کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8323535 | 1539893 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Neutrophil Elastase in the capacity of the “H2A-specific protease”
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کلمات کلیدی
PTMPBMCAQUAmESCposttranslational modification - اصلاح posttranslationalneutrophil elastase - الاستاز نوتروفیلMouse embryonic stem cells - سلول های بنیادی جنینی موشMass spectrometry - طیف سنجی جرمیAbsolute quantitation - مقدار مطلقperipheral blood monocytes - مونوسیتهای خون محیطیCathepsin L - کاتهپسین L
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The amino-terminal tail of histones and the carboxy-tail of histone H2A protrude from the nucleosome and can become modified by many different posttranslational modifications (PTM). During a mass spectrometric proteome analysis on haematopoietic cells we encountered a histone PTM that has received only little attention since its discovery over 35 years ago: truncation of the histone H2A C-tail at V114 which is mediated by the “H2A specific protease” (H2Asp). This enzyme is still referenced today but it was never identified. We first developed a sensitive AQUA approach for specific quantitation of the H2AV114 clipping. This clipping was found only in myeloid cells and further cellular fractionation lead to the annotation of the H2Asp as Neutrophil Elastase (NE). Ultimate proof was provided by NE incubation experiments and by studying histone extracts from NE Null mice. The annotation of the H2Asp not only is an indispensable first step in elucidating the potential biological role of this enzymatic interaction but equally provides the necessary background to critically revise earlier reports of H2A clipping.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 51, June 2014, Pages 39-44
Journal: The International Journal of Biochemistry & Cell Biology - Volume 51, June 2014, Pages 39-44
نویسندگان
M. Dhaenens, P. Glibert, S. Lambrecht, L. Vossaert, K. Van Steendam, D. Elewaut, D. Deforce,