Recombinant Mouse Mitochondrial peptide methionine sulfoxide reductase (Msra)

1. Our findings demonstrate that reversal of methionine oxidation is required for maintenance of cellular homeostasis in the absence of increased oxidative stress. These data provide the first link between autophagy and activation of Nrf2 in the setting of MsrA deletion PMID: 29649787
2. Study shows that cisplatin induces methionine oxidation, oxidative stress, mitochondrial damage, apoptosis, and necrosis, and that MsrA gene deletion accelerates these cisplatin-induced damages. This indicates that MsrA protects kidney against cisplatin-induced acute kidney injury. PMID: 28158949
3. MsrA protects against lipopolysaccharide-induced septic shock, and negatively regulates proinflammatory responses via inhibition of the ROS-MAPK-NF-kappaB signaling pathways. PMID: 28803836
4. Collectively, our results suggest that MsrA protects hepatocytes from APAP-induced cytotoxicity through the modulation of TXNRD1 expression. PMID: 28442342
5. results demonstrate that MsrA protects the liver from APAP-induced toxicity. The data provided herein constitute the first in vivo evidence of the involvement of MsrA in hepatic function under APAP challenge PMID: 28104395
6. Results suggest that lower MsrA activity modifies Amyloid-beta solubility properties and causes mitochondrial dysfunction in a mouse model of Alzheimer's disease. PMID: 26786779
7. MsrA acts as a negative regulator of vascular smooth muscle cell proliferation and neointimal hyperplasia after vascular injury through control of the Ras/Raf/ERK1/ERK2 signaling pathway. PMID: 26449752
8. ARD1 has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA. PMID: 25341044
9. These results suggest that COMT activity may be reduced by methionine oxidation, and point to Msr as a key molecular determinant for the modulation of COMT activity in the brain. PMID: 24735585
10. The MsrA and protein oxidation play a role in the regulation of glucose homeostasis. PMID: 23089224
11. MsrA protects the kidney against I/R injury, and that this protection is associated with reduced oxidative stress and inflammatory responses. PMID: 22657153
12. MsrA overexpression in MsrA-depleted cells led to the reduction of increased HO-1 expression, and suppressed nuclear accumulation of Nrf2. PMID: 23036869
13. Mammalian and yeast Msra reduced free methionine sulfoxide much more efficiently than Msrb. PMID: 22867795
14. Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A. PMID: 22661718
15. A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A. PMID: 22661719
16. The data suggest that MsrA is a regulator of cell growth that mediates the p53-p21 pathway. PMID: 22086179
17. MsrA-/- knockout mice maintain a larger brain dopamine reserve pool than wild-type control mice, a difference not likely caused by altered dopamine transporter expression. PMID: 21219974
18. We conclude that cytosolic MsrA protects the heart from ischemia-reperfusion damage PMID: 21841012
19. A c-terminal truncated form of MsrA was cloned from mouse embryonic stem cells. The truncated protein shows a different subcellular localization and pattern of expression response to anoxia/reoxygenation treatment on the stem cells. PMID: 21696616
20. Anoxia, acidosis, and intergenic interactions selectively regulate methionine sulfoxide reductase transcriptions in mouse embryonic stem cells PMID: 20872796
21. Results indicate that MsrA plays an important role in cellular defenses against oxidative stress in embryonic stem cells. PMID: 20506347
22. the lack of MsrA in cardiac myocytes reduces myocardial cell's capability against stress stimulations resulting in a cellular dysfunction in the heart. PMID: 20971073
23. Ablation of methionine sulfoxide reductase can affect dopamine signaling through altering dopamine D(2)-receptor physiology and may be related to symptoms associated with neurological disorders and diseases. PMID: 20374422
24. Dual sites of protein initiation control the localization and myristoylation of methionine sulfoxide reductase A PMID: 20368336
25. Data show that methionine sulfoxide reductase (Msr)B1, but not MsrA, is the major methionine sulfoxide reductase in liver of mice and it is among the proteins that are most easily regulated by dietary selenium. PMID: 19769460
26. Methionine oxidation of alpha-crystallin in combination with loss of MsrA repair causes loss of alpha-crystallin chaperone function. PMID: 19733220
27. msra expression is regulated by (dietary)selenium PMID: 12792026
28. Proper structure-function organization of MsrA plays a role in subcellular distribution of this protein in mouse cells. PMID: 15924425
29. Moreover, following selenium deficient diet (applied to decrease the expression levels of selenoproteins like MsrB), the latter effect was maintained while the basal levels of thiol decreased in both mouse strains. PMID: 17126812
30. It is suggested that a deficiency in MsrA activity fosters oxidative-stress that is manifested by the accumulation of faulty proteins (via methionine oxidation), deposition of aggregated proteins, and premature brain cell death. PMID: 17333008
31. Results show MsrA deletion increases light scattering in lenses of mice exposed to hyperbaric oxygen; identifies cyt c as oxidized in the knockout lenses. Also establishes MsrA can restore in vitro activity of cyt c through methionine sulfoxide repair. PMID: 19461988
32. MsrA regulates sensitivity to oxidative stress in mice but has no effect on aging, as determined by life span. PMID: 19487311

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KEGG: mmu:110265

STRING: 10090.ENSMUSP00000065754

UniGene: Mm.26713