کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8472167 | 1550303 | 2007 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Role of ficolin in innate immunity and its molecular basis
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
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چکیده انگلیسی
Ficolin is a multimeric protein consisting of an N-terminal collagen-like domain and a C-terminal fibrinogen-like domain. The structure is similar to mannose-binding lectin (MBL) and complement C1q owing to the collagen-like stalk. Accumulating data indicate that a key function of ficolin is to recognize the carbohydrate moieties on pathogens as a pattern-recognition molecule. Two or three kinds of ficolin have been identified in each species of mammals. They are similar but with some differences in the expression site, location site, ligand-binding specificity and ability to form complexes with MBL-associated serine proteases (MASPs). Like MBL, some ficolins are serum lectins and can form a complex with MASPs and small MBL-associated protein (sMAP). This complex activates the complement through “the lectin pathway”. Our recent study suggests that ficolin acts through two distinct routes: the lectin pathway and a primitive opsonophagocytosis. All these observations suggest that ficolins function in clearance of non-self, based on their location sites and their molecular features.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 371-379
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 371-379
نویسندگان
Yuichi Endo, Misao Matsushita, Teizo Fujita,