Skeletal muscle myocytes undergo protein loss and reactive oxygen- mediated NF-κB activation in response to tumor necrosis factor α

FASEB Journal

Volumn 12, Issue 10, 1998, Pages 871-880

  Li, Yi Ping ^a   Schwartz, Robert J ^a   Waddell, Ian D ^b   Holloway, Brian R ^b   Reid, Michael B ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b ASTRAZENECA   (United Kingdom)

Author keywords

Cachexia; Cytokines; Free radicals; Inflammatory disease; Myosin; Tumor necrosis factor; Ubiquitin

Indexed keywords

CATALASE; CYTOKINE; FREE RADICAL; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MYOSIN; MYOSIN HEAVY CHAIN; PROTEASOME; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CACHEXIA; DNA CONTENT; DNA SEQUENCE; INFLAMMATORY DISEASE; MOUSE; MUSCLE CELL; MYOTUBE; NEWBORN; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPLETION; RAT; SIGNAL TRANSDUCTION; SKELETAL MUSCLE;

ANIMALIA;

EID: 0031802331     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.10.971     Document Type: Article

References (64)

1. Espat, N. J., Copeland, E. M., and Moldawer, L. L. (1994) Tumor necrosis factor and cachexia: a current perspective. Surg. Oncol. 3, 253-262
2. Vreugdenhil, G., Lowenberg, B., VanEijk, H. G., and Swaak, J. G. (1992) Tumor necrosis factor-α is associated with disease activity and the degree of anemia in patients with rheumatoid arthritis. Eur. J. Clin. Invest. 22, 488-493
3. Nakashima, J., Tachibana, M., Ueno, M., Baba, S., and Tazaki, H. (1995) Tumor necrosis factor and coagulapathy in patient with prostate cancer. Cancer Res. 55, 4881-4885
4. Buck, M., and Chojkier, M. (1996) Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants. EMRO J. 15, 1753-1765
5. Garcia-Martinez, C., Lopez-Soriano, F. J., and Argiles, J. M. (1993) Acute treatment with tumour necrosis factor-α induces changes in protein metabolism in rat skeletal muscle. Mol. Cell. Biochem. 125, 11-18
6. Cheng, J., Turksen, K., Yu, Q., Schreiber, H., Teng, M., and Fuchs, E. (1992) Cachexia and graft-vs-host-disease-type skin changes in keratin promoter-driven TNF-α transgenic mice. Genes &Dev. 6, 1444-1456
7. Ahmad, S., Karlstad, M. D., Choudhry, M. A., and Sayeed, M. M. (1994) Sepsis-induced myofibrillar protein catabolism in rat skeletal muscle. Life Sci. 55, 1383-1391
8. Tessitore, L., Costelli, P., and Baccino, F. M. (1993) Humoral mediation for cachexia in tumour-bearing rats. Br. J. Cancer 67, 15-23
9. Lawson, D. H., Richmond, A., Nixon, D. W., and Rudman, D. (1982) Metabolic approach to cancer cachexia. Annu. Rev. Nutr. 2, 277-301
10. Morrison, S. D. (1989) Cancer cachexia. In Influence of Tumor Development on the Host (Liotta, A. L., ed) pp. 176-213, Kluwer Academic Publishers, Amsterdam
11. Mealy, K., van Lanschott, J. J., Robinson, B. G., Rounds, J., and Wilmore, D. W. (1990) Are the catabolic effects of tumor necrosis factor mediated by glucocorticoids? Arch. Surg. 125, 42-48
12. 2 production by human synovial cells and dermal fibroblasts. J. Exp. Med. 162, 2163-2168
13. Gelin, J., Moldawer, L. L., Lonnroth, C., Sherry, C., Chizzonite, T., and Lundholm, K. (1991) Role of endogenous tumor necrosis factor-α and nuerleukin-1 for experimental tumor growth and the development of cancer cachexia. Cancer Res. 51, 415-421
14. Michie, H. R., Sherman, M. L., Spriggs, D. R., Rounds, J., Christie, M., and Wilmore, D. W. (1989) Chronic TNF infusion causes anorexia but not acceleratt-d nitrogen loss. Ann. Surg. 209, 19-24
15. Socher, S. H., Freidman, A., and Martinez, D. (1988) Recombinant tumor necrosis factor induces acute reductions in food intake and body weight in mice. J. Exp. Med. 167, 1957-1962
16. 2 production in rat skeletal muscle in fever is signaled by a macrophage product distinct from interleukin-1 or other known monokines. J. Clin. Invest. 81, 1378-1383
17. Goodman, M. N. (1991) Tumor necrosis factor induces skeletal muscle protein breakdown in rats. Am. J. Physiol. 260, E727-E730
18. Rofe, A. M., Conyers, R. A. J., Bais, R., Gamble, J. R., and Vadas, M. A. (1987) The effects of recombinant tumour necrosis factor (cachectin) on metabolism in isolated rat adipocyte, hepatocyte and muscle preparations. Biochem. J. 247, 789-792
