- H.P. Esse van (1)
- F.J.M. Harren (1)
- F. Harren (1)
- E.T. Iakimova (3)
- V.M. Kapchina-Toteva (4)
- J.W. Klooster van t (1)
- L.J. Laarhoven (1)
- B.P.H.J. Thomma (1)
- J.J.M. Vervoort (1)
- P.J.G.M. Wit de (1)
- E.J. Woltering (7)
- K.A. Yadeta (1)
- E.T. Yakimova (1)
- Z.P. Yordanova (2)
Mastoparan-induced programmed cell death in the unicellular alga Chlamydomonas reinhardtti
Yordanova, Z.P. ; Woltering, E.J. ; Kapchina-Toteva, V.M. ; Iakimova, E.T. - \ 2013
Annals of Botany 111 (2013)2. - ISSN 0305-7364 - p. 191 - 205.
caspase-like activity - vacuolar processing enzyme - tomato suspension cells - hypersensitive response - green-alga - tracheary elements - oxidative burst - phospholipase-c - apoptotic-death - papaver-rhoeas
The present study was focused on the elucidation of stress-induced cell death signaling events in the unicellular alga Chlamydomonas reinhardtii exposed to treatment with wasp venom mastoparan. By applying pharmacological approach with specific inhibitors, we have investigated the involvement of ethylene, nitric oxide and lipid signaling in MP-treated C. reinhardtii. Superior sensitive laser-based detectors were used for real-time measurement of trace amounts of ethylene and nitric oxide. The morphological features in the cells undergoing programmed cell death were detected by using laser-scanning confocal microscopy. Data showed that mastoparan induces programmed cell death in C. reinhardtii 137 C(+) that is associated with phospholipid signaling, including phospholipases C and D, ethylene and nitric oxide and, the dead cells express apoptotic-like cellular disintegration, involving cytoplasm shrinkage and condensation of the nucleus.
Death proteases: alive and kicking
Woltering, E.J. - \ 2010
Trends in Plant Science 15 (2010)4. - ISSN 1360-1385 - p. 185 - 188.
programmed cell-death - caspase-like activity - plant embryogenesis - arabidopsis
Two recent discoveries significantly add to our understanding of plant programmed cell death (PCD). Hatsugai et al. showed that cell death is dependent on proper proteasome functioning. Sundström et al. showed that the in vivo substrate of a type II metacaspase is associated with cell viability. Both findings are major breakthroughs within the plant PCD field and highlight that the plant cell death machinery apparently employs a wide range of structurally unrelated proteases that, surprisingly, show a caspase-like preference for specific (evolutionarily conserved) substrates
Alternaria alternata AT Toxin Induces Programmed Cell Death in Tobacco
Yakimova, E.T. ; Yordanova, Z.P. ; Kapchina-Toteva, V.M. ; Woltering, E.J. - \ 2009
Journal of Phytopathology 157 (2009)10. - ISSN 0931-1785 - p. 592 - 601.
caspase-like activity - plant-disease resistance - host-specific toxin - hypersensitive response - aal-toxin - lipid-peroxidation - hydrogen-peroxide - oxidative burst - polyamines - pathogens
Detached tobacco leaves were infiltrated with an AT toxin preparation from the foliar pathogen Alternaria alternata tobacco pathotype. The AT toxin preparation caused formation of necrotic lesions within 5 days post-infiltration in a concentration-dependent manner. Cell death was accompanied by increased levels of the stress metabolites hydrogen peroxide, malondialdehyde, free proline and by enhanced total protease activity. Lesion development and the production of stress metabolites were suppressed if the infiltration site was pre-infiltrated with caspase-specific peptide inhibitors (irreversible caspase-1 inhibitor acyl-Tyr-Val-Ala-Asp-chloromethylketone (Ac-YVAD-CMK) and the broad range caspase inhibitor benzyoxycarbonyl-Asp-2,6-dichlorobenzoyloxymethylketone (Z-Asp-CH2-DCB)), the serine protease inhibitor N alpha-p-tosyl-L-lysine chloromethylketone and the polyamine spermine. Extensive accumulation of reactive oxygen species (ROS), as determined by staining with 3-3'-diaminobenzidine and 2',7'-dichlorofluorescein diacetate, was found in the AT toxin-challenged lesions. The data show that AT toxin-induced cell death in tobacco is a type of programmed cell death in which caspase-like proteases and ROS signalling play a prominent role.
