NOVEL APOPROTEIN A-I-CONTAINING LIPOPROTEIN PRODUCED BY A HUMAN HEPATOMA-DERIVED CELL-LINE HUH-7

The apoprotein A-I (apo A-I)-containing lipoprotein (LPHuH.7apoA-I) was isolated from the concentrated conditioned medium of human hepatoma-derived cell line HuH-7 by immunoaffinity chromatography. LpHuH-7apoA-I consists of two kinds of lipoproteins. One is a lipoprotein of large particle size (LpL) with broad electrophoretic mobility on agarose gel ranging from the origin to the position of prebeta-lipoprotein. LpL is protein-rich in composition (protein, 75.4% by weight) and is heterogeneous in size (34-17 nm in diameter) electron microscopically. However, the most intriguing properties of LpL are its partial electrophoretic mobility towards the cathode on agar gel. The other lipoprotein is of small particle size (Lps). It demonstrates prebeta-electrophoretic mobility on agarose gel. Lps is also protein-rich in composition (protein, 95.4% by weight) and is heterogeneous in size (16.5-8.4 nm in diameter) electron microscopically. LpL is obviously different from LP-X and LP-Y in property, although LP-X, LP-Y and a part of LpL migrate towards the cathode on agar gel elecrrophoresis. Lps is also different from human apo A-I-containing lipoprotein without apo A-II in property, although these two lipoproteins possess the same mobility on agarose gel elecrrophoresis. These results indicate that both LpL and Lps are novel lipoproteins which have not yet been reported. The major isoproteins of the apo A-I of LpHuH-7apoA-I are aPo A-I isoprotein 2 (apo A-I2), apo A-I isoprotein 4 (apo A-I4) and apo A-I isoprotein 5 (apo A-I 5), and are different from those of apo A-I in human plasma and in the conditioned medium of hepatoma-derived cell line HepG2. This result suggests the presence of a proteinase which converts proapoprotein A-I (apo A-I2) to apoprotein A-I (apo A-I4) in the conditioned medium of HuH-7. © 1990.