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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: Kooistra, T. · Hinsbergh, V. van · Havekes, L. · Kempen, H.J.
Type:article
Date:1984
Institution: Gaubius Instituut TNO
Source:FEBS Letters, 1, 170, 109-113
Identifier: 229531
doi: doi:10.1016/0014-5793(84)81379-4
Keywords: endothelium cell · in vitro study · liver · liver cell carcinoma · proapolipoprotein a1 · Apolipoprotein A-I · Apolipoproteins · Blood · Calcium · Carcinoma, Hepatocellular · Cell Line · Endothelium · Female · Human · Isoelectric Focusing · Lipoproteins · Liver Neoplasms · Magnesium · Molecular Weight · Pregnancy · Umbilical Veins

Abstract

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 Ca2+/Mg2+-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. Chemicals/CAS: Metaraminol, 54-49-9; Nitroprusside, 15078-28-1