Branchial and Antennal Gland Na+/K+-Dependent ATPase and Carbonic Anhydrase Activity During Salinity Acclimation of the Euryhaline Crayfish Pacifastacus Leniusculus

Abstract

SUMMARY Haemolymph and urine electrolyte status and branchial and antennal gland activities of Na+/K+-ATPase and carbonic anhydrase (CA) were determined in the crayfish Pacifastacus leniusculus after 3 weeks acclimation in fresh water (FW) and 350 and 750 mosmol kg−1 sea water (SW). In FW the crayfish maintained haemolymph osmolality around 370 mosmol kg−1 due to hyperionic regulation of the major electrolytes. Involved in this are ion uptake mechanisms situated on the gills, and mechanisms of ion reabsorption from the primary urinary filtrate in the antennal gland (AG). Both of these processes are associated with high activities of Na+/K+-ATPase and CA. The two enzymes are uniformly distributed on gill sets 2– 7, unlike the situation in euryhaline marine species. Additionally, activity levels of both enzymes are extremely high in the AG and can be correlated with the ability to produce a hypo-osmotic urine. In comparison, enzyme activity is negligible in marine species which produce isosmotic urine. Crayfish continued to hyperosmoregulate in 350 mosmol kg−1 SW. High levels of Na+/K+-ATPase confirmed the presence of a component active in the uptake of major electrolytes in the gills and also in the AG, where ion reabsorption persisted. In 750 mosmol kg−1 SW crayfish became isosmotic. Since ATPase is regulated chiefly by deactivation/activation of pre-existing enzyme, overall activity was mostly unchanged. CA activity was significantly reduced in both 350 and 750 mosmol kg−1 SW and correlated with the transition from osmoregulation to osmoconformity, suggesting that it is regulated primarily by deinduction/induction of new enzyme. The difference in the mechanism of regulation exhibited by these two enzymes is believed to relate to their subcellular distribution.