| First Author | Araki E | Year | 1995 |
| Journal | Amyloid | Volume | 2 |
| Issue | 2 | Pages | 100-106 |
| Mgi Jnum | J:27775 | Mgi Id | MGI:75260 |
| Doi | 10.3109/13506129509031894 | Citation | Araki E, et al. (1995) Transgenic mice expressing the amyloid beta protein- containing carboxyl-terminal fragment of the alzheimer amyloid precursor protein. Amyloid 2(2):100-106 |
| abstractText | The deposition of amyloid beta protein (A beta) in the brain is one of the main pathological features of Alzheimer's disease (AD). A beta is derived from the amyloid precursor protein (A beta PP). It was shown that the carboxyl-terminal 100 residues of A beta PP containing the A beta sequence could form amyloid-like fibrils, and could be neurotoxic in vitro. To investigate the relationship between this fragment and amyloidogenesis in vivo, we developed transgenic mice expressing the A beta- containing carboxyl-terminal fragment under the control of the neuron specific enolase promoter. In these mice, the mRNA from the transgene was expressed at a substantial level in the brain. However, immunohistochemical studies of the brains did not show any pathologic changes. These results suggest that the expression of the A beta containing carboxyl-terminal fragment itself may not directly lead to AD-like neuropathologic changes in vivo. |
