Mechanism of attenuation of protein loss in murine C2C12 myotubes by d-myo-inositol 1,2,6-triphosphate

Experimental Cell Research

Volumn 316, Issue 2, 2010, Pages 286-295

  Russell, Steven T ^a   Siren, Pontus M A ^b   Siren, Matti J ^c   Tisdale, Michael J ^a  

^a ASTON UNIVERSITY   (United Kingdom)

^b IAM   (Sweden)

^c JGK Memorial Research Library and Laboratory   (Finland)

Author keywords

Alpha trinositol; Protein degradation; Protein kinase R; Protein synthesis; Zinc

Indexed keywords

ANGIOTENSIN II; CASPASE 3; CASPASE 8; GAMMA INTERFERON; INITIATION FACTOR 2; INOSITOL 1,2,6 TRISPHOSPHATE; LIPOPOLYSACCHARIDE; METAL ION; PROTEASOME; PROTEIN KINASE R; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN; ZINC ION;

ALPHA CHAIN; ANIMAL TISSUE; ARTICLE; AUTOPHOSPHORYLATION; CACHEXIA; CATABOLISM; CHELATION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; MOUSE; MUSCLE ATROPHY; MYOTUBE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; SIGNAL TRANSDUCTION;

EUKARYOTA; MURINAE;

EID: 70450285095     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2009.08.013     Document Type: Article

References (31)