Cadmium toxicity in cultured tomato cells - Role of ethylene, proteases and oxidative stress in cell death signaling
Iakimova, E.T. ; Woltering, E.J. ; Kapchina-Toteva, V.M. ; Harren, F.J.M. ; Cristescu, S.M. - \ 2008
Cell Biology International 32 (2008)12. - ISSN 1065-6995 - p. 1521 - 1529.
disease resistance response - caspase-like activity - hydrogen-peroxide - phytochelatin accumulation - phosphatidic-acid - suspension cells - tobacco cells - nitric-oxide - apoptosis - plants
Our aim was to investigate the ability of cadmium to induce programmed cell death in tomato suspension cells and to determine the involvement of proteolysis, oxidative stress and ethylene. Tomato suspension cells were exposed to treatments with CdSO4 and cell death was calculated after fluorescein diacetate staining of the living cells. Ethylene was measured in a flow-through system using a laser-driven photo acoustic detector; hydrogen peroxide was determined by chemiluminescence in a ferricyanide-catalysed oxidation of luminol. We have demonstrated that cadmium induces cell death in tomato suspension cells involving caspase-like proteases, indicating that programmed cell death took place. Using range of inhibitors, we found that cysteine and serine peptidases, oxidative stress, calcium and ethylene are players in the cadmium-induced cell death signaling. Cadmium-induced cell death in tomato suspension cells exhibits morphological and biochemical similarities to plant hypersensitive response and to cadmium effects in animal systems.
The Cladosporium fulvum virulence protein Avr2 inhibits host proteases required for basal defense
Esse, H.P. van; Klooster, J.W. van t; Bolton, M.D. ; Yadeta, K.A. ; Baarlen, P. van; Boeren, S. ; Vervoort, J.J.M. ; Wit, P.J.G.M. de; Thomma, B.P.H.J. - \ 2008
The Plant Cell 20 (2008)7. - ISSN 1040-4651 - p. 1948 - 1963.
programmed cell-death - cf-2-dependent disease resistance - syringae effector avrrpt2 - caspase-like activity - avirulence gene avr9 - arabidopsis-thaliana - hypersensitive response - cysteine proteases - plant-pathogen - molecular-mechanisms
Cladosporium fulvum (syn. Passalora fulva) is a biotrophic fungal pathogen that causes leaf mold of tomato (Solanum lycopersicum). During growth in the apoplast, the fungus establishes disease by secreting effector proteins, 10 of which have been characterized. We have previously shown that the Avr2 effector interacts with the apoplastic tomato Cys protease Rcr3, which is required for Cf-2¿mediated immunity. We now show that Avr2 is a genuine virulence factor of C. fulvum. Heterologous expression of Avr2 in Arabidopsis thaliana causes enhanced susceptibility toward extracellular fungal pathogens, including Botrytis cinerea and Verticillium dahliae, and microarray analysis showed that Avr2 expression triggers a global transcriptome reflecting pathogen challenge. Cys protease activity profiling showed that Avr2 inhibits multiple extracellular Arabidopsis Cys proteases. In tomato, Avr2 expression caused enhanced susceptibility toward Avr2-defective C. fulvum strains and also toward B. cinerea and V. dahliae. Cys protease activity profiling in tomato revealed that, in this plant also, Avr2 inhibits multiple extracellular Cys proteases, including Rcr3 and its close relative Pip1. Finally, silencing of Avr2 significantly compromised C. fulvum virulence on tomato. We conclude that Avr2 is a genuine virulence factor of C. fulvum that inhibits several Cys proteases required for plant basal defense.
