A serum protein inhibitor of acid lipase and its possible role in lipid accumulation in cultured fibroblasts.
Histochemical examination of L929 fibroblasts indicates massive accumulation of intracellular lipids in cells grown in medium supplemented with 10% calf serum. The present study suggests that the accumulation of triacylglycerols in these cells may be due to the inhibition of acid lipase activity by a serum component present in the culture medium. This is based on the following observations. (a) Acid lipase appears to be the major intracellular enzyme responsible for triacylglycerol catabolism in L929 cells. (b) The acid lipase is strongly inhibited by either human of calf serum. Several lines of evidence show that the inhibitor is a serum protein: it is heat-labile, non-dialysable and is destroyed by trypsin. It is present mainly in Cohn's fraction IV and has mol.wt. approx. 50000. (c) Lipid accumulation in intact cells is reduced when cells are grown on a limited supply of serum (2%) and is elevated by the addition of Cohn's fraction IV, freed of lipoproteins, to the growth medium.
D000818:Animals; D001798:Blood Proteins / Q000494:pharmacology*; D005347:Fibroblasts / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D006651:Histocytochemistry; D007739:L Cells / Q000201:enzymology* / Q000378:metabolism; D008049:Lipase / Q000037:antagonists & inhibitors*; D050356:Lipid Metabolism; D051379:Mice; D014280:Triglycerides / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology
D001798:Blood Proteins; D014280:Triglycerides; D008049:Lipase; D014357:Trypsin