The relationship between skeletal muscle proteolysis and ubiquitin-proteasome proteolytic pathway in burned rats

Burns

Volumn 28, Issue 6, 2002, Pages 527-533

  Chai, Jiake ^a   Wu, Yanqiu ^a   Sheng, Zhiyong ^a  

^a 304TH HOSPITAL   (China)

Author keywords

Burn injury; Proteolysis; Rat; Skeletal muscle; Ubiquitin proteasome pathway

Indexed keywords

MESSENGER RNA; PROTEASOME; PROTEIN SUBUNIT; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BURN; CONTROLLED STUDY; CORRELATION ANALYSIS; ENZYME SUBUNIT; EXTENSOR DIGITORUM LONGUS MUSCLE; GENE EXPRESSION REGULATION; MALE; MUSCLE ATROPHY; MUSCLE FIBRIL; NONHUMAN; PROTEIN DEGRADATION; PROTEIN FUNCTION; RAT; RNA ANALYSIS; SKELETAL MUSCLE; SOLEUS MUSCLE;

ANIMALS; BLOOD PROTEINS; BURNS; CYSTEINE ENDOPEPTIDASES; MALE; MULTIENZYME COMPLEXES; MUSCLE, SKELETAL; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; RATS; RATS, WISTAR; RNA, MESSENGER; UBIQUITIN;

EID: 0036768523     PISSN: 03054179     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-4179(02)00049-9     Document Type: Article

References (35)

1. Schoenheimer R, Dynamic state of body constituents. Cambridge, MA: Harvard University Press, 1942. p. 17-9.
2. Kettelhut I.C., Wing S.S., Goldberg A.L. Endocrine regulation of protein breakdown in skeletal muscle. Diabetes Metab. Rev. 8:1988;751-772.
3. Lowell B.B., Ruderman N.B., Goodman M.N.et al. Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochem. J. 234(2):1986;237-240.
4. Goll D.E., Thompson V.F., Christiansen J.A. Role of calpain system in muscle growth. Biochimie. 74(3):1992;225-237.
5. Baracos V.E., Devivo C., Hoyle H.R.et al. Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. Am. J. Physiol. 25768:1995;E996-E1006.
6. Wing S.S., Goldberg A.L. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264:1993;E668-E676.
7. Medina R., Wing S.S., Goldberg A.L. Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem. J. 307:1995;631-637.
8. Medina R., Wing S.S., Haas A.et al. Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed. Biochim. Acta. 50:1991;347-356.
9. Furuno K., Goodman M.N., Goldberg A.L. Role of different proteolytic pathway in the degradation of muscle proteins during denervation atrophy. J. Biol. Chem. 265:1990;8550-8557.
10. Mitch W.E., Medina R., Grieber S.et al. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasome. J. Clin. Invest. 93:1994;2127-2133.
11. Tiao G., Fagan J.M., Samuels N.et al. Sepsis stimulates non-lysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94:1994;2255-2264.
12. 2+-activated, and ubiquitin-proteasome proteolytic pathway. J. Clin. Invest. 97:1996;1610-1617.
13. Chai J., Wu Y., Sheng Z. Effects of sepsis on proteolytic rate of different kinds of skeletal muscle in rats and investigation of its possible mechanism. Chin. Crit. Care Med. 13(5):2001;272-274.
14. Fang C.-H., Tiao G., James J.H.et al. Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway. J. Am. Coll. Surg. 180:1995;161-170.
15. Horst K., Mendel L.B., Benedict F.G. The metabolism of the albino rat during prolonged fasting at two different environmental temperature. J. Nutr. 3:1930;177-200.
16. Chomczynsky P., Sacchi N. Single-step method of RNA isolation by acid guanidinium isothiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
17. Wing S.S., Banville D. 14-kDa E2: structure of rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267:1994;39-48.
18. Kathy K., Sonja R., Harry F.A.et al. Suppression of proteasome C2 contralateral to the ischemic lesions in rat brain. Brain Res. 858:2000;386-392.
19. Liu S.F., Barnes P.J., Evans T.W.et al. Lipopolysaccharide treatment in vivo induces widespread tissue expression of inducible nitro oxide synthase mRNA. Biochem. Biophys. Res. Commun. 196:1993;1208-1213.
20. Hall-Angeras M., Angeras U.D., von Allmen T.et al. Influence of sepsis in rats on muscle protein turnover in vivo and in tissue incubated under different in vitro conditions. Metab. Clin. Exp. 40:1991;247-251.
21. Baracos V.E., Goldberg A.L. Maintenance of normal length improves protein balance and energy status in isolated rat skeletal muscle. Am. J. Physiol. 251:1986;C588-C596.
22. Young V.R., Munro H.N. N τ-methyhistidine(3-methyhistidine) and muscle protein turnover: an overview. Fed. Proc. 37:1978;2291-2300.
23. Maltin C.A., Delday M.I., Baillie A.G.et al. Fiber type composition in nine rat muscle. Am. J. Physiol. 257:1989;E823-E826.
24. Ciechanover A., Orian A., Schwartz A.L. The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications. J. Cell. Biochem. 34((s)):2000;40-51.
25. Wu Y., Chai J., Sheng Z. Study on the changes in expression of ubiquitin mRNA in skeletal muscle in burned rats. Chin. Crit. Care Med. 13(7):2001;423-426.
26. Haas A.L., Rose L.A. The mechanism of ubiquitin activating enzyme. J. Biol. Chem. 257:1982;10329-10337.
27. Pichart C.M., Rose I.A. Functional heterogeneity of ubiquitin carrier proteins. J. Biol. Chem. 260:1985;1573-1581.
28. Wing S.S., Banville D. 14-kDa E2: structure of rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267:1994;39-48.
29. Kisselev A.F., Akopian T.N., Goldberg A.L. Ranges of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J. Biol. Chem. 273:1998;1982-1989.
30. Kania M.A., Demartino G.N., Baumeister W.et al. The proteasome subunit C2 contains an important site for binding of PA28 (11S) activator. Eur. J. Biochem. 236:1996;510-516.
31. Shimbara N., Orino E., Sone S.et al. Regulation of gene expression of proteasomes (multi-protease complex) during growth and differentiation of human hematopoietic cells. J. Biol. Chem. 267:1992;18100-18109.
32. Grune T., Davies K.J. Breakdown of oxidized protein as a part of secondary antioxidant defenses in mammalian cells. Biofactors. 6:1997;165-172.
33. Tawa N.E., Odessey R., Goldberg A.L. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscle. J. Clin. Invest. 100:1997;197-203.
34. Hobler S.C., Tiao G., Fisher J.E.et al. Sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors. Am. J. Physiol. 274:1998;R30-R37.
35. Hershko A., Ciechanover A. The ubiquitin system. Annu. Rev. Biochem. 67:1998;425-479.