PRMT1 promotes hyperglycemia in a FoxO1-dependent manner, affecting glucose metabolism, during hypobaric hypoxia exposure, in rat model

Bayen, Susovon; Saini, Supriya; Gaur, Priya; Duraisamy, Arul J.; Sharma, Alpesh K.; Pal, Karan; Vats, Praveen; Singh, Shashi Bala

doi:10.1007/s12020-017-1463-6

Cited by 20 publications

(13 citation statements)

References 44 publications

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Section: Discussionmentioning

confidence: 99%

“…Arginine methylation is involved in many biologic processes through the mechanism of posttranslation modification of histones or nonhistone proteins (16,17). For example, PRMT1 promotes hyperglycemia by methylating the transcriptional factor forkhead box O1 and thus increasing the nuclear retention and the transcriptional activity of transcriptional factor forkhead box O1 (17). In the current study, we found that the expression of PRMT1 and H4R3me2a are increased in fibrotic kidneys and reduced by the treatment with PT1001B, suggesting that PRMT1 may modulate renal fibrosis through histone modificationmediated epigenetic gene regulation or even nonhistone modification-mediated transcription factor activation, which go far beyond ADMA synthesis.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Reduced asymmetric dimethylarginine accumulation through inhibition of the type I protein arginine methyltransferases promotes renal fibrosis in obstructed kidneys

Peng

Lin

et al. 2019

FASEB j.

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The role of asymmetric dimethylarginine (ADMA) in chronic kidney disease (CKD) is unclear. Through inhibition of type I protein arginine methyltransferases (PRMTs), a novel strategy, we aimed to determine the effect of ADMA on renal fibrosis and explore its underlying working mechanisms. After sham or unilateral ureter ligation (UUO) operation, 20–25 g male c57 mice were treated with vehicle or PT1001B, an inhibitor of type I PRMTs, for 13 d. Moreover, human kidney 2 (HK2) and normal rat kidney 49F (NRK‐49F) cells were treated with various concentrations of PT1001B or ADMA in the presence of 2.5 ng/ml TGF‐β. We found that treatment with PT1001B increased the deposition of extracellular matrix proteins, the expression of αsmooth muscle actin, and connective tissue growth factor in UUO‐induced fibrotic kidneys, which is correlated with reduced expression of PRMT1, reduced the production of ADMA, and increased expression of uromodulin. In TGF‐β‐stimulated HK2 and NRK‐49F cells, PT1001B dose‐dependently inhibited ADMA production, increased NO concentrations, and enhanced the expression of profibrotic proteins. Exogenous addition of ADMA inhibited the expression of profibrotic proteins dose‐dependently and attenuated the profibrotic effect of PT1001B. Moreover, ADMA reduced the NO concentration in PT1001B‐treated HK2 cells. Finally, we conclude that ADMA has an antifibrotic effect in obstructed kidneys, and future application of type I PRMT inhibitor should be done cautiously for patients with CKD.—Wu, M., Lin, P., Li, L., Chen, D., Yang, X., Xu, L., Zhou, B., Wang, C., Zhang, Y., Luo, C., Ye, C. Reduced asymmetric dimethylarginine accumulation through inhibition of the type I protein arginine methyltransferases promotes renal fibrosis in obstructed kidneys. FASEB J. 33, 6948–6956 (2019). http://www.fasebj.org

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Reduced asymmetric dimethylarginine accumulation through inhibition of the type I protein arginine methyltransferases promotes renal fibrosis in obstructed kidneys

Peng

Lin

et al. 2019

FASEB j.

