FEBS Letters | |
The presence and subcellular localization of caspase 3‐like proteinases in plant cells | |
Berecki, Géza2  Bruin, Wouter1  Korthout, Henrie A.A.J.1  van Duijn, Bert1  Wang, Mei1  | |
[1] Center for Phytotechnology UL/TNO, TNO Department of Applied Plant Sciences, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands;Center for Phytotechnology UL/TNO, Institute of Molecular Plant Sciences, Leiden, The Netherlands | |
关键词: Caspase 3; Mitochondrion; Micro-injection; Apoptosis; Plant; Chara; Ac-DEVD-AMC; N-acetyl-Asp-Glu-Val-Asp-7-amino-4-methylcoumarin; Ac-YVAD-AMC; N-acetyl-Tyr-Val-Ala-Asp-7-amino-4-methylcoumarin; APW; artificial pond water; DAF; days after flowering; d-ft; dextran conjugated fluorescein-tetramethylrhodamine; DTT; dithiothreitol; fmk; fluoromethylketone; EDTA; ethylenediaminetetraacetic acid; HR; hypersensitive response; PARP; poly-(ADP-ribose) polymerase; PCD; programmed cell death; PMSF; phenylmethylsulfonyl fluoride; PVP; polyvinylpyrrolidone; | |
DOI : 10.1016/S0014-5793(00)01643-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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