Drastic facilitation by α‐latrotoxin of bovine chromaffin cell exocytosis without measurable enhancement of Ca2+ entry or [Ca2+]i
@article{Michelena1997DrasticFB, title={Drastic facilitation by $\alpha$‐latrotoxin of bovine chromaffin cell exocytosis without measurable enhancement of Ca2+ entry or [Ca2+]i}, author={Pedro Michelena and Mar{\'i}a‐Teresa Fuente and Teresa Vega and Baldomero Lara and Manuela G. L{\'o}pez and Luis Gand{\'i}a and Antonio G. Garc{\'i}a}, journal={The Journal of Physiology}, year={1997}, volume={502} }
1 Latrotoxin (LTX, 1–3 nm) caused a gradual increase of the supontaneous catecholamine release rate in bovine adrenal chromaffin cells superfused with normal Krebs–Hepes solution containing 2.5 mm Ca2+. Ca2+ removal abolished this effect. LTX enhanced also the secretory responses to high K+ (35 or 70 mm) and to acetylcholine (ACh, 30 μm). 2 The application of Ca2+ pulses to cells previously superfused with a 0 Ca2+ solution (Krebs–Hepes deprived of CaCl2) induced secretory responses that…
24 Citations
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The effects of expression of a newly cloned Ca2+-independent receptor for α-Ltx (CIRL) on secretion from bovine chromaffin cells suggest that this receptor modulates the normal function of the regulated secretory pathway and that α- Ltx may act by reversing the inhibitory effects of the receptor.
Vesicle exocytosis stimulated by α‐latrotoxin is mediated by latrophilin and requires both external and stored Ca2+
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The results unite previously contradictory data about the toxin's effects and suggest that LTX‐stimulated exocytosis depends upon the co‐operative action of external and intracellular Ca2+ involving G proteins and PLC, whereas theCa2+‐independent release is largely non‐vesicular.
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α‐Latrotoxin forms calcium‐permeable membrane pores via interactions with latrophilin or neurexin
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- 2000
The results suggest that after anchoring to either of its nerve terminal receptors, α‐latrotoxin inserts into the membrane and constitutes a single type of transmembrane ion pore.
α-Latrotoxin and Its Receptors
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The mechanism of alpha-LTX pore formation, revealed by cryo-electron microscopy, involves toxin assembly into homotetrameric complexes which harbor a central channel and can insert into lipid membranes and cannot exert its actions without binding to specific receptors of the plasma membrane.
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