The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo.
We infused microgram quantities of active or inactive PMN elastase and cathepsin G into the renal arteries of rats. Both active and inactive elastase localized to the glomerular capillary wall equally, and in amounts that could be achieved physiologically in GN. However, elastase-perfused rats developed marked proteinuria (196 +/- 32 mg/24 h) compared with control rats receiving inactive elastase (19 +/- 2 mg/24 h, p less than 0.005). Similar results were seen with active and inactive cathepsin G. Neither elastase nor cathepsin G infusion was associated with histologic evidence of glomerular injury. We conclude that the PMN neutral serine proteinases elastase and cathepsin G can mediate marked changes in glomerular permeability in vivo due to their proteolytic activity, and thus, may contribute to the proteinuria observed in PMN-dependent models of GN.
D000818:Animals; D056649:Cathepsin G; D002403:Cathepsins / Q000502:physiology*; D005455:Fluorescent Antibody Technique; D007674:Kidney Diseases / Q000201:enzymology* / Q000473:pathology; D007678:Kidney Glomerulus / Q000473:pathology; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000502:physiology*; D011507:Proteinuria / Q000209:etiology; D051381:Rats; D012697:Serine Endopeptidases
D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; C534097:Ctsg protein, rat; D010196:Pancreatic Elastase