کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10870391 | 1074000 | 2014 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential
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کلمات کلیدی
DDMN-ethylmaleimideCOOHtBOOHSelenoprotein K5,5-Dimethyl-1,3-cyclohexanedionePLPCn-dodecyl-β-d-maltopyranoside - n-dodecyl-β-D-maltopyranosideDimedone - دیمدونSelenocysteine - سلنوسیستینNEM - نهHPETE - هتلیtert-butyl hydroperoxide - هیدروپراکسید تری بوتیلPhospholipid hydroperoxide - هیدروپراکسید فسفولیپیدcumene hydroperoxide - هیدروپراکسید کومنPeroxidase - پراکسیداز
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Selenoprotein K (SelK) is a membrane protein involved in antioxidant defense, calcium regulation and the ER-associated protein degradation pathway. We found that SelK exhibits a peroxidase activity with a rate that is low but within the range of other peroxidases. Notably, SelK reduced hydrophobic substrates, such as phospholipid hydroperoxides, which damage membranes. Thus, SelK might be involved in membrane repair or related pathways. SelK was also found to contain a diselenide bond-the first intramolecular bond of that kind reported for a selenoprotein. The redox potential of SelK was â257Â mV, significantly higher than that of diselenide bonds in small molecules or proteins. Consequently, SelK can be reduced by thioredoxin reductase. These finding are essential for understanding SelK activity and function.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 588, Issue 18, 17 September 2014, Pages 3311-3321
Journal: FEBS Letters - Volume 588, Issue 18, 17 September 2014, Pages 3311-3321
نویسندگان
Jun Liu, Zhengqi Zhang, Sharon Rozovsky,