Kominami E, Tsukahara T, Hara K, Katunuma N
Division of Enzyme Chemistry, Institute for Enzyme Research, University of Tokushima, Japan.
FEBS Lett. 1988 Apr 11;231(1):225-8. doi: 10.1016/0014-5793(88)80736-1.
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.