Abstract:
:In vitro experiments were conducted to test the hypothesis that 17alpha,20beta-dihydroxy-4-prengnen-3-one (17,20-P) regulates cortisol metabolism in Pacific salmon. In both rainbow trout and coho salmon, cortisol metabolism was significantly higher in the kidney compared to the liver. The rainbow trout kidney converted cortisol primarily into an unidentified water-soluble metabolite with a molecular mass of 354. The coho salmon kidney converted cortisol primarily into cortisol-21-sulfate. High physiological concentrations of 17,20-P had no effect on cortisol metabolism by the rainbow trout kidney, but almost completely inhibited the production of cortisol-21-sulfate by the coho salmon kidney. This was accompanied by a coincident increase in the production several neutral cortisol metabolites, including cortisone. Cortisone was also found to inhibit renal sulfotransferase (SULT) activity suggesting that there could be a local positive feedback mechanism initiated by the rise in 17,20-P that quickly reduces SULT activity as follows: the pre-spawning rise in 17,20-P inhibits SULT, cortisol is metabolized to cortisone instead of cortisol-21-sulfate, cortisone further inhibits SULT, more cortisone is produced, and so on. If SULT normally acts as a gatekeeper enzyme to protect the cell from cortisol excess, this mechanism would rapidly remove enzymatic protection and expose tissues to high local concentrations of cortisol. In addition, the inhibition of peripheral cortisol metabolism by 17,20-P could increase circulating concentrations of the corticosteroid. These events could be a part of the mechanism that leads to the symptoms of cortisol excess associated with the post-spawning mortality of semelparous Pacific salmon.
journal_name
Gen Comp Endocrinoljournal_title
General and comparative endocrinologyauthors
Barry TP,Marwah A,Nunez Sdoi
10.1016/j.ygcen.2009.06.003subject
Has Abstractpub_date
2010-01-01 00:00:00pages
53-9issue
1eissn
0016-6480issn
1095-6840pii
S0016-6480(09)00230-5journal_volume
165pub_type
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