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Titolo:
A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster
Autore:
Yokoyama, H; Mukae, N; Sakahira, H; Okawa, K; Iwamatsu, A; Nagata, S;
Indirizzi:
Osaka Univ, Sch Med, Dept Genet, Osaka 5650871, Japan Osaka Univ Osaka Japan 5650871 Sch Med, Dept Genet, Osaka 5650871, Japan Japan Sci & Technol Corp, Core Res Evolut Sci & Technol, Osaka 5650871, Japan Japan Sci & Technol Corp Osaka Japan 5650871 chnol, Osaka 5650871, Japan Kirin Brewery Co Ltd, Cent Lab Key Technol, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 17, volume: 275, anno: 2000,
pagine: 12978 - 12986
SICI:
0021-9258(20000428)275:17<12978:ANAMOC>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROGRAMMED CELL-DEATH; FRAGMENTATION FACTOR; CYSTEINE PROTEASE; CRYSTAL-STRUCTURE; C-ELEGANS; APOPTOSIS; INHIBITOR; ICAD; CARBOXYMETHYLATION; SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Nagata, S Osaka Univ, Sch Med, Dept Genet, 2-2 Yamada Oka,B 3, Osaka 5650871, Japan Osaka Univ 2-2 Yamada Oka,B 3 Osaka Japan 5650871 650871, Japan
Citazione:
H. Yokoyama et al., "A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster", J BIOL CHEM, 275(17), 2000, pp. 12978-12986

Abstract

Caspase activated DNase (CAD) is an enzyme that cleaves chromosomal DNA inapoptotic cells. Here, we identified a DNase in Drosophila Schneider cellsthat can be activated by caspase 3, and purified it as a complex of two subunits (p32 and p20). Using primers based on the amino acid sequence of thepurified proteins, a cDNA coding for Drosophila CAD (dCAD) was cloned. Thepolypeptide encoded by the cDNA contained 450 amino acids with a calculated M-r of 52,057, and showed significant homology with human and mouse CAD (22% identity). Mammalian CADs carry a nuclear localization signal at the C terminus. In contrast, dCAD lacked the corresponding sequence, and the purified dCAD did not cause DNA fragmentation in nuclei in a cell-free system. When dCAD was co-expressed in COS cells with Drosophila inhibitor of CAD (dICAD), a 52-kDa dCAD was produced as a heterotetrameric complex with dICAD. When the complex was treated with human caspase 3 or Drosophila caspase (drICE), the dICAD was cleaved, and released from dCAD. In addition, dCAD wasalso cleaved by these caspases, and behaved as a (p32)(2)(p20)(2) complex in gel filtration. When a Drosophila neuronal cell line was induced to apoptosis by treatment with a kinase inhibitor, both dCAD and dICAD were cleaved. These results indicated that unlike mammalian CAD, Drosophila CAD must be cleaved by caspases to be activated.

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Documento generato il 18/01/21 alle ore 14:31:48