Immunological characterization of epitopes on tau of Alzheimer's type and chemically modified tau-猫眼课题宝

阿尔茨海默病型 tau 蛋白和化学修饰 tau 蛋白表位的免疫学特征

DOI：

发表时间：

1997

期刊：

Molecular and Cellular Biochemistry

影响因子：

4.3

通讯作者：

中科院分区：

生物学3区

文献类型：

作者：

Gustavo Far¡as;Christian Gonz lez;R. Maccioni

The microtubule-associated protein tau is the main structural component of paired helical filaments (PHFs), which in turn are one of the major aberrant polymers found in Alzheimer's disease. Immunological studies were carried out using site-directed monoclonal and polyclonal antibodies that recognize tubulin binding epitopes on tau, to further understand the mechanisms of tau self-association into PHFs. Tau protein was subjected to either carbamoylation with potassium cyanate (KCNO) or glycation with glucose, and the immunoreactivity of the chemically-modified protein with these antibodies was compared with tau derived from paired helical filaments and with normal brain tau. The data on the immunoblot patterns of tau isoforms and the ELISA titration curves revealed significant differences between the modified tau and normal controls. However, the Western blot patterns of immunoreactive tau from the chemically-modified protein and from Alzheimer brains were similar. The data on the differences in the electrophoretic profiles and Western blots of normal brain tau as compared with solubilized paired helical filaments, insoluble tangles and tau proteins of the Alzheimer's type, provide new clues to understand the anomalous interactions of tau in Alzheimer's disease.