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Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells

BACKGROUND: Methionine Sulfoxide Reductase A (MsrA), an enzyme in the Msr gene family, is important in the cellular anti-oxidative stress defense mechanism. It acts by reducing the oxidized methionine sulfoxide in proteins back to sulfide and by reducing the cellular level of reactive oxygen species...

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Autores principales: Jia, Pingping, Zhang, Chi, Jia, Yuanyuan, Webster, Keith A, Huang, Xupei, Kochegarov, Andrei A, Lemanski, Sharon L, Lemanski, Larry F
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143090/
https://www.ncbi.nlm.nih.gov/pubmed/21696616
http://dx.doi.org/10.1186/1423-0127-18-46
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author Jia, Pingping
Zhang, Chi
Jia, Yuanyuan
Webster, Keith A
Huang, Xupei
Kochegarov, Andrei A
Lemanski, Sharon L
Lemanski, Larry F
author_facet Jia, Pingping
Zhang, Chi
Jia, Yuanyuan
Webster, Keith A
Huang, Xupei
Kochegarov, Andrei A
Lemanski, Sharon L
Lemanski, Larry F
author_sort Jia, Pingping
collection PubMed
description BACKGROUND: Methionine Sulfoxide Reductase A (MsrA), an enzyme in the Msr gene family, is important in the cellular anti-oxidative stress defense mechanism. It acts by reducing the oxidized methionine sulfoxide in proteins back to sulfide and by reducing the cellular level of reactive oxygen species. MsrA, the only enzyme in the Msr gene family that can reduce the S-form epimers of methionine sulfoxide, has been located in different cellular compartments including mitochondria, cytosol and nuclei of various cell lines. METHODS: In the present study, we have isolated a truncated form of the MsrA transcript from cultured mouse embryonic stem cells and performed eGFP fusion protein expression, confocal microscopy and real time RT-PCR studies. RESULTS: Results show a different expression response of this truncated transcript to oxygen deprivation and reoxygenation treatments in stem cells, compared to the longer full length form. In addition, a different subcellular localization pattern was noted with most of the eGFP fusion protein detected in the cytosol. CONCLUSION: One possibility for the existence of a truncated form of the MsrA transcripts could be that with a smaller protein size, yet retaining a GCWFG action site, this protein might have easier access to oxidize methionine residues on proteins than the longer form of the MsrA protein, thus having an evolutionary selection advantage. This research opens the door for further study on the role and function of the truncated MsrA embryonic mouse stem cells.
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spelling pubmed-31430902011-07-26 Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells Jia, Pingping Zhang, Chi Jia, Yuanyuan Webster, Keith A Huang, Xupei Kochegarov, Andrei A Lemanski, Sharon L Lemanski, Larry F J Biomed Sci Research BACKGROUND: Methionine Sulfoxide Reductase A (MsrA), an enzyme in the Msr gene family, is important in the cellular anti-oxidative stress defense mechanism. It acts by reducing the oxidized methionine sulfoxide in proteins back to sulfide and by reducing the cellular level of reactive oxygen species. MsrA, the only enzyme in the Msr gene family that can reduce the S-form epimers of methionine sulfoxide, has been located in different cellular compartments including mitochondria, cytosol and nuclei of various cell lines. METHODS: In the present study, we have isolated a truncated form of the MsrA transcript from cultured mouse embryonic stem cells and performed eGFP fusion protein expression, confocal microscopy and real time RT-PCR studies. RESULTS: Results show a different expression response of this truncated transcript to oxygen deprivation and reoxygenation treatments in stem cells, compared to the longer full length form. In addition, a different subcellular localization pattern was noted with most of the eGFP fusion protein detected in the cytosol. CONCLUSION: One possibility for the existence of a truncated form of the MsrA transcripts could be that with a smaller protein size, yet retaining a GCWFG action site, this protein might have easier access to oxidize methionine residues on proteins than the longer form of the MsrA protein, thus having an evolutionary selection advantage. This research opens the door for further study on the role and function of the truncated MsrA embryonic mouse stem cells. BioMed Central 2011-06-22 /pmc/articles/PMC3143090/ /pubmed/21696616 http://dx.doi.org/10.1186/1423-0127-18-46 Text en Copyright ©2011 Jia et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Jia, Pingping
Zhang, Chi
Jia, Yuanyuan
Webster, Keith A
Huang, Xupei
Kochegarov, Andrei A
Lemanski, Sharon L
Lemanski, Larry F
Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title_full Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title_fullStr Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title_full_unstemmed Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title_short Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
title_sort identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143090/
https://www.ncbi.nlm.nih.gov/pubmed/21696616
http://dx.doi.org/10.1186/1423-0127-18-46
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