Quinuclidinyl Benzilate Binding in House Fly Heads and Rat Brain

Jones, Stephen; Sumikawa, Katumi

doi:10.1111/j.1471-4159.1981.tb01614.x

Cited by 34 publications

(15 citation statements)

References 16 publications

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“…The Muscarinic cholinergic receptors have been studied in a few non-mammalian species (32)(33)(34), and found to have properties similar to those defined in rat brain, indicating phylogenetic conservation of this binding site. The pharmacologic profile of [3H]quinuclidinyl benzilate binding is comparable, for instance, between the house fly head and the rat brain (35). The regional distribution of muscarinic receptors has been reported in a variety of mammalian brains, including rat (18,36,37), monkey (38), and human (39).…”

Section: Discussionmentioning

confidence: 89%

Autoradiographic quantification of muscarinic cholinergic synaptic markers in bat, shrew, and rat brain

et al. 1994

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We employed radioligand binding autoradiography to determine the distributions of pre-and postsynaptic cholinergic radioligand binding sites in the brains of two species of bat, one species of shrew, and the rat. High affinity choline uptake sites were measured with [3H]hemicholinium, and presynaptic cholinergic vesicles were identified with [3H]vesamicol. Muscarinic cholinergic receptors were determined with [3H]scopolamine. The distribution patterns of the three cholinergic markers were simitar in all species examined, and identified known major cholinergic pathways on the basis of enrichments in both pre-and postsynaptic markers. In addition, there was excellent agreement, both within and across species, in the regional distributions of the two presynaptic cholinergic markers. Our results indicate that pharmacological identifiers of cholinergic pathways and synapses, including the cholinergic vesicle transport site, and the organizations of central nervous system cholinergic pathways are phylogenetically conserved among eutherian mammals.

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Section: Discussionmentioning

confidence: 89%

Autoradiographic quantification of muscarinic cholinergic synaptic markers in bat, shrew, and rat brain

et al. 1994

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“…There are other putative AChRs in fruit fly and house fly heads with muscarinic (Haim et al, 1979;Jones and Sumikawa, 1981) and mixed (Eldefrawi and O'Brien, 1970) pharmacology. The muscarinic sites are pharmacologically distinguishable from the nicotinic site described here, most clearly by the high affinity of the muscarinic site for classic muscarinic antagonists.…”

Section: S W Jones Et Almentioning

confidence: 99%

α‐Bungarotoxin Binding in House Fly Heads and Torpedo Electroplax

Jones

Sudershan

O’Brien

1981

Journal of Neurochemistry

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House fly heads contain a site that binds alpha-bungarotoxin with high affinity. It is present at about 23 pmol/g of heads and binds alpha-bungarotoxin (labeled with [3H]pyridoxamine phosphate) reversibly with a Kd of 6 nM. The effects of 48 drugs have been compared on the alpha-bungarotoxin binding sites of house fly and Torpedo. The pharmacology of the house fly sites is similar to that previously reported for neuronal alpha-bungarotoxin binding sites in both vertebrates and invertebrates and is distinguishable from that of the classic nicotinic neuromuscular acetylcholine receptor, as exemplified by that of Torpedo electroplax. Differences between the house fly site and Torpedo include higher affinities of the Torpedo receptor for decamethonium, hexamethonium, carbamylcholine, and acetyl-beta-methylcholine, but lower affinities for nicotine, atropine, and dihydro-beta-erythroidine.

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“…This effect is not the result of the inhibition of Ca2 +-activated proteases and raises the possibility that divalent cations such as Ca2+ and Mg2+ may be involved in the maintenance of the binding protein in its membrane-bound state. The behavior o f the fly-head binding protein may represent a species variation but other workers have reported a particulate localisation of a-bungarotoxin binding in housefly heads [29,301; however, in these two studies no quantitative measurement of overall recovery of binding activity in the various fractions was made. At this stage one can only conclude that the insect a-bungarotoxin-binding component behaves differently from the nicotinic acetylcholine receptor of vertebrate tissues.…”

Section: Acetylcholinesterase Activitjmentioning

confidence: 59%

Partial Purification and Characterisation of an Acetylcholine Receptor with Nicotinic Properties from the Supraoesophageal Ganglion of the Locust (Schistocerca gregaria)

Filbin

Lunt

Donnellan

1983

European Journal of Biochemistry

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An α‐bungarotosin‐binding component has been partially purified from the supraoesophageal ganglion of the locust, (Schistocerca gregaria). The component binds α‐bungarotosin with a Kd of about 1.7 nM and this value changes little throughout the purification procedure. The specific binding activity ranges from 1.18 pmol α‐bungarotoxin bound/mg protein for the membrane‐bound site up to a maximum of 230 pmol bound/mg protein for the partially purified component. The pharmacological properties of the membrane‐bound site are predominantly nicotinic. Affnity labelling of the binding species with 4‐(N‐maleimido)‐[3H]benzyltrimethylammonium suggests that the binding is associated with a peptide of Mr 58000. Polyacrylamide gel electrophoresis of the partially purified of binding component shows three major bands corresponding to Mr of 60000, 41000 and 25000. We suggest that the binding component can be tentatively identified as a nicotinic acetylcholine receptor.

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Quinuclidinyl Benzilate Binding in House Fly Heads and Rat Brain

Cited by 34 publications

References 16 publications

Autoradiographic quantification of muscarinic cholinergic synaptic markers in bat, shrew, and rat brain

Autoradiographic quantification of muscarinic cholinergic synaptic markers in bat, shrew, and rat brain

α‐Bungarotoxin Binding in House Fly Heads and Torpedo Electroplax

Partial Purification and Characterisation of an Acetylcholine Receptor with Nicotinic Properties from the Supraoesophageal Ganglion of the Locust (Schistocerca gregaria)

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