The ubiquitin-proteasome pathway: Review of a novel intracellular mechanism of muscle protein breakdown during sepsis and other catabolic conditions

Annals of Surgery

Volumn 225, Issue 3, 1997, Pages 307-316

  Hasselgren, Per Olof ^a   Fischer, Josef E ^b  

^a UNIVERSITY OF CINCINNATI   (United States)

^b SHRINERS HOSPITALS FOR CHILDREN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; MUSCLE PROTEIN; PROTEASOME; TRANSCRIPTION FACTOR; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

ANTIGEN PRESENTATION; ARTICLE; CELL CYCLE; HUMAN; HYDROLYSIS; MUSCLE METABOLISM; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN METABOLISM; PROTEIN SYNTHESIS; SEPSIS; SKELETAL MUSCLE;

CYSTEINE ENDOPEPTIDASES; HUMANS; MULTIENZYME COMPLEXES; MUSCLE PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; RNA, MESSENGER; SEPSIS; TRANSCRIPTION FACTORS; UBIQUITINS;

EID: 0030897196     PISSN: 00034932     EISSN: None     Source Type: Journal    
DOI: 10.1097/00000658-199703000-00011     Document Type: Article

References (59)

1. Rosenblatt S, Clowes GHA, George BC, Hirsch E, Lindberg B. Exchange of amino acids by muscle and liver in sepsis. Comparative studies in vivo and in vitro. Arch Surg 1983; 118:167-175.
2. Long CL, Birkhahn RH, Geiger JW, et al. Urinary excretion of 3-methylhistidine: an assessment of muscle protein catabolism in adult normal subjects and during malnutrition, sepsis and skeletal trauma. Metabolism 1981; 30:765-776.
3. Sehoenheimer R. The Dynamic State of Body Constituents. Cambridge, MA: Harvard University Press; 1942:25-46.
4. Goldberg AL, St John AC. Intracellular protein degradation in mammalian and bacterial cells: part II. Annu Rev Biochem 1976; 45:747-803.
5. Goldberg AL. The mechanism and functions of ATP-dopendent proteases in bacterial and animal cells. Eur J Biochem 1992; 203:9-23.
6. Hershko A, Ciechanover A. The ubiquitin system for protein degradation. Annu Rev Biochem 1992; 61:761-807.
7. Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opin Cell Biol 1995; 7:215-223.
8. Goldberg AL. Functions of the proteasome: the lysis at the end of the tunnel. Science 1995; 268:522-524.
9. Hasselgren PO. Protein Metabolism in Sepsis. Austin, TX: RG Landes Co; 1993.
10. Ciechanover A, Hod Y, Hershko A. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun 1978; 81:1100-1105.
11. Mayer RJ, Arnold J, Laszlo L, et al. Ubiquitin in health and disease. Biochim Biophys Acta 1991; 1089:141-157.
12. Jentsch S, Seufert W, Hauser HP. Genetic analysis of the ubiquitin system. Biochim Biophys Acta 1991; 1089:127-139.
13. Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994; 79:13-21.
14. Falquet L, Paquet N, Frutiger S, et al. A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett 1995; 359:73-77.
15. Papa FR, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 1993; 366:313-319.
16. Harris JR. Release of a macromolecular protein component from human erythrocyte ghosts. Biochim Biophys Acta 1968; 150:534-537.
17. Peters JM. Proteasomes: protein degradation machines of the cell. Trends Biochem Sci 1994; 15:377-382.
18. Koster AJ, Walz J, Lupas A, Baumeister W. Structural features of archaebacterial and eukaryotic proteasomes. Mol Biol Rep 1995; 21:11-20.
19. Taylor RG, Tassy C, Briand M, et al. Proteolytic activity of proteasome on myofibrillar structures. Mol Biol Rep 1995; 21:71-73.
20. Dahlman B, Kuehn L. The 20S/26S protreasomal pathway of protein degradation in muscle tissue. Mol Biol Rep 1995; 21:57-62.
21. Tanaka K, Molecular biology of proteasomes. Mol Biol Rep 1995; 21:21-26.
22. Mykles DL, Haire MF. Branded-chain-amino-acid-preferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins. Biochem J 1995; 306:285-291.
23. Löwe J, Stock D, Jap B, el al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 1995; 268:533-539.
24. Weissman JS, Sigler PB, Horwich AL. From the cradle to the grave: ring complexes in the life of a protein. Science 1995; 268:523-524.
25. DeMartino GN, Moomaw CR, Zagnitko OP, et al. PA700, an ATP-dependent activator of the 20S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J Biol Chem 1994; 269:20878-20884.
26. Hayashi S, Murakami Y. Rapid and regulated degradation of ornithine decarboxylase. Biochem J 1995; 306:1-10.
27. Gray CW, Slaughter CA, DeMartino GN. PA28 activator protein forms regulatory caps on proteasome stacked rings. J Mol Biol 1994; 236:7-15.
