| Literature DB >> 12927600 |
Cinzia Domenicotti1, Barbara Marengo, Daniela Verzola, Giacomo Garibotto, Nicola Traverso, Stefania Patriarca, Giuseppe Maloberti, Damiano Cottalasso, Giuseppe Poli, Mario Passalacqua, Edon Melloni, Maria Adelaide Pronzato, Umberto Maria Marinari.
Abstract
Protein kinases C (PKCs) are a family of isoenzymes sensitive to oxidative modifications and involved in the transduction signal pathways that regulate cell growth. As such, they can act as cellular sensors able to intercept intracellular redox changes and promote the primary adaptive cell response. In this study, we have demonstrated that PKC isoforms are specifically influenced by the amount of intracellular glutathione (GSH). The greatest GSH depletion is associated with a maximal reactive oxygen species (ROS) production and accompanied by an increase in the activity of the delta isoform and a concomitant inactivation of alpha. ROS generation induced early morphological changes in GSH-depleted neuroblastoma cells characterized, at the intracellular level, by the modulation of PKC-delta activity that was involved in the pathway leading to apoptosis. When cells were pretreated with rottlerin, their survival was improved by the ability of this compound to inhibit the activity of PKC-delta and to counteract ROS production. These results define a novel role of PKC-delta in the cell signaling pathway triggered by GSH loss normally associated with many neurodegenerative diseases and clinically employed in the treatment of neuroblastoma.Entities:
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Year: 2003 PMID: 12927600 DOI: 10.1016/s0891-5849(03)00332-0
Source DB: PubMed Journal: Free Radic Biol Med ISSN: 0891-5849 Impact factor: 7.376