Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages

FEBS Letters

Katunuma, Nobuhiko¹  Hara, Kenji¹  Kominami, Eiki¹ 

[1] Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan

关键词: Cathepsin B;    Cathepsin H;    Cathepsin L;    Proteinase inhibitor;    Intracellular processing;    (Rat macrophage);    SDS-PAGEE;    SDS-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(88)80737-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effects of various proteinase inhibitors on the processing of lysosomal cathepsins B, H and L were investigated in cultured rat peritoneal macrophages. The processing of newly synthesized pro-cathepsins B, H and L to the mature single-chain enzymes was sensitive to a metal chelator,1,10-phenanthroline, and a synthetic metalloendopeptidase substrate, Z-Gly-Leu-NH₂, and insensitive to inhibitors of serine proteinases, aspartic proteinases and cysteine proteinases. Inhibitors of cysteine proteinases, E-64-d and leupeptin, inhibited the processing of the single-chain forms of cathepsins B, H and L to the two-chain forms. These results suggest that (a) metal endopeptidase(s) is (are) involved in the propeptide processing of cathepsin B, H and L, and that proteolytic cleavages of the mature single-chain cathepsins are accomplished by cysteine proteinases in lysosomes.

【 授权许可】

Unknown