Molecular domains in epithelial salt cellNaCl of crustacean salt gland (Artemia)

Abstract

The salt secretory cell has two distinct patterns of plasma membrane development. First, the basolateral surface forms a tubular labyrinth. It contains the subunit alpha-2 of the Na(+)-K(+)-ATPase bound together with a beta subunit for structural attachment within the lipid bilayer. Second, the apical plasma membranes form a multiple array of extending tufts. These tufts contain the subunit alpha-1 of the Na(+)-K(+)-ATPase bound together with a beta subunit for structural integrity within the lipid bilayer. The presence of an active transporter for chloride remains as an open question. It has been taken as preliminary evidence from brine shrimp cystic fibrosis toxicity that a cystic fibrosis transmembrane conductance regulator chloride channel could be present in the apical region. The presence of cytoskeletal elements being involved in the construction of a hypo-osmoregulatory apparatus is supported by the homeobox gene products derived from APH-1 m RNA found in the salt gland.