28. Ma CP, Slaughter CA, DeMartino GN. Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain). J Biol Chem 1992; 267:10515-10523.
29. Hasselgren PO, James JH, Benson DW, et al. Total and myofibrillar protein breakdown in different types of rat skeletal muscle: effects of sepsis and regulation by insulin. Metabolism 1989; 38:634-640.
30. Hasselgren PO, James JH, Fischer JE. Inhibited muscle amino acid uptake in sepsis. Ann Surg 1986; 203:360-365.
31. Newsholme EA, Parry-Billings M. Properties of glutamine release from muscle and its importance for the immune system. JPEN J Parenter Enteral Nutr 1990; 14:63S-67S.
32. Windmueller HG, Spaeth AE. Respiratory fuels and nitrogen metabolism in vivo in small intestine of fed rats. J Biol Chem 1980; 255:107-112.
33. Zamir O, Hasselgren PO, Kunkel SL, et al. Evidence that tumor necrosis factor participates in the regulation of muscle proteolysis during sepsis. Arch Surg 1992; 127:170-174.
34. Zamir O, Hasselgren PO, O'Brien W, et al. Muscle protein breakdown during endotoxemia in rats and after treatment with interleukin-l receptor antagonist (IL-lra). Ann Surg 1992; 216:381-387.
35. Hall-Angerås M, Angerås U, Zamir O, et al. Effect of the glucocorticoid receptor antagonist RU38486 on muscle protein breakdown in sepsis. Surgery 1991; 109:468-473.
36. Tiao G, Fagan JM, Samuels N, et al. Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J Clin Invest 1994; 94:2255-2264.
37. Tiao GM, Fagan J, Lieberman M, et al. Sepsis increases proteasome-dependent proteolysis and mRNA levels for the proteasome subunit RC2 in skeletal muscle. Surg Forum 1995; 46:10-12.
38. Fang CH, Tiao G, James JH, et al. Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway. J Am Coll Surg 1995; 180:161-170.
39. Llovera M, Garcia-Martinez C, Agell N, et al. Ubiquitin gene expression is increased in skeletal muscle of tumour-bearing rats. FEBS Lett 1994; 338:311-318.
40. 2-adrenergic agonist (clenbuterol). Role of the ATP-ubiquitin-dependent proteolylic pathway. J Clin Invest 1995; 95:2367-2372.
41. Baracos VE, DeVivo C, Hoyle DHR, Goldberg AL. Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. Am J Physiol 1995; 268:E996-E1006.
42. Furuno K, Goldman MN, Goldberg AL. Role of differentproteolytic systems in the degradation of muscle proteins during denervation atrophy. J Biol Chem 1990; 265:8550-8557.
43. Medina R, Wing SS, Haas A, Goldberg AL. Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed Biochim Acta 1991; 50:347-356.
44. Wing SS, Goldberg AL. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am J Physiol 1993; 264:E668-K676.
45. Mitch WE, Medina R, Grieber S, et al. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes. J Clin Invest 1994; 93:2127-2133.
46. Price SR, England BK, Bailey JL, et al. Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. Am J Physiol 1994; 267:C955-C960.
47. Garcia-Martinez C, Agell N, Llovera M, et al. Tumor necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins. FEBS Lett 1993; 323:211-214.
48. Tiao G, Fagan J, Roegner V, et al. Energy-ubiquitin-dependent muscle proteolysis during sepsis in rats is regulated by glucocorticoids. J Clin Invest 1996; 97:339-348.
49. Fang CH, James JH, Ogle C, et al. Influence of burn injury on protein metabolism in different types of skeletal muscle and the role of glucocorticoids. J Am Coll Surg 1995; 180:33-42.
50. Goldberg AL, Rock KL. Proteolysis, proteasomes and antigen presentation. Nature 1992; 357:375-379.
51. Monaco JJ. A molecular model of MHC class-I-restricted antigen processing. Immunol Today 1992; 13:173-179.
52. Rock KL, Gramm C, Rothstein L, et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78:761-771.
53. Barinaga M. A new twist to the cell cycle. Science 1995; 269:631-632.
54. Pagano M, Tam SW, Theodoras AM, et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995; 269:682-685.
55. Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 1994; 78:773-785.
56. Finco TS, Baldwin AS. Mechanistic aspects of NF-κB regulation: the emerging role of phosphorylation and proteolysis. Immunity 1995; 3:263-272.
57. Germain RN, Margulies DH. The biochemistry and cell biology of antigen processing and presentation. Annu Rev Immunol 1993; 11:403-450.
58. Baeuerle PA, Henkel T. Function and activation of NF-κB in the immune system. Annu Rev Immunol 1994; 12:141-179.
59. Sen R, Baltimore D. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 1986; 46:705-716.