New red-shifted fluorescent biosensor for monitoring intracellular redox changes.
Identifieur interne : 000145 ( Main/Exploration ); précédent : 000144; suivant : 000146New red-shifted fluorescent biosensor for monitoring intracellular redox changes.
Auteurs : Claudia Vanesa Piattoni [Uruguay] ; Florencia Sardi [Uruguay] ; Florencia Klein [Uruguay] ; Sergio Pantano [Uruguay] ; Mariela Bollati-Fogolin [Uruguay] ; Marcelo Comini [Uruguay]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Espace intracellulaire, Glutathion, Protéines luminescentes.
- méthodes : Techniques de biocapteur.
- Cellules HEK293, Cellules HeLa, Dosage biologique, Fluorescence, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutathione, Luminescent Proteins.
- metabolism : Intracellular Space.
- methods : Biosensing Techniques.
- Biological Assay, Fluorescence, HEK293 Cells, HeLa Cells, Humans, Oxidation-Reduction.
Abstract
Maintenance of intracellular redox homeostasis is critical for cell survival, proliferation, differentiation, and signaling. In this regard, major changes in the intracellular redox milieu may lead to cell death whereas subtle increases in the level of certain oxidizing species may act as signals that regulate a plethora of cellular processes. Redox-sensitive variants of green fluorescent proteins (roGFP2 and rxYFP) were developed and proved useful to monitor intracellular redox changes in a non-invasive and online manner. With the aim to extend the spectral range of the fluorescent redox biosensors, we here describe the generation, biochemical characterization and biological validation of a new redox reporter based on the red-shifted mRuby2 protein (rxmRuby2). Spectrofluorimetric analysis performed with the recombinant biosensor shows a reversible redox response produced by two redox-active cysteine residues predicted by molecular modeling. rxmRuby2 is highly selective for the couple glutathione/glutathione disulfide in the presence of the oxidoreductase glutaredoxin. The estimated redox potential of rxmRuby2 (E° -265 ± 22 mV) makes it suitable for its use in reducing subcellular compartments. Titration assays demonstrated the capacity of rxmRuby2 to monitor redox changes within a physiological pH range. rxmRuby2 responded sensitively and reversibly to different redox stimuli applied to HeLa and HEK293 cells expressing transiently and/or stable the biosensor. Fusing rxmRuby2 to the Clover fluorescent protein allowed normalization of the redox signal to the expression level of the reporter protein and/or to other factors that may affect fluorescence. The new red-shifted redox biosensor show promises for deep-tissue and in vivo imaging applications.
DOI: 10.1016/j.freeradbiomed.2019.01.035
PubMed: 30735840
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: mcomini@pasteur.edu.uy.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biological Assay (MeSH)</term><term>Biosensing Techniques (methods)</term><term>Fluorescence (MeSH)</term><term>Glutathione (metabolism)</term><term>HEK293 Cells (MeSH)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Intracellular Space (metabolism)</term><term>Luminescent Proteins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293 (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Dosage biologique (MeSH)</term><term>Espace intracellulaire (métabolisme)</term><term>Fluorescence (MeSH)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines luminescentes (métabolisme)</term><term>Techniques de biocapteur (méthodes)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Luminescent Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Space</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Biosensing Techniques</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espace intracellulaire</term><term>Glutathion</term><term>Protéines luminescentes</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Techniques de biocapteur</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Assay</term><term>Fluorescence</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Cellules HeLa</term><term>Dosage biologique</term><term>Fluorescence</term><term>Humains</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Maintenance of intracellular redox homeostasis is critical for cell survival, proliferation, differentiation, and signaling. In this regard, major changes in the intracellular redox milieu may lead to cell death whereas subtle increases in the level of certain oxidizing species may act as signals that regulate a plethora of cellular processes. Redox-sensitive variants of green fluorescent proteins (roGFP2 and rxYFP) were developed and proved useful to monitor intracellular redox changes in a non-invasive and online manner. With the aim to extend the spectral range of the fluorescent redox biosensors, we here describe the generation, biochemical characterization and biological validation of a new redox reporter based on the red-shifted mRuby2 protein (rxmRuby2). Spectrofluorimetric analysis performed with the recombinant biosensor shows a reversible redox response produced by two redox-active cysteine residues predicted by molecular modeling. rxmRuby2 is highly selective for the couple glutathione/glutathione disulfide in the presence of the oxidoreductase glutaredoxin. The estimated redox potential of rxmRuby2 (E° -265 ± 22 mV) makes it suitable for its use in reducing subcellular compartments. Titration assays demonstrated the capacity of rxmRuby2 to monitor redox changes within a physiological pH range. rxmRuby2 responded sensitively and reversibly to different redox stimuli applied to HeLa and HEK293 cells expressing transiently and/or stable the biosensor. Fusing rxmRuby2 to the Clover fluorescent protein allowed normalization of the redox signal to the expression level of the reporter protein and/or to other factors that may affect fluorescence. The new red-shifted redox biosensor show promises for deep-tissue and in vivo imaging applications.