title: Elastase-like activity in cultured aortic endothelial cells.
abstract: Cultured porcine aortic endothelial cells were studied for cellular and secreted elastase activity. We describe an activity hydrolyzing the synthetic elastase substrate, succinyl(alanine)3 nitroanilide, but not elastin, which was shown to be membrane located and was not secreted to the culture medium. A different neutral proteinase activity degrading insoluble elastin was demonstrated in the culture medium following its fractionation by gel filtration high performance liquid chromatography (HPLC). Since no elastinolytic activity could be directly detected in the conditioned medium, it is likely that the chromatographic separation removed an endogenous inhibitor.
authors.affiliation: INSERM U 150, CNRS UA 334, Hôpital St-Louis, Paris, France.
authors.forename: S
authors.initials: S
authors.lastname: Menashi
authors.forename: W
authors.initials: W
authors.lastname: Hornebeck
authors.forename: L
authors.initials: L
authors.lastname: Robert
authors.forename: Y
authors.initials: Y
authors.lastname: Legrand
mesh_terms: D000818:Animals; D001011:Aorta / Q000201:enzymology; D002478:Cells, Cultured; D004549:Elastin; D004730:Endothelium, Vascular / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000378:metabolism*; D013347:Subcellular Fractions; D013552:Swine
chemical_list: D004549:Elastin; D010196:Pancreatic Elastase