 8:421-432.
33. Deval C, Mordier S, Obled C, et al. Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. Biochem J 2001; 360:143-150.
34. Zhao J, Brault JJ, Schild A, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007; 6:472 -483.
35. Mammucari C, Milan G, Romanello V, et al. FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab 2007; 6:458 -471.
36. Attaix D, Ventadour S, Taillandier D, et al. The ubiquitin-proteasome pathway: limitations and opportunities. J Support Oncol 2005; 3:221-222.
37. Russell ST, Eley H, Tisdale MJ. Role of reactive oxygen species in protein degradation in murine myotubes induced by proteolysis-inducing factor and angiotensin II. Cell Signal 2007; 19:1797 -1806.
38. Moore-Carrasco R, Busquets S, Almendro V, et al. The AP-1/NF-kappaB double inhibitor SP100030 can revert muscle wasting during experimental cancer cachexia. Int J Oncol 2007; 30:1239 -1245.
39. Assereto S, Stringara S, Sotgia F, et al. Pharmacological rescue of the dystrophin-glycoprotein complex in Duchenne and Becker skeletal muscle explants by proteasome inhibitor treatment. Am J Physiol Cell Physiol 2006;290:C577 -C582.
40. Jatoi A, AlbertsSR, FosterN, etal. Isbortezomib, aproteasomeinhibitor, effective in treating cancer-associated weight loss? Preliminary results from the North Central Cancer Treatment Group. Support Care Cancer 2005; 13:381-386.