An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo

Autores
Sanchez Lopez, Carolina; Labadie, Natalia; Lombardo, Veronica Andrea; Biglione, Franco Agustín; Manta, Bruno; Jacob, Reeba; Gladyshev, Vadim; Abdelilah Seyfried, Salim; Selenko, Philipp; Binolfi, Andrés
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Oxidation of protein methionines to methionine-sulfoxides (MetOx) is associated with several age-related diseases. In healthy cells, MetOx is reduced to methionine by two families of conserved methionine sulfoxide reductase enzymes, MSRA and MSRB that specifically target the S- or R-diastereoisomers of methionine-sulfoxides, respectively. To directly interrogate MSRA and MSRB functions in cellular settings, we developed an NMR-based biosensor that we call CarMetOx to simultaneously measure both enzyme activities in single reaction setups. We demonstrate the suitability of our strategy to delineate MSR functions in complex biological environments, including cell lysates and live zebrafish embryos. Thereby, we establish differences in substrate specificities between prokaryotic and eukaryotic MSRs and introduce CarMetOx as a highly sensitive tool for studying therapeutic targets of oxidative stress-related human diseases and redox regulated signaling pathways.
Fil: Sanchez Lopez, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Labadie, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Lombardo, Veronica Andrea. Universidad Nacional de Rosario. Centro de Estudios Interdisciplinarios; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Biglione, Franco Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Manta, Bruno. Harvard Medical School; Estados Unidos
Fil: Jacob, Reeba. Weizmann Institute Of Science.; Israel
Fil: Gladyshev, Vadim. Harvard Medical School; Estados Unidos
Fil: Abdelilah Seyfried, Salim. Universitat Potsdam; Alemania. Leibniz Universitat Hannover; Alemania
Fil: Selenko, Philipp. Weizmann Institute Of Science.; Israel
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
DIASTEREOISOMERS
IN-CELL NMR
METHIONINE OXIDATION
METHIONINE SULFOXIDE REDUCTASE
ZEBRAFISH
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/181929
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/181929
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivoSanchez Lopez, CarolinaLabadie, NataliaLombardo, Veronica AndreaBiglione, Franco AgustínManta, BrunoJacob, ReebaGladyshev, VadimAbdelilah Seyfried, SalimSelenko, PhilippBinolfi, AndrésDIASTEREOISOMERSIN-CELL NMRMETHIONINE OXIDATIONMETHIONINE SULFOXIDE REDUCTASEZEBRAFISHhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Oxidation of protein methionines to methionine-sulfoxides (MetOx) is associated with several age-related diseases. In healthy cells, MetOx is reduced to methionine by two families of conserved methionine sulfoxide reductase enzymes, MSRA and MSRB that specifically target the S- or R-diastereoisomers of methionine-sulfoxides, respectively. To directly interrogate MSRA and MSRB functions in cellular settings, we developed an NMR-based biosensor that we call CarMetOx to simultaneously measure both enzyme activities in single reaction setups. We demonstrate the suitability of our strategy to delineate MSR functions in complex biological environments, including cell lysates and live zebrafish embryos. Thereby, we establish differences in substrate specificities between prokaryotic and eukaryotic MSRs and introduce CarMetOx as a highly sensitive tool for studying therapeutic targets of oxidative stress-related human diseases and redox regulated signaling pathways.Fil: Sanchez Lopez, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Labadie, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Lombardo, Veronica Andrea. Universidad Nacional de Rosario. Centro de Estudios Interdisciplinarios; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Biglione, Franco Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Manta, Bruno. Harvard Medical School; Estados UnidosFil: Jacob, Reeba. Weizmann Institute Of Science.; IsraelFil: Gladyshev, Vadim. Harvard Medical School; Estados UnidosFil: Abdelilah Seyfried, Salim. Universitat Potsdam; Alemania. Leibniz Universitat Hannover; AlemaniaFil: Selenko, Philipp. Weizmann Institute Of Science.; IsraelFil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaWiley VCH Verlag2020-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/181929Sanchez Lopez, Carolina; Labadie, Natalia; Lombardo, Veronica Andrea; Biglione, Franco Agustín; Manta, Bruno; et al.; An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo; Wiley VCH Verlag; Chemistry- A European Journal; 26; 65; 6-2020; 14838-148430947-6539CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.202002645info:eu-repo/semantics/altIdentifier/doi/10.1002/chem.202002645info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:10:43Zoai:ri.conicet.gov.ar:11336/181929instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-10 13:10:43.991CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
title An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
spellingShingle An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
Sanchez Lopez, Carolina
DIASTEREOISOMERS
IN-CELL NMR
