Trypsin induces Ca2+‐activated Cl− currents in X. laevis oocytes

FEBS Letters

Durieux, Marcel E.²  Salafranca, Mina N.²  Lynch, Kevin R.¹ 

[1] Department of Pharmacology, University of Virginia, Box 238, University of Virginia Health Sciences Center, Charlottesville, VA 22903, USA;Department of Anesthesiology, University of Virginia, Box 238, University of Virginia Health Sciences Center, Charlottesville, VA 22903, USA

关键词: Oocyte;    Xenopus laevis;    Trypsin;    Voltage clamp;    Membrane receptor;    Lysophosphatidic acid;   

DOI  :  10.1016/0014-5793(94)80198-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protease trypsin induces Ca²⁺-activated Cl⁻ currents when applied in concentrations as low as 0.1 to defolliculated, voltage clamped X. laevis oocytes. The response is dose-dependent and specific, as other proteases (chymotrypsin, Lys-C and Arg-C), or trypsin pretreated with soybean trypsin inhibitor, did not induce currents. Intracellular trypsin injection did not induce responses. The current does not appear to result from proteolytic activation of the endogenous receptor for lysophosphatidic acid, the only known Ca²⁺-mobilizing receptor consistently present in oocytes. These results suggest the presence on the oocyte membrane of a specific receptor for trypsin.

【 授权许可】

Unknown