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

Filbin, Marie T.; Lunt, George G.; Donnellan, John F.

doi:10.1111/j.1432-1033.1983.tb07340.x

Cited by 27 publications

(3 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The biochemical evidence, however, indicates that the locust polypeptide (Mr = 65 000) is present in the native tissue in an oligomeric AChR . Protein bands with molecular sizes distinct from Mr = 65 000 have been reported, also, from several insect species (Filbin et al, 1983;Macallan et al, 1988) but their possible functional roles remain to be determined.…”

Section: Expression In Xenopus Oocytesmentioning

confidence: 99%

Sequence and functional expression of a single alpha subunit of an insect nicotinic acetylcholine receptor.

Marshall¹,

Buckingham²,

Shingai³

et al. 1990

The EMBO Journal

132

View full text Add to dashboard Cite

We report the isolation and sequence of a cDNA clone that encodes a locust (Schistocerca gregaria) nervous system nicotinic acetylcholine receptor (AChR) subunit (aLl). The calculated molecular weight of the unglycosylated polypeptide, which contains in the proposed extracellular domain two adjacent cysteine residues which are characteristic of a (ligand binding) subunits, is 60 641 daltons. Injection into Xenopus oocytes, of RNA synthesized from this clone in vitro, results in expression of functional nicotinic receptors in the oocyte membrane. In these, nicotine opens a cation channel; the receptors are blocked by both a-bungarotoxin (a-Bgt) and x-bungarotoxin (x-Bgt). Reversible block of the expressed insect AChR by mecamylamine, d-tubocurarine, tetraethylammonium, bicuculline and strychnine has also been observed. These data are entirely consistent with previously reported electrophysiological studies on in vivo insect nicotinic receptors and also with biochemical studies on an cx-Bgt affinity purified locust AChR. Thus, a functional receptor exhibiting the characteristic pharmacology of an in vivo insect nicotiniic AChR can be expressed in Xenopus oocytes by injection with a single subunit RNA.

show abstract

Section: Expression In Xenopus Oocytesmentioning

confidence: 99%

Sequence and functional expression of a single alpha subunit of an insect nicotinic acetylcholine receptor.

Marshall¹,

Buckingham²,

Shingai³

et al. 1990

The EMBO Journal

132

View full text Add to dashboard Cite

show abstract

“…Supraoesophageal ganglia were quickly removed from the heads of 2-week-old adult locusts as previously described by Filbin et al (1983). Fifty ganglia (approximately 100 mg of tissue) provided about 1.5 mg of final membrane protein.…”

Section: Preparation Of Synaptic Membranesmentioning

confidence: 99%

γ‐Aminobutyric Acid Receptor Complex of Insect CNS: Characterization of a Benzodiazepine Binding Site

Robinson

MacAllan

Lunt

et al. 1986

Journal of Neurochemistry

View full text Add to dashboard Cite

The specific binding of [N-methyl-3H]flunitrazepam ([3H]FNZP) to a membrane fraction from the supraoesophageal ganglion of the locust (Schistocerca gregaria) has been measured. The ligand binds reversibly with a KD of 47 nM. The binding is Ca2+-dependent, a property not found for the equivalent binding site in vertebrate brain. The pharmacological characteristics of the locust binding site show similarities to both central and peripheral benzodiazepine receptors in mammals. Thus binding is enhanced by gamma-aminobutyric acid (GABA), a feature of mammalian central receptors, whereas the ligand Ro 5-4864 was more effective in displacing [3H]FNZP than was clonazepam, which is the pattern seen in mammalian peripheral receptors. The locust benzodiazepine binding site was photoaffinity-labelled by [3H]FNZP, and two major proteins of Mr 45K and 59K were specifically labelled. In parallel experiments with rat brain membranes a single major protein of Mr 49K was labelled, a finding in keeping with many reports in the literature. We suggest that the FNZP binding site described here is part of the GABA receptor complex of locust ganglia. The insect receptor appears to have the same general organization as its mammalian counterpart but differs significantly in its detailed properties.

show abstract

“…After 2 years, Marie switched her attention to the locust supraesophageal ganglion and succeeded in using a-bungarotoxin to identify, again by radioliogand binding, a nicotinic acetylcholine receptor in the locust central nervous system. This work was published in the European Journal of Biochemistry, her first paper (Filbin et al 1983).…”

mentioning

confidence: 99%

Marie T. Filbin

Stephenson

2014

Journal of Neurochemistry

View full text Add to dashboard Cite

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

Cited by 27 publications

References 34 publications

Sequence and functional expression of a single alpha subunit of an insect nicotinic acetylcholine receptor.

Sequence and functional expression of a single alpha subunit of an insect nicotinic acetylcholine receptor.

γ‐Aminobutyric Acid Receptor Complex of Insect CNS: Characterization of a Benzodiazepine Binding Site

Marie T. Filbin

Contact Info

Product

Resources

About