Esterification and hydrolysis of vitamin A in the liver of brook trout (Salvelinus fontinalis) and the influence of a coplanar polychlorinated biphenyl.

Recent reports of extremely low retinoid stores in fish living in contaminated river systems prompted an initial investigation of the mechanisms of hepatic storage and mobilization in brook trout. Enzyme characterization in microsomes revealed a lecithin:retinol acyltransferase activity (LRAT) optimum in the alkaline range (pH 9.0; Vmax = 0.6 nmol per mg prot. h(-1); Km = 10.2 microM) which is not known to occur in mammals, in addition to a secondary optimum at pH 6.5 typical of mammals. Acyl CoA:retinol acyltransferase (ARAT) kinetic parameters were quite different to those of mammals. The substrate affinity of trout ARAT (Km = 1.6 microM) was approximately 22-fold greater than that of the rat while maximal velocity (Vmax = 0.2 nmol per mg prot. h(-1)) was 18-fold less. Retinyl ester hydrolase activity (REH) was optimal under acid conditions (pH 4.2; Vmax = 6.6 nmol per mg prot. h(-1); Km = 0.6 mM), was inhibited by a bile salt analogue and was greater in males than females. This REH was tentatively categorized as a bile salt-independent, acid retinyl ester hydrolase (BSI-AREH). REH was inhibited in a dose-dependent manner following in vivo exposure to a representative environmental contaminant the coplanar polychlorinated biphenyl (PCB), 3,3',4,4'-tetrachlorobiphenyl (TCBP). Inhibition may be an indirect effect because enzyme activity was not affected by in vitro exposure of control microsomes. REH inhibition in the brook trout may affect the uptake of retinyl esters (REs) from chylomicron remnants as well as the mobilization of stored REs.