- 作者: Pingping Jia; Chi Zhang; Yuanyuan Jia; Keith A Webster; Xupei Huang; Andrei A Kochegarov; Sharon L Lemanski; Larry F Lemanski
- 作者服務機構: Project to Cure Paralysis, University of Miami Miller School of Medicine, Miami, FL.,USA
- 中文摘要: --
- 英文摘要:
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. - 中文關鍵字: --
- 英文關鍵字: --