Inhibition of cysteine protease activity by NO-donors

Paolo Ascenzi, Luca Salvati, Martino Bolognesi, Marco Colasanti, Fabio Polticelli, Giorgio Venturini

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)137-153
Number of pages17
JournalCurrent Protein and Peptide Science
Volume2
Issue number2
DOIs
Publication statusPublished - 2001

ASJC Scopus subject areas

  • Biochemistry

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