کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2051587 | 1074204 | 2007 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin](/preview/png/2051587.png)
چکیده انگلیسی
Superoxide generation by NADPH oxidase 5 (NOX5) is regulated by Ca2+ through intramolecular activation of the C-terminal catalytic domain by the EF-hand-containing N-terminal regulatory domain. The C terminus contains a consensus calmodulin-binding domain (CaMBD), which, however, is not the binding site of the N-terminal regulatory domain. Here we show by pull down, cross-linking, fluorimetry and by enzymatic assays, that calmodulin binds to this CaMBD in a Ca2+-dependent manner, changes its conformation and increases the Ca2+ sensitivity of the N terminus-regulated enzymatic activity. This mechanism represents an additional sophistication in the regulation of superoxide production by NOX5.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 581, Issue 6, 20 March 2007, Pages 1202–1208
Journal: FEBS Letters - Volume 581, Issue 6, 20 March 2007, Pages 1202–1208
نویسندگان
Fabiana Tirone, Jos A. Cox,