Myristoylated methionine sulfoxide reductase A is a late endosomal protein

Lim, Joo Han; Lim, Jung Chae; Kim, Geumsoo; Levine, Rodney L.

doi:10.1074/jbc.ra117.000473

Cited by 17 publications

(25 citation statements)

References 58 publications

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“…The only exception was MetO, whose plasma concentration was elevated by 45% and 71% in pigs fed 5% and 10% IM, respectively. MetO is readily formed from methionine by ROS-dependent oxidation and reduced back to methionine by thioredoxin-dependent methionine sulfoxide reductases [49,50]. In our recent study with obese Zucker rats [15], we have also made this striking finding of a dose-dependent increase of plasma MetO concentration by feeding IM using targeted plasma metabolomics (unpublished data).…”

Section: Discussionmentioning

confidence: 76%

Comprehensive evaluation of the metabolic effects of insect meal from Tenebrio molitor L. in growing pigs by transcriptomics, metabolomics and lipidomics

Meyer

Geßner

Braune

et al. 2020

J Animal Sci Biotechnol

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Background: The hypothesis was tested that insect meal (IM) as protein source influences intermediary metabolism of growing pigs. To test this, 30 male, 5-week-old crossbred pigs were randomly assigned to 3 groups of 10 pigs each with similar body weights (BW) and fed isonitrogenous diets either without (CON) or with 5% IM (IM5) or 10% IM (IM10) from Tenebrio molitor L. for 4 weeks and key metabolic tissues (liver, muscle, plasma) were analyzed using omics-techniques. Results: Most performance parameters did not differ across the groups, whereas ileal digestibilities of most amino acids were 6.7 to 15.6%-units lower in IM10 than in CON (P < 0.05). Transcriptomics of liver and skeletal muscle revealed a total of 166 and 198, respectively, transcripts differentially expressed between IM10 and CON (P < 0.05). Plasma metabolomics revealed higher concentrations of alanine, citrulline, glutamate, proline, serine, tyrosine and valine and a lower concentration of asparagine in IM10 than in CON (P < 0.05). Only one out of fourteen quantifiable amino acid metabolites, namely methionine sulfoxide (MetS), in plasma was elevated by 45% and 71% in IM5 and IM10, respectively, compared to CON (P < 0.05). Plasma concentrations of both, major carnitine/ acylcarnitine species and bile acids were not different across groups. Lipidomics of liver and plasma demonstrated no differences in the concentrations of triacylglycerols, cholesterol and the main phospholipids, lysophospholipids and sphingolipids between groups. The percentages of all individual phosphatidylcholine (PC) and phosphatidylethanolamine (PE) species in the liver showed no differences between groups, except those with 6 double bonds (PC 38:6, PC 40:6, PE 38:6, PE 40:6), which were markedly lower in IM10 than in CON (P < 0.05). In line with this, the percentage of C22:6n-3 in hepatic total lipids was lower in IM10 than in the other groups (P < 0.05). Conclusions: Comprehensive analyzes of the transcriptome, lipidome and metabolome of key metabolic tissues indicate that partial or complete replacement of a conventional protein source by IM in the diet has only a weak impact on the intermediary metabolism of growing pigs. Thus, it is concluded that IM from Tenebrio molitor L. can be used as a dietary source of protein in pigs without causing adverse effects on metabolism.

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Section: Discussionmentioning

confidence: 76%

Comprehensive evaluation of the metabolic effects of insect meal from Tenebrio molitor L. in growing pigs by transcriptomics, metabolomics and lipidomics

Meyer

Geßner

Braune

et al. 2020

J Animal Sci Biotechnol

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“…The protein array we employed has 9483 human proteins, produced in baculovirus with glutathione-S-transferase (GST) tags [ 21 ]. We had earlier used these arrays to demonstrate a protein-protein interaction of methionine sulfoxide reductase A that had not been detected by a number of other techniques [ 22 ]. In this study, we interrogated the protein arrays with recombinant wild-type or M77Q calmodulin.…”

Section: Resultsmentioning

confidence: 99%

Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior

et al. 2018

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Methionine 77 in calmodulin can be stereospecifically oxidized to methionine sulfoxide by mammalian methionine sulfoxide reductase A. Whether this has in vivo significance is unknown. We therefore created a mutant mouse in which wild type calmodulin-1 was replaced by a calmodulin containing a mimic of methionine sulfoxide at residue 77. Total calmodulin levels were unchanged in the homozygous M77Q mutant, which is viable and fertile. No differences were observed on learning tests, including the Morris water maze and associative learning. Cardiac stress test results were also the same for mutant and wild type mice. However, young male and female mice were 20% smaller than wild type mice, although food intake was normal for their weight. Young M77Q mice were notably more active and exploratory than wild type mice. This behavior difference was objectively documented on the treadmill and open field tests. The mutant mice ran 20% longer on the treadmill than controls and in the open field test, the mutant mice explored more than controls and exhibited reduced anxiety. These phenotypic differences bore a similarity to those observed in mice lacking calcium/calmodulin kinase IIα (CaMKIIα). We then showed that MetO77 calmodulin was less effective in activating CaMKIIα than wild type calmodulin. Thus, characterization of the phenotype of a mouse expressing a constitutively active mimic of calmodulin led to the identification of the first calmodulin target that can be differentially regulated by the oxidation state of Met77. We conclude that reversible oxidation of methionine 77 in calmodulin by MSRA has the potential to regulate cellular function.

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“…We scanned the conserved domains of all algal selenoproteins. Figure 4C shows that a total of 36 domains were which are related to reducing methionine sulphoxide [45,46]. Another important function is also found in algae selenoproteins.…”

Section: Figure 4amentioning

confidence: 95%

The algal selenoproteomes

Jiang

Zheng

et al. 2020

Preprint

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Background: Selenium is an important trace element, and selenoprotein is its predominant form in vivo. The special structural features of selenoprotein genes have led to the development of a series of bioinformatics methods for the prediction and research of selenoprotein genes. There are some studies and reports on the evolution and distribution of selenoprotein genes in prokaryotes and multicellular eukaryotes, but the systematic analysis of single-cell eukaryotes, especially algae, is very limited. Results: In this study, we predicted selenoprotein genes in 137 species of algae by using a program we previously developed. More than 1000 selenoprotein genes were obtained. A database website was built to hold these algae selenoprotein genes (www.selenoprotein.com). These genes belong to 42 selenoprotein families, including three novel selenoprotein gene families. Conclusions: This study reveals the primordial state of the eukaryotic selenoproteome. It is an important clue to explore the significance of selenium for primordial eukaryotes and to build the whole evolutionary spectrum of selenoproteins for all life.

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Myristoylated methionine sulfoxide reductase A is a late endosomal protein

Cited by 17 publications

References 58 publications

Comprehensive evaluation of the metabolic effects of insect meal from Tenebrio molitor L. in growing pigs by transcriptomics, metabolomics and lipidomics

Comprehensive evaluation of the metabolic effects of insect meal from Tenebrio molitor L. in growing pigs by transcriptomics, metabolomics and lipidomics

Oxidation of Methionine 77 in Calmodulin Alters Mouse Growth and Behavior

The algal selenoproteomes

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