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Tight-binding inhibition of cathepsin S by cystatins.

Dieter Brömme, R Rinne, Heidrun Kirschke

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Abstract

Human cystatins A, B and C were purified, and their inhibition efficiency was tested with the cysteine proteinase cathepsin S. Cathepsin S was strongly inhibited by cystatins A and B in the subnanomolar range and by cystatin C in the picomolar range. Two steps of inhibition of cathepsin S by the cystatins which involve slow binding are discussed.

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What this paper is about

Human cystatins A, B and C were purified, and their inhibition efficiency was tested with the cysteine proteinase cathepsin S. Cathepsin S was strongly inhibited by cystatins A and B in the subnanomolar range and by cystatin C in the picomolar range. Two steps of inhibition of cathepsin S by the cystatins which involve slow binding are discussed.

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OpenAlex reports 42 citations for this work. Citation counts describe recorded attention and do not establish research quality.

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Available abstract

Human cystatins A, B and C were purified, and their inhibition efficiency was tested with the cysteine proteinase cathepsin S. Cathepsin S was strongly inhibited by cystatins A and B in the subnanomolar range and by cystatin C in the picomolar range. Two steps of inhibition of cathepsin S by the cystatins which involve slow binding are discussed.

Key concepts: Cystatin, Cathepsin B, Chemistry, Cathepsin O, Cathepsin L1, Cathepsin C, Cathepsin H, Cathepsin A

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