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Inhibition of Early but Not Late Proteolytic Processing Events Leads to the Missorting and Oversecretion of Precursor Forms of

By Lysosomal Enzymes In Dictyostelium Discoideum, Jan M. Richardson, Nancy A. Woychik, David L. Ebert, All L. Dimond and James A. Cardelli

Abstract

Abstract. Lysosomal enzymes are initially synthesized as precursor polypeptides which are proteolyticaUy cleaved to generate mature forms of the enzymatically active protein. The identification of the proteinases involved in this process and their intracellular location will be important initial steps in determining the role of proteolysis in the function and targeting of lysosomal enzymes. Toward this end, axenically growing Dictyostelium discoideum cells were pulse radiolabeled with [35S]methionine and chased in fresh growth medium containing inhibitors of aspartic, metallo, serine, or cysteine proteinases. Cells exposed to the serine/cysteine proteinase inhibitors leupeptin and antipain and the cysteine proteinase inhibitor benzyloxycarbonyl-L-phenylalanyl-L-alanine-diazomethyl ketone (Z

Year: 2013
OAI identifier: oai:CiteSeerX.psu:10.1.1.277.5796
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