Protein nitration is associated with increased proteolysis in skeletal muscle of bile duct ligation-induced cirrhotic rats

Metabolism: Clinical and Experimental

Volumn 59, Issue 4, 2010, Pages 468-472

  Wang, Ya Yu ^a,b   Lin, Shih Yi ^a,c   Chuang, Yu Han ^a   Mao, Chia Hung ^b   Tung, Kwong Chung ^b   Sheu, Wayne Huey Herng ^a,c  

^a TAICHUNG VETERANS GENERAL HOSPITAL   (Taiwan)

^b NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^c NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE REDUCTASE; MUSCLE PROTEIN; MYOSIN HEAVY CHAIN; N(G) NITROARGININE METHYL ESTER; NITRATE; NITRIC OXIDE; NITRITE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BILE DUCT LIGATION; CONTROLLED STUDY; LIVER CIRRHOSIS; MALE; MUSCLE ATROPHY; NITRATION; NITROSATIVE STRESS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN MODIFICATION; RAT; SKELETAL MUSCLE; UBIQUITINATION;

ANIMALS; BILE DUCTS; GLUTATHIONE; LIGATION; LIVER CIRRHOSIS, EXPERIMENTAL; MALE; MUSCLE PROTEINS; MUSCLE, SKELETAL; MYOSIN HEAVY CHAINS; NITRATES; NITRIC OXIDE; NITRITES; RATS; RATS, SPRAGUE-DAWLEY; UBIQUITINATION;

EID: 77949434456     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.metabol.2009.07.035     Document Type: Article

References (30)

1. Wiest R., and Groszmann R.J. The paradox of nitric oxide in cirrhosis and protal hypertension: too much, not enough. Hepatology 35 (2002) 478-491
2. Adams V., Wu J., Mobis-Winkler S., Linke A., Weigl C., Hilbrich L., et al. Increased inducible nitric oxide synthase in skeletal muscle with chronic heart failure. Biochem Mol Med 61 (1997) 152-160
3. Hussain S.N. Respiratory muscle dysfunction in sepsis. Mol Cell Biochem 179 (1998) 123-134
4. Hambrecht H., Adams V., Gielen S., Linke A., Möbius-Winkler S., Yu J., et al. Exercise intolerance in patients with chronic heart failure and increased expression of inducible nitric oxide synthase in skeletal muscle. J Am Coll Cardiol 33 (1999) 174-179
5. Agusti A., Morla M., Sauleda J., Saus C., and Busquets X. NF-κB activation and iNOS upregulation in skeletal muscle of patients with COPD and low body weight. Thorax 59 (2004) 483-487
6. Vassilakopoulos T., and Hussian S.N. Ventilatory muscle activation and inflammation: cytokines, reactive oxygen species, and nitric oxide. J Appl Physiol 102 (2007) 1087-1095
7. Tidball J.G., and Wehling-Henricks M. The role of free radicals in the pathophysiology of muscular dystrophy. J Appl Physiol 102 (2007) 1677-1686
8. Moylan J.S., and Reid M.B. Oxidative stress, chronic disease and muscle wasting. Muscle Nerve 35 (2007) 411-429
9. McCullough A.J., and Bugianesi E. Protein-calorie malnutrition and the etiology of cirrhosis. Am J Gastroenterol 92 (1997) 734-738
10. Muller M.J. Malnutrition in cirrhosis. J Hepatol 23 Suppl 1 (1995) 31-35
11. Crawford D.H.G., Shepherd R.W., Halliday J.W., Cooksley G.W., Golding S.D., Cheng W.S., et al. Body composition in nonalcoholic cirrhosis: the effect of disease etiology and severity on nutrition compartments. Gastroenterology 106 (1994) 1611-1617
12. Lin S.Y., Chen W.Y., Lee F.Y., Huang C.J., and Sheu W.H.H. Activation of ubiquitin-proteasome pathway in skeletal muscle of rats with bile duct ligation-induced liver cirrhosis. Am J Physiol Endocrinol Metab 288 (2005) E493-E501
13. Fernandez M., Pizcueta P., Garcia-Pagan J.C., Feu F., Cirera I., Bosch J., et al. Effects of ritanserin, a selective and specific S2-serotoninergic antagonist, on portal pressure and splanchnic hemodynamics in rats with long-term bile duct ligation. Hepatology 18 (1993) 389-393
14. Liu H., Ma Z., and Lee S.S. Contribution of nitric oxide to the pathogenesis of cirrhotic cardiomyopathy in bile duct-ligated rats. Gastroenterology 118 (2000) 937-944
15. Ball R.D., Krus D.L., and Alizadeh B. Myosin degradation fragments in skeletal muscle. J Mol Bio 193 (1987) 47-56
16. Balabanli{dotless} B., Kamisaki Y., Martin E., and Murad F. Requirements for heme and thiols for the nonenzymatic modification of nitrotyrosine. Proc Natl Acad Sci USA 96 (1999) 13136-13141
17. Pacher P., Beckman J.S., and Liaudet L. Nitric oxide in health disease. Physiol Rev 87 (2007) 315-424
18. Szabo C., Ischiropoulous H., and Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov 6 (2007) 626-680
19. Gow A.J., Farkouh C.R., Munson D.A., Posencheg M.A., and Ischiropoulos H. Biological significance of nitric-oxide mediated protein modifications. Am J Physiol 287 (2004) L262-L268
20. Grune T., Blasig I.E., Sitte N., Roloff B., Haseloff R., and Davies K.J.A. Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome. J Biol Chem 273 (1998) 10857-10862
21. Barreiro E., la Puente B., Busquets S., López-Soriano F.J., Gea J., and Argilés J.M. Both oxidative and nitrosative stress are associated with muscle wasting in tumour-bearing rats. FESB Lett 579 (2005) 1646-1652
22. Buck M., and Chojkier M. Muscle wasting and differentiation induced by oxidative stress in a model of cachexia prevented by inhibitors of nitric oxide synthesis and antioxidants. EMBO 15 (1996) 1753-1765
23. Bar-Shai M., and Reznick A.Z. Reactive nitrogen species induce nuclear factor-κB-mediated protein degradation in skeletal muscle cells. Free Radic Biol Med 40 (2006) 2112-2125
24. Clark K.A., McElhinny A.S., Beckerle M.C., and Gregorio C.C. Striated muscle cytoarchitecture: an intricate web of form and function. Ann Rev Cell Dev Biol 18 (2002) 636-706
25. Ikemoto M., Nikawa T., Takeda S., Watanabe C., Kitano T., Baldwin K.M., et al. Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway. FASEB J 15 (2001) 1279-1281
26. Schulze P.C., Fang J., Kassik K.A., Gannon J., Cupesi M., MacGillivray C., et al. Transgenic overexpression of locally acting insulin-like growth factor-1 inhibits ubiquitin-mediated muscle atrophy in chronic left-ventricular dysfunction. Circ Res 97 (2005) 418-426
27. Acharyya S., Ladner K.J., Nelsen L.L., Damrauer J., Reiser P.J., Swoap S., et al. Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J Clin Invest 114 (2004) 370-378
28. Solomon V., and Goldberg A.L. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biol Chem 271 (1996) 26690-26697
29. Tawa Jr. N.E., Odessey R., and Goldberg A.L. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest 100 (1997) 197-203
30. Wei C.L., Hon W.M., and Lee K.H. Chronic administration of aminoguanidine reduces vascular nitric oxide production and attenuates liver damage in bile duct-ligated rats. Liver Int 25 (2005) 647-656