Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1996-6-5
pubmed:abstractText
Suspension-cultured cells of Arabidopsis thaliana generated active oxygen species (AOS) (measured by luminol-dependent chemiluminescence) following challenge with the bacterial protein elicitor harpin or the protein kinase activator phorbol 12-myristate 13-acetate. These responses were blocked by inhibitors of superoxide dismutase (SOD), NADPH oxidase and protein kinase. Harpin treatment also resulted in an increase in cell death, a response reduced by inhibitors of AOS generation or AOS scavengers. Extracellular SOD activity was found to be present in cell culture medium. Immunoblotting of Arabidopsis extracts revealed the presence of proteins immunologically related to the human neutrophil NADPH oxidase complex, and cell-free reconstitution assays showed that human neutrophil cytosol combined with Arabidopsis membranes could initiate superoxide generation. These data suggest that the enzyme catalysing the generation of superoxide in elicited Arabidopsis cells is similar to the mammalian NADPH oxidase and that a signalling cascade leading to AOS generation involves protein phosphorylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbazoles, http://linkedlifedata.com/resource/pubmed/chemical/Ditiocarb, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/HrpZ protein, Pseudomonas syringae, http://linkedlifedata.com/resource/pubmed/chemical/Indole Alkaloids, http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Onium Compounds, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species, http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase, http://linkedlifedata.com/resource/pubmed/chemical/Superoxides, http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate, http://linkedlifedata.com/resource/pubmed/chemical/diphenyleneiodonium, http://linkedlifedata.com/resource/pubmed/chemical/harpin protein, Erwinia amylovora, http://linkedlifedata.com/resource/pubmed/chemical/neutrophil cytosolic factor 1, http://linkedlifedata.com/resource/pubmed/chemical/staurosporine aglycone
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
382
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
213-7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8612756-Arabidopsis, pubmed-meshheading:8612756-Bacterial Outer Membrane Proteins, pubmed-meshheading:8612756-Carbazoles, pubmed-meshheading:8612756-Ditiocarb, pubmed-meshheading:8612756-Enzyme Inhibitors, pubmed-meshheading:8612756-Humans, pubmed-meshheading:8612756-Indole Alkaloids, pubmed-meshheading:8612756-NADH, NADPH Oxidoreductases, pubmed-meshheading:8612756-NADPH Oxidase, pubmed-meshheading:8612756-Neutrophils, pubmed-meshheading:8612756-Onium Compounds, pubmed-meshheading:8612756-Phosphoproteins, pubmed-meshheading:8612756-Protein Kinase Inhibitors, pubmed-meshheading:8612756-Protein Kinases, pubmed-meshheading:8612756-Reactive Oxygen Species, pubmed-meshheading:8612756-Superoxide Dismutase, pubmed-meshheading:8612756-Superoxides, pubmed-meshheading:8612756-Tetradecanoylphorbol Acetate
pubmed:year
1996
pubmed:articleTitle
Generation of active oxygen in elicited cells of Arabidopsis thaliana is mediated by a NADPH oxidase-like enzyme.
pubmed:affiliation
Department of Biological Sciences, University of the West of England, Bristol, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't