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Proteinases in renal cell death

X Yang1, R G Schnellmann

  • 1Department of Physiology and Pharmacology, College of Veterinary Medicine, University of Georgia, Athens, USA.

Journal of Toxicology and Environmental Health
|July 1, 1996
PubMed
Summary

Cysteine and aspartic proteinases contribute to renal proximal tubule cell death. Inhibitors suggest dying cells release proteinases that harm neighboring cells, highlighting a novel mechanism in kidney injury.

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Area of Science:

  • Nephrology
  • Cell Biology
  • Biochemistry

Background:

  • Proteinases play a critical role in cellular processes, including cell death.
  • Understanding the specific types of proteinases involved in renal proximal tubule (RPT) cell death is crucial for developing targeted therapies.
  • Previous research has not fully elucidated the contribution of different proteinase classes to RPT injury.

Purpose of the Study:

  • To investigate the role of specific proteinases in mediating renal proximal tubule (RPT) cellular death.
  • To determine whether cysteine, serine, or aspartic proteinases are involved in RPT cell death induced by specific toxins.

Main Methods:

  • Rabbit RPT suspensions were exposed to antimycin A or tetrafluoroethyl-L-cysteine (TFEC) to induce cell death.
  • Specific inhibitors targeting cysteine (E-64), serine (TLCK, DCS), and aspartic (pepstatin) proteinases were used.
  • Lactate dehydrogenase (LDH) release was measured as a marker of cell death, and lysosomal membrane potential was assessed using neutral red release.

Main Results:

  • E-64 (cysteine proteinase inhibitor) and pepstatin (aspartic proteinase inhibitor) significantly reduced LDH release induced by antimycin A or TFEC.
  • Serine proteinase inhibitors (TLCK, DCS, leupeptin, antipain) did not protect RPT cells from toxin-induced death.
  • Inhibition of lysosomal cathepsins B and L by E-64 correlated with cytoprotection, but protection was observed only after some cell death had occurred.

Conclusions:

  • Lysosomal cysteine and aspartic proteinases, but not serine proteinases, are implicated in RPT cell death induced by antimycin A or TFEC.
  • The delayed protective effect of E-64 suggests that proteinases are released from dying cells and contribute to the death of adjacent viable cells.
  • These findings reveal a potential autocrine or paracrine mechanism of RPT injury mediated by released lysosomal enzymes.

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