期刊
JOURNAL OF NEGATIVE RESULTS IN BIOMEDICINE
卷 16, 期 -, 页码 -出版社
BMC
DOI: 10.1186/s12952-017-0066-3
关键词
Alzheimer disease; Amyloid beta protein; Amyloid precursor protein; Antibody; Cross reactivity; Experimental design
资金
- NIHR
- National Institute for Health Research [NF-SI-0611-10084] Funding Source: researchfish
Background: Alzheimer disease (AD) research has focussed mainly on the amyloid beta protein (A beta). However, many A beta-and P3-type peptides derived from the amyloid precursor protein (APP) and peptides thought to derive from A beta catabolism share sequence homology. Additionally, conformations can change dependent on aggregation state and solubility leading to significant uncertainty relating to interpretations of immunoreactivity with antibodies raised against A beta. We review evidence relating to the reactivities of commonly used antibodies including 6F3D, 6E10 and 4G8 and evaluate their reactivity profiles with respect to AD diagnosis and research. Results: Antibody cross-reactivities between A beta-type, P3-type and A beta-catabolic peptides confound interpretations of immunoreactivity. More than one antibody is required to adequately characterise A beta. The relationships between anti-A beta immunoreactivity, neuropathology and proposed APP cleavages are unclear. Conclusions: We find that the concept of A beta lacks clarity as a specific entity. Anti-A beta antibody cross-reactivities lead to significant uncertainty in our understanding of the APP proteolytic system and its role in AD with profound implications for current research and therapeutic strategies.
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