Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1997-10-17
pubmed:abstractText
Hydrogen peroxide (H2O2) has been implicated in many stress conditions. Control of H2O2 levels is complex and dissection of mechanisms generating and relieving H2O2 stress is difficult, particularly in intact plants. We have used transgenic tobacco with approximately 10% wild-type catalase activity to study the role of catalase and effects of H2O2 stress in plants. Catalase-deficient plants showed no visible disorders at low light, but in elevated light rapidly developed white necrotic lesions on the leaves. Lesion formation required photorespiratory activity since damage was prevented under elevated CO2. Accumulation of H2O2 was not detected during leaf necrosis. Alternative H2O2-scavenging mechanisms may have compensated for reduced catalase activity, as shown by increased ascorbate peroxidase and glutathione peroxidase levels. Leaf necrosis correlated with accumulation of oxidized glutathione and a 4-fold decrease in ascorbate, indicating that catalase is critical for maintaining the redox balance during oxidative stress. Such control may not be limited to peroxisomal H2O2 production. Catalase functions as a cellular sink for H2O2, as evidenced by complementation of catalase deficiency by exogenous catalase, and comparison of catalase-deficient and control leaf discs in removing external H2O2. Stress analysis revealed increased susceptibility of catalase-deficient plants to paraquat, salt and ozone, but not to chilling.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-14731626, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-1536938, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-16347719, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-16668520, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-16668524, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-16668591, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-7569979, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-7672510, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-7789534, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-7937973, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-7954825, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8351519, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8552710, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8626753, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8658196, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8723347, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8736777, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8736783, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-8811865, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-9383446, http://linkedlifedata.com/resource/pubmed/commentcorrection/9305623-949968
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Ascorbate Peroxidases, http://linkedlifedata.com/resource/pubmed/chemical/Ascorbic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide, http://linkedlifedata.com/resource/pubmed/chemical/Catalase, http://linkedlifedata.com/resource/pubmed/chemical/Chlorophyll, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Disulfide, http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide, http://linkedlifedata.com/resource/pubmed/chemical/Ozone, http://linkedlifedata.com/resource/pubmed/chemical/Paraquat, http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases, http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4806-16
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:9305623-Ascorbate Peroxidases, pubmed-meshheading:9305623-Ascorbic Acid, pubmed-meshheading:9305623-Carbon Dioxide, pubmed-meshheading:9305623-Catalase, pubmed-meshheading:9305623-Chlorophyll, pubmed-meshheading:9305623-Cold Temperature, pubmed-meshheading:9305623-Glutathione, pubmed-meshheading:9305623-Glutathione Disulfide, pubmed-meshheading:9305623-Hydrogen Peroxide, pubmed-meshheading:9305623-Light, pubmed-meshheading:9305623-Oxidative Stress, pubmed-meshheading:9305623-Ozone, pubmed-meshheading:9305623-Paraquat, pubmed-meshheading:9305623-Peroxidases, pubmed-meshheading:9305623-Photosynthesis, pubmed-meshheading:9305623-Plant Leaves, pubmed-meshheading:9305623-Plants, Genetically Modified, pubmed-meshheading:9305623-Plants, Toxic, pubmed-meshheading:9305623-Reactive Oxygen Species, pubmed-meshheading:9305623-Sodium Chloride, pubmed-meshheading:9305623-Tobacco
pubmed:year
1997
pubmed:articleTitle
Catalase is a sink for H2O2 and is indispensable for stress defence in C3 plants.
pubmed:affiliation
Department of Genetics, Flanders Interuniversity Institute for Biotechnology (VIB), Universiteit Gent, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't