Polarized secretion of urokinase-type plasminogen activator by epithelial cells
Autor: | Anne Estreicher, Arnaud Gos, Pia Ragno, Annelise Isabelle Wohlwend, Dominique Belin, Jean-Dominique Vassalli |
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Rok vydání: | 1992 |
Předmět: |
Plasminogen Activator Inhibitor 1/metabolism
Isoflurophate Cell Biology Transfection Ammonium Chloride Epithelium Kringle domain Colchicine/pharmacology Cell Line Mice Plasminogen Activator Inhibitor 1 Tumor Cells Cultured medicine Extracellular Extracellular Matrix/physiology Animals Humans ddc:576.5 Secretion Urokinase-Type Plasminogen Activator/genetics/ metabolism/secretion Urokinase Isoflurophate/pharmacology Ammonium Chloride/pharmacology Cell Membrane Cell Membrane/ enzymology Epithelium/enzymology Cell Biology Urokinase-Type Plasminogen Activator Extracellular Matrix Cell biology medicine.anatomical_structure Biochemistry Cell culture Hela Cells Colchicine Plasminogen activator HeLa Cells medicine.drug |
Zdroj: | Experimental Cell Research, Vol. 203, No 1 (1992) pp. 236-243 |
ISSN: | 0014-4827 |
DOI: | 10.1016/0014-4827(92)90060-l |
Popis: | Numerous epithelial cell types produce and secrete plasminogen activators (PAs) and/or PA inhibitors (PAIs). When epithelial cells were grown on polycarbonate filters and their apical and basolateral secretion products analyzed, PA activity accumulated in a highly polarized fashion; depending upon the cell line, the compartment of PA accumulation was either apical (MDCK I cells and HBL-100 cells) or basolateral (LLC-PK1, CaCo-2, and HeLa cells). By contrast, PAI-1 was recovered in roughly equal amounts in both compartments. Basolateral accumulation of urokinase-type plasminogen activator (uPA), but not its apical targeting, required an acidic compartment and the integrity of the cytoskeleton. Polarity of uPA accumulation did not result from removal of the free enzyme from the opposite compartment through its binding to the cell surface. Transfection with wild-type or mutated murine uPA demonstrated that neither the "growth factor" domain nor the kringle domain is required for the appropriate sorting of the protein. We propose that polarized secretion of PAs is one mechanism whereby cells spatially control extracellular proteolysis. |
Databáze: | OpenAIRE |
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