Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4961
Title: Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: a cell biochemical and proteomic investigation.
Authors: Magi, Barbara
Ettorre, A
Liberatori, S
Bini, Luca
Andreassi, Marco 
Frosali, S
Neri, P
Pallini, Vitaliano
DI STEFANO, A.
Issue Date: 2004
Project: None 
Journal: CELL DEATH AND DIFFERENTIATION
Abstract: 
We previously reported that photodynamic therapy (PDT) using Purpurin-18 (Pu-18) induces apoptosis in HL60 cells. Using flow cytometry, two-dimensional electrophoresis coupled with immunodetection of carbonylated proteins and mass spectrometry, we now show that PDT-induced apoptosis is associated with increased reactive oxygen species generation, glutathione depletion, changes in mitochondrial transmembrane potential, simultaneous downregulation of mitofilin and carbonylation of specific proteins: glucoseregulated protein-78, heat-shock protein 60, heat-shock protein cognate 71, phosphate disulphide isomerase, calreticulin, b-actin, tubulin-a-1-chain and enolase-a. Interestingly, all carbonylated proteins except calreticulin and enolase-a showed a pI shift in the proteome maps. Our results suggest that PDT with Pu-18 perturbs the normal redox balance and shifts HL60 cells into a state of oxidative stress, which systematically induces the carbonylation of specific chaperones. As these proteins normally produce a prosurvival signal during oxidative stress, we hypothesize that their carbonylation represents a signalling mechanism for apoptosis induced by PDT.
Description: 
37249
URI: http://hdl.handle.net/20.500.12779/4961
ISSN: 1350-9047
DOI: 10.1038/sj.cdd.4401427
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