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“…On one hand, PRMTs can directly affect cell biology by modulating their protein substrates. For instance, PRMT1 promotes hyperglycemia by methylating the transcriptional factor forkhead box O1 (FOXO1) and thus increasing its nuclear retention and the transcriptional activity [112]. On the other hand, PRMTs impact on (patho)physiology via its far end metabolite product, ADMA.…”

Section: Perspectivementioning

confidence: 99%

The Biological Axis of Protein Arginine Methylation and Asymmetric Dimethylarginine

Fulton

Brown

Zheng

2019

IJMS

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Protein post-translational modifications (PTMs) in eukaryotic cells play important roles in the regulation of functionalities of the proteome and in the tempo-spatial control of cellular processes. Most PTMs enact their regulatory functions by affecting the biochemical properties of substrate proteins such as altering structural conformation, protein–protein interaction, and protein–nucleic acid interaction. Amid various PTMs, arginine methylation is widespread in all eukaryotic organisms, from yeasts to humans. Arginine methylation in many situations can drastically or subtly affect the interactions of substrate proteins with their partnering proteins or nucleic acids, thus impacting major cellular programs. Recently, arginine methylation has become an important regulator of the formation of membrane-less organelles inside cells, a phenomenon of liquid–liquid phase separation (LLPS), through altering π-cation interactions. Another unique feature of arginine methylation lies in its impact on cellular physiology through its downstream amino acid product, asymmetric dimethylarginine (ADMA). Accumulation of ADMA in cells and in the circulating bloodstream is connected with endothelial dysfunction and a variety of syndromes of cardiovascular diseases. Herein, we review the current knowledge and understanding of protein arginine methylation in regards to its canonical function in direct protein regulation, as well as the biological axis of protein arginine methylation and ADMA biology.

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“…Elevated levels of the phosphofructokinase gene (PFKL), 6-phosphofructo-2-kinase/fructose-2, 6-biphospatase 4 (PFKFB4) and fructose-biphosphate aldolase C (ALDOC) were seen in the RP/RP group compared with the RP/C group, which points to an activated glucose metabolism. The GO term differences in the group comparisons remained unaltered when the analysis was done without the two RP/C samples that did not cluster with the other RP F0 diet samples, with again an up-regulation of transaminase activity in the RP/C group and an up-regulation of protein arginine methyltransferase in the RP/RP group, which indeed has been described to play a role in glucose metabolism (26) .…”

Section: Functional Analysesmentioning

confidence: 91%

Direct and maternal reduced balanced protein diet influences the liver transcriptome in chickens

et al. 2020

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The objective of this study was to evaluate, by means of RNA-sequencing, the direct and transgenerational effect of a reduced balanced protein diet on broiler breeder metabolism. Chickens of the F0 generation were fed a control (C) or reduced balanced protein (RP) diet and their F1 progeny was fed a C or RP diet as well, resulting in four groups of chickens, C/C, C/RP, RP/C and RP/RP. While both a direct and a maternal effect were seen on body weight, breast muscle weight and abdominal fat weight in the F1 generation, the direct effect was the most dominant one. The liver transcriptome in the F1 generation showed that amino acid metabolism was upregulated in chickens that received control feed when compared to their respective contemporaries that received the reduced protein diet. Interestingly, chickens hatched from control fed hens but reared on reduced protein diet (C/RP group) activated a fatty acid metabolism, expressing more FADS1, FADS2 and ELOVL2, when compared to control fed chickens hatched from control fed hens (C/C group), while chickens hatched from reduced protein fed hens that received themselves the same reduced protein diet (RP/RP group) triggered their glucose metabolism more, showing elevated levels of PFKL, PFKFB4 and ALDOC mRNA compared to the chickens hatched from reduced protein fed hens but reared on a control diet (RP/C group). This suggests that the maternal protein diet has an impact on the metabolism of broilers when they are reared on a reduced balanced protein diet.

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PRMT1 promotes hyperglycemia in a FoxO1-dependent manner, affecting glucose metabolism, during hypobaric hypoxia exposure, in rat model

Abstract: PRMT1 might have a potential importance as a therapeutic target for the treatment of HH-induced maladies.

Cited by 20 publications

References 44 publications

Reduced asymmetric dimethylarginine accumulation through inhibition of the type I protein arginine methyltransferases promotes renal fibrosis in obstructed kidneys

Reduced asymmetric dimethylarginine accumulation through inhibition of the type I protein arginine methyltransferases promotes renal fibrosis in obstructed kidneys

The Biological Axis of Protein Arginine Methylation and Asymmetric Dimethylarginine

Direct and maternal reduced balanced protein diet influences the liver transcriptome in chickens

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