Neutrophil elastase processing of gelatinase A is mediated by extracellular matrix

The modification of Gelatinase A by neutrophil elastase depends on the presence of matrix components. In the absence of gelatin, Gelatinase A is proteolytically modified by neutrophil elastase by the hydrolysis of bonds in the fibro-nectin like gelatin binding domain. However in the presence of gelatin, cleavage takes place in the carboxyl-terminal domain and a truncated active form gelatinase is formed. Gelatinase A is a metalloproteinase which is overexpressed in tumor cells.