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Titolo:
PROTEIN MODIFICATION BY LIPID-PEROXIDATION PRODUCTS - FORMATION OF MALONDIALDEHYDE-DERIVED N-EPSILON-(2-PROPENAL)LYSINE IN PROTEINS
Autore:
UCHIDA K; SAKAI K; ITAKURA K; OSAWA T; TOYOKUNI S;
Indirizzi:
NAGOYA UNIV,SCH AGR SCI,LAB FOOD & BIODYNAM NAGOYA AICHI 46401 JAPAN AICHI UNIV EDUC,FAC EDUC KARIYA AICHI 448 JAPAN KYOTO UNIV,GRAD SCH MED,DEPT PATHOL & BIOL DIS,SAKYO KU KYOTO 606 JAPAN
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 1, volume: 346, anno: 1997,
pagine: 45 - 52
SICI:
0003-9861(1997)346:1<45:PMBLP->2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY-LIPOPROTEIN; HUMAN MONOCYTE-MACROPHAGES; OXIDATIVE MODIFICATION; URINARY METABOLITE; IDENTIFICATION; CHEMISTRY; ALDEHYDES; ACIDS; LDL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
K. Uchida et al., "PROTEIN MODIFICATION BY LIPID-PEROXIDATION PRODUCTS - FORMATION OF MALONDIALDEHYDE-DERIVED N-EPSILON-(2-PROPENAL)LYSINE IN PROTEINS", Archives of biochemistry and biophysics, 346(1), 1997, pp. 45-52

Abstract

Malondialdehyde (MDA), a naturally occurring dialdehyde produced in the membrane lipid peroxidation, is known to react with lysine residuesof proteins, but the MDA-lysine adducts generated in the proteins have not been characterized adequately, In the present study, we provide evidence that the enaminal-type MDA-lysine adduct, N-epsilon-(2-propenal)lysine, is formed in human low-density lipoprotein (LDL) upon reaction with MDA or Cu2+. We found that the incubation of N-alpha-acetyllysine with MDA generated N-alpha-acetyl-N-epsilon-(2-propenal)lysine asthe predominant product. In addition, a polyclonal antiserum raised against the MDA-modified protein was found to contain antibody populations that could be purified by affinity gel prepared by covalent attachment of N-alpha-acetyl-N-epsilon-(2-propenal)lysine. It was concluded that the affinity-purified anti-N-epsilon-(2-propenal)lysine antibody was highly specific to the enaminal derivative of both lysine residuesand phosphatidylethanolamine, based on the observations that (i) MDA was the only aldehyde which generated immunoreactive materials in proteins; (ii) among structurally defined MDA-lysine adducts tested, the antibody recognized the enaminal adduct only; and (iii) immunoreactivity to N-(2-propenal)serine was still significant but much weaker than its reactivity to N-(2-propenal)ethanolamine. Furthermore, analysis of antibody recognition sites with a variety of N-(2-propenal)alkylaminesrevealed that the mono-specific antibody recognized the N-2-propenal-N-ethyl moiety [-(CH2)(2)-NH-CH=CH-CHO] of enaminal adducts, Determination by a competitive enzyme-linked immunosorbent assay demonstrated that N-epsilon-(2-propenal)lysine accounted for 33.7 and 3.1% of the lysine residues that disappeared during in vitro incubation of LDL with MDA and Cu2+, respectively. These results suggest that N-epsilon-(2-propenal)lysine represents a major form of MDA covalently attached to proteins. (C) 1997 Academic Press.

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Documento generato il 18/02/20 alle ore 14:12:24