Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.
Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.
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DOI：
10.1016/s0021-9258(18)48531-6
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发表时间：
1992-01
期刊：
影响因子：
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通讯作者：
S. G. Greenberg;P. Davies;J D Schein;L I Binder
中科院分区：
文献类型：
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作者：
S. G. Greenberg;P. Davies;J D Schein;L I Binder
Tau (tau) 是阿尔茨海默病中发现的成对螺旋丝 (PHF) 的主要成分。目前的研究探讨了 PHF 相关 tau 蛋白 (tau PHF) 的独特特性是否源于正常可溶性 tau (tau s) 的翻译后修饰。经过氢氟酸 (HF) 处理后，tau PHF 蛋白具有热稳定性和酸稳定性，可溶于 2-(N-吗啉代)乙磺酸缓冲液，并表现出与正常 tau 相同的分子量、pI 和免疫化学特性。碱性磷酸酶处理解离的 PHF 会导致类似但范围较小的电泳变化和 PHF-1 免疫反应性降低。因此，正常 tau 的磷酸化似乎是 tau PHF 独特特性的原因。尽管我们的结果表明所有正常 tau 亚型都存在于 PHF 中，但在 HF 处理的 PHF 和 tau 样品中，各个 tau 物种的相对丰度有所不同。此外，HF 处理后 PHF 的丢失表明翻译后修饰有助于 PHF 的结构稳定性。
Tau (tau) is a major constituent of paired helical filaments (PHF) found in Alzheimer's disease. The current study examines the possibility that the distinct properties of PHF-associated tau proteins (tau PHF) result from post-translational modifications of normal soluble tau (tau s). Following hydrofluoric acid (HF) treatment, tau PHF proteins are heat- and acid-stable, soluble in 2-(N-morpholino)ethanesulfonic acid buffers and display the same molecular weight, pI, and immunochemical properties as normal tau s. Alkaline phosphatase treatment of dissociated PHF results in similar, although less extensive, electrophoretic changes and a reduction in PHF-1 immunoreactivity. Therefore, phosphorylation of normal tau s appears to be responsible for the distinct properties of tau PHF. Although our results suggest that all of the normal tau isoforms are in PHF, the relative abundance of individual tau species differs in HF-treated PHF and tau s samples. Moreover, the loss of PHF following HF treatment suggests that post-translational modifications contribute to the structural stability of PHF.