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Caspase activity is not sufficient to execute cell death.

Abstract：

:Molecular studies of the physiological cell death process have focused attention on the role of effector caspases as critical common elements of the lethal mechanism. Diverse death signals act afferently via distinct signaling pathways to activate these resident proenzyme molecules post-translationally. Whether this molecular convergence represents the mechanistic point of irreversible commitment to cell death has not been established. That a number of caspase substrates are proteins that serve important roles in cellular homeostasis has led to the view that the acquisition of this activity must be the determinative step in cell death. Observations that caspases serve in a regulatory role to catalyze the appearance of new activities involved in orderly cellular dissolution challenge this model of death as a simple process of proteolytic destruction. We found previously that caspase-dependent nuclear cyclin dependent kinase 2 (Cdk2) activity appears to be necessary for cell death. Employing direct cytofluorimetric analyses of intracellular caspase activity and colony forming assays, we now show that transient blockade of caspase-dependent Cdk2 activity confers long-lived sparing from death on cells otherwise triggered to die and fully replete with caspase activity. These data demonstrate that caspases, while necessary for apoptosis, are not sufficient to exert lethality. Caspase activation per se does not represent an irreversible point of commitment to physiological cell death.

journal_name

Exp Cell Res

journal_title

Experimental cell research

authors

Lukovic D,Komoriya A,Packard BZ,Ucker DS

doi

10.1016/s0014-4827(03)00289-1

keywords:

subject

Has Abstract

pub_date

2003-10-01 00:00:00

pages

384-95

issue

2

eissn

0014-4827

issn

1090-2422

pii

S0014482703002891

journal_volume

289

pub_type

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