Department of Physiology, University of Toronto, Toronto, ON, Canada.
J Alzheimers Dis. 2011;27(2):243-52. doi: 10.3233/JAD-2011-110353.
Alzheimer's disease (AD) is the most common form of dementia characterized by the presence of amyloid-β (Aβ) plaques and neurofibrillary tangles. The mechanisms leading to AD are not completely understood; however, recent evidence suggests that alterations in Fyn, a Src family kinase, might contribute to AD pathogenesis. A number of studies have demonstrated that Fyn is involved in synaptic plasticity, a cellular mechanism for learning and memory. In addition, Fyn plays a role in the regulation of Aβ production and mediates Aβ-induced synaptic deficits and neurotoxicity. Fyn also induces tyrosine phosphorylation of tau. Although many studies have implicated a role for Fyn in AD, the precise cellular and molecular mechanisms require further investigation. Novel insights into the role of Fyn in AD may help identify alternative pharmacological approaches for the treatment of AD.
阿尔茨海默病（AD）是最常见的痴呆症形式，其特征是存在淀粉样蛋白-β（Aβ）斑块和神经原纤维缠结。导致 AD 的机制尚不完全清楚；然而，最近的证据表明，Src 家族激酶 Fyn 的改变可能有助于 AD 的发病机制。许多研究表明，Fyn 参与突触可塑性，这是学习和记忆的细胞机制。此外，Fyn 在调节 Aβ 产生和介导 Aβ 诱导的突触缺陷和神经毒性方面发挥作用。Fyn 还诱导 tau 的酪氨酸磷酸化。尽管许多研究表明 Fyn 在 AD 中的作用，但确切的细胞和分子机制需要进一步研究。对 Fyn 在 AD 中的作用的新认识可能有助于确定治疗 AD 的替代药物治疗方法。