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30735840</PMID><DateCompleted><Year>2020</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>134</Volume><PubDate><Year>2019</Year><Month>04</Month></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>New red-shifted fluorescent biosensor for monitoring intracellular redox changes.</ArticleTitle><Pagination><MedlinePgn>545-554</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(18)31609-5</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2019.01.035</ELocationID><Abstract><AbstractText>Maintenance of intracellular redox homeostasis is critical for cell survival, proliferation, differentiation, and signaling. In this regard, major changes in the intracellular redox milieu may lead to cell death whereas subtle increases in the level of certain oxidizing species may act as signals that regulate a plethora of cellular processes. Redox-sensitive variants of green fluorescent proteins (roGFP2 and rxYFP) were developed and proved useful to monitor intracellular redox changes in a non-invasive and online manner. With the aim to extend the spectral range of the fluorescent redox biosensors, we here describe the generation, biochemical characterization and biological validation of a new redox reporter based on the red-shifted mRuby2 protein (rxmRuby2). Spectrofluorimetric analysis performed with the recombinant biosensor shows a reversible redox response produced by two redox-active cysteine residues predicted by molecular modeling. rxmRuby2 is highly selective for the couple glutathione/glutathione disulfide in the presence of the oxidoreductase glutaredoxin. The estimated redox potential of rxmRuby2 (E° -265 ± 22 mV) makes it suitable for its use in reducing subcellular compartments. Titration assays demonstrated the capacity of rxmRuby2 to monitor redox changes within a physiological pH range. rxmRuby2 responded sensitively and reversibly to different redox stimuli applied to HeLa and HEK293 cells expressing transiently and/or stable the biosensor. Fusing rxmRuby2 to the Clover fluorescent protein allowed normalization of the redox signal to the expression level of the reporter protein and/or to other factors that may affect fluorescence. The new red-shifted redox biosensor show promises for deep-tissue and in vivo imaging applications.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Piattoni</LastName><ForeName>Claudia Vanesa</ForeName><Initials>CV</Initials><AffiliationInfo><Affiliation>Cell Biology Unit, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sardi</LastName><ForeName>Florencia</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Klein</LastName><ForeName>Florencia</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>BioMolecular Simulation Group, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pantano</LastName><ForeName>Sergio</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>BioMolecular Simulation Group, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bollati-Fogolin</LastName><ForeName>Mariela</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Cell Biology Unit, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo, Mataojo 2020, CP 11400, Montevideo, Uruguay. Electronic address: mcomini@pasteur.edu.uy.</Affiliation></AffiliationInfo></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>2019</Year><Month>02</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008164">Luminescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001681" MajorTopicYN="N">Biological Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015374" MajorTopicYN="N">Biosensing Techniques</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005453" MajorTopicYN="Y">Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042541" MajorTopicYN="N">Intracellular Space</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Clover</Keyword><Keyword MajorTopicYN="Y">Glutathione</Keyword><Keyword MajorTopicYN="Y">Molecular simulation</Keyword><Keyword MajorTopicYN="Y">Oxidation</Keyword><Keyword MajorTopicYN="Y">Ruby</Keyword><Keyword MajorTopicYN="Y">Thiol</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>09</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>01</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>01</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>2</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>2</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30735840</ArticleId><ArticleId IdType="pii">S0891-5849(18)31609-5</ArticleId><ArticleId IdType="doi">10.1016/j.freeradbiomed.2019.01.035</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Uruguay</li></country></list><tree><country name="Uruguay"><noRegion><name sortKey="Piattoni, Claudia Vanesa" sort="Piattoni, Claudia Vanesa" uniqKey="Piattoni C" first="Claudia Vanesa" last="Piattoni">Claudia Vanesa Piattoni</name></noRegion><name sortKey="Bollati Fogolin, Mariela" sort="Bollati Fogolin, Mariela" uniqKey="Bollati Fogolin M" first="Mariela" last="Bollati-Fogolin">Mariela Bollati-Fogolin</name><name sortKey="Comini, Marcelo" sort="Comini, Marcelo" uniqKey="Comini M" first="Marcelo" last="Comini">Marcelo Comini</name><name sortKey="Klein, Florencia" sort="Klein, Florencia" uniqKey="Klein F" first="Florencia" last="Klein">Florencia Klein</name><name sortKey="Pantano, Sergio" sort="Pantano, Sergio" uniqKey="Pantano S" first="Sergio" last="Pantano">Sergio Pantano</name><name sortKey="Sardi, Florencia" sort="Sardi, Florencia" uniqKey="Sardi F" first="Florencia" last="Sardi">Florencia Sardi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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