Turnover of oxidatively modified proteins: the usage of in vitro and metabolic labeling

Free Radical Biology and Medicine

Volumn 46, Issue 1, 2009, Pages 8-13

  Catalgol, Betul ^a,b   Grune, Tilman ^a  

^a UNIVERSITY OF HOHENHEIM   (Germany)

^b ISTANBUL UNIVERSITY   (Turkey)

Author keywords

Free radicals; Metabolic radiolabeling; Protein degradation; Protein oxidation; Protein turnover

Indexed keywords

CELL PROTEIN; CYSTEINE; HISTIDINE; ISOLEUCINE; LEUCINE; LYSINE; METHIONINE; THREONINE; VALINE;

CELL LYSATE; CELLULAR DISTRIBUTION; CYTOSOL; IN VITRO STUDY; ISOTOPE LABELING; LIQUID SCINTILLATION COUNTING; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN METABOLISM; PROTEIN SYNTHESIS; QUANTITATIVE ANALYSIS; SHORT SURVEY; TISSUE DISTRIBUTION;

AMINO ACIDS; ANIMALS; BIOCHEMISTRY; CELL EXTRACTS; CELLS; HUMANS; ISOTOPE LABELING; MULTIPROTEIN COMPLEXES; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; PROTEINS; RADIOACTIVITY; RADIOISOTOPES; SENSITIVITY AND SPECIFICITY;

EID: 57449113835     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2008.09.024     Document Type: Short Survey

References (34)

1. Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324 (1997) 1-18
2. Davies K.J.A. Protein damage and degradation by oxygen radicals. I. General aspects. J. Biol. Chem. 262 (1987) 9895-9901
3. Grune T., Reinheckel T., and Davies K.J.A. Degradation of oxidized proteins in mammalian cells. FASEB J. 11 (1997) 526-534
4. Grune T. Oxidative stress, aging and the proteasomal system. Biogerontology 1 (2000) 31-40
5. Lasch P.T., Petras T., Ullrich O., Backmann D., Naumann D., and Grune T. Hydrogen peroxide induced structural alterations of RNase A. J. Biol. Chem. 276 (2001) 9492-9502
6. Giulivi C., Pacifici R.E., and Davies K.J.A. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Arch. Biochem. Biophys. 311 (1994) 329-341
7. Grune T., Jung T., Merker K., and Davies K.J.A. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36 (2004) 2519-2530
8. Mellman W.J., Schimke R.T., and Hayflick L. Catalase turnover in human diploid cell cultures. Exp. Cell Res. 73 (1972) 399-409
9. Bradley M.O., Hayflick L., and Schimke R.T. Protein degradation in human fibroblasts (WI-38): effects of aging, viral transformation, and amino acid analogs. J. Biol. Chem. 251 (1976) 3521-3529
10. Dice J.F., Dehlinger P.J., and Schimke R.T. Studies on the correlation between size and relative degradation rate of soluble proteins. J. Biol. Chem. 248 (1973) 4220-4228
11. Dice J.F., and Schimke R.T. Turnover of chromosomal proteins from rat liver. Arch. Biochem. Biophys. 158 (1973) 97-105
12. Dice J.F., and Schimke R.T. Turnover and exchange of ribosomal proteins from rat liver. J. Biol. Chem. 247 (1972) 98-111
13. Reinheckel T., Grune T., and Davies K.J.A. The measurement of protein degradation in response to oxidative stress. In: Keyse S.M. (Ed). Methods in Molecular Biology, Vol. 99, Stress Response: Methods and protocols, Part 5 (2000), Humana Press, Totowa, NJ 49-60
14. Sitte N., Huber M., Grune T., Ladhoff A., Doecke W.D., Zglinicki T.V., and Davies K.J.A. Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. FASEB J. 14 (2000) 1490-1498
15. Grune T., Reinheckel T., Joshi M., and Davies K.J.A. Proteolysis in cultured liver epithelial cells during oxidative stress: role of the multicatalytic proteinase complex, proteasome. J. Biol. Chem. 270 (1995) 2344-2351
16. Grune T., Reinheckel T., and Davies K.J.A. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J. Biol. Chem. 271 (1996) 15504-15509
17. Demasi M., and Davies K.J.A. Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism. FEBS Lett. 542 (2003) 89-94
18. McDuffee A.T., Senisterra G., Huntley S., Lepock J.R., Sekhar K.R., Meredith M.J., Borrelli M.J., Morrow J.D., and Freeman M.L. Proteins containing non-native disulfide bonds generated by oxidative stress can act as signals for the induction of the heat shock response. J. Cell. Physiol. 171 (1997) 143-151
19. Takiue M., Fujii H., Natake T., and Matsui Y. Analytical measurements of multiple beta-emitter mixtures with a liquid scintillation spectrometer. J. Radioanal. Nucl. Chem. Lett. 155 (1991) 183-193
20. Silverman J.A., and Amenta J.S. Sources of error in estimating radioactivity in protein from cell cultures by liquid scintillation counting. Anal. Biochem. 141 (1984) 538-544
21. 14C]-labeled compounds. Braz. J. Med. Biol. Res. 36 (2003) 1733-1739
22. Rice R.H., and Means G.E. Radioactive labeling of proteins in vitro. J. Biol. Chem. 246 (1971) 831-832
23. Koshland M.E., Englberger F.M., Erwin M.J., and Gaddone S.M. Modification of amino acid residues in anti-p-asobenzenearsonic acid antibody during extensive iodination. J. Biol. Chem. 238 (1963) 1343-1348
24. Means G.E., and Feeney R.E. Reductive alkylation of amino groups in proteins. Biochemistry 7 (1968) 2192-2201
25. Jentoft N., and Dearborn D.G. Labeling of proteins by reductive methylation using sodium cyanoborohydride. J. Biol. Chem. 254 (1979) 4359-4365
26. Bonifacino J.S. Metabolic labeling with amino acids. In: Bonifacino J.S. (Ed). Current Protocols in Molecular Biology, Unit 10.18, Analysis of Proteins, Supplement 44 (1998), Wiley, New York 1-10
27. 35S]cysteine in the absence of cells. Anal. Biochem. 269 (1999) 179-188
28. Ullrich O., and Grune T. Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells. Free Radic. Biol. Med. 31 (2001) 887-893
29. Poppek D., Keck S., Ermak G., Jung T., Stolzing A., Ullrich O., Davies K.J.A., and Grune T. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem. J. 400 (2006) 511-520
30. Mehlhase J., Sandig K., Pantopoulos K., and Grune T. Oxidation-induced ferritin turnover in microglial cells: role of proteasome. Free Radic. Biol. Med. 38 (2005) 276-285
31. Stolzing A., Wegner A., and Grune T. Degradation of oxidized extracellular proteins by microglia. Arch. Biochem. Biophys. 400 (2002) 171-179
32. Stolzing A., and Grune T. Neuronal apoptotic bodies: phagocytosis and degradation by primary microglial cells. FASEB J. 18 (2004) 743-745
33. Stolzing A., Widmer R., Jung T., Voss P., and Grune T. Degradation of glycated bovine serum albumin in microglial cells. Free Radic. Biol. Med. 40 (2006) 1017-1027
34. Pacifici R.E., and Davies K.J.A. Protein degradation as an index of oxidative stress. Methods Enzymol. 186 (1990) 485-502