کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1941134 1536793 2006 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Resistance of cathepsin L compared to elastase to proteolysis when complexed with the serpin endopin 2C, and recovery of cathepsin L activity
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Resistance of cathepsin L compared to elastase to proteolysis when complexed with the serpin endopin 2C, and recovery of cathepsin L activity
چکیده انگلیسی

This study demonstrates unique differences in the conformational nature of cathepsin L compared to elastase when complexed with the serpin endopin 2C, assessed by susceptibilities of protease/endopin 2C complexes to proteolysis by trypsin. Complexed and uncomplexed cathepsin L were resistant to degradation by trypsin, which indicated that trypsin cleavage sites within cathepsin L remain inaccessible when this cysteine protease is complexed with the endopin 2C serpin. In contrast, elastase in complexes with endopin 2C was degraded by trypsin, but uncomplexed elastase was not degraded. These results demonstrate a change in the conformational properties of trypsin cleavage sites within elastase when it is complexed with endopin 2C, compared to uncomplexed elastase. Cathepsin L complexes with endopin 2C were short-lived, but elastase complexes were stable. Furthermore, cathepsin L dissociated from complexes demonstrated recovery of cathepsin L activity, and reducing conditions provided optimum recovery of cathepsin L activity. These findings suggest that cathepsin L, when complexed with endopin 2C, maintains its general conformation in a manner that allows recovery of cathepsin L activity upon dissociation from endopin 2C. These results demonstrate differences in the relative conformational properties of the cysteine protease cathepsin L, compared to the serine protease elastase, in complexes with the serpin endopin 2C.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 340, Issue 4, 24 February 2006, Pages 1238–1243
نویسندگان
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