کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5704023 | 1602561 | 2017 | 28 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A structural and functional study of Gln147 deamidation in αA-crystallin, a site of modification in human cataract
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کلمات کلیدی
RCMreduced and carboxymethylatedαA-CrystallinsHSPDEAENOESYTOCSYHSQCADHDTTNuclear Overhauser Effect SpectroscopY - Spectroscopy اثر Overhauser هسته ایαB-crystallin - αB-کریستالینCataract - آب مرواریدpost-translational modification - اصلاح post-translationalAlcohol dehydrogenase - الکل دهیدروژنازDeamidation - انحلالThT - بلهThioflavin T - تیوفلاوین Tdithiothreitol - دیتیوتریتولAgeing - سالخوردهTotal correlation spectroscopy - طیف سنجی مجموع همبستگیMALS - مالشwild type - نوع وحشیmulti-angle light scattering - پراکندگی نور چند زاویهSmall heat-shock protein - پروتئین کوچک شوک حرارتheteronuclear single quantum coherence - یکپارچگی کوانتومی تک هسته ای
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
ایمونولوژی و میکروب شناسی (عمومی)
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چکیده انگلیسی
Deamidation of Glu147 in human αA-crystallin is common in aged cataractous lenses (Hains and Truscott, Invest. Ophthalmol. Vis. Sci. 2010, 51, 3107). Accordingly, this modification may have a causative effect in cataract. αA-crystallin is a small heat-shock molecular chaperone protein that prevents aggregation of proteins and is the principal defence against crystallin unfolding and aggregation in the ageing lens. Deamidated Q147E αA-crystallin was structurally characterised using a variety of spectroscopic and biophysical methods, including NMR, circular dichroism and fluorescence spectroscopy and dynamic light scattering. The effect of Glu147 deamidation on αA-crystallin in vitro chaperone ability was determined for a variety of aggregating proteins. Compared to the wild type protein, Q147E αA-crystallin generally exhibited slightly reduced chaperone ability and a small loss of overall structure in its central α-crystallin domain while also showing significantly enhanced thermal stability and a tendency to form slightly larger oligomers. As αA-crystallin is the major lens protein, even a small loss of function could combine with other sources of age-related damage to the crystallins to contribute to lens opacification.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Eye Research - Volume 161, August 2017, Pages 163-173
Journal: Experimental Eye Research - Volume 161, August 2017, Pages 163-173
نویسندگان
Nicholas J. Ray, Damien Hall, John A. Carver,