Cholinergic receptors on cultured neurones from the central nervous system of embryonic cockroaches

Lees, George; Beadle, David J.; Botham, Roger P.

doi:10.1016/0006-8993(83)90080-x

Cited by 49 publications

(9 citation statements)

References 21 publications

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“…Like [3H]QNB binding sites, [1251]a-BGT sites are found in very high concentrations (>2,000 fmollmg protein) in TG preparations. Although higher than that previously reported for most vertebrate and invertebrate preparations (Morley et al, 1979;Salvaterra and Foders, 1979), this value compares very closely with the density of toxin binding sites reported recently for cultured embryonic cockroach central neurons (Lees et al, 1983) and may be due in large part to the relative enrichment of cholinergic terminals in the ganglion arising from massive sensory input.…”

Section: Properties Of Tg Toxin Binding Sitessupporting

confidence: 87%

“…9B) and thus represents nonspecific toxin uptake and/or binding to nonneuronal elements. In general, density of label was low over the cortical rind (region of neuronal parikarya; see Lees et al, 1983) and over peripheral nerve pathways, areas that are devoid of synapses. Specific toxin binding sites were largely confined to regions within ganglionic neuropile.…”

Section: Localization Of Putative Achrs In Tgmentioning

confidence: 98%

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Muscarinic and Nicotinic Cholinergic Binding Sites in the Terminal Abdominal Ganglion of the Cricket (Acheta domesticus)

Meyer

Reddy

1985

Journal of Neurochemistry

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Cricket (Acheta domesticus) terminal abdominal ganglia (TG) contain high concentrations (approximately 2 pmol/mg protein) of muscarinic and nicotinic cholinergic binding sites, based on the capacity of TG to bind specifically the labelled ligands L-[3H]quinuclidinyl benzilate ([3H]QNB) and [125I]alpha-bungarotoxin ([125I]alpha-BGT) with high affinity. For both ligands, binding is saturable and reversible. Competitive displacement experiments indicate that the [3H]QNB and [125I]alpha-BGT binding sites probably represent pharmacologically distinct classes of putative TG acetylcholine receptors (AChRs). Results from physiological recording and autoradiographic localization experiments demonstrate that a portion of the putative nicotinic AChRs is localized in synaptic regions of the well-characterized cercal sensory-giant interneuron pathway in the TG, where they are likely to serve as functional synaptic AChRs. Unlike nicotinic ligands, muscarinic agents do not appear to be pharmacologically active in this pathway. Therefore, in the insect CNS, putative muscarinic and nicotinic AChRs coexist at high density, but can be pharmacologically distinguished from one another on the basis of criteria derived from both ligand binding and physiological methods.

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Section: Properties Of Tg Toxin Binding Sitessupporting

confidence: 87%

Section: Localization Of Putative Achrs In Tgmentioning

confidence: 98%

Muscarinic and Nicotinic Cholinergic Binding Sites in the Terminal Abdominal Ganglion of the Cricket (Acheta domesticus)

Meyer

Reddy

1985

Journal of Neurochemistry

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“…No inhibition of nicotinic-cholinergic transmission by ct-Btx has been observed in grasshopper dorsal unpaired median neurons (Goodman and Spitzer, 1979). On the other hand, cx-Btx at 2892 0 A concentrations of 10-7 to 10-8 M can block ACh responses in certain cockroach neurons (Lees et al, 1983;David and Satelle, 1984). Clear evidence for the identity of a-Btx binding sites and a neuronal AChR in the migratory locust has been provided by reconstitution experiments with affinity-purified AChR preparations (Hanke and Breer, 1986).…”

