Retinyl ester storage is altered in liver stellate cells and in HL60 cells transfected with cellular retinol-binding protein type I.

It is suggested that cellular retinol-binding proteins are important for intracellular metabolism of retinol. Retinol bound to cellular retinol-binding proteins may be esterified with long chain fatty acids by the enzyme lecithin: retinol acyltransferase or may be oxidized to retinoic acid metabolites used in the mechanism of action of vitamin A. The aim of this present report was to determine whether altered levels of cellular retinol-binding protein type I influenced retinol storage and activation. Two different cell types have been examined after transfection with vectors producing sense or antisense mRNA for cellular retinol-binding protein type I. When HL60 cells were transfected with the expression vector for sense cellular retinol-binding protein type I high amounts of cellular retinol-binding protein type I mRNA and protein were produced. We observed that HL60 cells esterified less retinol than control cells without cellular retinol-binding protein type I. Cellular retinol-binding protein type I had, however, no effects on the proliferation or differentiation of HL60 cells by retinoids. Liver stellate cells transfected with the vector for sense cellular retinol-binding protein type I esterified more retinol than cells transfected with the expression vector for antisense cellular retinol-binding protein type I, while retinol esterification in control cells was intermediate. In conclusion, our data show that cellular retinol-binding protein type I influences retinol esterification both in liver stellate cells and in HL60 cells.