The presence and subcellular localization of caspase 3-like proteinases in plant cells
article
Caspases play a very important role in initiating and executing apoptotic processes in animal cells. In this study we show that plant mitochondria were able to initiate the activation of caspase 3 in a Xenopus cell free system. Caspase 3-like activity was found to be present in plant cells and could only be inhibited by the specific caspase 3 inhibitor N-acetyl-Asp-Glu-Val-Asp-fluoromethylketone (Ac-DEVD-fmk) and not by cysteine protease inhibitors. By micro-injection of the caspase 3 substrate in living Chara cells we showed that caspase 3-like activity was mainly present in the cytosol rather than in the vacuole. This is the first time that in vivo caspase 3-like activity has been demonstrated in plants. Copyright (C) 2000 Federation of European Biochemical Societies. Chemicals/CAS: Caspase 3, EC 3.4.22.-; Caspases, EC 3.4.22.-; Detergents; Octoxynol, 9002-93-1; Plant Proteins; Protease Inhibitors; Sodium Chloride, 7647-14-5
Topics
ApoptosisCharaMicro-injectionMitochondrioncysteine proteinase inhibitorpolypeptideproteinase inhibitortriton x 100cellular distributionenzyme activationfluorescencemitochondrionnonhumanplant cellXenopusAnimalsCaspase 3CaspasesCell-Free SystemCytosolDetergentsDose-Response Relationship, DrugEnzyme ActivationHordeumHydrogen-Ion ConcentrationMicroinjectionsMicroscopy, FluorescenceOctoxynolPlant ProteinsPlantsProtease InhibitorsSodium ChlorideVacuoles
TNO Identifier
235592
ISSN
00145793
Source
FEBS Letters, 475(2), pp. 139-144.
Pages
139-144