Section: Discussionmentioning

confidence: 99%

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Schloss¹,

Hermans-Borgmeyer²,

Betz³

et al. 1988

The EMBO Journal

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The ard gene of Drosophila melanogaster encodes a structural homologue of vertebrate nicotinic acetylcholine receptors (AChR) and is expressed exclusively in nervous tissue. To study the nature of the ARD protein, antibodies were raised against fusion constructs containing two regions of this polypeptide. One segment is putatively extracellular (amino acids 65‐212), the other domain is exposed to the cytoplasm (amino acids 305‐444). The ARD antisera obtained served to investigate the physical relationship between the ARD protein and alpha‐bungarotoxin (alpha‐Btx) binding sites occurring in Drosophila. Two different high‐affinity binding sites for [125I]alpha‐Btx, a highly potent antagonist of vertebrate muscle AChR, were detected in fly head membranes. Equilibrium binding and kinetic studies revealed Kd values of approximately 0.1 nM (site 1) and approximately 4 nM (site 2). The estimated maximal binding (Bmax) was approximately 240 and 1080 fmol/mg protein respectively. Both sites exhibited a nicotinic‐cholinergic pharmacology. Immunoprecipitation experiments with the ARD antisera indicated that the ARD protein is associated with the [125I]alpha‐Btx binding site 1 only. These data support the previously postulated hypothesis that the ARD protein is part of an alpha‐Btx binding neuronal AChR of Drosophila. Furthermore, they indicate heterogeneity in nicotinic‐cholinergic binding sites in the insect nervous system.

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“…Most physiological evidence favors a postsynaptic localization for nicotinic AChRs in the insect CNS (Harrow et al, 1979), and this view is supported by autoradiographic data on the distribution of labeled toxin binding sites in cricket TG (Meyer and Reddy, 1985) and in other insects (Hildebrand et al, 1979;Schmidt-Nielsen et al, 1977). Although there is some recent evidence for the existence of extrasynaptic (e.g., perikaryal) insect nicotinic AChRs (Harrow and Sattelle, 1983;Lees et al, 1983) there is as yet no support for the existence of presynaptic loci for AChRs in insects. Our findings, then, for the rapid loss of TG nicotinic binding sites following cereal deafferentation are most likely to reflect the loss of postsynaptic sites, a major portion of which reside in synaptic neuropil and may represent functional AChRs.…”

Section: Regulation Of Putative Nicotinic Achrs and Achementioning

confidence: 95%

Metabolic changes in deafferented central neurons of an insect, Acheta domesticus. II. Effects on cholinergic binding sites and acetylcholinesterase

Meyer¹,

Reddy²,

Edwards³

1986

J. Neurosci.

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Following the finding that cereal deafferentation of developing giant interneurons in the terminal abdominal ganglion (TG) of the cricket Ache& dome&us reduces TG protein metabolism within target interneuron dendrites and somata (Meyer and Edwards, 1982), it is now shown that deafferentation alters the turnover of three macromolecules associated with cholinergic transmission in the cereal sensory-giant interneuron pathway.The labeled specific ligands 3H-quinuclidinyl benzilate and 1251-cY-bungarotoxin were used to assay populations of putative TG muscarinic and nicotinic cholinergic receptors, respectively, in control and deafferented groups of ganglia. The AChE activity of TG was also determined by assay and histochemical methods.Long-term deafferentation sustained throughout postembryonic development markedly reduces the densities of both muscarinic and nicotinic binding sites in the TG, short-term deafferentation of adult TG also leads to characteristic alterations in the properties of all three choline@ markers within several days. Rapid changes seen in adults thus correlate with ultrastructural data demonstrating loss of afferent terminals within hours of sensory appendage removal.We propose that peripheral innervation-dependent regulatory mechanisms operate in both the developing and adult insect nervous system. Such mechanisms may influence transsynaptitally the synthesis and turnover of specilic macromolecules, some of which may reside on the cell surface of insect central neurons that are part of the cereal sensory-giant intemeuron system.

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Cholinergic receptors on cultured neurones from the central nervous system of embryonic cockroaches

Cited by 49 publications

References 21 publications

Muscarinic and Nicotinic Cholinergic Binding Sites in the Terminal Abdominal Ganglion of the Cricket (Acheta domesticus)

Muscarinic and Nicotinic Cholinergic Binding Sites in the Terminal Abdominal Ganglion of the Cricket (Acheta domesticus)

Neuronal acetylcholine receptors in Drosophila: the ARD protein is a component of a high-affinity alpha-bungarotoxin binding complex.

Metabolic changes in deafferented central neurons of an insect, Acheta domesticus. II. Effects on cholinergic binding sites and acetylcholinesterase

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