The presence and subcellular localization of caspase 3-like proteinases in plant cells.
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.
Korthout
H A
HA
Center for Phytotechnology UL/TNO, TNO Department of Applied Plant Sciences, Leiden, The Netherlands. korthout@voeding.tno.nl
Berecki
G
G
Bruin
W
W
van Duijn
B
B
Wang
M
M
D000818:Animals; D053148:Caspase 3; D020169:Caspases / Q000096:biosynthesis* / Q000737:chemistry*; D002474:Cell-Free System; D003600:Cytosol / Q000201:enzymology; D003902:Detergents / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D004789:Enzyme Activation; D001467:Hordeum / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008845:Microinjections; D008856:Microscopy, Fluorescence; D017830:Octoxynol / Q000494:pharmacology; D010940:Plant Proteins / Q000096:biosynthesis* / Q000737:chemistry*; D010944:Plants / Q000201:enzymology; D011480:Protease Inhibitors / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D014617:Vacuoles / Q000201:enzymology; D014981:Xenopus
D003902:Detergents; D010940:Plant Proteins; D011480:Protease Inhibitors; D012965:Sodium Chloride; D017830:Octoxynol; D053148:Caspase 3; D020169:Caspases