Blood Amyloid-β Oligomerization as a Biomarker of Alzheimer's Disease: A Blinded Validation Study.

Background: Oligomeric amyloid-β (Aβ) is one of the major contributors to the pathomechanism of Alzheimer's disease (AD); Aβ oligomerization in plasma can be measured using a Multimer Detection System-Oligomeric Aβ (MDS-OAβ) after incubation with spiked synthetic Aβ.

Objective: We evaluated the clinical sensitivity and specificity of the MDS-OAβ values for prediction of AD.

Methods: The MDS-OAβ values measured using inBlood™ OAβ test in heparin-treated plasma samples from 52 AD patients in comparison with 52 community-based subjects with normal cognition (NC).

Oligomeric forms of amyloid-β protein in plasma as a potential blood-based biomarker for Alzheimer's disease.

Background: Soluble amyloid-β (Aβ) oligomers are the major toxic substances associated with the pathology of Alzheimer's disease (AD). The ability to measure Aβ oligomer levels in the blood would provide simple and minimally invasive tools for AD diagnostics. In the present study, the recently developed Multimer Detection System (MDS) for AD, a new enzyme-linked immunosorbent assay for measuring Aβ oligomers selectively, was used to detect Aβ oligomers in the plasma of patients with AD and healthy control individuals.

Dynamic changes of oligomeric amyloid β levels in plasma induced by spiked synthetic Aβ.

Background: A reliable blood-based assay is required to properly diagnose and monitor Alzheimer's disease (AD). Many attempts have been made to develop such a diagnostic tool by measuring amyloid-β oligomers (AβOs) in the blood, but none have been successful in terms of method reliability. We present a multimer detection system (MDS), initially developed for the detection of prion oligomers in the blood, to detect AβOs.

Magnetic microparticle-based multimer detection system for the detection of prion oligomers in sheep.

Transmissible spongiform encephalopathies (TSEs) are zoonotic fatal neurodegenerative diseases in animals and humans. TSEs are commonly known as bovine spongiform encephalopathy in cattle, scrapie in sheep and goats, chronic wasting disease in cervids, and Creutzfeldt-Jakob disease in humans. The putative transmissible agents are infectious prion proteins (PrP(Sc)), which are formed by the conversion of the normal prion protein on the glycoprotein cell surface in the presence of other PrP(Sc).