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.
Ascenzi, P., Salvati, L., Bolognesi, M., Colasanti, M., Polticelli, F., & Venturini, G. (2001). Inhibition of cysteine protease activity by NO-donors. CURRENT PROTEIN & PEPTIDE SCIENCE, 2, 137-153 [10.2174/1389203013381170].
|Titolo:||Inhibition of cysteine protease activity by NO-donors|
|Data di pubblicazione:||2001|
|Citazione:||Ascenzi, P., Salvati, L., Bolognesi, M., Colasanti, M., Polticelli, F., & Venturini, G. (2001). Inhibition of cysteine protease activity by NO-donors. CURRENT PROTEIN & PEPTIDE SCIENCE, 2, 137-153 [10.2174/1389203013381170].|
|Appare nelle tipologie:||1.1 Articolo in rivista|