کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8472165 | 1550303 | 2007 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
C1q binding and complement activation by prions and amyloids
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کلمات کلیدی
FDDPrPscCreutzfeld–Jacob diseaseC1qPrPcCJDTSEPrPAPPAβFBDBSEAlzheimer - آلزایمرAmyloid - آمیلوئیدScrapie - اسکرپیtransmissible spongiform encephalopathy - انسفالوپاتی اسپون های مضرAlzheimer's disease - بیماری آلزایمرBovine spongiform encephalopathy - جنون گاویFamilial British dementia - زوال خانواده خانوادگی بریتانیاFamilial Danish dementia - زوال خانواده دانمارکیAmyloid β peptide - پتید بتا آمیلوئیدPrion protein - پروتئین پریونamyloid precursor protein - پروتئین پیش ماده آمیلوئیPrion - پریون
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
C1q binds to many non-self and altered-self-materials. These include microorganisms, immune complexes, apoptotic and necrotic cells and their breakdown products, and amyloids. C1q binding to amyloid fibrils found as extracellular deposits in tissues, and subsequent complement activation are involved in the pathology of several amyloid diseases, such as Alzheimer's disease. Prion diseases, such as scrapie also involve formation of amyloid by polymerization of the host prion protein (PrP). Complement activation is likely to contribute to neuronal damage in the end stages of prion diseases, but is also thought to participate in the initial infection, dissemination and replication stages. Infectious prion particles are likely to bind C1q and activate the complement system. Bound complement proteins may then influence the uptake and transport of prion particles by dendritic cells (DCs) and their subsequent proliferation at sites such as follicular DCs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 355-362
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 355-362
نویسندگان
Robert B. Sim, Uday Kishore, Christian L. Villiers, Patrice N. Marche, Daniel A. Mitchell,