Physiology and molecular biology of petal senescence
Doorn, W.G. van; Woltering, E.J. - \ 2008
Journal of Experimental Botany 59 (2008)3. - ISSN 0022-0957 - p. 453 - 480.
programmed cell-death - dianthus-caryophyllus l. - carnation flower senescence - caspase-like activity - sandersonia-aurantiaca flowers - ethylene-insensitive flowers - vacuolar processing enzyme - protease gene-expression - ipomoea-tricolor cav - leaf senescence
Petal senescence is reviewed, with the main emphasis on gene expression in relation to physiological functions. Autophagy seems to be the major mechanism for large-scale degradation of macromolecules, but it is still unclear if it contributes to cell death. Depending on the species, petal senescence is controlled by ethylene or is independent of this hormone. EIN3-like (EIL) transcription factors are crucial in ethylene-regulated senescence. The presence of adequate sugar levels in the cell delays senescence and prevents an increase in the levels of EIL mRNA and the subsequent up-regulation of numerous senescence-associated genes. A range of other transcription factors and regulators are differentially expressed in ethylene-sensitive and ethylene-insensitive petal senescence. Ethylene-independent senescence is often delayed by cytokinins, but it is still unknown whether these are natural regulators. A role for caspase-like enzymes or metacaspases has as yet not been established in petal senescence, and a role for proteins released by organelles such as the mitochondrion has not been shown. The synthesis of sugars, amino acids, and fatty acids, and the degradation of nucleic acids, proteins, lipids, fatty acids, and cell wall components are discussed. It is claimed that there is not enough experimental support for the widely held view that a gradual increase in cell leakiness, resulting from gradual plasma membrane degradation, is an important event in petal senescence. Rather, rupture of the vacuolar membrane and subsequent rapid, complete degradation of the plasma membrane seems to occur. This review recommends that more detailed analysis be carried out at the level of cells and organelles rather than at that of whole petals
Involvement of ethylene and lipid signalling in cadmium-induced programmed cell death in tomato suspension cells
Iakimova, E.T. ; Kapchina-Toteva, V.M. ; Laarhoven, L.J. ; Harren, F. ; Woltering, E.J. - \ 2006
Plant Physiology and Biochemistry 44 (2006)10. - ISSN 0981-9428 - p. 581 - 589.
caspase-like activity - phosphatidic-acid - hydrogen-peroxide - tobacco cells - induced apoptosis - plants - activation - release - stress - phytochelatins
Cadmium-induced cell death was studied in suspension-cultured tomato (Lycopersicon esculentum Mill.) cells (line MsK8) treated with CdSO4. Within 24 h, cadmium treatment induced cell death in a concentration-dependent manner. Cell cultures showed recovery after 2¿3 days which indicates the existence of an adaptation mechanism. Cadmium-induced cell death was alleviated by the addition of sub ¿M concentrations of peptide inhibitors specific to human caspases indicating that cell death proceeds through a mechanism with similarities to animal programmed cell death (PCD, apoptosis). Cadmium-induced cell death was accompanied by an increased production of hydrogen peroxide (H2O2) and simultaneous addition of antioxidants greatly reduced cell death. Inhibitors of phospholipase C (PLC) and phospholipase D (PLD) signalling pathway intermediates reduced cadmium-induced cell death. Treatment with the G-protein activator mastoparan and a cell permeable analogue of the lipid signal second messenger phosphatidic acid (PA) induced cell death. Ethylene, while not inducing cell death when applied alone, stimulated cadmium-induced cell death. Application of the ethylene biosynthesis inhibitor aminoethoxy vinylglycine (AVG) reduced cadmium-induced cell death, and this effect was alleviated by simultaneous treatment with ethylene. Together the results show that cadmium induces PCD exhibiting apoptotic-like features. The cell death process requires increased H2O2 production and activation of PLC, PLD and ethylene signalling pathways
Death proteases come alive
Woltering, E.J. - \ 2004
Trends in Plant Science 9 (2004)10.. - ISSN 1360-1385 - p. 469 - 472.
programmed cell-death - caspase-like activity - apoptosis - gene - p35 - involvement - expression - inhibitors - resistance - disease
Cell death in plants exhibits morphological features comparable to caspase-mediated apoptosis in animals, suggesting that plant cell death is executed by (caspase-like) proteases. However, to date, no caspase homologues have been identified in plants and therefore the existence and nature of these plant caspase-like proteases is the subject of much debate. The recent characterization of cell death-associated plant proteases with aspartate-specific cleavage activity demonstrates the involvement in plant programmed cell death of proteolytic activities functionally resembling animal caspases. These findings might explain the observed similarity in cell death morphology between animal and plant cells.