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FEBS Lett. 2010 Jun 3;584(11):2279-84. doi: 10.1016/j.febslet.2010.03.036. Epub 2010 Mar 27.

Evolution of 11beta-hydroxysteroid dehydrogenase-type 1 and 11beta-hydroxysteroid dehydrogenase-type 3.

Author information

1
Department of Medicine, University of California, San Diego, La Jolla, CA 92093-0693, USA. mbaker@ucsd.edu

Abstract

A key regulator of glucocorticoid action is 11beta-hydroxysteroid dehydrogenase-type 1 (11beta-HSD1), which catalyzes the conversion of cortisone to cortisol, the biologically active glucocorticoid. 11beta-HSD1 is a paralog of 11beta-HSD3, whose physiological function remains unclear. As reported here, 11beta-HSD3 has orthologs in sea urchin, amphioxus and Ciona, while 11beta-HSD1 first appears in sharks. Thus, 11beta-HSD3 arose before the evolution of glucocorticoid signaling, suggesting different ancestral function(s) for 11beta-HSD3. Four perplexing findings arise from this evolutionary analysis: (1) 11beta-HSD1 is not present in a ray-finned fish genome, (2) zebrafish and fathead minnow contain two isoforms of 11beta-HSD3; (3) neither rat nor mouse contain 11beta-HSD3 and (4) amphioxus contains 16 11beta-HSD3 paralogs.

PMID:
20350543
DOI:
10.1016/j.febslet.2010.03.036
[Indexed for MEDLINE]
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