| First Author | Detrait E | Year | 2014 |
| Journal | Behav Brain Res | Volume | 271 |
| Pages | 277-85 | PubMed ID | 24937053 |
| Mgi Jnum | J:217012 | Mgi Id | MGI:5612918 |
| Doi | 10.1016/j.bbr.2014.06.013 | Citation | Detrait E, et al. (2014) Lack of synaptic vesicle protein SV2B protects against amyloid-beta(2)(5)(-)(3)(5)-induced oxidative stress, cholinergic deficit and cognitive impairment in mice. Behav Brain Res 271:277-85 |
| abstractText | SV2B is a synaptic protein widely distributed throughout the brain, which is part of the complex vesicle protein machinery involved in the regulation of synaptic vesicle endocytosis and exocytosis, and therefore in neurotransmitters release. The aims of the present work were twofold: (1) phenotype SV2B knockout mice (SV2B KO) in a battery of cognitive tests; and (2) examine their vulnerability to amyloid-beta25-35 (Abeta25-35) peptide-induced toxicity. SV2B KO mice showed normal learning and memory abilities in absence of Abeta25-35 injection. SV2B KO mice were protected against the learning deficits induced after icv injection of an oligomeric preparation of amyloid-beta25-35 peptide, as compared to wild-type littermates (SV2B WT). These mice failed to show Abeta25-35-induced impairments in a number of cognitive domains: working memory measured by a spontaneous alternation procedure, recognition memory measured by a novel object recognition task, spatial reference memory assessed in a Morris water-maze, and long-term contextual memory assessed in a inhibitory avoidance task. In addition, SV2B KO mice were protected against Abeta25-35-induced oxidative stress and decrease in ChAT activity in the hippocampus. These data suggest that SV2B could be a key modulator of amyloid toxicity at the synaptic site. |
