Regulation of lipoprotein lipase secretion by mouse peritoneal macrophages.
Resident mouse peritoneal macrophages in culture spontaneously secrete lipoprotein lipase. Secretion of lipoprotein lipase was 10-fold greater in thioglycollate-elicited and 6-fold greater in mineral oil-elicited macrophages. The increase in enzyme secretion was dependent on protein synthesis and glycosylation of the newly synthesized enzyme. The addition of 1 to 500 ng per ml of lipopolysaccharide to the culture medium resulted in a dose-dependent inhibition of lipoprotein lipase secretion. Thus, secretion of macrophage lipoprotein lipase is a regulated process, and may be increased as part of the response to inflammation. This may have important implications in the atherogenic process in the arterial wall.
D000818:Animals; D002478:Cells, Cultured; D004731:Endotoxins / Q000494:pharmacology; D007249:Inflammation / Q000201:enzymology; D008070:Lipopolysaccharides / Q000494:pharmacology; D008071:Lipoprotein Lipase / Q000378:metabolism*; D008264:Macrophages / Q000201:enzymology*; D051379:Mice; D010529:Peritoneal Cavity / Q000166:cytology; D012636:Secretory Rate / Q000187:drug effects; D002787:Sterol Esterase / Q000378:metabolism; D013864:Thioglycolates / Q000494:pharmacology
D004731:Endotoxins; D008070:Lipopolysaccharides; D013864:Thioglycolates; D002787:Sterol Esterase; D008071:Lipoprotein Lipase