Inhibition of Cysteine Protease Activity by NO-donors

Title: Inhibition of Cysteine Protease Activity by NO-donors

Volume: 2 Issue: 2

Author(s): Paolo Ascenzi, Luca Salvati, Martino Bolognesi, Marco Colasanti, Fabio Polticelli and Giorgio Venturini

Affiliation:

Keywords: Cysteine Protease Activity, membrane-bound protein, Rhinovirus 3C Protease, Cruzain, reservosomes, fluorescent S-nitroso, cathepsin-B catalytic, NO-donors, macromolecular nitrosylating agent

Abstract: Cysteine proteases represent a broad class of proteolytic enzymes widely distributed among living organisms. Although well known as typical lysosomal enzymes, cysteine proteases are actually recognized as multi-function enzymes, being involved in antigen processing and presentation, in membrane-bound protein cleavage, as well as in degradation of the cellular matrix and in processes of tissue remodeling. Very recently, it has been shown that the NO(-donor)-mediated chemical modification of the Cys catalytic residue of cysteine proteases, including Coxsackievirus and Rhinovirus cysteine proteases, cruzain, Leishmania infantum cysteine protease, falcipain, papain, as well as mammalian caspases, cathepsins and calpain, blocks the enzyme activity in vitro and in vivo. Here, inhibition of representative cysteine proteases by NO(-donors) is reviewed.

Cite this article as:

Ascenzi Paolo, Salvati Luca, Bolognesi Martino, Colasanti Marco, Polticelli Fabio and Venturini Giorgio, Inhibition of Cysteine Protease Activity by NO-donors, Current Protein & Peptide Science 2001; 2 (2) . https://dx.doi.org/10.2174/1389203013381170