Enterocyte microvillus can phosphorylate molecules which inhibit endogenous phosphorylation of its proteins

D- and L-amino acids (arginine, lysine) and hydroxylated molecules (sorbitol, ethyl-ethanolamine), all of which increase the intestinal transfer of calcium, are phosphorylated by jejunal and ileal microvilli. All these molecules inhibit the endogenous phosphorylation of microvilli proteins. D- and L-valine, which are not phosphorylated in the same conditions, have no effect on the phosphorylation of microvilli proteins. These observations are in good agreement with the scheme previously proposed for the increase of calcium intestinal transfer by L-lysine: phosphorylation of L-lysine by mucous membrane may interfere with that of membrane proteins, the phosphorylation of which would lower the permeability to that cation. Autoradiographies of the electrophoretogram show that the principal phosphorylable microvilli proteins have the same electrophoretic properties as those of the dimer and the monomer of alkaline phosphatase from the same intestinal loci. The ability of the enzyme to be phosphorylated and its well-known transphosphorylating activity upon hydroxylated molecules suggest that it could, in different ways, affect intestinal transfer of calcium.