Effect of a cancer cachectic factor on protein synthesis/degradation in murine C2C12 myoblasts: Modulation by eicosapentaenoic acid

Cancer Research

Volumn 59, Issue 21, 1999, Pages 5507-5513

  Smith, Helen J ^a   Lorite, Maria J ^a   Tisdale, Michael J ^a  

^a ASTON UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; ICOSANOID; ICOSAPENTAENOIC ACID; INSULIN; MONOCLONAL ANTIBODY; PROSTAGLANDIN E2;

ANIMAL CELL; ARTICLE; CACHEXIA; CONTROLLED STUDY; MOUSE; MUSCLE TUMOR; MYOBLAST; NONHUMAN; PRIORITY JOURNAL; PROSTAGLANDIN RELEASE; PROTEIN DEGRADATION; PROTEIN SYNTHESIS INHIBITION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

ANIMALS; ARACHIDONIC ACID; BLOOD PROTEINS; CELL LINE; DOSE-RESPONSE RELATIONSHIP, DRUG; EICOSAPENTAENOIC ACID; HYDROXYEICOSATETRAENOIC ACIDS; INSULIN; MICE; MUSCLE, SKELETAL; PROTEIN SYNTHESIS INHIBITORS; PROTEINS;

EID: 0033229932     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Fearon, K. C., and Preston, T. Body composition in cancer cachexia. Infusionstherapie, 17 (Suppl. 3): 63-66, 1990.
2. Llovera, M., Lopez-Soriano, F. J., and Argile's, J. M. Effects of tumor necrosis factor-α on muscle protein turnover in female Wistar rats. J. Natl. Cancer Inst., 85: 1334-1339, 1993.
3. Bistrian, B. R., Schwartz, J., and Istfan, N. W. Cytokines, muscle proteolysis and the catabolic response to infection and inflammation. Proc. Soc. Exp. Biol. Med., 200: 220-223, 1992.
4. Espat, N. J., Auffenberg, T., Rosenberg, J. J., Martin, R. D., Fang, C. H., Hasselgren, P. O., Copeland, E. M., and Moldawer, L. L. Ciliary neurotrophic factor is catabolic and shares with IL-6 the capacity to induce an acute phase response. Am. J. Physiol., 271: R185-R190, 1996.
5. Todorov, P., Cariuk, P., McDevitt, T., Coles, B., Fearon, K., and Tisdale, M. Characterization of a cancer cachectic factor. Nature (Lond.), 379: 739-742, 1996.
6. Todorov, P. T., Deacon, M., and Tisdale, M. J. Structural analysis of a tumor-produced sulfated glycoprotein capable of initiating muscle protein degradation. J. Biol. Chem., 272: 12279-12288, 1997.
7. 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 product isolated from the urine of cachectic cancer patients. Br. J. Cancer, 76: 606-613, 1997.
8. Beck, S. A., Smith, K. L., and Tisdale, M. J. Anticachectic and antitumor effect of eicosapentaenoic acid and its effect on protein turnover. Cancer Res., 51: 6089-6093, 1991.
9. Lorite, M. J., Cariuk, P., and Tisdale, M. J. Induction of muscle protein degradation by a tumour factor. Br. J. Cancer, 76: 1035-1040, 1997.
10. Yaffe, D., and Saxel, O. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature (Lond.), 270: 725-727, 1977.
11. Brienetti, A., Maddux, B. A., Wong, K. Y., and Goldfine, I. D. Muscle cell differentiation is associated with increased insulin receptor biosynthesis and mRNA levels. J. Clin. Investig., 83: 192-198, 1989.
12. 2 block the stimulation of protein synthesis by insulin in L6 myoblasts. Biochem. J., 270: 737-739, 1990.
13. Hussey, H. J., and Tisdale, M. J. Mechanism of the anti-tumour effect of 2,3,5-trimethyl-6-(3-pyridylmethyl)1,4-benzoquinone (CV-6504). Br. J. Cancer, 75: 845-849, 1997.
14. 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 tumor product. Cancer Res., 56: 1256-1261, 1996.
15. 12 satellite cells-evidence for phospholipase-D-dependent and phospholipase-D-independent pathways. J. Cell. Physiol., 165: 273-283, 1995.
16. Kimball, S. R., and Jefferson, L. S. Mechanism of the inhibition of protein synthesis by vasopressin in rat liver. J. Biol. Chem., 265: 16794-16798, 1990.
17. Smith, K. L., and Tisdale, M. J. Mechanism of muscle protein degradation in cancer cachexia. Br. J. Cancer, 68: 314-318, 1993.
18. De Blaauw, I., Deutz, N. E. P., and von Meyenfeldt, M. F. Metabolic changes in cancer cachexia. Clin. Nutr., 16: 169-176, 1997.
19. 2 release by leukocytic pyrogen (interleukin-1). A mechanism for the increased degradation of muscle proteins during fever. N. Engl. J. Med., 308: 553-558, 1983.
20. Strelkov, A. B., Fields, A. L., and Baracos, V. E. Effects of systemic inhibition of prostaglandin production on protein metabolism in tumor-bearing rats. Am. J. Physiol., 257: C261-C269, 1989.
21. 2α influence rates of protein turnover in skeletal and cardiac muscle. J. Biol. Chem., 257: 1632-1638, 1982.
22. 2 and muscle proteolysis: effect of burn injury and cycloheximide. Am. J. Physiol., 250: R207-R210, 1986.
23. 2 and the regulation of protein degradation in skeletal muscle. Muscle Nerve, 10: 556-559, 1987.
24. 2 does not regulate total or myofibrillar protein breakdown in incubated skeletal muscle from normal or septic rats. Biochem. J., 270: 45-50, 1990.
25. Hussey, H. J., Bibby, M. C., and Tisdale, M. J. Novel anti-tumour activity of 2,3,5-trimethyl-6-(3-pyridylmethyl)-1,4-benzoquinone (CV-6504) against established murine adenocarcinomas (MAC). Br. J. Cancer, 73: 1187-1192, 1996.