Glomerular lysozyme binding in protein-overload proteinuria.
Binding of the cationic molecule lysozyme to the glomerular basement membrane and to the glomerular epithelial cell coat was investigated in the glomerulus of normal female Wistar rats and in rats in which heavy proteinuria was induced by the daily administration of 1 g of bovine serum albumin. In normal rats the binding of lysozyme to the anionic groups in the glomerular basement membrane and the cell coat had no effect on the ultrastructure of the glomerular epithelial cell, in particular the foot processes were unchanged. In the proteinuric rats the lysozyme-binding to the glomerular basement membrane and the epithelial cell coat was completely lost in the damaged glomeruli. In the apparently normal glomeruli present in these proteinuric animals binding was similar to that seen in normal rats. These results suggest that in protein-overload proteinuria there is a loss of glomerular anion and hence a reduction in the glomerular charge barrier. This may account, at least in part, for the increased glomerular leak of negatively charged serum albumin in this experimental model of proteinuria.
Bliss
D J
DJ
Brewer
D B
DB
D000818:Animals; D001485:Basement Membrane / Q000201:enzymology; D005260:Female; D007678:Kidney Glomerulus / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009113:Muramidase / Q000378:metabolism*; D011507:Proteinuria / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D009113:Muramidase