Glutamine starvation of monocytes inhibits the ubiquitin-proteasome proteolytic pathway

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1638, Issue 2, 2003, Pages 138-148

  Zellner, Maria ^a   Gerner, Christopher ^b   Eliasen, Maja Munk ^a   Wurm, Susanne ^a   Pollheimer, Jürgen ^a   Spittler, Andreas ^a   Brostjan, Christine ^a   Roth, Erich ^a   Oehler, Rudolf ^a  

^a UNIVERSITY OF VIENNA   (Austria)

^b MEDICAL UNIVERSITY OF VIENNA   (Austria)

Author keywords

Amino acid starvation; Glutamine; Monocyte; Proteasome; Protein breakdown

Indexed keywords

BETA ACTIN; GLUTAMINE; INTERLEUKIN 1BETA; UBIQUITIN;

ARTICLE; CONTROLLED STUDY; CRITICAL ILLNESS; GEL ELECTROPHORESIS; HUMAN; HUMAN CELL; IMMUNE DEFICIENCY; MONONUCLEAR CELL; PRIORITY JOURNAL; PROTEIN CALORIE MALNUTRITION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN MALNUTRITION; PROTEIN STABILITY; REDUCTION;

EID: 0038645316     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4439(03)00062-0     Document Type: Article

References (39)

