Cadmium induced mitochondrial redox changes in germinating pea seed.
Identifieur interne : 000A51 ( Main/Exploration ); précédent : 000A50; suivant : 000A52Cadmium induced mitochondrial redox changes in germinating pea seed.
Auteurs : Moêz Smiri [Tunisie] ; Abdelilah Chaoui ; Nicolas Rouhier ; Chibani Kamel ; Eric Gelhaye ; Jean-Pierre Jacquot ; Ezzedine El FerjaniSource :
- Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine [ 1572-8773 ] ; 2010.
Descripteurs français
- KwdFr :
- Chlorure de cadmium (pharmacologie), Germination (effets des médicaments et des substances chimiques), Germination (physiologie), Glutarédoxines (métabolisme), Glutathione reductase (métabolisme), Graines (enzymologie), Mitochondries (effets des médicaments et des substances chimiques), Mitochondries (métabolisme), NADP (métabolisme), Oxydoréduction (MeSH), Pois (effets des médicaments et des substances chimiques), Pois (enzymologie), Thioredoxin-disulfide reductase (métabolisme).
- MESH :
- effets des médicaments et des substances chimiques : Germination, Mitochondries, Pois.
- enzymologie : Graines, Pois.
- métabolisme : Glutarédoxines, Glutathione reductase, Mitochondries, NADP, Thioredoxin-disulfide reductase.
- pharmacologie : Chlorure de cadmium.
- physiologie : Germination.
- Oxydoréduction.
English descriptors
- KwdEn :
- Cadmium Chloride (pharmacology), Germination (drug effects), Germination (physiology), Glutaredoxins (metabolism), Glutathione Reductase (metabolism), Mitochondria (drug effects), Mitochondria (metabolism), NADP (metabolism), Oxidation-Reduction (MeSH), Peas (drug effects), Peas (enzymology), Seeds (enzymology), Thioredoxin-Disulfide Reductase (metabolism).
- MESH :
- chemical , metabolism : Glutaredoxins, Glutathione Reductase, NADP, Thioredoxin-Disulfide Reductase.
- chemical , pharmacology : Cadmium Chloride.
- drug effects : Germination, Mitochondria, Peas.
- enzymology : Peas, Seeds.
- metabolism : Mitochondria.
- physiology : Germination.
- Oxidation-Reduction.
Abstract
Mitochondria play an essential role in producing the energy required for seedling growth following imbibition. Heavy metals, such as cadmium impair mitochondrial functioning in part by altering redox regulation. The activities of two protein redox systems present in mitochondria, thioredoxin (Trx) and glutaredoxin (Grx), were analysed in the cotyledons and embryo of pea (Pisum sativum L.) germinating seeds exposed to toxic Cd concentration. Compared to controls, Cd-treated germinating seeds showed a decrease in total soluble protein content, but an increase in -SH content. Under Cd stress conditions, Grx and glutathione reductase (GR) activities as well as glutathione (GSH) concentrations decreased both in cotyledons and the embryo. Similar results were obtained with the Trx system: Trx and NADPH-dependent thioredoxin reductase (NTR) activities were not stimulated, whereas total NAD(P) contents diminished in the embryo. However, Cd enhanced the levels of all components of the Trx system in the cotyledons. On the other hand, Cd caused a significant increase in oxidative stress parameters such as the redox ratio of coenzymes (oxidized to reduced forms) and NAD(P)H oxidase activities. These results indicate that Cd induces differential redox responses on different seed tissues. We suggest that neither Grx system nor Trx one may improve the redox status of mitochondrial thiols in the embryo of germinating pea seeds exposed to Cd toxicity, but in the cotyledons the contribution of Trx/NTR/NADPH can be established in despite the vulnerability of the coenzyme pools due to enzymatic oxidation.
DOI: 10.1007/s10534-010-9344-y
PubMed: 20512401
Affiliations:
Links toward previous steps (curation, corpus...)
