Intracellular regulation of protein degradation during sepsis is different in fast- and slow-twitch muscle

American Journal of Physiology - Regulatory Integrative and Comparative Physiology

Volumn 272, Issue 3 41-3, 1997, Pages

  Tiao, Greg ^a,b   Lieberman, Michael ^a   Fischer, Josef E ^a,b   Hasselgren, Per Olof ^a,b,c  

^a UNIVERSITY OF CINCINNATI   (United States)

^b SHRINERS HOSPITALS FOR CHILDREN   (United States)

^c UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

catabolism; energy dependent proteolysis; extensor digitorum longus muscle; soleus muscle; ubiquitin

Indexed keywords

MESSENGER RNA; PROTEIN; UBIQUITIN;

ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CATABOLISM; CONTROLLED STUDY; EXTENSOR DIGITORUM LONGUS MUSCLE; FAST MUSCLE FIBER; GENE EXPRESSION REGULATION; MALE; MUSCLE METABOLISM; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN DEGRADATION; SEPSIS; SLOW MUSCLE FIBER; SOLEUS MUSCLE; TISSUE SPECIFICITY;

EID: 0030951073     PISSN: 03636119     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpregu.1997.272.3.r849     Document Type: Article

References (32)

1. Baracos, V. E., and A. L. Goldberg. Maintenance of normal length improves protein balance and energy status in isolated rat skeletal muscles. Am. J. Physiol. 251 (Cell Physiol. 20): C588-C596, 1986.
2. Bone, R. C. The pathogenesis of sepsis. Ann. Intern. Med. 115: 457-469, 1991.
3. Chaudry, I. H., K. A. Wichterman, and A. E. Baue. Effect of sepsis on tissue adenine nucleotide levels. Surgery 85: 205-211, 1979.
4. Chomczynski, P., and N. Sacchi. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
5. Ciechanover, A. The ubiquitin-proteasome pathway. Cell 79: 13-21, 1994.
6. Dahlmann, B., and L. Kuehn. The 20S/26S proteasomal pathway of protein degradation in muscle tissue. Mol. Biol. Rep. 21: 57-62, 1995.
7. Fagan, J. M., E. F. Wajnberg, L. A. Culbert, and L. Waxman. ATP depletion stimulates calcium-dependent protein breakdown in chick skeletal muscle. Am. J. Physiol. 262 (Endocrinol. Metab. 25): E637-E643, 1992.
8. Fang, C. H., J. H. James, C. K. Ogle, J. E. Fischer, and P. O. Hasselgren. Influence of burn injury on protein metabolism in different types of skeletal muscle and the role of glucocorticoids. J. Am. Coll. Surg. 180: 33-42, 1995.
9. Fang, C. H., G. Tiao, J. H. James, C. K. Ogle, J. E. Fischer, and P. O. Hasselgren. Burn injury stimulates multiple proteolytic pathways in skeletal muscle including the ubiquitin-energy-dependent pathway. J. Am. Coll. Surg. 180: 161-170, 1995.
10. Flaim, K. E., M. E. Copenhaver, and L. S. Jefferson. Effects of diabetes on protein synthesis in fast-and slow-twitch rat skeletal muscle. Am. J. Physiol. 239 (Endocrinol. Metab. 2): E88-E95, 1980.
11. Furuno, K., M. N. Goodman, and A. L. Goldberg. Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J. Biol. Chem. 265: 8550-8557, 1990.
12. Hasselgren, P. O. Protein Metabolism in Sepsis. Austin, TX: R. G. Landes, 1993.
13. Hasselgren, P. O., M. Hall-Angerås, U. Angerås, D. W. Benson, J. H. James, and J. E. Fischer. Regulation of total and myofibrillar protein breakdown in rat extensor digitorum longus and soleus muscle incubated flaccid or at resting length. Biochem. J. 267: 37-44, 1990.
14. Hasselgren, P. O., J. H. James, D. W. Benson, M. Hall-Angerås, U. Angerås, D. T. Hiyama, S. Li, and J. E. Fischer. Total and myofibrillar protein breakdown in different types of rat skeletal muscle: effects of sepsis and regulation by insulin. Metabolism 38: 634-640, 1989.
