Erratum: Snail1-induced partial epithelial-to-mesenchymal transition drives renal fibrosis in mice and can be targeted to reverse established disease.

Grande, M Teresa; Sánchez-Laorden, Berta; López-Blau, Cristina; Frutos, Cristina A. de; Boutet, Agnès; Arévalo, Miguel; Rowe, R. Grant; Weiss, Stephen J.; López‐Novoa, José M.; Nieto, M. Ángela

doi:10.1038/nm0216-217d

Cited by 12 publications

(7 citation statements)

References 1 publication

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“…As a strong repressor of E-cadherin gene's transcription, SNAI1 is recognized as an immediate-early gene target of the TGF-β1/SMAD3 pathway and involved in both physiological and pathological EMT. 38 , 39 , 40 , 41 In this study, we observed that TTC36 reduced the expression of SNAI1 and ACTA2 in cultured HK2 cells without TGF-β1 treatment ( Fig. 4 C), suggesting an oppositive role of TTC36 in the regulation of EMT which remains further investigations.…”

Section: Discussionmentioning

confidence: 53%

Tetratricopeptide repeat domain 36 deficiency mitigates renal tubular injury by inhibiting TGF-β1-induced epithelial–mesenchymal transition in a mouse model of chronic kidney disease

Yan

Peng

et al. 2022

Genes & Diseases

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Section: Discussionmentioning

confidence: 53%

Tetratricopeptide repeat domain 36 deficiency mitigates renal tubular injury by inhibiting TGF-β1-induced epithelial–mesenchymal transition in a mouse model of chronic kidney disease

Yan

Peng

et al. 2022

Genes & Diseases

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“…During the development of renal fibrosis, renal epithelial cells undergo a partial EMT and promote production and release of profibrotic growth factors/cytokines, including TGF-␤ 1 . Since Twist1 is the substrate of PRMT1 (1) and activation of Twist is required for the development of EMT in renal tubular cells (8), it is possible that PRMT1 may also be implicated in renal fibrosis through the induction of partial EMT by activation of Twist1. This hypothesis merits further investigation.…”

Section: Discussionmentioning

confidence: 99%

Protein arginine methyltransferase 1 mediates renal fibroblast activation and fibrogenesis through activation of Smad3 signaling

Yang

Chen

Zhuang

2020

American Journal of Physiology-Renal Physiology

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Protein arginine methyltransferase 1 (PRMT1), which primarily causes asymmetric arginine methylation of histone and nonhistone proteins, has been found to activate gene expression and mediate multiple pathological processes. Its role in renal fibrosis, however, remains unclear. In the present study, we observed that PRMT1 and its specific epigenetic marker, asymmetric di-methylated histone 4 arginine 3 (H4R3Me2a), were highly expressed in cultured renal interstitial fibroblasts. Treatment of PRMT1 with AMI-1, a selective inhibitor of PRMT1, or silencing PRMT1 with siRNA inhibited serum-induced and transforming growth factor (TGF)-β1-induced expression of α-smooth muscle actin (α-SMA) and collagen type I, two hallmarks of renal fibroblast activation, in a dose-dependent and time-dependent manner. In a murine model of renal fibrosis induced by unilateral ureteral obstruction, PRMT1 expression and H4R3Me2a were also upregulated, which was coincident with increased expression of α-SMA, collagen type I, and fibronectin. Administration of AMI-1 reduced PRMT1 and H4R3Me2a expression, attenuated extracellular matrix protein deposition, and inhibited renal fibroblast activation and proliferation. Moreover, AMI-1 treatment inhibited Smad3 phosphorylation and TGF-β receptor I expression but prevented Smad7 downregulation both in the kidney after unilateral ureteral obstruction injury and in cultured renal interstitial fibroblasts exposed to TGF-β1. Collectively, these results demonstrate that PRMT1 may mediate renal fibroblast activation and renal fibrosis development through activation of the TGF-β/Smad3 signaling pathway. They also suggest that PRMT1 inhibition may be a potential therapeutic approach for the treatment of fibrotic kidney disease.

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“…Damaged tubular epithelial cells secrete large amounts of profibrotic factors, which promote fibrosis formation ( 23 ). In this process, damaged tubular epithelial cells promote expression of key genes such as α-SMA and snail ( 24 , 25 ). In this study, the E-cadherin was down regulated, while the interstitial cell surface marker α-SMA was up-regulated when HK-2 cells were co-cultured with RPMI-8226 cells.…”

Section: Discussionmentioning

confidence: 99%

Pyrrolidinedithiocarbamic Acid Ammonium Salt Inhibits Apop-tosis and Phenotypic Transformation of Co-Culture of Myeloma Cells and Renal Tubular Epithelial Cells by Reducing the Secretion of Light Chain Protein

Yu¹,

Bao²,

Cui³

et al. 2020

ijph

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Background: We investigate the effects of NFκB inhibitor pyrrolidinedithiocarbamic acid ammonium salt (PDTC) on the viability, apoptosis and cell phenotype of HK-2 cells in the co-culture system of myeloma cells in renal tubular epithelial cells. Methods: This study was performed in Qiqihar Medical University, Qiqihar, China from Jun 2018 to Jan 2019. RPMI-8226 cells and HK-2 cells were inoculated in the co-culture chamber and cultured to establish the co-culture system. An immunoturbidimetric assay was performed to detect κ light chain and λ light chain in RPMI-8226 cells. The effect of PDTC on the secretion of κ light chain and λ light chain of RPMI-8226 cells was detected by immunoturbidimetry and the ratio was calculated. Results: PDTC significantly increased the viability of HK-2 cells. PDTC reduced the apoptosis of renal tubular epithelial cells. After PDTC treatment, the expression of cell surface marker E-cadherin decreased, and the expression of α-SMA increased, which induced the renal interstitial fibrosis. The secretion of κ light chain and λ light chain of RPMI-8226 cells was significantly decreased after the addition of PDTC, but the ratio was not changed. Conclusion: PDTC can inhibit the cell activity, promote apoptosis, and reduce the secretion of secretion of κ light chain and λ light chain through inhibiting the NF-κB pathway activation of myeloma cell RPMI-8226.

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Erratum: Snail1-induced partial epithelial-to-mesenchymal transition drives renal fibrosis in mice and can be targeted to reverse established disease.

Abstract: In the version of this article initially published, the labels to the left of the two micrographs in Figure 2c are reversed. Also, in Figure 4g, MKi67, used as a cell proliferation marker, is misspelled. The errors have been corrected in the HTML and PDF versions of the article.

Cited by 12 publications

References 1 publication

Tetratricopeptide repeat domain 36 deficiency mitigates renal tubular injury by inhibiting TGF-β1-induced epithelial–mesenchymal transition in a mouse model of chronic kidney disease

Tetratricopeptide repeat domain 36 deficiency mitigates renal tubular injury by inhibiting TGF-β1-induced epithelial–mesenchymal transition in a mouse model of chronic kidney disease

Protein arginine methyltransferase 1 mediates renal fibroblast activation and fibrogenesis through activation of Smad3 signaling

Pyrrolidinedithiocarbamic Acid Ammonium Salt Inhibits Apop-tosis and Phenotypic Transformation of Co-Culture of Myeloma Cells and Renal Tubular Epithelial Cells by Reducing the Secretion of Light Chain Protein

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