19. Llovera, M., Garcia-Martinet, C., Lopez-Soriano, F. J., and Argiles, J. M. (1997) TNF can directly induce the expression of ubiquitin-dependent proteolytic system in rat soleus muscles. Biochem. Biophys. Res. Commun. 230, 238-241
20. Schutze, S., Machleidt, T., and Kronke, M. (1992) Mechanisms of tumor necrosis factor action. Semin. Oncol. 2, 16-24
21. Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-785
22. Chen, Z., Hagler, J., Palombella, V. J., Melandri, F., Scherer, D., Ballard, D., and Maniatis, T. (1995) Signal-induced site-specific phosphorylation targets I-κBα to the ubiquitin-proteasome pathway. Genes & Dev. 9, 1586-1597
23. Schulze-Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., and Fiers, W. (1992) Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial function. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267, 5317-5323
24. Hennet, T., Richter, C., and Peterhans, E. (1993) Tumour necrosis factor-α induces superoxide anion generation in mitochondria of L929 cells. Biochem. J. 289, 587-592
25. Flohe, L., Brigelius-Flohe, R., Saliou, C., Traber, M. G., and Packer, L. (1997) Redox regulation of NF-κB activation. Free Radical Biol. Med. 22, 1115-1126
26. Brennan, P., and O'Neill, L. (1995) Effects of oxidants and antioxidants on nuclear factor κB activation in three different cell lines: Evidence against a universal hypothesis involving oxygen radicals. Biochem. Biophys. Acta 1260, 167-175
27. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275
28. Li, Y.-P., Baskin, F., Davis, R., Wu, D., and Hersh, L. B. (1995) A cell type-specific silencer in the human choline acetyltransferase gene requiring two distinct and interactive E boxes. Mol. Brain Res. 30, 106-114
29. Zar, J. H. (1974) Biostatistical Analysis, Prentice-Hall, Inc., Engelwood Cliffs, N.J
30. Rock, K. L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., and Goldberg, A. L. (1994) Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-771
31. Beckman, J. S., and Freeman, B. A. (1986) Antioxidant enzymes as mechanistic probes of oxygen-dependent toxicity. In Physiology of Oxygen Radicals (Taylor, A. E., Matalon, S., and Ward, P. A., eds) pp. 39-53, American Physiological Society, Bethesda, Maryland
32. Reid, M. B., Haack, K. E., Franchek, K M., Valberg, P. A., Kobzik, L., and West, M. S. (1992) Reactive oxygen in skeletal muscle: I. Intracellular oxidant kinetics and fatigue in vitro. J. Appl. Physiol. 73, 1797-1804
33. Beutler, B., Mahoney, J., LeTrang, N., Pekala, P., and Cerami, A. (1985) Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced Raw264.7 cells. J. Exp. Med. 161, 984-995
34. Beutler, B., and Cerami, A. (1986) Cachectin and tumor necrosis factor as two sides of the same biological coin. Nature (London) 320, 584-588
35. Hsu, H., Shu, H.-B., Pan, M.-G., and Goeddel, D. V. (1996) TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84, 299-308
36. Liu, Z.-G., Hsu, H., Goeddel, D. V., and Karin, M. (1996) Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell 87, 565-576
37. Barnes, P. J., and Karin, M. (1997) Nuclear factor-κB - a pivotal transcription factor in chronic inflammatory disease. New Engl. J. Med. 336, 1066-1071
38. Sen, R., and Baltimore, D. (1986) Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46, 705-716
39. Siebenlist, U., Franzoso, G., and Brown, K. (1994) Structure, regulation, and function of NF-κB. Annu. Rev. Cell Biol. 10, 405-455
40. Baeuerle, P. A., and Baltimore, D. (1996) NF-κB: ten years after. Cell 87, 13-20
41. Beg, A. A., Finco, T. S., Nantermet, P. V., and Baldwin, A. S., Jr. (1993) Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of I-κBα: a mechanism for NF-κB activation. Mol. Cell. Biol. 13, 3301-3310
42. Gareia-Martinez, C., Agell, N., Llovera, M., Lopez-Soriano, F. J., and Argiles, J. M. (1993) Tumour necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins. FEBS Lett. 323, 211-214
