Abstract.
Aminopeptidase N was demonstrated in human dermal fibroblasts as an ectoenzyme. The enzyme has wide substrate specificity, with a K m of 0.63 mM and V max of 338 nmol min−1 mg−1. Addition of fetal calf serum to the culture medium increased aminopeptidase N activity up to 63% by 10% serum in a 48-h culture. Treatment of fibroblasts by dexamethasone increased ectoaminopeptidase N activity in a dose- and time-dependent manner. Maximal increase of aminopeptidase N occurred after treatment with 1 μM dexamethasone for 3 days. Actinomycin D, a blocker of RNA synthesis, and cycloheximide, an inhibitor of protein synthesis, did not alter basal aminopeptidase N activity. However, they prevented stimulation by dexamethasone. RU 38486, a glucocorticoid receptor antagonist, suppressed the dexamethasone-induced increase in aminopeptidase N activity. This study shows that human dermal fibroblasts contain ectoaminopeptidase N controlled by glucocorticoids through a receptor-mediated mechanism.
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Received 3 April 1998; accepted 21 April 1998
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Stefanović, V., Vlahović, P. & Mitić-Zlatković, M. Receptor-mediated induction of human dermal fibroblast ectoaminopeptidase N by glucocorticoids. CMLS, Cell. Mol. Life Sci. 54, 614–617 (1998). https://doi.org/10.1007/s000180050189
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DOI: https://doi.org/10.1007/s000180050189