RAGE binds C1q and enhances C1q-mediated phagocytosis

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• 作者：Wanchao Ma^a ; Vivek Rai^b ; Barry I. Hudson^b ; Fei Song^b ; Ann Marie Schmidt^b ; Gaetano R. Barile^a ; ^{grb17@columbia.edu}
• 关键词：SLE ; systemic lupus erythematosus ; AGEs ; advanced glycation end-products ; RAGE ; receptor for AGEs ; sRAGE ; soluble form of RAGE ; SPR ; surface plasmon resonance ; BSA ; bovine serum albumin ; HSA ; human serum albumin ; FBS ; fetal bovine serum ; A-beta ; amyloid-b
• 刊名：Cellular Immunology
• 出版年：2012
• 期刊代码：279_00088749
• 类别：med
• 出版时间：2012
• 卷：274
• 期：1-2
• 页码：72-82
• 文件大小：1269 K

摘要

RAGE, the multiligand receptor of the immunoglobulin superfamily of cell surface molecules, is implicated in innate and adaptive immunity. Complement component C1q serves roles in complement activation and antibody-independent opsonization. Using soluble forms of RAGE (sRAGE) and RAGE-expressing cells, we determined that RAGE is a native C1q globular domain receptor. Direct C1q-sRAGE interaction was demonstrated with surface plasmon resonance (SPR), with minimum K_d 5.6 渭M, and stronger binding affinity seen in ELISA-like experiments involving multivalent binding. Pull-down experiments suggested formation of a receptor complex of RAGE and Mac-1 to further enhance affinity for C1q. C1q induced U937 cell adhesion and phagocytosis was inhibited by antibodies to RAGE or Mac-1. These data link C1q and RAGE to the recruitment of leukocytes and phagocytosis of C1q-coated material.