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N-terminal region of myelin basic protein reduces fibrillar amyloid-β deposition in Tg-5xFAD mice.

Abstract：

:Alzheimer's disease is a progressive neurodegenerative disorder that is characterized by extensive deposition of fibrillar amyloid-β (Aβ) in the brain. Previously, myelin basic protein (MBP) was identified to be a potent inhibitor to Aβ fibril formation, and this inhibitory activity was localized to the N-terminal residues 1-64, a fragment designated MBP1. Here, we show that the modest neuronal expression of a fusion protein of the biologically active MBP1 fragment and the enhanced green fluorescent protein (MBP1-EGFP) significantly improved the performance of spatial learning memory in Tg-5xFAD mice, a model of pathologic Aβ accumulation in brain. The levels of insoluble Aβ and fibrillar amyloid were significantly reduced in bigenic Tg-5xFAD/Tg-MBP1-EGFP mice. Quantitative stereological analysis revealed that the reduction in amyloid was because of a reduction in the size of fibrillar plaques rather than a decrease in plaque numbers. The current findings support previous studies showing that MBP1 inhibits Aβ fibril formation in vitro and demonstrate the ability of MBP1 to reduce Aβ pathology and improve behavioral performance.

journal_name

Neurobiol Aging

journal_title

Neurobiology of aging

authors

Ou-Yang MH,Xu F,Liao MC,Davis J,Robinson JK,Van Nostrand WE

doi

10.1016/j.neurobiolaging.2014.10.006

subject

Has Abstract

pub_date

2015-02-01 00:00:00

pages

801-11

issue

2

eissn

0197-4580

issn

1558-1497

pii

S0197-4580(14)00644-7

journal_volume

36

pub_type

杂志文章

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