Cerulenin inhibited the secretion of extracellular proteins by washed cell suspensions of . α-Amylase and protease secretion were inhibited by 80% and 75%, respectively, over 3 h. Cerulenin at 100 μg ml inhibited incorporation of [1,2C]- acetate into intracellular lipid by about 75% without affecting cell growth, total protein synthesis or membrane protein synthesis. The inhibitory effect of cerulenin on α-amylase and protease secretion could be partially reversed if cell suspensions were supplemented with either fatty acids prepared from the lipids extracted from or various individual pure fatty acids. Cerulenin significantly altered the ratio of lipid to protein in isolated membranes. However, this alteration was not affected by adding fatty acids which restored enzyme secretion. These results suggest that cerulenin may affect the availability of lipid directly concerned with the secretion process. The differential effect of cerulenin on the production of extracellular proteins and membrane proteins also suggests that the synthesis of these two classes of proteins occurs via mechanisms that differ.


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