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xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mitochondria play an essential role in producing the energy required for seedling growth following imbibition. Heavy metals, such as cadmium impair mitochondrial functioning in part by altering redox regulation. The activities of two protein redox systems present in mitochondria, thioredoxin (Trx) and glutaredoxin (Grx), were analysed in the cotyledons and embryo of pea (Pisum sativum L.) germinating seeds exposed to toxic Cd concentration. Compared to controls, Cd-treated germinating seeds showed a decrease in total soluble protein content, but an increase in -SH content. Under Cd stress conditions, Grx and glutathione reductase (GR) activities as well as glutathione (GSH) concentrations decreased both in cotyledons and the embryo. Similar results were obtained with the Trx system: Trx and NADPH-dependent thioredoxin reductase (NTR) activities were not stimulated, whereas total NAD(P) contents diminished in the embryo. However, Cd enhanced the levels of all components of the Trx system in the cotyledons. On the other hand, Cd caused a significant increase in oxidative stress parameters such as the redox ratio of coenzymes (oxidized to reduced forms) and NAD(P)H oxidase activities. These results indicate that Cd induces differential redox responses on different seed tissues. We suggest that neither Grx system nor Trx one may improve the redox status of mitochondrial thiols in the embryo of germinating pea seeds exposed to Cd toxicity, but in the cotyledons the contribution of Trx/NTR/NADPH can be established in despite the vulnerability of the coenzyme pools due to enzymatic oxidation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20512401</PMID><DateCompleted><Year>2011</Year><Month>02</Month><Day>24</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1572-8773</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine</Title><ISOAbbreviation>Biometals</ISOAbbreviation></Journal><ArticleTitle>Cadmium induced mitochondrial redox changes in germinating pea seed.</ArticleTitle><Pagination><MedlinePgn>973-84</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10534-010-9344-y</ELocationID><Abstract><AbstractText>Mitochondria play an essential role in producing the energy required for seedling growth following imbibition. Heavy metals, such as cadmium impair mitochondrial functioning in part by altering redox regulation. The activities of two protein redox systems present in mitochondria, thioredoxin (Trx) and glutaredoxin (Grx), were analysed in the cotyledons and embryo of pea (Pisum sativum L.) germinating seeds exposed to toxic Cd concentration. Compared to controls, Cd-treated germinating seeds showed a decrease in total soluble protein content, but an increase in -SH content. Under Cd stress conditions, Grx and glutathione reductase (GR) activities as well as glutathione (GSH) concentrations decreased both in cotyledons and the embryo. Similar results were obtained with the Trx system: Trx and NADPH-dependent thioredoxin reductase (NTR) activities were not stimulated, whereas total NAD(P) contents diminished in the embryo. However, Cd enhanced the levels of all components of the Trx system in the cotyledons. On the other hand, Cd caused a significant increase in oxidative stress parameters such as the redox ratio of coenzymes (oxidized to reduced forms) and NAD(P)H oxidase activities. These results indicate that Cd induces differential redox responses on different seed tissues. We suggest that neither Grx system nor Trx one may improve the redox status of mitochondrial thiols in the embryo of germinating pea seeds exposed to Cd toxicity, but in the cotyledons the contribution of Trx/NTR/NADPH can be established in despite the vulnerability of the coenzyme pools due to enzymatic oxidation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Smiri</LastName><ForeName>Moêz</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Bio-Physiologie Cellulaires, Faculté des Sciences de Bizerte, 7021, Zarzouna, Tunisie. moez.smiri@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaoui</LastName><ForeName>Abdelilah</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Kamel</LastName><ForeName>Chibani</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>El Ferjani</LastName><ForeName>Ezzedine</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>05</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biometals</MedlineTA><NlmUniqueID>9208478</NlmUniqueID><ISSNLinking>0966-0844</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>J6K4F9V3BA</RegistryNumber><NameOfSubstance UI="D019256">Cadmium Chloride</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019256" MajorTopicYN="N">Cadmium Chloride</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018525" MajorTopicYN="N">Germination</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName 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PubStatus="pubmed"><Year>2010</Year><Month>6</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>2</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20512401</ArticleId><ArticleId IdType="doi">10.1007/s10534-010-9344-y</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Tunisie</li></country></list><tree><noCountry><name sortKey="Chaoui, Abdelilah" sort="Chaoui, Abdelilah" uniqKey="Chaoui A" first="Abdelilah" last="Chaoui">Abdelilah Chaoui</name><name sortKey="El Ferjani, Ezzedine" sort="El Ferjani, Ezzedine" uniqKey="El Ferjani E" first="Ezzedine" last="El Ferjani">Ezzedine El Ferjani</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Kamel, Chibani" sort="Kamel, Chibani" uniqKey="Kamel C" first="Chibani" last="Kamel">Chibani Kamel</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></noCountry><country name="Tunisie"><noRegion><name sortKey="Smiri, Moez" sort="Smiri, Moez" uniqKey="Smiri M" first="Moêz" last="Smiri">Moêz Smiri</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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