Gelatinase

Proteolytic enzymes cleave the proteins of the extracellular matrix, but preferably gelatine hydrolytically into its components, polypeptides peptides and amino acids.
Gelatinases belong to the family of matrix metalloproteases (MMPs), which play an important role in the conversion or degradation of the extracellular cell matrix. They are released by neutrophil granulocytes during acute inflammations and cause, among other things, an increase in permeability. For example, the oxygen deficiency in an ischemic stroke initiates a first-aid degradation cascade, whereby the gelatinase-induced degradation apparently has an initiating function. Tight junctions are also attacked and destroyed by the matrix metalloproteinases, which causes neurons to die in the nervous tissue. Gelatinases are also produced by various bacteria (e.g. Pseudomonas aeruginosa).

1. Hästbacka J et al (2015) Matrix metalloproteinases -8 and -9 and tissue inhibitor of metalloproteinase-1 in burn patients. A prospective observational study. PLoS One 10: e0125918.