Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis

Ge Yuan; Cai Yaomin; Bonneau Laurent; Rotari Vitalie; Danon Antoine; McKenzie Edward A.; McLellan Hazel; Mach Lukas; Gallois Patrick

Conţinutul numărului revistei

Articolul precedent

Articolul urmator

305

Ultima descărcare din IBN:
2023-06-30 05:50

SM ISO690:2012

GE, Yuan, CAI, Yaomin, BONNEAU, Laurent, ROTARI, Vitalie, DANON, Antoine, MCKENZIE, Edward A., MCLELLAN, Hazel, MACH, Lukas, GALLOIS, Patrick. Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis. In: Cell Death and Differentiation, 2016, nr. 9(23), pp. 1493-1501. ISSN 1350-9047. DOI: https://doi.org/10.1038/cdd.2016.34

EXPORT metadate:
Google Scholar
Crossref
CERIF

DataCite
Dublin Core

Cell Death and Differentiation

Numărul 9(23) / 2016 / ISSN 1350-9047 /ISSNe 1476-5403

Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis

DOI:https://doi.org/10.1038/cdd.2016.34

Pag. 1493-1501

Ge Yuan¹, Cai Yaomin²³, Bonneau Laurent², Rotari Vitalie²⁴, Danon Antoine³, McKenzie Edward A.², McLellan Hazel⁵, Mach Lukas⁶, Gallois Patrick²

¹ Ocean University of China,
² University of Manchester,
³ Institut National de la Recherche Agronomique,
⁴ Moldova State University,
⁵ James Hutton Institute, Invergowrie, Dundee,
⁶ University of Natural Resources and Life Sciences, Wien

Disponibil în IBN: 15 august 2022

Descarcă PDF

Rezumat

Programmed cell death (PCD) is used by plants for development and survival to biotic and abiotic stresses. The role of caspases in PCD is well established in animal cells. Over the past 15 years, the importance of caspase-3-like enzymatic activity for plant PCD completion has been widely documented despite the absence of caspase orthologues. In particular, caspase-3 inhibitors blocked nearly all plant PCD tested. Here, we affinity-purified a plant caspase-3-like activity using a biotin-labelled caspase-3 inhibitor and identified Arabidopsis thaliana cathepsin B3 (AtCathB3) by liquid chromatography with tandem mass spectrometry (LC-MS/MS). Consistent with this, recombinant AtCathB3 was found to have caspase-3-like activity and to be inhibited by caspase-3 inhibitors. AtCathepsin B triple-mutant lines showed reduced caspase-3-like enzymatic activity and reduced labelling with activity-based caspase-3 probes. Importantly, AtCathepsin B triple mutants showed a strong reduction in the PCD induced by ultraviolet (UV), oxidative stress (H₂O₂, methyl viologen) or endoplasmic reticulum stress. Our observations contribute to explain why caspase-3 inhibitors inhibit plant PCD and provide new tools to further plant PCD research. The fact that cathepsin B does regulate PCD in both animal and plant cells suggests that this protease may be part of an ancestral PCD pathway pre-existing the plant/animal divergence that needs further characterisation.

Cuvinte-cheie
Amino Acid Sequence, apoptosis, Arabidopsis, Arabidopsis Proteins, Caspase Inhibitors, Cathepsin B, chromatography, High Pressure Liquid, Endoplasmic Reticulum Stress, hydrogen peroxide, oxidative stress, Paraquat, phylogeny, plants, Genetically Modified, Recombinant Proteins, Seedlings, Tandem Mass Spectrometry, Ultraviolet Rays

