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Titolo:
Carcinogen substrate specificity of human COX-1 and COX-2
Autore:
Wiese, FW; Thompson, PA; Kadlubar, FF;
Indirizzi:
Natl Ctr Toxicol Res, Div Mol Epidemiol, Jefferson, AR 72079 USA Natl Ctr Toxicol Res Jefferson AR USA 72079 miol, Jefferson, AR 72079 USA Univ Arkansas Med Sci, Div Toxicol, Little Rock, AR 72205 USA Univ Arkansas Med Sci Little Rock AR USA 72205 Little Rock, AR 72205 USA
Titolo Testata:
CARCINOGENESIS
fascicolo: 1, volume: 22, anno: 2001,
pagine: 5 - 10
SICI:
0143-3334(200101)22:1<5:CSSOHC>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
APC(DELTA-716) KNOCKOUT MICE; ENDOPEROXIDE-H SYNTHASE-1; PROSTAGLANDIN G/H SYNTHASE-1; INTESTINAL POLYP DEVELOPMENT; DOCOSAHEXAENOIC ACID DHA; MUTAGENIC ACTIVATION; MEDIATED METABOLISM; AROMATIC-AMINES; MESSENGER-RNA; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Kadlubar, FF Natl Ctr Toxicol Res, Div Mol Epidemiol, Jefferson, AR 72079 USA Natl Ctr Toxicol Res Jefferson AR USA 72079 on, AR 72079 USA
Citazione:
F.W. Wiese et al., "Carcinogen substrate specificity of human COX-1 and COX-2", CARCINOGENE, 22(1), 2001, pp. 5-10

Abstract

The activation of carcinogenic aromatic and heterocyclic amines and benzo[a]pyrene-7,8-diol to intracellular electrophiles by prostaglandin H synthase (COX) is well documented for ovine sources of this enzyme. Here, the arachidonic acid-dependent activation of substrates by human (h)COX-1 and-2 is examined, utilizing recombinant enzymes. The COX-dependent activation of benzidine (BZ), 4-aminobiphenyl, (+)benzo[a]pyrene-7,8-diol, (+)benzo[a]pyrene-7,8-diol, 2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline (MeIQx), 2-amino-3-methylimidazo [4,5-f]quinoline (IQ), 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine (PhIP), and 4,4'-methylenebis (2-chloroaniline) (MOCA) is assessed by means of COX-catalyzed, covalent DNA binding. The hCOX isozymes activated all substrates tested, activation varied from barely detectable forIQ (0.76 and 1.52 pmol bound/mg DNA for COX-1 and -2, respectively) to a high of 65 and 117 pmol bound/mg DNA for COX-1 and -2, respectively, for theactivation of MOCA, BZ, which is an excellent peroxidase substrate, did not exhibit high DNA binding levels in hCOX assays and this phenomenon was found to be due to high levels of binding to protein, which effectively competed with the DNA for binding in the assay, The demonstrated ability of the COX enzymes to activate a variety of environmental and dietary carcinogens indicates a potential role for COX in the activation pathway of aromatic and heterocyclic amines and polycyclic hydrocarbons at extra-hepatic sites during early or late stages of carcinogenesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 08:28:45