Delacourte A, Sautière P E, Wattez A, Mourton-Gilles C, Petter A, Bons N
INSERM U. 422, Lille, France.
C R Acad Sci III. 1995 Jan;318(1):85-9.
Tau proteins extracted from the brain of 12 adult microcebes ranging from 2 to 9 years old were characterized by Western blots, using immunological probes against normal and pathological human Tau proteins. In microcebes, the molecular weight of Tau proteins increases during aging, with variants of 52-54, 64, 67 kDa in the young adult and variants of 60 and 70 kDa in the oldest animal studied. The increase of the apparent molecular weight is due to a change of conformation and a stabilization in the "hyperphosphorylated" state, as revealed with phosphorylation-dependent monoclonal antibodies Tau-1 and AD2. Furthermore, AD1 specifically detected Alzheimer-type epitopes on the 60 kDa Tau isoform from a very old microcebe. These results suggest that Microcebus murinus is an interesting model for the study of the biochemical dysfunctions that occur in the human brain during aging and Alzheimer disease.
从12只年龄在2至9岁的成年侏儒鼠大脑中提取的tau蛋白，通过蛋白质免疫印迹法进行表征，使用针对正常和病理性人类tau蛋白的免疫探针。在侏儒鼠中，tau蛋白的分子量随着年龄增长而增加，在年轻成年动物中为52 - 54 kDa、64 kDa、67 kDa变体，在研究的最年长动物中为60 kDa和70 kDa变体。表观分子量的增加是由于构象变化以及在“过度磷酸化”状态下的稳定，这通过磷酸化依赖性单克隆抗体Tau - 1和AD2得以揭示。此外，AD1在一只非常年老的侏儒鼠的60 kDa tau异构体上特异性检测到阿尔茨海默病类型的表位。这些结果表明，小鼠狐猴是研究人类大脑在衰老和阿尔茨海默病过程中发生的生化功能障碍的一个有趣模型。
