کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8791934 | 1602548 | 2018 | 46 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characterization of an N-terminal mutant of αA-crystallin αA-R21Q associated with congenital cataract
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کلمات کلیدی
PBSSECIC50ADHACDsHSP4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acidAlcohol dehydrogenase - الکل دهیدروژنازBis-ANS - بیس-ANSPhosphate buffered saline - فسفات بافر شورhalf maximal inhibitory concentration - نیمه حداکثر غلظت مهاریsmall heat shock protein - پروتئین شوک حرارتی کوچکSize exclusion chromatography - کروماتوگرافی اندازهای طردی
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
ایمونولوژی و میکروب شناسی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Characterization of an N-terminal mutant of αA-crystallin αA-R21Q associated with congenital cataract Characterization of an N-terminal mutant of αA-crystallin αA-R21Q associated with congenital cataract](/preview/png/8791934.png)
چکیده انگلیسی
Several mutations associated with congenital cataracts in human beings target conserved arginine residues in αA-crystallin. The N-terminal region of αA-crystallin is a “mutational hotspot,” with multiple cataract-related mutations reported in this region. Two mutations at arginine 21 in the N-terminal domain of αA-crystallin - αA-R21L and αA-R21W have been associated with congenital cataract. A third mutant of R21, αA-R21Q, was recently identified to be associated with congenital cataract in a South Australian family. The point mutation was reported to compromise the quaternary structure of αA-crystallin by preventing its assembly into higher ordered oligomers. To assess the effect of the αA-R21Q mutation on αA-crystallin function, recombinant αA-R21Q was expressed, purified and characterized in vitro. Compared to wild-type αA-crystallin, the recombinant αA-R21Q exhibits enhanced chaperone-like activity, increased surface hydrophobicity, lesser stability in urea and increased susceptibility to digestion by trypsin. αA-R21Q demonstrated increased binding affinity towards unfolding ADH and bovine lens fiber cell membranes. αA-R21Q homo-oligomers and hetero-oligomers also prevented H2O2-induced apoptosis in ARPE-19â¯cells. Taken together, αA-R21Q exhibited a gain of function despite subtle structural differences as compared to wild-type αA-crystallin. This study further validates the involvement of arginine 21 in regulating αA-crystallin structure and function.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Eye Research - Volume 174, September 2018, Pages 185-195
Journal: Experimental Eye Research - Volume 174, September 2018, Pages 185-195
نویسندگان
Ashutosh S. Phadte, Puttur Santhoshkumar, K. Krishna Sharma,