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Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells | Jia et al. Journal of Biomedical Science 2011 18 46 http www.jbiomedsci.eom content 18 1 46 BIN sc The cost of publication in Journal of Biomedical Science Is borne by the National Science Council Taiwan JOURNAL OF BIOMEDICAL SCIENCE RESEARCH Open Access Identification of a truncated form of methionine sulfoxide reductase a expressed in mouse embryonic stem cells 1 2 1 2 3 5 Pingping Jia Chi Zhang Yuanyuan Jia Keith A Webster Xupei Huang Andrei A Kochegarov Sharon L Lemanski4 and Larry F Lemanski4 5 Abstract 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
