Intracellular localization of lipoprotein lipase in adipose cells.
Subcellular localization of lipoprotein lipase has been examined in differentiated Ob17 adipose cells. No patent activity is detectable in carefully homogenized cells. All latent activity can be unmasked by disrupting membrane structures with neutral detergents. The sequestration of lipoprotein lipase in closed membrane structures is supported by experiments of immunotitration with anti-lipoprotein lipase antibodies and by experiments showing a full protection of the masked activity against proteolytic attack by trypsin. The intracellular distribution of lipoprotein lipase investigated by immunofluorescence staining and by isopycnic centrifugation indicates that a large proportion of the enzyme is located in the Golgi apparatus, in which the activation of the enzyme is likely to take place (C. Vannier et al. (1985) J. Biol. Chem. 260, 4424-4431). Altogether, the results are in favor of a localization of lipoprotein lipase in adipose cells as being typical of that of a secretory protein and underline the absence of lipoprotein lipase in the cell cytoplasm.
D000273:Adipose Tissue / Q000166:cytology / Q000201:enzymology*; D000818:Animals; D002454:Cell Differentiation; D002460:Cell Line; D002500:Centrifugation, Isopycnic; D005455:Fluorescent Antibody Technique; D006056:Golgi Apparatus / Q000201:enzymology; D008823:Micelles; D008854:Microscopy, Electron; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology; D014018:Tissue Distribution
D008823:Micelles; D011092:Polyethylene Glycols; D017830:Octoxynol; C010615:Nonidet P-40