The effect of α-latrotoxin on the neurosecretory PC12 cell line: Studies on toxin binding and stimulation of transmitter release
Reference (39)
- et al.
Release, storage and uptake of catecholamines by a clonal cell line of nerve growth factor (NGF) responsive pheochromocytoma cells
Brain Res.
(1977) - et al.
The effect of α-latrotoxin on the neurosecretory PC12 cell line: electron microscopy and cytotoxicity studies
Neuroscience
(1983) - et al.
The action of black widow spider venom on cholinergic mechanisms in synaptosomes
J. Neurochem.
(1980) - et al.
Calcium dependence of catecholamine release from bovine adrenal medullary cells after exposure to intense electric field
J. Memb. Biol.
(1982) - et al.
Calcium Movement in Excitable Cells
(1975) - et al.
Freeze-fracture studies of frog neuromuscular junction during intense release of neurotransmitter
J. Cell Biol.
(1979) - et al.
Ca2+-dependent recycling of synaptic vesicles of the frog neuromuscular junction
J. Cell Biol.
(1980) - et al.
Changes in the fine structure of the neuromuscular junction of the frog caused by black widow spider venom
J. Cell Biol.
(1972) - et al.
Discrete and discontinuous action of brown widow spider venom on the presynaptic nerve terminals of frog muscle
J. Physiol., Lond.
(1975) - et al.
Black widow spider venom: effect of the purified toxin on lipid bilayer membranes
Science, N.Y.
(1976)
Purification from black widow spider venom of a protein factor causing the depletion of synaptic vesicles of neuromuscular junction
J. Cell Biol.
Acetylcholine compartments in mouse diaphragm. Comparison of the effects of black widow spider venom, electrical stimulation and high concentration of potassium
J. Cell Biol.
Black widow spider toxin-induced calcium fluxes and transmitter release in a neurosecretory cell line
Nature, Lond.
A toxin purified from the venom of black widow spider affects uptake and release of radioactive γ aminobutyrate and N-epinephrine from rat brain synaptosomes
Ear. J. Biochem.
Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
Properties of the nerve growth factor receptor of a clonal line of rat pheochromocytoma (PC12) cell
Expl. Cell Res.
Effects and mechanisms of polypeptide neurotoxins that act presynaptically
A. Rev. Pharmac. Toxicol.
Use of black widow spider venom to study the release of neurotransmitters
Effects of calcium and magnesium on the frequency of miniature end plate potentials during prolonged tetanization
J. Physiol., Lond.
Cited by (70)
Synaptotagmin 1-mediated cell membrane penetration and dopamine release enhancement by latroeggtoxin-VI
2022, International Journal of Biological MacromoleculesCitation Excerpt :For instance, PC12 cells played an important role in uncovering the action mechanism of α-latrotoxin, a representative proteinaceous neurotoxin in the venom of L. tredecimguttatus. α-Latrotoxin was shown to bind to the receptors at the plasma membrane of PC12 cells, causing cell membrane depolarization, calcium influx, and massive neurotransmitter release [19–21]. In our present study, we focused on the investigation of the molecular mechanisms underlying the cell membrane penetration and dopamine release enhancement by LETX-VI, using PC12 cells as a model.
Neurobiology and therapeutic applications of neurotoxins targeting transmitter release
2019, Pharmacology and TherapeuticsCitation Excerpt :When injected systemically, the primary target of α-latrotoxin is the neuromuscular junction, where the toxin triggers exocytosis of acetylcholine contained in clear synaptic vesicles (Ceccarelli, Hurlbut, & Iezzi, 1988; Matteoli et al., 1988). Induced by α-latrotoxin, secretion of peptides and catecholamines from sensory neurons and endocrine cells has also been widely documented (Barnett, Liu, & Misler, 1996; De Potter, Partoens, Schoups, Llona, & Coen, 1997; Meldolesi, Madeddu, Torda, Gatti, & Niutta, 1983). In fact, α-latrotoxin has proved capable of activating massive release of all mediators from all secretory cell types tested so far (Silva, Lelianova, Hopkins, Volynski, & Ushkaryov, 2009).
Presynaptic neurotoxins: An expanding array of natural and modified molecules
2012, Cell CalciumCitation Excerpt :In neurons, the Ca2+-independent secretion is restricted to small synaptic vesicles containing glutamate, γ-aminobutyric acid and acetylcholine, but not catecholamines or peptides [54,59,60]. Endocrine cells do not normally respond to α-latrotoxin in the absence of Ca2+ [61–63], although Ca2+-independent secretion was observed in some endocrine cells [64–66]. The Ca2+-independent action of α-latrotoxin is unusual: it strictly requires the presence of divalent cations (particularly Mg2+) [43] and, as we shall see below, toxin tetramerisation.
Insecticidal toxins from black widow spider venom
2007, ToxiconMechanism of α-latrotoxin action at nerve endings of neurohypophysis
2003, Brain ResearchCitation Excerpt :Indeed, a recent report using a mutant α-latrotoxin (LTX N4C), which fails to form ion conductive pores but retains receptor binding properties found that the mutant latrotoxin retained an ability to elicit neurotransmitter release, although the release response was less than observed with wild type toxin [2,58]. The ability of α-latrotoxin to associate with and incorporate into lipid bilayers and cell membranes to form cationic selective membrane pores has been extensively characterized [15,23,34,48,54,56]. However, although there has been considerable focus on understanding the action of α-latrotoxin at nerve endings, to our knowledge the present results demonstrate the first α-latrotoxin-mediated currents to be recorded directly from mammalian nerve endings.
Latrotoxin stimulates secretion in permeabilized cells by regulating an intracellular Ca<sup>2+</sup>- and ATP-dependent event: A role for protein kinase C
2000, Journal of Biological ChemistryCitation Excerpt :Fig. 1 Bdemonstrates that adding α-Ltx after the trypsinized cells were permeabilized did not restore the α-Ltx effect. The lectin concanavalin A has also been reported to prevent binding of α-Ltx to membranes (22, 23). Indeed, a recently cloned Ca2+-independent receptor for α-Ltx (6) is extensively glycosylated (24, 25).