1992/02/01 by Thomas Wısnıewskı, Blas Frangione · 7 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Chemistry · #Amyloidosis: Diagnosis, Treatment, Outcomes #Alzheimer's disease research and treatments #Bioinformatics and Genomic Networks #Amyloid (mycology) #Pathological #Apolipoprotein E #Immunohistochemistry #Serum amyloid P component #Apolipoprotein B #Amyloidosis #Biochemistry of Alzheimer's disease #Amyloid fibril #P3 peptide #Pathology #Biology #Chemistry #Biochemistry #Alzheimer's disease #Amyloid β #Medicine #Amyloid precursor protein #Immunology #Inflammation #Disease #Cholesterol #C-reactive protein
paper · pdf · doi:10.1016/0304-3940(92)90444-c
openalex publication_date 1992/02/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Many biochemically diverse proteins can give rise to amyloid fibrils; however, they are all accompanied by P component and glucosaminoglycans. With antibodies specific to apolipoprotein E (apo E) we used immunohistochemical techniques to test for the presence of this protein in both cerebral and systemic amyloid. We found apo E immunoreactivity in all tested types of cerebral and systemic amyloid. In amyloid deposits apo E P, component and glucosaminoglycans may be acting as 'pathological molecular chaperones'. The latter we define as a group of unrelated proteins that induce beta-pleated conformation in amyloidogenic polypeptides.