METHIONINE OXIDATION
METHIONINE SULFOXIDE REDUCTASE
ZEBRAFISH
title_short An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
title_full An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
title_fullStr An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
title_full_unstemmed An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
title_sort An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo
dc.creator.none.fl_str_mv Sanchez Lopez, Carolina
Labadie, Natalia
Lombardo, Veronica Andrea
Biglione, Franco Agustín
Manta, Bruno
Jacob, Reeba
Gladyshev, Vadim
Abdelilah Seyfried, Salim
Selenko, Philipp
Binolfi, Andrés
author Sanchez Lopez, Carolina
author_facet Sanchez Lopez, Carolina
Labadie, Natalia
Lombardo, Veronica Andrea
Biglione, Franco Agustín
Manta, Bruno
Jacob, Reeba
Gladyshev, Vadim
Abdelilah Seyfried, Salim
Selenko, Philipp
Binolfi, Andrés
author_role author
author2 Labadie, Natalia
Lombardo, Veronica Andrea
Biglione, Franco Agustín
Manta, Bruno
Jacob, Reeba
Gladyshev, Vadim
Abdelilah Seyfried, Salim
Selenko, Philipp
Binolfi, Andrés
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv DIASTEREOISOMERS
IN-CELL NMR
METHIONINE OXIDATION
METHIONINE SULFOXIDE REDUCTASE
ZEBRAFISH
topic DIASTEREOISOMERS
IN-CELL NMR
METHIONINE OXIDATION
METHIONINE SULFOXIDE REDUCTASE
ZEBRAFISH
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Oxidation of protein methionines to methionine-sulfoxides (MetOx) is associated with several age-related diseases. In healthy cells, MetOx is reduced to methionine by two families of conserved methionine sulfoxide reductase enzymes, MSRA and MSRB that specifically target the S- or R-diastereoisomers of methionine-sulfoxides, respectively. To directly interrogate MSRA and MSRB functions in cellular settings, we developed an NMR-based biosensor that we call CarMetOx to simultaneously measure both enzyme activities in single reaction setups. We demonstrate the suitability of our strategy to delineate MSR functions in complex biological environments, including cell lysates and live zebrafish embryos. Thereby, we establish differences in substrate specificities between prokaryotic and eukaryotic MSRs and introduce CarMetOx as a highly sensitive tool for studying therapeutic targets of oxidative stress-related human diseases and redox regulated signaling pathways.
Fil: Sanchez Lopez, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Labadie, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Lombardo, Veronica Andrea. Universidad Nacional de Rosario. Centro de Estudios Interdisciplinarios; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Biglione, Franco Agustín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Manta, Bruno. Harvard Medical School; Estados Unidos
Fil: Jacob, Reeba. Weizmann Institute Of Science.; Israel
Fil: Gladyshev, Vadim. Harvard Medical School; Estados Unidos
Fil: Abdelilah Seyfried, Salim. Universitat Potsdam; Alemania. Leibniz Universitat Hannover; Alemania
Fil: Selenko, Philipp. Weizmann Institute Of Science.; Israel
Fil: Binolfi, Andrés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description Oxidation of protein methionines to methionine-sulfoxides (MetOx) is associated with several age-related diseases. In healthy cells, MetOx is reduced to methionine by two families of conserved methionine sulfoxide reductase enzymes, MSRA and MSRB that specifically target the S- or R-diastereoisomers of methionine-sulfoxides, respectively. To directly interrogate MSRA and MSRB functions in cellular settings, we developed an NMR-based biosensor that we call CarMetOx to simultaneously measure both enzyme activities in single reaction setups. We demonstrate the suitability of our strategy to delineate MSR functions in complex biological environments, including cell lysates and live zebrafish embryos. Thereby, we establish differences in substrate specificities between prokaryotic and eukaryotic MSRs and introduce CarMetOx as a highly sensitive tool for studying therapeutic targets of oxidative stress-related human diseases and redox regulated signaling pathways.
publishDate 2020
dc.date.none.fl_str_mv 2020-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/181929
Sanchez Lopez, Carolina; Labadie, Natalia; Lombardo, Veronica Andrea; Biglione, Franco Agustín; Manta, Bruno; et al.; An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo; Wiley VCH Verlag; Chemistry- A European Journal; 26; 65; 6-2020; 14838-14843
0947-6539
CONICET Digital
CONICET
url http://hdl.handle.net/11336/181929
identifier_str_mv Sanchez Lopez, Carolina; Labadie, Natalia; Lombardo, Veronica Andrea; Biglione, Franco Agustín; Manta, Bruno; et al.; An NMR‐based biosensor to measure stereo‐specific methionine sulfoxide reductase (MSR) activities in vitro and in vivo; Wiley VCH Verlag; Chemistry- A European Journal; 26; 65; 6-2020; 14838-14843
0947-6539
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/chem.202002645
info:eu-repo/semantics/altIdentifier/doi/10.1002/chem.202002645
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley VCH Verlag
publisher.none.fl_str_mv Wiley VCH Verlag
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.993085

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