Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages
Open Access
- 11 April 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 231 (1) , 225-228
- https://doi.org/10.1016/0014-5793(88)80736-1
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.Keywords
This publication has 20 references indexed in Scilit:
- Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophagesFEBS Letters, 1988
- Molecular cloning and sequencing of cDNA for rat cathepsin H Homology in pro‐peptide regions of cysteine proteinasesFEBS Letters, 1987
- Intracellular transport and processing of lysosomal cathepsin HBiochemical and Biophysical Research Communications, 1987
- Molecular cloning and sequencing of cDNA for rat cathepsin LFEBS Letters, 1987
- Intracellular transport and processing of lysosomal cathepsin BBiochemical and Biophysical Research Communications, 1987
- The major excreted protein (MEP) of transformed mouse cells and cathepsin L have similar protease specificityBiochemical and Biophysical Research Communications, 1986
- Golgi/granule processing of peptide hormone and neuropeptide precursors: A minireviewJournal of Cellular Biochemistry, 1984
- Homology of amino acid sequences of rat liver cathepsins B and H with that of papain.Proceedings of the National Academy of Sciences, 1983
- Purification and characterization of a transformation-dependent protein secreted by cultured murine fibroblastsBiochemistry, 1981
- [41] Cathepsin B, cathepsin H, and cathepsin LPublished by Elsevier ,1981