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ALZHEIMER'S SOLUBLE AMYLOID BETA PROTEIN IS SECRETED BY HEPG2 CELLS AS AN APOLIPOPROTEIN
Author(s) -
KOUDINOV ALEXEI R.,
KOUDINOVA NATALIA V.
Publication year - 1997
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1996.0126
Subject(s) - secretion , immunoprecipitation , apolipoprotein b , lipoprotein , intracellular , cholesterol , apolipoprotein e , cell culture , amyloid (mycology) , secretory protein , chemistry , antibody , biochemistry , cerebrospinal fluid , amyloid beta , microbiology and biotechnology , biology , gene , medicine , immunology , peptide , disease , inorganic chemistry , genetics , neuroscience
Recently we reported that the soluble form of amyloid beta protein (sAβ) in normal human plasma and cerebrospinal fluid is associated with lipoprotein (LP) particles. In this paper we tested the sAβ secretion by cells in association with LP in the model of the human hepatoma HepG2 cell line. These cells secreted sAβ to the culture media and expressed intracellular sAβ immunoreactivity. Soluble Aβ in the cell supernatant was detected in 200–300kDa LP complexes in association with apoA‐I, apoJ, transthyrethin and phospholipids, triglycerides and free and esterified cholesterol. This was assessed by size exclusion HPLC, immunoprecipitation with corresponding antibodies and by analysis of sAβ associated metabolically‐labeled lipids, respectively. Our results suggest that sAβ to LP association represents a unique mechanism, governing the normal biology of sAβ.