Abstract
Peroxides generated on peptides and proteins within cells, as a result of radical attack or reaction with singlet oxygen, are longer-lived than H(2)O(2) due to their poor removal by protective enzymes. These peroxides readily oxidize cysteine residues and can inactivate thiol-dependent enzymes. We show here that Trp- and Tyr-derived peptide peroxides, generated by singlet oxygen, inhibit caspase activity in the lysates of apoptotic Jurkat cells. N-Ac-Trp-OMe peroxide was the most effective inhibitor, and was 30-fold more effective than H(2)O(2) under identical conditions. As such, protein peroxides could modulate the progression of apoptosis in cells in which they are generated.
Originalsprog | Engelsk |
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Tidsskrift | FEBS Letters |
Vol/bind | 527 |
Udgave nummer | 1-3 |
Sider (fra-til) | 289-92 |
Antal sider | 4 |
ISSN | 0014-5793 |
Status | Udgivet - 11 sep. 2002 |