Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid

作者：Adam A. Golabek, Marcos A. Marques, Maciej M. Lalowski, Thomas Wısnıewskı · 发表于：Neuroscience Letters · 年份：1995 · DOI：10.1016/0304-3940(95)11565-7 · 被引用次数：100 · 研究领域：Alzheimer's disease research and treatments、Clusterin in disease pathology、Amyloidosis: Diagnosis, Treatment, Outcomes

A major neuropathological feature of Alzheimer's disease (AD) is the deposition of amyloid beta (A beta) in the form of senile plaques. The A beta peptide exists both in a beta-pleated sheet fibrillar form in amyloid deposits and as a normal soluble protein in biological fluids. Numerous proteins have been identified immunohistochemically to be associated with senile plaques, where A beta is the major constituent. Some of the latter have also been suggested to be carriers of the normal soluble A beta (sA beta) including apolipoprotein J (apoJ), apolipoprotein E (apoE) and transthyretin (TTR). We have found, using several different methods, that numerous proteins can bind synthetic A beta peptides when high concentrations are used; however, using an affinity anti-sA beta column we confirm that apoJ is the major binding protein in pooled human cerebrospinal fluid. On the other hand it is known that apoE co-purifies with A beta biochemically extracted from senile plaques. In AD tissue there may be a change in the major apolipoprotein binding A beta from apoJ to apoE.