| Literature DB >> 12565837 |
Kazuyuki Takata1, Yoshihisa Kitamura, Jun-ichi Kakimura, Keiichi Shibagaki, Daiju Tsuchiya, Takashi Taniguchi, Mark A Smith, George Perry, Shun Shimohama.
Abstract
In Alzheimer's disease (AD), fibrillar amyloid-beta (Abeta) peptides form senile plaques associated with activated microglia. Recent studies have indicated that microglial Abeta clearance is facilitated by several activators such as transforming growth factor-beta1 (TGF-beta1). The relationship between microglia and Abeta formation and deposition is still unclear. In the present study, high mobility group protein-1 (HMG1) inhibited the microglial uptake of Abeta (1-42) in the presence and absence of TGF-beta1. In addition, HMG1 bound to Abeta (1-42) and stabilized the oligomerization. In AD brains, protein levels of HMG1 were significantly increased in both the cytosolic and particulate fractions, and HMG1 and Abeta were colocalized in senile plaques associated with microglia. These results suggest that HMG1 may regulate the homeostasis of extracellular Abeta (1-42) and Abeta oligomerization.Entities:
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Year: 2003 PMID： 12565837 DOI： 10.1016/s0006-291x(03)00024-x
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575