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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Mar;80(5):1261–1264. doi: 10.1073/pnas.80.5.1261

Endogenous inhibitors of lysosomal proteinases.

S Pontremoli, E Melloni, F Salamino, B Sparatore, M Michetti, B L Horecker
PMCID: PMC393575  PMID: 6572386

Abstract

Specific inhibitors of three lysosomal proteinases are present in the cytosolic and lysosomal compartments of rabbit liver. The cytosolic inhibitors, purified by chromatography on DEAE-Trisacryl and Sephadex G-75, show specificities toward cathepsin M, cathepsins B and L, and fructose 1,6-bisphosphatase converting enzyme (CE), respectively, and are designated IM, IB/L, and ICE. Inhibitors with similar specificities have been isolated from the intralysosomal compartment. Two of these inhibitors, IM and ICE, are also present in the lysosomal membranes. The lysosomal distribution parallels that of the respective proteinases. The inhibitors are polypeptides with molecular weights of 5,000-10,000 for the two forms of IB/L, 12,500 for IM, and 10,000-40,000 for the ICE species.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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