The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo.
The Journal of experimental medicine, 1988•rupress.org
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 …
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 …
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.
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