کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10757120 | 1050392 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
N-linked glycosylation of the superoxide-producing NADPH oxidase Nox1
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کلمات کلیدی
DUOXNOX1p22phoxPNGase Fpeptide: N-glycosidase FNOx - NOXROS - ROSEndo H - اندو هendoglycosidase H - اندوگلیکوزیداز HNADPH oxidase - اکسیداز NADPH dual oxidase - دو اکسیدازSuperoxide - سوپر اکسیدendoplasmic reticulum - شبکه آندوپلاسمی Glycosylation - گلیکوزیله شدنReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Nox1 is a membrane-integrated protein that belongs to the Nox family of superoxide-producing NADPH oxidases. Here we show that human Nox1 undergoes glycosylation at Asn-162 and Asn-236 in the second and third extracellular loops, respectively. Simultaneous threonine substitution for these residues completely abrogates the glycosylation, but does not prevent Nox1 from forming a heterodimer with p22phox, trafficking to the cell surface, or producing superoxide. In the absence of p22phox, Nox1 is transported to the plasma membrane mainly as a form with high mannose N-glycans, although their conversion into complex N-glycans is induced by expression of p22phox. These findings indicate that glycosylation and subsequent N-glycan maturation of Nox1 are both dispensable for its cell surface recruitment. Superoxide production by unglycosylated Nox1 is largely dependent on p22phox, which is abrogated by glutamine substitution for Pro-156 in p22phox, a mutation leading to a defective interaction with the Nox1-activating protein Noxo1. Thus p22phox directly contributes to Nox1 activation in a glycosylation-independent manner, besides its significant role in Nox1 glycan maturation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 3, 17 January 2014, Pages 1060-1065
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 3, 17 January 2014, Pages 1060-1065
نویسندگان
Kei Miyano, Hideki Sumimoto,