کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801734 | 1055632 | 2016 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Methylation of arginine by PRMT1 regulates Nrf2 transcriptional activity during the antioxidative response
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کلمات کلیدی
Heme oxygenase-1Txnrd1PRMT1tBHPGCLMCARM1Coactivator-associated arginine methyltransferase 1NQO1HO-1Nrf2DMEMPEIDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده Dulbeccot-Butyl hydroperoxide - t-butyl hydroperoxideThioredoxin reductase 1 - تریوردوکسین ردوکتاز 1Oxidative stress - تنش اکسیداتیوNF-E2-related factor 2 - عامل NF-E2 2antioxidant response element - عنصر پاسخ آنتی اکسیدانARE - هستندpolyethyleneimine - پلی اتیلنیمینglutamate-cysteine ligase modifier subunit - کلرید کلسیم کلسترول کلسیم
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Methylation of arginine by PRMT1 regulates Nrf2 transcriptional activity during the antioxidative response Methylation of arginine by PRMT1 regulates Nrf2 transcriptional activity during the antioxidative response](/preview/png/10801734.png)
چکیده انگلیسی
The cap 'n' collar (CNC) family of transcription factors play important roles in resistance of oxidative and electrophilic stresses. Among the CNC family members, NF-E2-related factor 2 (Nrf2) is critical for regulating the antioxidant and phase II enzymes through antioxidant response element (ARE)-mediated transactivation. The activity of Nrf2 is controlled by a variety of post-translational modifications, including phosphorylation, ubiquitination, acetylation and sumoylation. Here we demonstrate that the arginine methyltransferase-1 (PRMT1) methylates Nrf2 protein at a single residue of arginine 437, both in vitro and in vivo. Using the heme oxygenase-1 (HO-1) as a model of phase II enzyme gene, we found that methylation of Nrf2 by PRMT1 led to a moderate increase of its DNA-binding activity and transactivation, which subsequently protected cells against the tBHP-induced glutathione depletion and cell death. Collectively, our results define a novel modification of Nrf2, which operates as a fine-tuning mechanism for the transcriptional activity of Nrf2 under the oxidative stress.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1863, Issue 8, August 2016, Pages 2093-2103
Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research - Volume 1863, Issue 8, August 2016, Pages 2093-2103
نویسندگان
Xin Liu, Hongyuan Li, Lingxia Liu, Yang Lu, Yanyan Gao, Pengyu Geng, Xiaoxue Li, Baiqu Huang, Yu Zhang, Jun Lu,