Literature DB >> 6172816

Glomerular lysosomal enzymes in aminonucleoside nephrosis.

J A Velosa, S V Shah, S L Ou, H E Abboud, T P Dousa.   

Abstract

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.

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Year:  1980        PMID: 6172816     DOI: 10.1159/000172751

Source DB:  PubMed          Journal:  Ren Physiol        ISSN: 0378-5858


  2 in total

1.  Expression of Cathepsin L and Its Intrinsic Inhibitors in Glomeruli of Rats With Puromycin Aminonucleoside Nephrosis.

Authors:  Ayano Kubo; Isao Shirato; Teruo Hidaka; Miyuki Takagi; Yu Sasaki; Katsuhiko Asanuma; Kazumi Ishidoh; Yusuke Suzuki
Journal:  J Histochem Cytochem       Date:  2018-07-27       Impact factor: 2.479

2.  Endocytosis of cationized horseradish peroxidase by glomerular epithelial cells is reduced in puromycin glomerulopathy.

Authors:  Y Wang; B Evans; J H Thomas; T Nunan; J I Gaunt; R W Morris; D R Davies
Journal:  Int J Exp Pathol       Date:  1990-12       Impact factor: 1.925

  2 in total

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