The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex
- 1 July 1993
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 293 (1) , 27-30
- https://doi.org/10.1042/bj2930027
Abstract
The amyloid fibrils deposited in Alzheimer's neuritic plaque cores and cerebral blood vessels are mainly composed of aggregated forms of a unique peptide, 39-42 amino acids long, named amyloid beta (A beta). A similar, although soluble, A beta (‘sA beta’) has been identified in cerebrospinal fluid, plasma and cell supernatants, indicating that it is normally produced by proteolytic processing of its precursor protein, amyloid precursor protein (APP). Using direct binding experiments we have isolated and characterized an 80 kDa circulating protein that specifically interacts with a synthetic peptide identical with A beta. The protein was unmistakably identified as SP-40,40 or ApoJ, a cytolytic inhibitor and lipid carrier, by means of amino acid sequence and immunoreactivity with specific antibodies. Immunoprecipitation with anti-SP-40,40 retrieved soluble A beta from cerebrospinal fluid, indicating that the interaction occurs in vivo.Keywords
This publication has 49 references indexed in Scilit:
- Apolipoprotein E: Binding to Soluble Alzheimer′s β-AmyloidBiochemical and Biophysical Research Communications, 1993
- Fibril formation by primate, rodent, and Dutch-hemorrhagic analogs of Alzheimer amyloid .beta.-proteinBiochemistry, 1992
- SP‐40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridgesFEBS Letters, 1992
- Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formationBiochemical and Biophysical Research Communications, 1991
- Abnormal and deficient processing of β-amyloid precursor protein in familial Alzheimer's disease lymphoblastoid cellsBiochemical and Biophysical Research Communications, 1991
- A serum protein SP40,40 modulates the formation of membrane attack complex of complement on erythrocytesMolecular Immunology, 1989
- Ten to fourteen residue peptides of Alzheimer's disease protein are sufficient for amyloid fibril formation and its characteristic xray diffraction patternBiochemical and Biophysical Research Communications, 1987
- In vitro formation of amyloid fibrils from two synthetic peptides of different lengths homologous to alzheimer's disease β-proteinBiochemical and Biophysical Research Communications, 1986
- Purification and characterization of a sulfated glycoprotein secreted by Sertoli cellsBiochemistry, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970