Hyperphosphorylation of microtubule-associated protein tau in senescence-accelerated mouse (SAM)
Hyperphosphorylation of microtubule-associated protein tau in senescence-accelerated mouse (SAM)
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DOI：
10.1016/j.mad.2005.07.008
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发表时间：
2005-12-01
影响因子：
5.3
通讯作者：
Pallàs, M
中科院分区：
文献类型：
--
作者：
Canudas, AM;Gutierrez-Cuesta, J;Pallàs, M
Tau 是一种主要在轴突上发现的神经元微管相关蛋白。 Tau 磷酸化调节该蛋白的正常和病理功能。过度磷酸化会损害 tau 蛋白的微管结合功能，导致大脑中微管不稳定，最终导致受影响神经元的退化。许多丝氨酸/苏氨酸激酶，包括 GSK-3 beta 和 Cdk5 可以磷酸化 tau。 SAMR1 和 SAMP8 是小鼠衰老品系。我们发现，与耐药菌株 SAMR1 相比，SAMP8（衰老小鼠）中 tau 的过度磷酸化形式有所增加。此外，描述了 Cdk5 表达和激活的增加，但 GSK3 β 同种型的分析未能显示 SAMP8 与年龄匹配的 SAMR1 相比的差异。总之，tau 蛋白过度磷酸化发生在 SAMP-8（早期衰老）小鼠中，表明该小鼠模型中衰老与 tau 蛋白修饰之间存在联系。 (c) 2005 年，爱思唯尔爱尔兰有限公司出版。
Tau is a neuronal microtubule-associated protein found predominantly on axons. Tau phosphorylation regulates both normal and pathological functions of this protein. Hyperphosphorylation impairs the microtubule binding function of tau, resulting in the destabilization of microtubules in brain, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases, including GSK-3 beta and Cdk5 can phosphorylate tau. SAMR1 and SAMP8 are murine strains of senescence. We show an increase in hyperphosphorylated forms of tau in SAMP8 (senescent mice) in comparison with resistant strain SAMR1 Moreover, an increase in Cdk5 expression and activation is described but analysis of GSK3 beta isoforms failed to show differences in SAMP8 in comparison to age-matched SAMR1. In conclusion, tau hyperphosphorylation occurs in SAMP-8 (early senescent) mice, indicating a link between aging and tau modifications in this murine model. (c) 2005 Published by Elsevier Ireland Ltd.