15. Hasselgren, P. O., V. Tricoli, D. Wieczorek, K. A. Steigerwald, U. Angerås, M. Hall-Angerås, and J. E. Fischer. Reduced levels of mRNA for myofibrillar proteins in skeletal muscle from septic rats. Life Sci. 49: 753-760, 1991.
16. Hasselgren, P. O., B. W. Warner, J. H. James, H. Takehara, and J. E. Fischer. Effect of insulin on amino acid uptake and protein turnover in skeletal muscle from septic rats. Evidence for insulin resistance of protein breakdown. Arch. Surg. 122: 228-233, 1987.
17. Hershko, A., and A. Ciechanover. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61: 761-807, 1992.
18. Li, J. B., and A. L. Goldberg. Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles. Am. J. Physiol. 231: 441-448, 1976.
19. Miller, J. B. MRF expression pattern reveals multiple origins for skeletal muscle cells. J. Natl. Inst. Health Res. 7: 42-43, 1995.
20. Mitch, W. E., R. Medina, S. Grieber, R. C. May, B. K. England, S. R. Price, J. L. Bailey, and A. L. Goldberg. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine-triphosphate-dependent pathway involving ubiquitin and proteasomes. J. Clin. Invest. 93: 2127-2133, 1994.
21. Pedersen, P., B. W. Warner, H. S. Bjornson, D. T. Hiyama, S. Li, D. F. Rigel, P. O. Hasselgren, and J. E. Fischer. Hemodynamic and metabolic alterations during experimental sepsis in young and adult rats. Surg. Gynecol. Obstet. 168: 148-156, 1989.
22. Rannels, S. R., and L. S. Jefferson. Effects of glucocorticoids on muscle protein turnover in perfused rat hemicorpus. Am. J. Physiol. 238 (Endocrinol. Metab. 1): E564-E572, 1980.
23. Suzuki, K., and J. S. Bond (Editors). Intracellular Protein Catabolism. Advances in Experimental Medicine and Biology. New York: Plenum, 1996, vol. 389.
24. Tawa, N. E., I. C. Kettelhut, and A. L. Goldberg. Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E326-E334, 1992.
25. Tiao, G., J. Fagan, V. Roegner, M. Lieberman, J. J. Wang, J. E. Fischer, and P. O. Hasselgren. Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids. J. Clin. Invest. 97: 339-348, 1996.
26. Tiao, G., J. M. Fagan, N. Samuels, J. H. James, K. Hudson, M. Lieberman, J. E. Fischer, and P. O. Hasselgren. Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94: 2255-2264, 1994.
27. Vary, T. C., and S. R. Kimball. Sepsis-induced changes in protein synthesis: differential effects on fast- and slow-twitch muscles. Am. J. Physiol. 262 (Cell Physiol. 31): C1513-C1519, 1992.
28. Voisin, L., K. Gray, K. M. Flowers, S. R. Kimball, L. S. Jefferson, and T. V. Vary. Altered expression of eukaryotic initiation factor 2B in skeletal muscle during sepsis. Am. J. Physiol. 270 (Endocrinol. Metab. 33): E43-E50, 1996.
29. Wiborg, O., M. S. Pedersen, A. Wind, L. G. Berglund, K. A. Marcker, and J. Vuust. The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. Eur. Mol. Biol. Organ. J. 4: 755-759, 1985.
30. Wing, S. S., and A. Goldberg. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E668-E676, 1993.
31. Young, V. R., and H. N. Munro. N-Methylhistidine (3-methylhistidine) and muscle protein turnover: an overview. Federation Proc. 37: 2291-2300, 1978.
32. Zamir, O., P. O. Hasselgren, J. A. Frederick, and J. E. Fischer. Is the metabolic response to sepsis in skeletal muscle different in infants and adults? An experimental study in rats. J. Pediatr. Surg. 27: 1399-1403, 1992.