Hydrogen sulfide stimulates catecholamine secretion in rainbow trout (Oncorhynchus mykiss)

We tested the hypothesis that endogenously produced hydrogen sulfide ([H.sub.2]S) can potentially contribute to the adrenergic stress response in rainbow trout by initiating catecfiolamine secretion from chromaffin cells. During acute hypoxia (water [Po.sub.2] = 35 mmHg), plasma [H.sub.2]S levels were significantly elevated concurrently with a rise in circulating catecholamine concentrations. Tissues enriched with chromaffin cells (posterior cardinal vein and anterior kidney) produced [H.sub.2]S in vitro when incubated with L-cysteine. In both tissues, the production of [H.sub.2]S was eliminated by adding the cystathionine [beta]-synthase inhibitor, aminooxyacetate. Cystathionine [beta]-synthase and cystathionine [gamma]-lyase were cloned and sequenced and the results of real-time PCR demonstrated that with the exception of white muscle, mRNA for both enzymes was broadly distributed within the tissues that were examined. Electrical field stimulation of an in situ saline-perfused posterior cardinal vein preparation caused the appearance of [H.sub.2]S and catecholamines in the outflowing perfusate. Perfusion with the cholinergic receptor agonist carbachol (1 x [10.sup.-6] M) or depolarizing levels of KC1 (1 x [l0.sup.-2] M) caused secretion of catecholamines without altering [H.sub.2]S output, suggesting that neuronal excitation is required for [H.sub.2]S release. Addition of [H.sub.2]S (at concentrations exceeding 5 x [10.sup.-7] M) to the perfusion fluid resulted in a marked stimulation of catecholamine secretion that was not observed when [Ca.sup.2+] -free perfusate was used. These data, together with the finding that [H.sub.2]S-induced catecholamine secretion was unaltered by the nicotinic receptor blocker hexamethonium, suggest that [H.sub.2]S is able to directly elicit catecholamine secretion via membrane depolarization followed by [Ca.sup.2+] -mediated exocytosis. adrenaline; noradrenaline; hypoxia; chromaffin cell; stress; cystathionine [gamma]-lyase; cystathionine [beta]-synthase