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PMID: 3360126 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages.

FEBS letters ·Vol. 231 ·No. 1 ·1988-04-11 ·Pages 225-8

Kominami E, Tsukahara T, Hara K, Katunuma N

Abstract

The intracellular processing and release of three lysosomal cysteine proteinases, cathepsin B, H and L, by rat peritoneal macrophages were investigated by pulse-chase experiments. Newly synthesized procathepsins B (39 kDa), H(41 kDa) and L (39 kDa) after 15 min labeling were processed to the mature, single-chain enzymes within 1 h. The single-chain forms of cathepsin B, H and L were further processed to two-chain forms at different rates: conversion of cathepsin L to the two-chain form was rapid, whereas the conversions cathepsin B and H took at least 6 h. Macrophages released 30% of the procathepsins B and L, and 10% of the procathepsin H.

MeSH Terms
Animals Carbon Radioisotopes Cells, Cultured Cysteine Endopeptidases/biosynthesis,genetics,isolation & purification Lysosomes/enzymology Macrophages/enzymology Methionine/metabolism Molecular Weight Protein Processing, Post-Translational Rats Rats, Inbred Strains Sulfur Radioisotopes
Chemicals
Carbon Radioisotopes Sulfur Radioisotopes Methionine Cysteine Endopeptidases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Kominami E
Division of Enzyme Chemistry, Institute for Enzyme Research, University of Tokushima, Japan.
Tsukahara T
Hara K
Katunuma N
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1988-04-11
Pages
225-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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