Partial biochemical characterization of the activated esterase required in the complement-dependent chemotaxis of rabbit polymorphonuclear leukocytes.

It was shown in the preceding paper that incubation of the rabbit polymorphonuclearleukocyteswith phosphonate esters leads to an irreversible inhibition of the ability of the leukocyte to respond to the chemotactic factor. This "cell-dependent inhibition" was attributed to the inactivation by the phosphonates of an esterase existing in or on the leukocyte in an already activated state. As shown in this paper, incubating the leukocyte with phosphonate in the presence of certain esters prevents this cell-dependent inhibition. The protection is specific; the ester must be an acetate. Ethyl formate, ethyl propionate, ethyl butyrate, glucose 6-phosphate, fructose 1,6-diphosphate, ATP, tosyl arginine methyl ester, or acetyl tyrosine ethyl ester do not protect. The protection is independent of the phosphonate used to inhibit, and the degree of protection depends on the relative concentrations of acetate and phosphonate. Those acetates which protect are also the esters which inhibit chemotaxis when added to the leukocyte in the upper part of the chemotaxis chamber. It is concluded that the activated esterase is an enzyme capable of specifically splitting, or binding acetates, or doing both. Presumably the esterase is some type of acetylesterase or acetylase. The known aliesterase present in the leukocyte is not the activated esterase. Inhibition of the activated esterase by phosphonates has no effect on endogenous or exogenous glycolysis.