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-Hydroxysteroid Dehydrogenase Type 1 Is Induced in Human Monocytes upon Differentiation to Macrophages1
Department of Atherosclerosis and Endocrinology, Merck Research Laboratories, Rahway, NJ 07065
11
-hydroxysteroid dehydrogenases (11-HSD) perform prereceptor
metabolism of glucocorticoids through interconversion of the active
glucocorticoid, cortisol, with inactive cortisone. Although the
immunosuppressive and anti-inflammatory activities of
glucocorticoids are well documented, the expression of 11-HSD
enzymes in immune cells is not well understood. Here we demonstrate
that 11-HSD1, which converts cortisone to cortisol, is expressed
only upon differentiation of human monocytes to macrophages. 11-HSD1
expression is concomitant with the emergence of peroxisome proliferator
activating receptor 
, which was used as a surrogate marker of
monocyte differentiation. The type 2 enzyme, 11-HSD2, which converts
cortisol to cortisone, was not detectable in either monocytes or
cultured macrophages. Incubation of monocytes with IL-4 or IL-13
induced 11-HSD1 activity by up to 10-fold. IFN-, a known
functional antagonist of IL-4 and IL-13, suppressed the induction of
11-HSD1 by these cytokines. THP-1 cells, a human macrophage-like
cell line, expressed 11-HSD1 and low levels of 11-HSD2. The
expression of 11-HSD1 in these cells is up-regulated 4-fold by LPS.
In summary, we have shown strong expression of 11-HSD1 in cultured
human macrophages and THP-1 cells. The presence of the enzyme in these
cells suggests that it may play a role in regulating the immune
function of these cells.
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