Kinetics of hydrolysis of endocytosed substrates by mammalian cultured cells: Early introduction of lysosomal enzymes into the endocytic pathway

Document Type

Article

Abstract

The kinetics of exposure of endocytosed material to two lysosomal enzymes were determined for a number of cultured cell lines using fluorogenic substrates. Hydrolysis of endocytosed substrates for cathepsin B and acid phosphatase was observed to begin within 3–10 min of substrate addition and to proceed linearly for up to 60 min thereafter. Hydrolysis of the cathepsin B substrate was not affected by inhibition of protein synthesis with cycloheximide, indicating that the enzymes present in early endosomes are not exclusively newly synthesized. As had been observed previously for a cathepsin B substrate (Roederer, M., Bowser, R., and Murphy, R.F., J. Cell. Physiol., 131:200–209, 1987), hydrolysis of the acid phosphatase substrate was not blocked at temperatures below 20°C. The results suggest that the endosome is the primary site of initial exposure of endocytosed material to hydrolytic enzymes. Copyright © 1990 Wiley‐Liss, Inc.

Publication Date

1-1-1990

Publication Title

Journal of Cellular Physiology

ISSN

00219541

E-ISSN

10974652

Volume

143

Issue

1

First Page

110

Last Page

117

PubMed ID

1969418

Digital Object Identifier (DOI)

10.1002/jcp.1041430115

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