title: Changes in lysosome populations in the rat kidney cortex induced by passive Heymann glomerulonephritis.
abstract: Acute passive Heymann glomerulonephritis in rats induced heavy proteinuria and highly increased urinary activity of N-acetyl-beta-D-glucosaminidase, acid beta-galactosidase and acid phosphatase. The cortical activity of these acid hydrolases was increased essentially in the large lysosomes as demonstrated by subfractionation of the lysosome-rich mitochondrial-lysosomal fraction, by rate zonal centrifugation. Banding density of small lysosomes shifted or reduced to slightly lower value (1.225 g/ml), which is between the banding densities of small 'light' (1.20 g/ml) and small 'dense' lysosomes (1.235 g/ml) in normal rat kidney cortex. Labelled protein reabsorbed in the proximal tubule is recovered in these populations of small lysosomes as well as in the large lysosomes or 'protein droplets'. Glomerulonephritis also induced a new population of small 'light' lysosomes (density 1.185-1.195 g/ml) enriched in cathepsin D. The previously demonstrated morphological, biochemical, and physiological heterogeneity of renal lysosomes was confirmed and emphasized in the kidney cortex of glomerulonephritic rats. The main changes in the lysosomal populations appear to reflect the increased protein reabsorption as confirmed by the proteinuria.
mesh_terms: D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D005455:Fluorescent Antibody Technique; D005921:Glomerulonephritis / Q000201:enzymology* / Q000276:immunology; D006867:Hydrolases / Q000378:metabolism; D007672:Kidney Cortex / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D001616:beta-Galactosidase / Q000378:metabolism
chemical_list: D006867:Hydrolases; D000135:Acid Phosphatase; D001616:beta-Galactosidase; D000118:Acetylglucosaminidase