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Titolo:
Variants of peroxiredoxins expression in response to hydroperoxide stress
Autore:
Mitsumoto, A; Takanezawa, Y; Okawa, K; Iwamatsu, A; Nakagawa, Y;
Indirizzi:
Kitasato Univ, Sch Pharmaceut Sci, Minato Ku, Tokyo 1088641, Japan Kitasato Univ Tokyo Japan 1088641 t Sci, Minato Ku, Tokyo 1088641, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan , Yokohama, Kanagawa, Japan
Titolo Testata:
FREE RADICAL BIOLOGY AND MEDICINE
fascicolo: 6, volume: 30, anno: 2001,
pagine: 625 - 635
SICI:
0891-5849(20010315)30:6<625:VOPEIR>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
THIOL-SPECIFIC ANTIOXIDANT; RESOLUTION 2-DIMENSIONAL ELECTROPHORESIS; POLYACRYLAMIDE-GEL ELECTROPHORESIS; ACTIVATED PROTEIN-KINASE; NECROSIS-FACTOR-ALPHA; HEAT-SHOCK PROTEIN; OXIDATIVE STRESS; THIOREDOXIN PEROXIDASE; SACCHAROMYCES-CEREVISIAE; GENE-EXPRESSION;
Keywords:
H2O2; peroxiredoxin; modification; 2D-PAGE; free radicals;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
63
Recensione:
Indirizzi per estratti:
Indirizzo: Nakagawa, Y Kitasato Univ, Sch Pharmaceut Sci, Minato Ku, 5-9-1 Shirokane,Tokyo 1088641, Japan Kitasato Univ 5-9-1 Shirokane Tokyo Japan 1088641 8641, Japan
Citazione:
A. Mitsumoto et al., "Variants of peroxiredoxins expression in response to hydroperoxide stress", FREE RAD B, 30(6), 2001, pp. 625-635

Abstract

We examined patterns of the proteins that were expressed in human umbilical vein endothelial cells (HUVEC) in response to oxidative stress by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). When HUVEC were exposed to H2O2 at 100 muM for 60 min, the intensities of eight spots increasedand those of eight spots decreased on 2D gels, as compared with control gels, after staining with silver. These changes were also observed after exposure of cells to hydroperoxides such as cumene hydroperoxide and tert-butylhydroperoxide, but not after exposure to other reagents that induce oxidative stress such as S-alkylating compounds, nitric oxide, and salts of heavymetals. Therefore, these proteins were designated hydroperoxide responsiveproteins (HPRPs). Microsequencing analysis revealed that these HPRPs corresponded to at least six pairs of proteins. Of these, four pairs of HPRPs were thioredoxin peroxidase I (TPx I), TPx II, TPx III, and the product of human ORF06, all of which belong to the peroxiredoxin (Prx) family and all ofwhich are involved in the elimination of hydroperoxides. The other two pairs corresponded to heat shock protein 27 (HSP27) and glyceraldehyde-3-phosphate dehydrogenase (G3PDH), respectively. The variants that appeared in response to hydroperoxides had molecular masses similar to the respective native forms, but their pi values were lower by 0.2-0.3 pH units than those of the corresponding native proteins. These variants were detected on 2D gels after cells had been exposed to hydroperoxides in the presence of an inhibitor of protein synthesis. All variants were generated within 30 min of exposure to 100 muM H2O2. The variants of TPx I and TPx II appeared within 2 min of the addition of H2O2 to the culture medium. The HPRPs returned to their respective native forms after the removal of stress. Our results indicated that at least six proteins were structurally modified in response to hydroperoxides. Analysis by 2D-PAGE of P-32-labeled proteins revealed that the variant of HSP27 was its phosphorylated form while the other HPRPs were notmodified by phosphorylation. Taken together, the results suggest that 2D-PAGE can reveal initial responses to hydroperoxide stress at the level of protein modification. Moreover, it is possible that the variants of four types of Prx might reflect intermediate states in the process of hydroperoxide elimination. (C) 2001 Elsevier Science.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/01/21 alle ore 02:57:16