The fibril forming region of the beta-amyloid precursor differs from that of the amyloid A precursor in its interaction with lipids

Autor:	J S, Liang, R E, Fine, C R, Abraham, J D, Sipe
Rok vydání:	1996
Předmět:	Iodine Radioisotopes Amyloid beta-Protein Precursor Kinetics Serum Amyloid A Protein Structure-Activity Relationship Apolipoproteins Binding Sites Cholesterol Phosphatidylcholines Humans Binding Competitive Recombinant Proteins
Zdroj:	Biochemical and biophysical research communications. 219(3)
ISSN:	0006-291X
Popis:	Since the amyloid A (AA) precursoir, serum amyloid A (apoSAA), has been shown to bind cholesterol (C) in the AA fibril forming region, we investigated the interaction of the beta-amyloid precursor protein (AbetaPP) and beta-amyloid (Abeta) peptide with C and phosphatidyl choline (PC) by measuring changes in binding to microtiter wells at physiological pH and ionic strength. While either C or PC inhibited AbetaPP binding to the same extent that C inhibited apoSAA binding, neither C nor PC had any effect on binding of the Abeta peptide, although antibodies to Abeta1-40 did block binding. The binding of (125)I-Abeta1-40 and (125)I-AbetaPP was inhibited by apoE3 and apoE4, but not by either apoSAA or bovine serum albumin. Bound (125)I-AbetaPP was partially released into medium containing C, PC, apoE3, apoE4, or antibodies to AbetaPP. Our results indicate that AbetaPP but not Abeta peptide can be retained in solution in the presence of C and PC and suggest that this failure to interact with lipids may account for the greater insolubility of Abeta fibrils than AA fibrils.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7b161fa3bc92753d283898f9a0dc9c65 https://pubmed.ncbi.nlm.nih.gov/8645287 Zobrazit plný text záznamu Full Text from ScienceDirect