Trachynilysin, a Neurosecretory Protein Isolated from Stonefish (Synanceia trachynis) Venom, Forms Nonselective Pores in the Membrane of NG108-15 Cells
Open Access
- 1 October 2002
- journal article
- Published by Elsevier BV
- Vol. 277 (42), 39119-39127
- https://doi.org/10.1074/jbc.m203433200
Abstract
Trachynilysin, a protein toxin isolated from the venom of the stonefish Synanceia trachynis, has been reported to elicit massive acetylcholine release from motor nerve endings of isolated neuromuscular preparations and to increase both cytosolic Ca2+ and catecholamine release from chromaffin cells. In the present study, we used the patch clamp technique to investigate the effect of trachynilysin on the cytoplasmic membrane of differentiated NG108-15 cells in culture. Trachynilysin increased membrane conductance the most when the negativity of the cell holding membrane potential was reduced. The trachynilysin-induced current was carried by cations and reversed at about −3 mV in standard physiological solutions, which led to strong membrane depolarization and Ca2+ influx. La3+ blocked the trachynilysin current in a dose-, voltage-, and time-dependent manner, and antibodies raised against the toxin antagonized its effect on the cell membrane. The inside-out configuration of the patch clamp technique allowed the recording of single channel activity from which various multiples of 22 pS elementary conductance were resolved. These results indicate that trachynilysin forms pores in the NG108-15 cell membrane, and they advance our understanding of the toxin's mode of action on motor nerve endings and neurosecretory cells.Keywords
This publication has 44 references indexed in Scilit:
- α‐Latrotoxin forms calcium‐permeable membrane pores via interactions with latrophilin or neurexinEuropean Journal of Neuroscience, 2000
- The Calcium-Independent Receptor of α-Latrotoxin Is Not a NeurexinBiochemical and Biophysical Research Communications, 1996
- Pore Formation by the Cytotoxic Islet Amyloid Peptide AmylinPublished by Elsevier BV ,1996
- High Affinity Binding of α-Latrotoxin to Recombinant Neurexin IαPublished by Elsevier BV ,1995
- Tamoxifen blocks both proliferation and voltage-dependent K+ channels of neuroblastoma cellsCellular Signalling, 1990
- α-latrotoxin and related toxinsPharmacology & Therapeutics, 1989
- Permeation of divalent cations through α-latrotoxin channels in lipid bilayers: steady-state current-voltage relationshipsThe Journal of Membrane Biology, 1987
- αLatrotoxin of the black widow spider venom opens a small, non-closing cation channelBiochemical and Biophysical Research Communications, 1986
- Black Widow Spider Venom: Effect of Purified Toxin on Lipid Bilayer MembranesScience, 1976
- POTENTIAL, IMPEDANCE, AND RECTIFICATION IN MEMBRANESThe Journal of general physiology, 1943