A NOVEL AMYLOID COMPONENT

淀粉样蛋白作为老年斑的核心并沿着血管壁积聚 阿尔茨海默氏病患者的脑组织中。 淀粉样蛋白的主要成分是一种由39-43个氨基酸组成的肽， 淀粉样β/A4-蛋白（A/β）来源于一种前体， 十万道尔顿。 最近的免疫学研究表明， 急性时相蛋白与淀粉样蛋白有关， 淀粉样蛋白可能由多种蛋白质组成。 然而，在生物化学上，Abeta仍然是唯一被鉴定的成分， 多年来 然而，最近，我们发现了一种新的成分 在AD淀粉样蛋白中的生物化学作用，并建议使用 分子生物学、生物化学、免疫学和细胞生物学 技术. 完全消化纯化的AD淀粉样蛋白，溶解在70%甲酸中， 用溴化氰和无色杆菌蛋白酶消化 除了ABeta片段，我还得到了两个未知的肽 顺序 这些序列用于产生抗血清。 两种抗血清 这些序列的一部分用于产生寡核苷酸， 通过PCR扩增来自脑cDNA文库的DNA片段。 A 247- 扩增出一段核苷酸DNA片段。 这个短DNA的测序 证明了这种DNA编码的蛋白质含有一个完美的 与淀粉样蛋白中的肽序列相匹配 一个全长cDNA， 使用以下方法分离含有两种新淀粉样蛋白序列蛋白质 该PCR扩增探针。 我们把含有这些肽的蛋白质称为 NACP用于进一步的免疫组织化学和免疫化学分析， 蛋白 将使用反义策略来鉴定生物 NACP的功能。 最后，NAC或NACP与 将研究APP或Abeta。 NAC和NACP的表征 应该进一步阐明AD的淀粉样变性，并可能有助于 找出这种毁灭性疾病的病因

Amyloid accumulates as a core of senile plaques and along the vessel wall in the brain tissue of patients afflicted with Alzheimer's disease (AD). The major constituent of amyloid is a 39-43 amino acid peptide called amyloid Beta/A4-protein (A/Beta) derived from a precursor of around 100,000 daltons. Recent immunological studies have demonstrated many acute phase proteins are associated with amyloid, raising the possibility that amyloid might be composed of more than one type of protein. However, biochemically, Abeta had remained the only component identified for many years. However, recently, we have identified a new component in an AD amyloid biochemically and propose to study this protein using molecular biological, biochemical, immunological, and cell biological techniques. The complete digestion of purified AD amyloid, solubilized in 70% formic acid, and digested by cyanogen bromide and Achromobacter lyticus protease I yielded, in addition to ABeta fragments, two peptides of unknown sequence. These sequences were used to raise antisera. Two antisera portion of these sequences was used to generate oligonucleotide that were used by PCR to amplify DNA fragments from a brain cDNA library. A 247- nucleotide DNA segment was amplified. The sequencing of this short DNA demonstrated that this DNA encodes a protein that contains a perfect match with the peptide sequence found n amyloid. A full-length cDNA for the protein containing both two new amyloid sequence was isolated using this PCR amplified probe. We call the protein containing these peptide NACP for further immunohistochemical and immunochemical analysis of this protein. Antisense strategy will be used to identify the biological function of NACP. Finally, potential interaction between NAC or NACP and APP or Abeta will be investigated. Characterization of NAC and NACP should shed further light on the amyloidogenesis in AD and might help in finding the etiology of this devastating disease.