کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8472157 | 1550303 | 2007 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Serine proteases of the classical and lectin pathways: Similarities and differences
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کلمات کلیدی
autoactivationMASPtPAIGFBPMBLCCPEGFInnate immunity - ایمنی ذاتیCub - تولهSubstrate specificity - خصوصیات زیربناییComplement system - دستگاه کمپلمان، سیستم کمپلمان3D structure - ساختار 3DSerine protease - سرین پروتئازepidermal growth factor - عامل رشد اپیدرمیTissue-type plasminogen activator - فعال کننده بافت پلاسمینوژنMannose-binding lectin - لکتین اتصال دهنده مانوزmap - نقشهMBL-associated serine protease - پروتئاز serine مرتبط با MBLInsulin-like growth factor-binding protein - پروتئین متصل به پروتئین رشد دهنده انسولینcomplement control protein - پروتئین کنترل مکمل
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Serine proteases of the classical and lectin pathways: Similarities and differences Serine proteases of the classical and lectin pathways: Similarities and differences](/preview/png/8472157.png)
چکیده انگلیسی
C1r, C1s, MBL-associated serine protease (MASP)-1, MASP-2 and MASP-3 are mosaic serine proteases of the classical and lectin pathways of complement. They form a family of enzymes with identical domain organization and similar overall structure, but with different enzymatic properties. MASP-2 of the lectin pathway can autoactivate and cleave C4 and C2 components. In the classical pathway two enzymes mediate these functions: C1r autoactivates and activates C1s, while C1s cleaves C4 and C2. The substrate specificity and the biological function of MASP-1 and MASP-3 have not yet been completely resolved. MASP-1 can autoactivate and the activated MASP-1 has more relaxed substrate specificity than the other members of the family. It was demonstrated that MASP-1 can specifically cleave C2, C3 and fibrinogen, but the physiological relevance of these findings has to be proved. We do not know how MASP-3 becomes activated and its biological function is also not clear. In this review, we will summarize current knowledge about the structure and function of these proteases. Special emphasis will be laid on the specificity, autoactivation and evolution of these enzymes.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 267-277
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 267-277
نویسندگان
Péter Gál, László Barna, Andrea Kocsis, Péter Závodszky,