کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1936459 1050691 2008 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
چکیده انگلیسی

The molecular mechanism by which heparin modulates the processing of procathepsin L in the extracellular environment is proposed. We show that heparin reduces the stability of the pro form of cathepsin L at pH 5 by binding to a putative heparin binding motif (BBXB) in the pro-domain. Mutations to this motif on procathepsin L reduce heparin binding affinity and heparin-induced destabilization; in contrast, heparin only slightly destabilizes the mature cathepsin L domain. Gel analysis further shows that heparin makes procathepsin L a much better substrate for cathepsin L. Thus, heparin enhances the rate of zymogen activation by destabilization upon binding to the BBXB motif. Determining the mechanism by which procathepsin L is activated in the extracellular matrix is important to the understanding of the role that cathepsin L plays in tumour invasion.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 366, Issue 3, 15 February 2008, Pages 862–867
نویسندگان
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