Abstract
The effect of trypsin on the voltage-activated chloride conductance ( G Cl) of toad skin was investigated. Serosal application of >0.1 mg ml −1 trypsin decreased the voltage-activated G Cl without notable delay. The maximal inhibition to 38% of the control values, exerted within 15 min, was in some experiments partly or completely reversible. Chymotrypsin had much lower effect than trypsin. Mucosal application of trypsin did not have any effect. Trypsin did neither interfere with the conductive pathway opened by supramaximal concentrations of cAMP nor with the inhibitory effect of epinephrine on the voltage-activated G Cl. The effect of trypsin required influx of Ca 2+ from the extracellular space. It is concluded that protease-activated receptors or trypsin-sensitive proteins in the basolateral membrane of toad skin epithelial cells interfere with regulative steps involved in the voltage-activation of G Cl. This may be harmful for the segregation of epithelial cells using this enzyme.
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