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Presence of 11 β‐hydroxysteroid dehydrogenase enzyme in the human prostate tumor cell line LNCaP
Author(s) -
Nath Nagendra,
Lakshmi Vijaya,
Rosenthal Julian C.
Publication year - 1993
Publication title -
the prostate
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.295
H-Index - 123
eISSN - 1097-0045
pISSN - 0270-4137
DOI - 10.1002/pros.2990230305
Subject(s) - carbenoxolone , lncap , endocrinology , dehydrogenase , cell culture , medicine , enzyme , cortisone , enzyme assay , glucocorticoid , biology , corticosterone , hydroxysteroid dehydrogenase , lactate dehydrogenase , prostate , chemistry , biochemistry , hormone , cancer , intracellular , genetics , gap junction
11 β‐Hydroxysteroid dehydrogenase (11β‐HSD) is the enzyme that catalyzes the reversible oxidation of the biologically active steroid cortisol and corticosterone to their inactive metabolites cortisone and dehydrocorticosterone. We report its presence in significant levels in the human prostate carcinoma cell line LNCaP cultured in medium RPMI‐1640 with 10% fetal calf serum (FCS). The 11‐dehydrogenase activity of 11β‐HSD is present, while the 11‐reductase activity is undetectable in these tumor cells under the present culture conditions. The enzyme activity is found to be linear with time of incubation, and is proportional to plated cell density. The enzymatic activity can be determined in cultures maintained for longer times. Carbenoxolone, the potential inhibitor of the 11β‐HSD, inhibits 95% of the dehydrogenase activity of the tumor cells when used in nM concentration. The presence of this enzyme in tumor cell line indicates that 11β‐HSD plays an important role in maintaining the active glucocorticoid levels in the prostate. © 1993 Wiley‐Liss, Inc.