Loss of methionine sulfoxide reductases increases resistance to oxidative stress

Lai, Lo; Sun, Junhui; Tarafdar, Sreya; Liu, Chengyu; Murphy, Elizabeth; Kim, Geumsoo; Levine, Rodney L.

doi:10.1016/j.freeradbiomed.2019.10.006

Cited by 18 publications

(9 citation statements)

References 64 publications

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“…The MsrA deficiency in this model contributes to fibrosis development by increasing collagen deposition and augmenting fibrosis markers [48]. Therefore, MsrA regulates the Met metabolism and the production of H 2 S in the kidney [49].…”

Section: Figurementioning

confidence: 84%

Mitochondrial Redox Signaling and Oxidative Stress in Kidney Diseases

et al. 2021

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Mitochondria are essential organelles in physiology and kidney diseases, because they produce cellular energy required to perform their function. During mitochondrial metabolism, reactive oxygen species (ROS) are produced. ROS function as secondary messengers, inducing redox-sensitive post-translational modifications (PTM) in proteins and activating or deactivating different cell signaling pathways. However, in kidney diseases, ROS overproduction causes oxidative stress (OS), inducing mitochondrial dysfunction and altering its metabolism and dynamics. The latter processes are closely related to changes in the cell redox-sensitive signaling pathways, causing inflammation and apoptosis cell death. Although mitochondrial metabolism, ROS production, and OS have been studied in kidney diseases, the role of redox signaling pathways in mitochondria has not been addressed. This review focuses on altering the metabolism and dynamics of mitochondria through the dysregulation of redox-sensitive signaling pathways in kidney diseases.

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Section: Figurementioning

confidence: 84%

Mitochondrial Redox Signaling and Oxidative Stress in Kidney Diseases

et al. 2021

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“…Studies have shown that loss of any of these Msr enzymes under normal diet conditions is survivable, but can make the organism more sensitive to oxidative stress. Counterintuitively, knockout of the four Msr enzymes, MsrA and MsrB1-3, has been shown to increase oxidative stress resistance, presumably through compensatory mechanisms among the antioxidant defense system [51] . In addition to repairing oxidized methionine, Msr have been proposed to act more generally in oxidant defense as part of a methionine redox system [52] .…”

Section: Discussionmentioning

confidence: 99%

Metabolic Benefits of Methionine Restriction in Adult Mice Do Not Require Functional Methionine Sulfoxide Reductase a (MsrA)

Thyne

Salmon

2021

Preprint

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Methionine restriction (MR) extends lifespan and improves several markers of health in rodents. However, the proximate mechanisms of MR on these physiological benefits have not been fully elucidated. The essential amino acid methionine plays numerous biological roles and limiting its availability in the diet directly modulates methionine metabolism. There is growing evidence that redox regulation of methionine has regulatory control on some aspects of cellular function but interactions with MR remain largely unexplored. We tested the functional role of the ubiquitously expressed methionine repair enzyme methionine sulfoxide reductase A (MsrA) on the metabolic benefits of MR in mice. MsrA catalytically reduces both free and protein-bound oxidized methionine, thus playing a key role in its redox state. We tested the extent to which MsrA is required for metabolic effects of MR in adult mice using mice lacking MsrA. As expected, MR in control mice reduced body weight, altered body composition, and improved glucose metabolism. Interestingly, lack of MsrA did not impair the metabolic effects of MR on these outcomes. Moreover, females had blunted MR responses regardless of MsrA status compared to males. Overall, our data suggests that MsrA is not required for the metabolic benefits of MR in adult mice.

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“…The preferable substrate of MAO-A was serotonin (5-hydroxytryptamine, 5-HT), while MAO-B showed higher affinity towards benzylamine and phenylethylamine. 157,158 …”

Section: Fluorescent Probes For Ros-associated Proteins In Diseasesmentioning

confidence: 99%

“…The preferable substrate of MAO-A was serotonin (5-hydroxytryptamine, 5-HT), while MAO-B showed higher affinity towards benzylamine and phenylethylamine. 157,158 Inspired by the characteristic structures of MAO-A inhibitors, Ma et al reported a strategy to design and synthesize a uorescent probe (59) for the specic imaging of MAO-A (Fig. 39).…”

Section: Neurodegenerative Diseasementioning

confidence: 99%