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Evolution of 11β‐hydroxysteroid dehydrogenase‐type 1 and 11β‐hydroxysteroid dehydrogenase‐type 3
Author(s) -
Baker Michael E.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.03.036
Subject(s) - biology , evolutionary biology , 11β hydroxysteroid dehydrogenase type 1 , glucocorticoid , dehydrogenase , endocrinology , enzyme , biochemistry
A key regulator of glucocorticoid action is 11β‐hydroxysteroid dehydrogenase‐type 1 (11β‐HSD1), which catalyzes the conversion of cortisone to cortisol, the biologically active glucocorticoid. 11β‐HSD1 is a paralog of 11β‐HSD3, whose physiological function remains unclear. As reported here, 11β‐HSD3 has orthologs in sea urchin, amphioxus and Ciona, while 11β‐HSD1 first appears in sharks. Thus, 11β‐HSD3 arose before the evolution of glucocorticoid signaling, suggesting different ancestral function(s) for 11β‐HSD3. Four perplexing findings arise from this evolutionary analysis: (1) 11β‐HSD1 is not present in a ray‐finned fish genome, (2) zebrafish and fathead minnow contain two isoforms of 11β‐HSD3; (3) neither rat nor mouse contain 11β‐HSD3 and (4) amphioxus contains 16 11β‐HSD3 paralogs.