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11 β ‐Hydroxysteroid‐dehydrogenase isoforms: tissue distribution and implications for clinical medicine
Author(s) -
Diederich S.,
Quinkler M.,
Burkhardt P.,
Großmann C.,
Bähr V.,
Oelkers W.
Publication year - 2000
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1046/j.1365-2362.2000.0300s3021.x
Subject(s) - hydroxysteroid dehydrogenases , isozyme , mineralocorticoid , glucocorticoid , gene isoform , biology , enzyme , dehydrogenase , biochemistry , medicine , endocrinology , gene
11β‐hydroxylation is essential for glucocorticoid and mineralocorticoid activity of a steroid. The enzyme catalyzing this reaction is termed 11β‐hydroxysteroid‐dehydrogenase (11β‐HSD). Two isoenzymes of 11β‐HSD have been characterized in human tissues. Whereas 11β‐HSD‐I works mainly as a reductase, 11β‐HSD‐II only functions as an oxidizing (inactivating) enzyme for physiological glucocorticoids. Thus, the tissue distribution of both enzymes plays a crucial role for the specific glucocorticoid status of an organ. This review summarizes our knowledge of tissue distribution of both 11β‐HSD isoenzymes, their physiological function and pathophysiological role in certain clinical abnormalities, and their relevance to the metabolism of synthetic glucocorticoid and mineralocorticoid compounds.