The Functions of the Mammalian Methionine Sulfoxide Reductase System and Related Diseases

Jiang, Beichen; Moskovitz, Jackob

doi:10.3390/antiox7090122

Cited by 47 publications

(38 citation statements)

References 55 publications

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“…It has been demonstrated that the oxidation of methionine impairs the reverse transport of cholesterol through apolipoprotein A-I [43]. Furthermore, a dysfunction in Met SO reductase has been linked with increased cell proliferation, degradation of extracellular matrix, interfering with key signaling processes, and cancer severity [44].…”

Section: Discussionmentioning

confidence: 99%

Blood Metabolites Associate with Prognosis in Endometrial Cancer

et al. 2019

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Endometrial cancer has a high prevalence among post-menopausal women in developed countries. We aimed to explore whether certain metabolic patterns could be related to the characteristics of aggressive disease and poorer survival among endometrial cancer patients in Western Norway. Patients with endometrial cancer with short survival (n = 20) were matched according to FIGO (International Federation of Gynecology and Obstetrics, 2009 criteria) stage, histology, and grade, with patients with long survival (n = 20). Plasma metabolites were measured on a multiplex system including 183 metabolites, which were subsequently determined using liquid chromatography-mass spectrometry. Partial least square discriminant analysis, together with hierarchical clustering, was used to identify patterns which distinguished short from long survival. A proposed signature of metabolites related to survival was suggested, and a multivariate receiver operating characteristic (ROC) analysis yielded an area under the curve (AUC) of 0.820–0.965 (p ≤ 0.001). Methionine sulfoxide seems to be particularly strongly associated with poor survival rates in these patients. In a subgroup with preoperative contrast-enhanced computed tomography data, selected metabolites correlated with the estimated abdominal fat distribution parameters. Metabolic signatures may predict prognosis and be promising supplements when evaluating phenotypes and exploring metabolic pathways related to the progression of endometrial cancer. In the future, this may serve as a useful tool in cancer management.

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Section: Discussionmentioning

confidence: 99%

Blood Metabolites Associate with Prognosis in Endometrial Cancer

et al. 2019

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“…Furthermore, methionine oxidation can also impact on protein activity indirectly by coupling oxidative signals to protein phosphorylation-dephosphorylation [ 15 , 16 ]. On the other hand, there is abundant evidence that the dysregulation of this methionine oxidation-reduction cycle could be the basis of multiple diseases [ 17 ]. Not surprisingly, the interest in characterizing methionine oxidation has been revived and a number of proteome-wide studies of methionine oxidation has been reported in the past few years [ 18 , 19 , 20 , 21 , 22 , 23 , 24 ].…”

Section: Introductionmentioning

confidence: 99%

Susceptibility of Protein Methionine Oxidation in Response to Hydrogen Peroxide Treatment–Ex Vivo Versus In Vitro: A Computational Insight

Aledo

2020

Antioxidants

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Methionine oxidation plays a relevant role in cell signaling. Recently, we built a database containing thousands of proteins identified as sulfoxidation targets. Using this resource, we have now developed a computational approach aimed at characterizing the oxidation of human methionyl residues. We found that proteins oxidized in both cell-free preparations (in vitro) and inside living cells (ex vivo) were enriched in methionines and intrinsically disordered regions. However, proteins oxidized ex vivo tended to be larger and less abundant than those oxidized in vitro. Another distinctive feature was their subcellular localizations. Thus, nuclear and mitochondrial proteins were preferentially oxidized ex vivo but not in vitro. The nodes corresponding with ex vivo and in vitro oxidized proteins in a network based on gene ontology terms showed an assortative mixing suggesting that ex vivo oxidized proteins shared among them molecular functions and biological processes. This was further supported by the observation that proteins from the ex vivo set were co-regulated more often than expected by chance. We also investigated the sequence environment of oxidation sites. Glutamate and aspartate were overrepresented in these environments regardless the group. In contrast, tyrosine, tryptophan and histidine were clearly avoided but only in the environments of the ex vivo sites. A hypothetical mechanism of methionine oxidation accounts for these observations presented.

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“…It should be noted that MsrB1 is mainly expressed in the cytosol and nucleus (by contrast, MsrB2 and MsrB3 are only found in the mitochondria and/or endoplasmic reticulum) [ 6 ]. Selenium and selenoproteins like MsrB1 have been found to be important for human health [ 7 ] but their physiological and cellular roles remain to be established.…”

Section: Introductionmentioning

confidence: 99%

The Selenoprotein MsrB1 Instructs Dendritic Cells to Induce T-Helper 1 Immune Responses

et al. 2020

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Immune activation associates with the intracellular generation of reactive oxygen species(ROS). To elicit effective immune responses, ROS levels must be balanced. Emerging evidenceshows that ROS‐mediated signal transduction can be regulated by selenoproteins such asmethionine sulfoxide reductase B1 (MsrB1). However, how the selenoprotein shapes immunityremains poorly understood. Here, we demonstrated that MsrB1 plays a crucial role in the ability ofdendritic cells (DCs) to provide the antigen presentation and costimulation that are needed forcluster of differentiation antigen four (CD4) T‐cell priming in mice. We found that MsrB1 regulatedsignal transducer and activator of transcription‐6 (STAT6) phosphorylation in DCs. Moreover, bothin vitro and in vivo, MsrB1 potentiated the lipopolysaccharide (LPS)‐induced Interleukin‐12 (IL‐12)production by DCs and drove T‐helper 1 (Th1) differentiation after immunization. We propose thatMsrB1 activates the STAT6 pathway in DCs, thereby inducing the DC maturation and IL‐12production that promotes Th1 differentiation. Additionally, we showed that MsrB1 promotedfollicular helper T‐cell (Tfh) differentiation when mice were immunized with sheep red blood cells.This study unveils as yet unappreciated roles of the MsrB1 selenoprotein in the innate control ofadaptive immunity. Targeting MsrB1 may have therapeutic potential in terms of controllingimmune reactions.

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The Functions of the Mammalian Methionine Sulfoxide Reductase System and Related Diseases

Cited by 47 publications

References 55 publications

Blood Metabolites Associate with Prognosis in Endometrial Cancer

Blood Metabolites Associate with Prognosis in Endometrial Cancer

Susceptibility of Protein Methionine Oxidation in Response to Hydrogen Peroxide Treatment–Ex Vivo Versus In Vitro: A Computational Insight

The Selenoprotein MsrB1 Instructs Dendritic Cells to Induce T-Helper 1 Immune Responses

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