Linked Life Data

19822524

Source:http://linkedlifedata.com/resource/pubmed/id/19822524

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
51
pubmed:dateCreated
2009-12-16
pubmed:abstractText
Heavy metals are known to generate reactive oxygen species that lead to the oxidation and fragmentation of proteins, which become toxic when accumulated in the cell. In this study, we investigated the role of the proteasome during cadmium stress in the leaves of Arabidopsis thaliana plants. Using biochemical and proteomics approaches, we present the first evidence of an active proteasome pathway in plants. We identified and characterized the peptidases acting sequentially downstream from the proteasome in animal cells as follows: tripeptidyl-peptidase II, thimet oligopeptidase, and leucine aminopeptidase. We investigated the proteasome proteolytic pathway response in the leaves of 6-week-old A. thaliana plants grown hydroponically for 24, 48, and 144 h in the presence or absence of 50 mum cadmium. The gene expression and proteolytic activity of the proteasome and the different proteases of the pathway were found to be up-regulated in response to cadmium. In an in vitro assay, oxidized bovine serum albumin and lysozyme were more readily degraded in the presence of 20 S proteasome and tripeptidyl-peptidase II than their nonoxidized form, suggesting that oxidized proteins are preferentially degraded by the Arabidopsis 20 S proteasome pathway. These results show that, in response to cadmium, the 20 S proteasome proteolytic pathway is up-regulated at both RNA and activity levels in Arabidopsis leaves and may play a role in degrading oxidized proteins generated by the stress.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
35412-24
pubmed:dateRevised
2010-12-21
pubmed:meshHeading
pubmed-meshheading:19822524-Aminopeptidases, pubmed-meshheading:19822524-Animals, pubmed-meshheading:19822524-Arabidopsis, pubmed-meshheading:19822524-Arabidopsis Proteins, pubmed-meshheading:19822524-Cadmium, pubmed-meshheading:19822524-Cattle, pubmed-meshheading:19822524-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:19822524-Enzyme Activation, pubmed-meshheading:19822524-Gene Expression Regulation, Enzymologic, pubmed-meshheading:19822524-Gene Expression Regulation, Plant, pubmed-meshheading:19822524-Muramidase, pubmed-meshheading:19822524-Plant Leaves, pubmed-meshheading:19822524-Proteasome Endopeptidase Complex, pubmed-meshheading:19822524-Serine Endopeptidases, pubmed-meshheading:19822524-Serum Albumin, Bovine, pubmed-meshheading:19822524-Stress, Physiological, pubmed-meshheading:19822524-Up-Regulation
pubmed:year
2009
pubmed:articleTitle
Evidence for the Existence in Arabidopsis thaliana of the Proteasome Proteolytic Pathway: ACTIVATION IN RESPONSE TO CADMIUM.
pubmed:affiliation
Laboratoires de Physiologie Cellulaire Végétale, CEA, IRTSV, UMR5168 CNRS/CEA/INRA, Université Joseph Fourier, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't