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Journal of Experimental Biology, Vol 199, Issue 5 1195-1208, Copyright © 1996 by Company of Biologists

JOURNAL ARTICLES

Ca2+ transport processes of lobster hepatopancreatic brush-border membrane vesicles

Z Zhuang and G Ahearn

45Ca2+ uptake by hepatopancreatic brush-border membrane vesicles of Atlantic lobster (Homarus americanus) occurred by a combination of three independent processes: (1) an amiloride-sensitive carrier-mediated transport system; (2) an amiloride-insensitive carrier-mediated transport system; and (3) a verapamil-inhibited channel process responsive to transmembrane potential. Both carrier-mediated processes were antiporters and capable of exchanging external Ca2+ with intravesicular Na+ or H+. The kinetic parameters of both carrier-mediated processes have been reported previously. External amiloride and Zn2+ were both competitive inhibitors of 45Ca2+ influx, reducing entry of the divalent cation at a single binding site with Ki values of 370 µmol l-1 for amiloride and 940 µmol l-1 for Zn2+. It is concluded that the mechanisms controlling Ca2+ entry into hepatopancreatic epithelial cells include a previously reported electrogenic 2Na+/1H+ antiporter, an electroneutral 2Na+/1Ca2+ antiporter and a verapamil-sensitive Ca2+ channel, which might also be used for the entry of Zn2+ and possibly other heavy metals. Evidence from an equilibrium-shift experiment, based on the thermodynamics of a coupled transport process, suggested that both monovalent (Na+) and divalent (Ca2+ and Zn2+) cations may enter hepatopancreatic epithelial cells through a common carrier-mediated transport protein. This suite of hepatopancreatic brush-border Ca2+ transport processes qualitatively resembles that previously reported for the luminal membrane of lobster antennal glands and suggests that crustacean epithelial cells from different organs may handle this divalent cation by similar means.
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