AMYLOID ANGIOPATHY, EARLY PLAQUES, AND AGING

淀粉样变性包括一组异质性疾病， 在临床表现和组成和分布 不溶性淀粉样纤维。 据信，所有类型的 淀粉样变性涉及可溶性前体的过度产生， 沉积发生在遗传或其他方面 在降解这些分子方面有缺陷。 提出了一种 三分问题的核心要素 发病机制：固有的化学淀粉碘的潜力， 前体蛋白;异常蛋白质代谢的可能性， 以及疾病微环境组织因子的存在， 可以促进前体蛋白转化为它们的 不溶性淀粉样产物。 最近，我们发现，散发性甲状腺癌的淀粉样纤维 脑淀粉样血管病和一种常染色体显性遗传的 荷兰血统的家族性淀粉样血管病（也 指定为荷兰淀粉样变性的遗传性脑出血 型）类似于阿尔茨海默病淀粉样蛋白B-蛋白。 这些 研究结果表明，B-淀粉样蛋白沉积障碍形成了一个 一系列重叠的临床病理学状况， 从主要血管受累的患者到 具有血管和薄壁组织的组合， 不同比例，临床表现为中风和痴呆， 分别 我们还发现，这些疾病表现出 不同的神经炎斑块样结构，或“类神经炎性” 病变，”这表明它们代表了早期阶段的B- 蛋白质沉积 类似的淀粉样沉积物经常会遇到 在神经系统无症状的老年人中， 因此，明确他们之间的关系很重要。 我们提出以下建议：1）生化和免疫组化 无症状老年人早期淀粉样蛋白沉积的研究 脑淀粉样血管病患者。 2)鉴定 老年人的淀粉样蛋白前体。 3)细胞研究 细胞内淀粉样蛋白前体的起源和合成 在文化中成长。 本研究对了解原发性高血压的基本病因有一定意义。 与衰老中淀粉样蛋白沉积相关的机制，淀粉样蛋白 血管病和阿尔茨海默病;它可能是有用的， 在病理和临床水平上的诊断目的。

Amyloidosis comprises a heterogeneous group of diseases that vary in clinical expression and the composition and distribution of insoluble amyloid fibrils. It is believed that all types of amyloidosis involve overproduction of a soluble precursor, and that deposition occurs in patients who are genetically or otherwise defective in degrading these molecules. We put forward a tripartite division of the elements central to the issue of pathogenesis: the inherent chemical amyliodogenic potential of the precursor protein; the possibility of aberrant protein metabolism, and the existence of disease microenviromental tissue factors that may facilitate the conversion of precursor proteins into their insoluble amyloid products. Recently we have shown that the amyloid fibrils of sporadic cerebral amyloid angiopathy and an autosomal dominant form of familial amyloid angiopathy in patients of Dutch origin (also designated Hereditary Cerebral Hemorrhage with Amyloidosis of Dutch Type) are similar to Alzheimer Disease amyloid B-protein. These findings indicate that B-amyloid deposition disorders form a spectrum of overlapping clinicopathological conditions which range from patients with predominant vascular involvement to patients having a combination of vascular and parenchyma involvement in varying proportions, manifested clinically by stroke and dementia, respectively. We have also found that these disorders exhibit varying neuritic plaque-like structures, or "preamyloidotic lesions," suggesting that they represent an early stage of B- protein deposition. Similar amyloid deposits are often encountered in a significant percent of neurologically asymptomatic aged individuals; hence it is important to clarify their relationship. We propose the following: 1) Biochemical and immunohistochemical studies of early amyloid deposits in asymptomatic elders and patients with cerebral amyloid angiopathy. 2) Identification of the amyloid protein precursor in aged humans. 3) Study of cellular origin and synthesis of the amyloid protein precursor in cells grown in culture. This study is relevant for understanding the basic etiopathogenetic mechanisms associated with amyloid deposition in aging, amyloid angiopathy, and Alzheimer's Disease; it may be useful for diagnostic purposes at a pathological and clinical level.