Glomerular lysosomal enzymes in aminonucleoside nephrosis.
Lysosomal hydrolases produce degradation of glomerular basement membrane and may play a key role in catabolism of glycoproteins of extracellular matrix in glomeruli. Therefore we investigated activities of some lysosomal enzymes and stability of lysosomes in glomeruli of normal and nephrotic rats. Nephrosis was induced in rats by single injections of puromycin aminonucleoside. In glomeruli from nephrotic rats we found lower activities of beta-fucosidase and arylsulfatase, but activity of acid phosphatase was higher compared with control rats. Osmotic stability of lysosomes measured by release of beta-glucuronidase was decreased in nephrotic rats. Abnormal activity of lysosomal enzymes and altered physiology of lysosomes in glomeruli may be a pathogenic factor in the altered glycoprotein metabolism in nephrotic syndrome and perhaps also in other glomerular diseases.
D000818:Animals; D010450:Endopeptidases / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis / Q000378:metabolism; D006651:Histocytochemistry; D007678:Kidney Glomerulus / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology / Q000502:physiology; D008297:Male; D009401:Nephrosis / Q000139:chemically induced / Q000201:enzymology*; D011692:Puromycin Aminonucleoside; D051381:Rats; D011919:Rats, Inbred Strains; D013194:Staining and Labeling
D006023:Glycoproteins; D011692:Puromycin Aminonucleoside; D010450:Endopeptidases