In vitro studies on origin and site of action of enzyme activity responsible for conversion of human proapoprotein A-I into apoprotein A-I

article



Kooistra, T.

Hinsbergh, V. van

Havekes, L.

Kempen, H.J.
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
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endothelium cellin vitro studyliverliver cell carcinomaproapolipoprotein a1Apolipoprotein A-IApolipoproteinsBloodCalciumCarcinoma, HepatocellularCell LineEndotheliumFemaleHumanIsoelectric FocusingLipoproteinsLiver NeoplasmsMagnesiumMolecular WeightPregnancyUmbilical Veins
TNO Identifier
229531
Repository link
https://resolver.tno.nl/uuid:ccc6bc5e-3921-4bff-aed7-2e3ee4bfad06
ISSN
00145793
Source
FEBS Letters, 170(1), pp. 109-113.
Pages
109-113
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