MacDonald Alan B
St. Catherine of Siena Medical Center, Department of Pathology, 50 Rte 25 A, Smithtown, NY 11787, USA.
Med Hypotheses. 2006;67(3):592-600. doi: 10.1016/j.mehy.2006.02.035. Epub 2006 May 3.
Here is hypothesized a truly revolutionary notion that rounded cystic forms of Borrelia burgdorferi are the root cause of the rounded structures called plaques in the Alzheimer brain. Rounded "plaques' in high density in brain tissue are emblematic of Alzheimer's disease (AD). Plaques may be conceptualized as rounded "pock mark-like" areas of brain tissue injury. In this century, in brain tissue of AD, plaques are Amyloid Plaques according to the most up to date textbooks. In the last century, however, Dr. Alois Alzheimer did not require amyloid as the pathogenesis for either the disease or for the origin of its plaques. Surely, amyloid is an event in AD, but it may not be the primal cause of AD. Indeed in plaques, amyloid is regularly represented by the "congophilic core" structure which is so named because the waxy amyloid material binds the congo red stain and is congophilic. However an accepted subset of plaques in AD is devoid of a congophilic amyloid core region (these plaques "cotton wool" type plaques, lack a central congophilic core structure). Furthermore, there is "plaque diversity" in Alzheimer's; small, medium and large plaques parallel variable cystic diameters for Borrelia burgdorferi. Perturbations of AD plaque structure (i.e. young plaques devoid of a central core and older plaques with or without a central core structure) offer room for an alternate pathway for explanation of ontogeny of the plaque structures. If amyloid is not required to initiate all of the possible plaques in Alzheimer's, is it possible that amyloid just a by product of a more fundamental primal path to dementia? If a byproduct status is assigned to amyloid in the realm of plaque formation, then is amyloid also an epiphenomenon rather than a primary pathogenesis for Alzheimer's disease. In the "anatomy is destiny" model, cysts of borrelia are always round. Why then not accept roundness as a fundamental "structure determines function" argument for the answer to the mystery of why Alzheimer plaques are always round? Parataxis causality, a concept borrowed from philosophy, is the error that comes from linking two events, which occur contemporaneously or in close proximity to one another with a cause and effect relationship. Parataxis tells us that what appears to be cause and effect in the couplet "amyloid plaque" merely by a proximity relationship may be "spurious causality" which is a cognitive dead end.
这里提出了一个真正具有革命性的观点，即伯氏疏螺旋体的圆形囊状形态是阿尔茨海默病大脑中被称为斑块的圆形结构的根本原因。脑组织中高密度的圆形“斑块”是阿尔茨海默病（AD）的标志。斑块可被概念化为脑组织损伤的圆形“痘痕样”区域。在本世纪，根据最新的教科书，AD脑组织中的斑块是淀粉样斑块。然而，在上个世纪，阿洛伊斯·阿尔茨海默博士并不认为淀粉样蛋白是该疾病或其斑块起源的发病机制。当然，淀粉样蛋白是AD中的一个事件，但它可能不是AD的主要原因。实际上，在斑块中，淀粉样蛋白通常由“嗜刚果红核心”结构代表，因其蜡状淀粉样物质与刚果红染料结合且嗜刚果红而得名。然而，AD中公认的一部分斑块没有嗜刚果红淀粉样核心区域（这些斑块是“棉絮”样斑块，缺乏中央嗜刚果红核心结构）。此外，阿尔茨海默病中存在“斑块多样性”；小、中、大斑块与伯氏疏螺旋体的可变囊状直径相对应。AD斑块结构的扰动（即没有中央核心的年轻斑块和有或没有中央核心结构的老年斑块）为解释斑块结构的个体发生提供了另一种途径。如果启动AD中所有可能的斑块不需要淀粉样蛋白，那么淀粉样蛋白有可能只是通往痴呆症的更基本原始路径的副产品吗？如果在斑块形成领域将淀粉样蛋白的状态归为副产品，那么淀粉样蛋白是否也是一种附带现象而非阿尔茨海默病的主要发病机制呢？在“解剖即命运”模型中，疏螺旋体的囊肿总是圆形的。那么，为什么不接受圆形作为一个基本的“结构决定功能”的论据，来解释阿尔茨海默斑块为何总是圆形这个谜团呢？并列因果关系是一个从哲学中借用的概念，它是将两个同时发生或彼此接近的事件用因果关系联系起来所产生的错误。并列因果关系告诉我们，在“淀粉样斑块”这一对中看似因果关系的，仅仅是由于接近关系，可能是“虚假因果关系”，这是一个认知上的死胡同。
