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Trypsin inhibits voltage-activated chloride conductance of toad skin

W Nagel1, U Katz

  • 1Physiologisches Institut Universität München, Germany. W.Nagel@lrz.uni-muenchen.de

Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology
|April 27, 1999
PubMed

Insights

Trypsin significantly reduces voltage-activated chloride conductance (GCl) in toad skin by acting on the basolateral membrane. This enzyme

Area of Science:

  • Physiology
  • Biochemistry
  • Cell Biology

Background:

  • Toad skin exhibits voltage-activated chloride conductance (GCl).
  • Proteases can modulate cellular functions through specific receptors or protein interactions.

Purpose of the Study:

  • To investigate the effect of trypsin on voltage-activated GCl in toad skin.
  • To elucidate the mechanism and localization of trypsin's action.

Main Methods:

  • Serosal and mucosal application of trypsin and chymotrypsin to toad skin.
  • Measurement of voltage-activated GCl.
  • Assessment of calcium influx dependence.
  • Investigation of interactions with cAMP and epinephrine pathways.

Main Results:

  • Serosal trypsin (> 0.1 mg ml-1) rapidly decreased voltage-activated GCl, with maximal inhibition of 38% within 15 minutes.
  • The inhibitory effect was partially or completely reversible in some cases.
  • Chymotrypsin showed a much weaker effect, and mucosal trypsin had no effect.
  • Trypsin's action was dependent on extracellular calcium influx and did not affect cAMP- or epinephrine-mediated GCl modulation.

Conclusions:

  • Trypsin interferes with voltage-activated GCl via protease-activated receptors or trypsin-sensitive proteins in the basolateral membrane of toad skin epithelial cells.
  • This interaction may disrupt epithelial cell segregation processes.
  • The findings highlight the role of specific proteases in regulating ion transport across epithelial tissues.

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