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首页> 美国卫生研究院文献>Biochemical Journal >Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site.
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Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site.

机译：头在阿尔茨海默氏症的神经原纤维缠结中。 N和C末端区域与成对的螺旋丝和假定的异常磷酸化位点的位置差异相关。

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To investigate the extent to which whole tau proteins, structurally abnormal tau and fragments of tau are incorporated into neurofibrillary tangles in Alzheimer's disease, an immunocytochemical mapping study using a panel of antibodies to several synthetic human tau peptides has been performed. Neurofibrillary tangles were immunolabelled in situ, and paired helical filaments (PHF), the principal structural component of tangles, were immunolabelled after isolation and Pronase treatment. N-Terminal and C-terminal domains of tau were found to be present in tangles in situ. SDS-treated PHF were found to contain most of the C-terminal half of tau and were also labelled by antibodies to ubiquitin. Only some of these PHF were labelled by antisera to tau sequences towards the N-terminus, and this enabled the identification of a region of tau in which proteolytic cleavage may occur. The ultrastructural appearance of the immunolabelling suggested that both the N- and C-terminal domains of tau extend outwards from the axis of PHF. After Pronase treatment. PHF were strongly labelled only by an antiserum to PHF and by the antiserum to the most C-terminal tau synthetic peptide. The latter antiserum also strongly labelled extracellular tangles in situ, whereas these extracellular tangles were poorly labelled by the antisera to the other synthetic peptides. One anti-(tau peptide) serum labelled a population of neurofibrillary tangles in situ only after alkaline phosphatase pretreatment of tissue sections. Our results show that, although peptides along the length of the tau molecule are associated with neurofibrillary tangles in situ, only the C-terminal one-third of the molecule is tightly associated with PHF, since this region of tau is resistant to SDS treatment of PHF. We also report the existence in PHF in situ of a masked tau epitope which is partially unmasked by dephosphorylation. These results are indicative of post-translational changes in tangle-associated tau in degenerating neurons in Alzheimer's disease.
机译：为了研究整个tau蛋白，结构异常的tau和tau片段掺入阿尔茨海默氏病的神经原纤维缠结的程度，已经进行了免疫细胞化学作图研究，使用了一组针对几种合成人tau肽的抗体。神经原纤维缠结被原位免疫标记，成对的螺旋细丝（PHF）是缠结的主要结构成分，在分离和Pronase处理后被免疫标记。发现tau的N端和C端结构域原位存在于缠结中。发现经SDS处理的PHF包含tau的大部分C末端，并且还被泛素抗体标记。这些PHF中只有一些被抗血清标记指向N端的tau序列，这使得能够鉴定可能发生蛋白水解切割的tau区域。免疫标记的超微结构表明，tau的N和C末端结构域均从PHF轴向外延伸。经Pronase处理。仅通过对PHF的抗血清和对最C端tau合成肽的抗血清强烈标记PHF。后者的抗血清还在原位强烈标记细胞外缠结，而这些细胞外缠结对其他合成肽的抗血清标记能力较差。仅在碱性磷酸酶预处理组织切片后，一种抗（tau肽）血清才在原位标记一群神经原纤维缠结。我们的研究结果表明，尽管沿tau分子长度的肽原位与神经原纤维缠结相关，但只有分子的C端三分之一与PHF紧密相关，因为tau的这一区域对SDS处理具有抗性。 PHF。我们还报告了被掩盖的tau表位原位存在于PHF中，该表位被去磷酸化部分掩盖。这些结果表明在阿尔茨海默氏病变性神经元中缠结相关的tau的翻译后变化。

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