Caspase-dependent activation of cyclin-dependent kinases during Fas-induced apoptosis in Jurkat cells.
Proc Natl Acad Sci U S A
; 95(12): 6785-90, 1998 Jun 09.
Article
em En
| MEDLINE
| ID: mdl-9618490
ABSTRACT
The activation of cyclin-dependent kinases (cdks) has been implicated in apoptosis induced by various stimuli. We find that the Fas-induced activation of cdc2 and cdk2 in Jurkat cells is not dependent on protein synthesis, which is shut down very early during apoptosis before caspase-3 activation. Instead, activation of these kinases seems to result from both a rapid cleavage of Wee1 (an inhibitory kinase of cdc2 and cdk2) and inactivation of anaphase-promoting complex (the specific system for cyclin degradation), in which CDC27 homolog is cleaved during apoptosis. Both Wee1 and CDC27 are shown to be substrates of the caspase-3-like protease. Although cdk activities are elevated during Fas-induced apoptosis in Jurkat cells, general activation of the mitotic processes does not occur. Our results do not support the idea that apoptosis is simply an aberrant mitosis but, instead, suggest that a subset of mitotic mechanisms plays an important role in apoptosis through elevated cdk activities.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Cisteína Endopeptidases
/
Proteína Quinase CDC2
/
Proteínas Serina-Treonina Quinases
/
Apoptose
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Quinases Ciclina-Dependentes
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Receptor fas
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Caspases
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Quinases relacionadas a CDC2 e CDC28
Limite:
Humans
Idioma:
En
Ano de publicação:
1998
Tipo de documento:
Article