Effect of Neutrophil Cathepsin G on Elastin Degradation by Neutrophil Elastase

Abstract

Human neutrophil cathepsin G was unable to significantly stimulate the degradation of either bovine or human elastin by neutrophil elastase, using 4 different procedures to monitor digestion. A range of stimulations from 1.1 to 2.9-fold was found, with a 2.0-fold stimulation being the average with the assays tested. Little stimulation of elastolysis was found with either human or bovine lung elastin as substrate. Apparently, cathepsin G does not play a predominant role as an elastolytic enzyme; rather, its role may be one of binding to non-productive sites on the elastin surface.