DataCite XML Export

<?xml version='1.0' encoding='utf-8'?>
<resource xmlns:xsi='http://www.w3.org/2001/XMLSchema-instance' xmlns='http://datacite.org/schema/kernel-3' xsi:schemaLocation='http://datacite.org/schema/kernel-3 http://schema.datacite.org/meta/kernel-3/metadata.xsd'>
<identifier identifierType='DOI'>10.1038/cdd.2016.34</identifier>
<creators>
<creator>
<creatorName>Ge, Y.</creatorName>
<affiliation>Universitatea Ocean din China, China</affiliation>
</creator>
<creator>
<creatorName>Cai, Y.</creatorName>
<affiliation>University of Manchester, Regatul Unit</affiliation>
</creator>
<creator>
<creatorName>Bonneau, L.</creatorName>
<affiliation>University of Manchester, Regatul Unit</affiliation>
</creator>
<creator>
<creatorName>Rotari, V.I.</creatorName>
<affiliation>University of Manchester, Regatul Unit</affiliation>
</creator>
<creator>
<creatorName>Danon, A.</creatorName>
<affiliation>Institut National de la Recherche Agronomique, Franţa</affiliation>
</creator>
<creator>
<creatorName>McKenzie, E.</creatorName>
<affiliation>University of Manchester, Regatul Unit</affiliation>
</creator>
<creator>
<creatorName>McLellan, H.</creatorName>
<affiliation>Institutul James Hutton, Invergowrie, Dundee, Marea Britanie</affiliation>
</creator>
<creator>
<creatorName>Mach, L.</creatorName>
<affiliation>Universitatea de Resurse Naturale și Științe ale Vieții, Viena, Austria</affiliation>
</creator>
<creator>
<creatorName>Gallois, P.</creatorName>
<affiliation>University of Manchester, Regatul Unit</affiliation>
</creator>
</creators>
<titles>
<title xml:lang='en'>Inhibition of cathepsin B by caspase-3 inhibitors blocks programmed cell death in Arabidopsis</title>
</titles>
<publisher>Instrumentul Bibliometric National</publisher>
<publicationYear>2016</publicationYear>
<relatedIdentifier relatedIdentifierType='ISSN' relationType='IsPartOf'>1350-9047</relatedIdentifier>
<subjects>
<subject>Amino Acid Sequence</subject>
<subject>apoptosis</subject>
<subject>Arabidopsis</subject>
<subject>Arabidopsis Proteins</subject>
<subject>Caspase Inhibitors</subject>
<subject>Cathepsin B</subject>
<subject>chromatography</subject>
<subject>High Pressure Liquid</subject>
<subject>Endoplasmic Reticulum Stress</subject>
<subject>hydrogen peroxide</subject>
<subject>oxidative stress</subject>
<subject>Paraquat</subject>
<subject>phylogeny</subject>
<subject>plants</subject>
<subject>Genetically Modified</subject>
<subject>Recombinant Proteins</subject>
<subject>Seedlings</subject>
<subject>Tandem Mass Spectrometry</subject>
<subject>Ultraviolet Rays</subject>
</subjects>
<dates>
<date dateType='Issued'>2016-09-01</date>
</dates>
<resourceType resourceTypeGeneral='Text'>Journal article</resourceType>
<descriptions>
<description xml:lang='en' descriptionType='Abstract'><p>&nbsp;</p><p>Programmed cell death (PCD) is used by plants for development and survival to biotic and abiotic stresses. The role of caspases in PCD is well established in animal cells. Over the past 15 years, the importance of caspase-3-like enzymatic activity for plant PCD completion has been widely documented despite the absence of caspase orthologues. In particular, caspase-3 inhibitors blocked nearly all plant PCD tested. Here, we affinity-purified a plant caspase-3-like activity using a biotin-labelled caspase-3 inhibitor and identified Arabidopsis thaliana cathepsin B3 (AtCathB3) by liquid chromatography with tandem mass spectrometry (LC-MS/MS). Consistent with this, recombinant AtCathB3 was found to have caspase-3-like activity and to be inhibited by caspase-3 inhibitors. AtCathepsin B triple-mutant lines showed reduced caspase-3-like enzymatic activity and reduced labelling with activity-based caspase-3 probes. Importantly, AtCathepsin B triple mutants showed a strong reduction in the PCD induced by ultraviolet (UV), oxidative stress (H<sub>2</sub>O<sub>2</sub>, methyl viologen) or endoplasmic reticulum stress. Our observations contribute to explain why caspase-3 inhibitors inhibit plant PCD and provide new tools to further plant PCD research. The fact that cathepsin B does regulate PCD in both animal and plant cells suggests that this protease may be part of an ancestral PCD pathway pre-existing the plant/animal divergence that needs further characterisation.&nbsp;</p></description>
</descriptions>
<formats>
<format>application/pdf</format>
</formats>
</resource>