TY - JOUR
T1 - Inhibition of cysteine protease activity by NO-donors
AU - Ascenzi, Paolo
AU - Salvati, Luca
AU - Bolognesi, Martino
AU - Colasanti, Marco
AU - Polticelli, Fabio
AU - Venturini, Giorgio
PY - 2001
Y1 - 2001
N2 - 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.
AB - 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.
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U2 - 10.2174/1389203013381170
DO - 10.2174/1389203013381170
M3 - Article
C2 - 12370021
AN - SCOPUS:0034980711
VL - 2
SP - 137
EP - 153
JO - Current Protein and Peptide Science
JF - Current Protein and Peptide Science
SN - 1389-2037
IS - 2
ER -