Premium
Intravenous immunoglobulin enhances the clearance of fibrillar amyloid‐β peptide
Author(s) -
Istrin Gili,
Bosis Eran,
Solomon Beka
Publication year - 2006
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20886
Subject(s) - antibody , peptide , amyloid (mycology) , chemistry , immunoglobulin g , biochemistry , immunology , medicine , inorganic chemistry
Intravenous immunoglobulin (IVIg), a purified immunoglobulin fraction manufactured from the blood of healthy humans, is an FDA‐approved treatment for many immune and inflammatory diseases. Recent studies have demonstrated that IVIg therapy has several positive effects on patients with Alzheimer's disease (AD). These include improving cognitive functions and lowering the level of soluble amyloid‐β peptide (AβP) in the brain. Nonetheless, the mechanism by which IVIg mediates the clearance of AβP from the AD brain currently remains unknown. In this study we investigated the molecular basis for the direct and indirect effects of IVIg on AβP clearance using the BV‐2 cellular microglia line. Specifically, we show that IVIg dissolves preformed AβP fibrils in vitro. Moreover, IVIg increases cellular tolerance to AβP, enhances microglial migration toward AβP deposits, and mediates phagocytosis of AβP. Thus, several mechanisms can be considered when examining the effects of IVIg. Our work supports the hypothesis that IVIg interferes by more than one mechanism in clearing AβP from the brains of Alzheimer's patients. © 2006 Wiley‐Liss, Inc.