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Ceramide-induced apoptosis is mediated by caspase activation independently from retinoblastoma protein post-translational modification.

Abstract：

:Recent evidence suggests that untimely retinoblastoma protein (RB) dephosphorylation and/or proteolytic degradation might provide key events down-stream cysteine protease (caspase) activation in apoptosis induction. We have dealt with this issue by studying apoptosis induced by N-hexanoylsphingosine (C6-Cer) in CHP-100 human neuroepithelioma cells, maintained in complete growth medium. We report that C6-Cer-induced apoptosis occurred predominantly in G1/S phases of the cycle and was associated with RB dephosphorylation, in the setting of negligible Bcl-2 expression. Apoptosis was also associated with poly(ADP-ribose) polymerase (PARP) cleavage, thus indicating activation of CPP32/Yama/apopain (caspase-3); however, while the tripeptide caspase inhibitor Z-Val-Ala-DL-Asp-fluoromethylketone was able to prevent both C6-Cer-induced PARP cleavage and apoptosis, it was ineffective in preventing RB dephosphorylation. Moreover proteolytic RB cleavage occurred only to a marginal extent after C6-Cer treatment. These results indicate that apoptosis induced by ceramide in CHP-100 cells is caspase-mediated, but RB post-translational modification does not provide a key step, downstream caspase activation, in apoptosis execution.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Spinedi A,Amendola A,Di Bartolomeo S,Piacentini M

doi

10.1006/bbrc.1998.8184

subject

Has Abstract

pub_date

1998-02-24 00:00:00

pages

852-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98184-0

journal_volume

243

pub_type

杂志文章

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