کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8326607 1539977 2007 12 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Folding, activity and targeting of mutated human cathepsin D that cannot be processed into the double-chain form
چکیده انگلیسی
The precursor of human cathepsin D (CD) is converted into the single-chain and the double-chain active polypeptides by subsequent proteolysis reactions taking place in the endosomal-lysosomal compartment and involving specific aminoacid sequences. We have mutagenized the region of aminoacids (comprising the β-hairpin loop) involved in the latter proteolytic maturation step and generated a mutant CD that cannot be converted into the mature double-chain form. This mutant CD expressed in rodent cells reaches the lysosome and is stable as single-chain polypeptide, bears high-mannose type sugars, binds to pepstatin A and is enzymatically active, indicating that it is correctly folded. The present work provides new insights on the aminoacid region involved in the terminal processing of human CD and on the function of the processing β-hairpin loop.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 39, Issue 3, 2007, Pages 638-649
نویسندگان
, , , , ,