1. Tan H.L., and Fearon K.C.H. Cachexia: prevalence and impact in medicine. Curr. Opin. Clin. Nutr. Metab. Care 11 (2008) 400-407
2. Cariuk P., Lorite M.J., Todorov P.T., Field W.N., Wigmore S.J., and Tisdale M.J. Induction of cachexia in mice by a produce isolated from the urine of cachectic cancer patients. Br. J. Cancer 76 (1997) 606-613
3. Brink M., Wellen J., and Delafontaine P. Angiotensin II causes weight loss and decreases circulating insulin-like growth factor 1 in rats through a pressor-independent mechanism. J. Clin. Invest. 97 (1996) 2509-2516
4. Llovera M., Lopez-Soriano F.J., and Argiles J.M. Effects of tumor necrosis factor-α on protein turnover in female Wistar rats. J. Natl. Cancer Inst. 85 (1993) 1334-1339
5. Dehoux M.J., van Beneden R.P., Gernandez-Clemin L., Lause P.L., and Thissen J.P. Induction of Mafbx and Murf ubiquitin ligase mRNAs in rat skeletal muscle after LPS injection. FEBS Lett. 544 (2003) 214-217
6. Eley H.L., and Tisdale M.J. Skeletal muscle atrophy, a link between depression of protein synthesis and increase in degradation. J. Biol. Chem. 282 (2007) 7087-7097
7. Eley H.L., Russell S.T., and Tisdale M.J. Attenuation of depression of muscle protein synthesis induced by lipopolysaccharide, tumor necrosis factor and angiotensin II by β-hydroxy-β-methylbutyrate. Am. J. Physiol. 295 (2008) E1409-E1416
8. Rowlands A.G., Panniers R., and Henshaw E.C. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263 (1998) 5526-5533
9. Carlberg U., Nisson A., and Nygard O. Functional properties of phosphorylated elongation factor 2. Eur. J. Biochem. 191 (1990) 639-645
10. Lecker S.H., Solomon V., Mitch W.E., and Goldberg A.L. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 129 (1999) 227S-237S
11. Eley H.L., Russell S.T., and Tisdale M.J. Mechanism of attenuation of muscle protein degradation induced by tumor necrosis factor-α and angiotensin II by β-hydroxy-β-methylbutyrate. Am. J. Physiol. 295 (2008) E1417-E1426
12. Cai D., Frantz J.D., Tawa Jr. N.E., Melendez P.A., Oh B.C., Lidov G.H.W., Hasselgren P.-O., Frontera W.R., Lee J., Glass D.J., and Shoelson S.E. IKKβ/NF-κB activation causes severe muscle wasting in mice. Cell 119 (2004) 285-298
13. Saelens X., Kalai M., and Vandenabeele P. Translation inhibition in apoptosis. Caspase-dependent PKR activation and eIF2α phosphorylation. J. Biol. Chem. 276 (2001) 41620-41628
14. Russell S.T., Siren P.M.A., Siren M.J., and Tisdale M.J. Attenuation of skeletal muscle atrophy in cancer cachexia by d-myo-inositol 1, 2, 6-triphosphate. Cancer Chemother. Pharmacol. (2009) 10.1007/s00280-008-0899-z
15. Todorov P.T., McDevitt T.M., Cariuk P., Coles B., Deacon M., and Tisdale M.J. Induction of muscle protein degradation and weight loss by a tumour product. Cancer Res. 56 (1996) 1256-1261
16. Orino E., Tanaka K., Tamura T., Sone S., Ogura T., and Ichihara A. ATP-dependent reversible association of proteasomes with multiple protein components to form 26S complexes that degrade ubiquitinated proteins in human HL-60 cells. FEBS Lett. 284 (1991) 206-210
17. Whitehouse A.S., and Tisdale M.J. Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-κB. Br. J. Cancer 89 (2003) 1116-1122
18. Li Y.-P., Schwartz R.J., Waddell I.D., Holloway B.R., and Reid M.B. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-κB activation in response to tumor-necrosis factor α. FASEB J. 12 (1998) 871-880
19. Russell S.T., Eley H.L., and Tisdale M.J. Role of reactive oxygen species in protein degradation in murine myotubes induced by proteolysis-inducing factor and angiotensin II. Cell. Signal. 19 (2007) 1797-1806
20. Andrews N.C., and Faller D.V. A rapid micropreparation technique for extraction of DNA-binding proteins from limited numbers of mammalian cells. Nucleic Acid Res. 19 (1991) 2499
21. Acharyya S., Ladner K.J., Nelsen L.L., Damrauer J., Reiser P.J., Swoap S., and Guttridge D.C. Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J. Clin. Invest. 114 (2004) 370-378
22. 12 myotubes. Br. J. Cancer 90 (2004) 1850-1857
23. Wyke S.M., and Tisdale M.J. NF-κB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle. Br. J. Cancer 92 (2005) 711-721
24. 2+ system in solution. J. Inorg. Biochem. 84 (2001) 107-111
25. Suen K.-C., Yu M.-S., So K.-F., Chang R.C.-C., and Hugon J. Upstream signaling pathways leading to the activation of double-stranded RNA-dependent serine/threonine protein kinase in β-amyloid peptide neurotoxicity. J. Biol. Chem. 278 (2003) 49819-49827
26. Juin P., Pelletier M., Oliver L., Tremblasis K., Gregoire M., Meflah K., and Vallette F.M. Induction of caspase-3-like activity by calcium in normal cytosolic extracts triggers nuclear apoptosis in a cell-free system. J. Biol. Chem. 273 (1998) 17559-17564
27. Prostko C.R., Dholakia J.N., Brostrom M.A., and Brostrom C.O. Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores. J. Biol. Chem. 270 (1995) 6211-6215
28. 2+ and regulates ion transport. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 11749-11754
29. Dubi N., Gheber L., Fishman D., Sekler I., and Hershfinkel M. Extracellular zinc and zinc-citrate, acting through a putative zinc-sensing receptor regulate growth and survival of prostate cancer cells. Carinogenesis 29 (2008) 1692-1700
30. Smith H.J., and Tisdale M.J. Signal transduction pathways involved in proteolysis-inducing factor induced proteasome expression in murine myotubes. Br. J. Cancer 89 (2003) 1783-1788
31. Russell S.T., Wyke S.M., and Tisdale M.J. Mechanism of induction of muscle protein degradation by angiotensin II. Cell. Signal. 18 (2006) 1087-1096