Bons N, Jallageas V, Silhol S, Mestre-Frances N, Petter A, Delacourte A
Laboratoire de neuromorphologie fonctionnelle, Université de Montpellier-II, France.
C R Acad Sci III. 1995 Jan;318(1):77-83.
The immunocytochemistry of Tau proteins in the cortical pyramidal neurons of the adult microcebes has been studied, using antibodies against human normal and pathological Tau proteins. Some changes related to the age and to some pathologies were observed. In fact, during the adult life, Tau proteins appeared as very thin granulations scattered in the whole neuronal cytoplasm. With age, a part of these proteins aggregated and became like thick granules at the neuron periphery; the distribution was not uniform, and numerous neurons with aggregated Tau proteins were observed in amyloid plaque-containing brains. Abnormally phosphorylated Tau proteins were also observed in some aged animals, using an absorbed anti-PHF recognizing the pathological Tau proteins characteristic of Alzheimer's disease. This present work confirms that the microcebe is a good model for studying disfunctions involved in the normal cerebral aging and in some neurodegenerative disorders which affect humans.
利用抗人正常和病理性Tau蛋白的抗体，对成年小头畸形个体皮质锥体细胞中的Tau蛋白进行了免疫细胞化学研究。观察到了一些与年龄和某些病理相关的变化。事实上，在成年期，Tau蛋白表现为散布在整个神经元细胞质中的非常细的颗粒。随着年龄增长，这些蛋白的一部分聚集并在神经元周边变成粗大颗粒；分布不均匀，在含有淀粉样斑块的大脑中观察到许多带有聚集Tau蛋白的神经元。使用识别阿尔茨海默病特征性病理性Tau蛋白的吸收性抗PHF，在一些老龄动物中也观察到了异常磷酸化的Tau蛋白。本研究证实，小头畸形个体是研究正常脑老化以及某些影响人类的神经退行性疾病所涉及功能障碍的良好模型。
