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In vitro studies on origin and site of action of enzyme activity responsible for conversion of human proapoprotein A‐I into apoprotein A‐I
Author(s) -
Kooistra Teake,
Victor van Hinsbergh,
Louis Havekes,
Herman Jan Kempen
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81379-4
Subject(s) - hep g2 , enzyme , in vitro , secretion , chemistry , hepatocellular carcinoma , biochemistry , umbilical cord , human plasma , microbiology and biotechnology , apolipoprotein b , biology , cancer research , cholesterol , immunology , chromatography
Human hepatocellular carcinoma cells (Hep G2) were shown to secrete apo A‐I as a proprotein. No apo A‐I synthesis could be detected with endothelial cells from human umbilical cord veins. Conversion of proapo A‐I into apo A‐I is a slow (of the order of hours) process, mediated by a Ca 2+ /Mg 2+ ‐dependent enzyme which is present on the surface of plasma lipoprotein particles, endothelial cells and Hep G2 cells, and is probably synthesized by Hep G2 cells.