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Glomerular lysosomal enzymes in aminonucleoside nephrosis
Renal Physiology
|January 1, 1980
Summary
Lysosomal enzyme activity and lysosome stability in rat glomeruli were altered in nephrotic syndrome. These changes may contribute to glycoprotein metabolism disruption in glomerular diseases.
Area of Science:
- Nephrology
- Cell Biology
- Biochemistry
Background:
- Lysosomal hydrolases are involved in extracellular matrix glycoprotein catabolism in glomeruli.
- Lysosomal dysfunction may play a role in glomerular diseases.
Purpose of the Study:
- To investigate lysosomal enzyme activities and lysosome stability in the glomeruli of rats with puromycin aminonucleoside-induced nephrosis.
- To understand the role of lysosomal alterations in nephrotic syndrome.
Main Methods:
- Induction of nephrosis in rats using puromycin aminonucleoside.
- Measurement of lysosomal enzyme activities (beta-fucosidase, arylsulfatase, acid phosphatase, beta-glucuronidase) in isolated glomeruli.
- Assessment of lysosomal osmotic stability.
Main Results:
- Nephrotic rat glomeruli showed decreased beta-fucosidase and arylsulfatase activities.
- Acid phosphatase activity was elevated in nephrotic rat glomeruli.
- Lysosomal osmotic stability was reduced in nephrotic rats, indicated by increased beta-glucuronidase release.
Conclusions:
- Altered lysosomal enzyme profiles and impaired lysosome physiology in glomeruli are associated with nephrotic syndrome.
- These glomerular lysosomal abnormalities may be pathogenic factors in glycoprotein metabolism disturbances in nephrotic syndrome and other glomerular diseases.