| First Author | Ou-Yang MH | Year | 2015 |
| Journal | Neurobiol Aging | Volume | 36 |
| Issue | 2 | Pages | 801-11 |
| PubMed ID | 25457550 | Mgi Jnum | J:219504 |
| Mgi Id | MGI:5621084 | Doi | 10.1016/j.neurobiolaging.2014.10.006 |
| Citation | Ou-Yang MH, et al. (2015) N-terminal region of myelin basic protein reduces fibrillar amyloid-beta deposition in Tg-5xFAD mice. Neurobiol Aging 36(2):801-11 |
| abstractText | Alzheimer's disease is a progressive neurodegenerative disorder that is characterized by extensive deposition of fibrillar amyloid-beta (Abeta) in the brain. Previously, myelin basic protein (MBP) was identified to be a potent inhibitor to Abeta 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 Abeta accumulation in brain. The levels of insoluble Abeta 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 Abeta fibril formation in vitro and demonstrate the ability of MBP1 to reduce Abeta pathology and improve behavioral performance. |
