Evidence for a mechanism for the initiation of acid hydrolase secretion by macrophages that is functionally independent of alternative pathway complement activation

Publisher Website
Google Scholar
Abstract
A mechanism for the initiation of selective acid hydrolase secretion from mouse macrophages by weak bases that is functionally independent of complement activation is proposed. The release of .beta.-galactosidase from macrophages exposed to methylamine and chloroquine was highly dependent on the pH of the incubation medium; the degree of lysosomal secretion correlated closely with the amount of free base in solution at each pH investigated. The secretion of .beta.-galactosidase induced by methylamine was additively enhanced by a fixed dose of zymosan; chloroquine additively enhanced the secretion of .beta.-galactosidase during exposure to zymosan. Chloroquine did not additively enhance the release of lysosomal enzyme effected by exposure to methylamine. Two new secretagogues, imidazole and benzamidine, like chloroquine, failed to initiate any activation of the alternative complement pathway. The possible relationship between secretagogue induced vacuolization and lysosomal secretion is discussed.