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Kieffer, P.* ; Schröder, P. ; Dommes, J.* ; Hoffmann, L.* ; Renaut, J.* ; Hausman, J.F.*

Proteomic and enzymatic response of poplar to cadmium stress.

J. Proteomics 72, (Sp. Iss. SI), 379-396 (2009)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
This study highlights proteomic and enzymatic changes in roots and leaves of actively growing poplar plants upon a cadmium stress exposure. Proteomic changes in response to a short-term (14 days), as well as a longer term (56 days) treatment are observed between the different organs. In leaves, stress-related proteins, like heat shock proteins, proteinases and pathogenesis-related proteins increased in abundance. A response similar to a hypersensitive response upon plant-pathogen interaction seemed to be induced. Concerning roots it appeared that the metabolic impact of cadmium was more deleterious than in leaves. This is evidenced by the early increase in abundance of many typical stress-related proteins like heat shock proteins, or glutathione-S-transferases, while most proteins from the primary metabolism (glycolysis, tricarboxylic acid cycle, nitrogen metabolism, sulfur metabolism) were severely decreased in abundance. Additionally the impact of cadmium on the glutathione metabolism could be assessed by activity assays of several important enzymes. Cadmium treatment had an inhibitory effect on glutathione reductase and ascorbate peroxidase in leaves, but not in roots. Conversely, glutathione-S-transferase showed a higher activity (and abundance) in roots but not in leaves.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Cadmium; Enzymatic activity assays; Roots; Leaves; Glutathione-S-transferase; DIGE; heavy-metal accumulation; glutathione-s-transferases; arabidopsis-thaliana; biomass production; oxidative stress; clonal variation; coppice culture; plants; toxicity; tolerance
ISSN (print) / ISBN 1874-3919
e-ISSN 1876-7737
Journal Journal of Proteomics
Quellenangaben Volume: 72, Issue: 3, Pages: 379-396, Article Number: , Supplement: (Sp. Iss. SI)
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Research Unit Microbe-Plant Interactions (AMP)