1. Newsholme P., Curi R., Gordon S., Newsholme E.A. Metabolism of glucose, glutamine, long-chain fatty acids and ketone bodies by murine macrophages. Biochem. J. 239:1986;121-125.
2. Curthoys N.P., Watford M. Regulation of glutaminase activity and glutamine metabolism. Annu. Rev. Nutr. 15:1995;133-159.
3. Neu J., Shenoy V., Chakrabarti R. Glutamine nutrition and metabolism: where do we go from here? FASEB J. 10:1996;829-837.
4. Roth E., Funovics J., Mühlbacher F., Schemper M., Mautitz W., Sporn P., Fritsch A. Metabolic disorders in severe abdominal sepsis: glutamine deficiency in skeletal muscle. Clin. Nutr. 1:1982;25.
5. Parry-Billings M., Evans J., Calder P., Newsholme E. Does glutamine contribute to immunosuppression after major burns? Lancet. 336:1990;523-525.
6. Ziegler T.R., Young L.S., Benfell K., Scheltinga M., Hortos K., Bye R., Morrow F.D., Jacobs D.O., Smith R.J., Antin J.H. Clinical and metabolic efficacy of glutamine-supplemented parenteral nutrition after bone marrow transplantation. A randomized, double-blind, controlled study. Ann. Intern. Med. 116:1992;821-828.
7. MacBurney M., Young L.S., Ziegler T.R., Wilmore D.W. A cost-evaluation of glutamine-supplemented parenteral nutrition in adult bone marrow transplant patients. J. Am. Diet. Assoc. 94:1994;1263-1266.
8. Wischmeyer P.E. Glutamine and heat shock protein expression. Nutrition. 18:2002;225-228.
9. Houdijk A.P., Rijnsburger E.R., Jansen J., Wesdorp R.I., Weiss J.K., McCamish M.A., Teerlink T., Meuwissen S.G., Haarman H.J., Thijs L.G., van Leeuwen P.A. Randomised trial of glutamine-enriched enteral nutrition on infectious morbidity in patients with multiple trauma. (see comments) Lancet. 352:1998;772-776.
10. Neu J., Roig J.C., Meetze W.H., Veerman M., Carter C., Millsaps M., Bowling D., Dallas M.J., Sleasman J., Knight T., Auestad N. Enteral glutamine supplementation for very low birth weight infants decreases morbidity. J. Pediatr. 131:1997;691-699.
11. Murphy C., Newsholme P. Importance of glutamine metabolism in murine macrophages and human monocytes to L-arginine biosynthesis and rates of nitrite or urea production. Clin. Sci. (Lond). 95:1998;397-407.
12. Spittler A., Winkler S., Götzinger P., Oehler R., Willheim M., Tempfer C., Weigel G., Függer R., Boltz Nitulescu G., Roth E. Influence of glutamine on the phenotype and function of human monocytes. Blood. 86:1995;1564-1569.
13. Murphy C., Newsholme P. Macrophage-mediated lysis of a beta-cell line, tumour necrosis factor-alpha release from bacillus Calmette-Guerin (BCG)-activated murine macrophages and interleukin-8 release from human monocytes are dependent on extracellular glutamine concentration and glutamine metabolism. Clin. Sci. (Lond). 96:1999;89-97.
14. Spittler A., Sautner T., Gornikiewicz A., Manhart N., Oehler R., Bergmann M., Fugger R., Roth E. Postoperative glycyl-glutamine infusion reduces immunosuppression: partial prevention of the surgery induced decrease in HLA-DR expression on monocytes. Clin. Nutr. 20:2001;37-42.
15. Spittler A., Oehler R., Goetzinger P., Holzer S., Reissner C.M., Leutmezer F., Rath V., Wrba F., Fuegger R., Boltz Nitulescu G., Roth E. Low glutamine concentrations induce phenotypical and functional differentiation of U937 myelomonocytic cells. J. Nutr. 127:1997;2151-2157.
16. Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell. 78:1994;773-785.
17. Li X., Yang Y., Ashwell J.D. TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2. Nature. 416:2002;345-347.
18. Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:1994;761-771.
19. Ben-Neriah Y. Regulatory functions of ubiquitination in the immune system. Nat. Immunol. 3:2002;20-26.
20. Lundin A., Richardsson A., Thore A. Continuous monitoring of ATP-converting reactions by purified firefly luciferase. Anal. Biochem. 75:1976;611-620.
21. Oehler R., Schmierer B., Zellner M., Prohaska R., Roth E. Endothelial cells downregulate expression of the 70 kDa heat shock protein during hypoxia. Biochem. Biophys. Res. Commun. 274:2000;542-547.
22. Gerner C., Frohwein U., Gotzmann J., Bayer E., Gelbmann D., Bursch W., Schulte-Hermann R. The Fas-induced apoptosis analyzed by high throughput proteome analysis. J. Biol. Chem. 275:2000;39018-39026.
23. Wray W., Boulikas T., Wray V., Hancock R. Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118:1981;197-203.
24. Newsholme P. Why is L-glutamine metabolism important to cells of the immune system in health, postinjury, surgery or infection? J. Nutr. 131:2001;2515S-2522S. (discussion 2523S-4S).
25. Appel R.D., Bairoch A., Hochstrasser D.F. A new generation of information retrieval tools for biologists: the example of the ExPASy WWW server. Trends Biochem. Sci. 19:1994;258-260.
26. Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 20:1999;3551-3567.
27. Lecker S.H., Solomon V., Mitch W.E., Goldberg A.L. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J. Nutr. 129:1999;227S-237S.
28. Zhou X., Thompson J. Regulation of protein turnover by glutamine in heat-shocked skeletal myotubes. Biochim. Biophys. Acta. 1357:1997;234-242.
29. Newsholme P., Gordon S., Newsholme E.A. Rates of utilization and fates of glucose, glutamine, pyruvate, fatty acids and ketone bodies by mouse macrophages. Biochem. J. 242:1987;631-636.
30. Karinch A.M., Pan M., Lin C.M., Strange R., Souba W.W. Glutamine metabolism in sepsis and infection. J. Nutr. 131:2001;2535S-2538S. (discussion 2550S-1S).
31. Holecek M., Skopec F., Skalska H., Sprongl L. Effect of alanyl-glutamine on leucine and protein metabolism in endotoxemic rats. JPEN. J. Parenter. Enteral Nutr. 24:2000;215-222.
32. Holecek M. Relation between glutamine, branched-chain amino acids, and protein metabolism. Nutrition. 18:2002;130-133.
33. Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7:1995;215-223.
34. Ferrell K., Wilkinson C.R., Dubiel W., Gordon C. Regulatory subunit interactions of the 26S proteasome, a complex problem. Trends Biochem. Sci. 25:2000;83-88.
35. Kamikubo T., Hayashi T. Changes in proteasome activity following transient ischemia. Neurochem. Int. 28:1996;209-212.
36. Orino E., Tanaka K., Tamura T., Sone S., Ogura T., Ichihara A. ATP-dependent reversible association of proteasomes with multiple protein components to form 26S complexes that degrade ubiquitinated proteins in human HL-60 cells. FEBS Lett. 284:1991;206-210.
37. Gronostajski R.M., Pardee A.B., Goldberg A.L. The ATP dependence of the degradation of short- and long-lived proteins in growing fibroblasts. J. Biol. Chem. 260:1985;3344-3349.
38. Stevenson F.T., Torrano F., Locksley R.M., Lovett D.H. Interleukin 1: the patterns of translation and intracellular distribution support alternative secretory mechanisms. J. Cell. Physiol. 152:1992;223-231.
39. Moors M.A., Mizel S.B. Proteasome-mediated regulation of interleukin-1beta turnover and export in human monocytes. J. Leukoc. Biol. 68:2000;131-136.