Antibodies to the β‐amyloid peptide cross‐react with conformational epitopes in human fibrinogen subunits from peripheral blood
Open Access
- 7 May 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 264 (1), 43-47
- https://doi.org/10.1016/0014-5793(90)80760-g
Abstract
Antibodies to the Alzheimer disease (AD) β‐amyloid peptide (βAP) were used to identify βAP precursor fragments in blood. The antibodies detected 3 major polypeptides with apparent molecular weights (MW) of 47‐64000 in Western blots of plasma derived clot proteins, but these proteins corresponded to human A‐α, B‐β and γ‐fibrinogen since they reacted with 2 different anti‐fibrinogen antisera, and the anti‐βAP and anti‐fibrinogen antibodies recognized purified fibrinogen and fibrin. These data are significant for efforts to develop immunochemical assays to diagnose and monitor the progression of AD.Keywords
This publication has 23 references indexed in Scilit:
- Molecular pathology of amyloidogenic proteins and the role of vascular amyloidosis in Alzheimer's diseaseNeurobiology of Aging, 1989
- The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-IINature, 1989
- Amyloid A4 Protein and Its Precursor in Down's Syndrome and Alzheimer's DiseaseNew England Journal of Medicine, 1989
- Cellular and molecular biology of alzheimer's diseaseBioEssays, 1989
- Expression of the Alzheimer amyloid precursor gene transcripts in the human brainNeuron, 1988
- Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activityNature, 1988
- Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's diseaseNature, 1988
- A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitorsNature, 1988
- The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptorNature, 1987
- Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid proteinBiochemical and Biophysical Research Communications, 1984