Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
ACTIVATION OF A CPP32-LIKE PROTEASE DURING L1210 CELL APOPTOSIS INDUCED BY THIOL DEPRIVATION
Autore:
LEE SH; FUJITA N; TSURUO T;
Indirizzi:
UNIV TOKYO,INST MOL & CELLULAR BIOSCI,BUNKYO KU,1-1-1 YAYOI TOKYO 113JAPAN UNIV TOKYO,INST MOL & CELLULAR BIOSCI,BUNKYO KU TOKYO 113 JAPAN JAPANESE FDN CANC RES,CTR CANC CHEMOTHERAPY,TOSHIMA KU TOKYO 170 JAPAN
Titolo Testata:
Apoptosis
fascicolo: 1, volume: 2, anno: 1997,
pagine: 77 - 83
SICI:
1360-8185(1997)2:1<77:AOACPD>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
T-LYMPHOMA CELLS; BCL-2 EXPRESSION; MONOCLONAL-ANTIBODIES; IN-VITRO; DEATH; MOUSE; CYSTEINE; 2-MERCAPTOETHANOL; INVOLVEMENT; INHIBITION;
Keywords:
APOPTOSIS; BCL-2; CPP32; THIOL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
S.H. Lee et al., "ACTIVATION OF A CPP32-LIKE PROTEASE DURING L1210 CELL APOPTOSIS INDUCED BY THIOL DEPRIVATION", Apoptosis, 2(1), 1997, pp. 77-83

Abstract

Reduced thiols (e.g., cysteine) are important in the maintenance of lymphocyte cell viability and growth. L1210 monocytic leukaemia cells were known to have a limited ability to uptake cystine, and they require cysteine for cell growth. L1210 cells underwent apoptosis when cultured without thiol-bearing and dithiol-cleaving compounds, adding thiols suppressed the apoptosis and promoted cell growth. A specific inhibitor of interleukin-1 beta-converting enzyme (ICE)-like and CPP32-like proteases could suppress L1210 cell apoptosis induced by thiol deprivation. The cell lysates of apoptotic L1210 cells exhibited protease activity that could cleave DEVD-AMC, but not YVAD-AMC, and so CPP3P-like proteases, but not ICE-like proteases, were activated and participatedin apoptosis. The addition of thiols could suppress CPP3P-like protease activation. Although the cell death-suppressor bcl-2-family proteins (bcl-2 and bcl-X-L) were recently found to suppress the activation of CPP32-like proteases, the expression levels of death-suppressor bcl-2-family proteins did not change when thiols were added. These resultssuggest that reduced thiols maintain L1210 cell survival by inhibiting the activation of CPP32-like proteases without changing the anti-apoptotic bcl-2-family protein expression.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 12:16:04