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Trypsin induces Ca(2+)-activated Cl- currents in X. laevis oocytes
M E Durieux1, M N Salafranca, K R Lynch
1Department of Anesthesiology, University of Virginia, Charlottesville 22903.
FEBS Letters
|January 17, 1994
Summary
The protease trypsin activates calcium-activated chloride currents in Xenopus laevis oocytes. This suggests a specific cell membrane receptor for trypsin exists on these oocytes.
Area of Science:
- Cell biology
- Molecular biology
- Physiology
Background:
- Xenopus laevis oocytes are a common model for studying ion channel function.
- Calcium-activated chloride currents play roles in various cellular processes.
- The specific mechanisms triggering these currents are not fully understood.
Purpose of the Study:
- To investigate the effect of the protease trypsin on Xenopus laevis oocytes.
- To determine if trypsin can induce calcium-activated chloride currents.
- To explore the potential mechanism and specificity of this interaction.
Main Methods:
- Defolliculated, voltage-clamped Xenopus laevis oocytes were used.
- Trypsin was applied extracellularly at varying concentrations.
- Other proteases and pretreated trypsin were tested for comparison.
- Intracellular injection of trypsin was also performed.
Main Results:
- Trypsin induced dose-dependent calcium-activated chloride currents at concentrations as low as 0.1 mg/ml.
- Specificity was observed, as other proteases did not induce currents.
- Pretreated trypsin and intracellular injection failed to elicit a response.
- The current was not due to activation of the lysophosphatidic acid receptor.
Conclusions:
- A specific receptor for trypsin is likely present on the Xenopus laevis oocyte membrane.
- Trypsin-induced currents are not mediated by known calcium-mobilizing receptors.
- This finding opens new avenues for understanding oocyte signaling pathways.