43. Garcia-Martinez, C., Llovera, M., Agell, N., Lopez-Soriano, F. J., and Argiles, J. M. (1994) Ubiquitin gene expression in skeletal muscle is increased by tumour necrosis factor-α. Biochem. Biophys. Res. Commun. 201, 682-686
44. Garcia-Martinez, C., Llovera, M., Agell, N., Lopez-Soriano, F. J., and Argiles, J. M. (1995) Ubiquitin gene expession in skeletal muscle is increased during sepsis: involvement of TNF-α but not IL-1. Biochm, Biophys. Res. Commun. 217, 839-844
45. Llovera, M., Carbo, N., Garcia-Martinez., C., Costelli, P., Tessitore, L., Baccino, F. M., Agell, N., Bagby, G. J., Lopez-Soriano, F. J., and Argiles, J. M. (1996) Anti-TNF treatment reverts increased muscle ubiquitin gene expression in tumour-bearing rats. Biochem. Biophys. Res. Commun. 221, 653-655
46. Tawa, N. E., Odessey, R., and Goldberg, A. L. (1997) Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscle. J. Clin. Invest. 100, 197-203
47. Mitch, W. E., and Goldberg, A. L. (1996) Mechanisms of muscle wasting; the role of the ubiquitin-protcasome pathway. New Engl. J. Med. 335, 1897-1905
48. Hochstrasser, M. (1995) Ubiquitin, protensomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223
49. Sen, C. K., Khanna, S., Resznick, A. Z., Roy, S., and Packer, L. (1997) Glutathione regulation of tumor necrosis factorα-induced NF-κB activation in skeletal muscle-derived L6 cells. Biochem. Biophys. Res. Commun. 237, 645-649
50. Reid, M. B., Shoji, T., Moody, M. R., and Entman, M. L. (1992) Reactive oxygen in skeletal muscle: II. Extracellular release of free radicals. J. Appl. Physiol. 73, 1805-1809
51. Reid, M. B., Khawli, F. A., and Moody, M. R. (1993) Reactive oxygen in skeletal muscle: III. Contractility of unfatigued muscle. J. Appl. Physiol. 75, 1081-1087
52. Reid, M. B. (1996) Reactive oxygen and nitric oxide in skeletal muscle. News Physiol. Sci. 11, 114-119
53. Sen, C. K., and Packer, L. (1996) Antioxidant and redox regulation of gene transcription. FASEB J. 10, 709-720
54. Demple, B., and Amabile-Cuevas, C. F. (1991) Redox redux: the control of oxidative stress responses. Cell 67, 837-839
55. Meyer, M., Schreck, R., Muller, J. M., and Baeuerle, P. A. (1994) Redox control of gene expression by eukaryotic transcription factors NF-κB, AP-1 and SRF/TCF. In Oxidative Stress, Cell Activation and Viral Infection (Pasquier, C., Olivier, R. Y., Auclair, C., and Packer, L., eds) pp. 217-235, Birkhauser Verlag, Basel, Switzerland
56. Kretz-Remy, C., Mehlen, P., Mirault, M.-E., and Arrigo, A.-P. (1996) Inhibition of I-κBα phosphorylation and degradation and subsequent NF-κB activation by glutathione peroxidase over-expression. J. Cell Biol. 133, 1083-1093
57. Schreck, R., Rieber, P., and Baeuerle, P. A. (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10, 2247-2258
58. Schmidt, K. N., Traenckner, E. B., Meier, B., and Baeuerle, P. A. (1995) Induction of oxidative stress by okadaic acid is required for activation of transcription factor NF-κB. J. Biol. Chem. 10, 27136-27142
59. Sappey, C., Legrand-Poels, S., Best-Belpomme, M., Favier, A., Rentier, B., and Piette, J. (1994) Stimulation of glutathione peroxidase activity decreases HIV type activation after oxidative stress. AIDS Res. Hum. Retroviruses 10, 1451-1461
60. Makropoulos, V., Bruening, T., and Schultze-Osthoff, K. (1996) Selenium-mediated inhibition of transcription factor NF-κB and HIV-1 LTR promoter activity. Arch. Toxicol. 70, 277-283
61. Israel, N., Gougerot-Pocidalo, M. A., Aillet, F., and Virelizier, J. L. (1992) NF-κB translation and HIV long terminal repeat activity in human T and mohocytic cell lines. J. Immunol. 149, 3386-3393
62. Shindoh, C., Hida, W., Qhkawara, Y., Yamuchi, K., Ohno, I., Takashima, T., and Shirato, K. (1995) TNF-α mRNA expression in diaphragm muscle after endotoxin administration. Am. J. Resp. Crit. Care Med. 152, 1690-1691
63. Supinski, G., Nethery, D., and Dimarco, A. (1993) Effect of free radical scavengers on endotoxin-induced respiratory muscle dysfunction. Am. Rev. Resp. Dis. 148, 1318-1324
64. Shindoh, C., Dimarco, A., Nethery, D., and Supinski, G. (1992) Effect of PEG-superoxide disniutase on the diaphragmatic response to endotoxin. Am. Rev. Resp. Dis. 145, 1350-1354