Use of Monoclonal Antibodies to Study the Structure and Function of Nicotinic Acetylcholine Receptors on Electric Organ and Muscle and to Determine the Structure of Nicotinic Acetylcholine Receptors on Neurons

1988 ◽  
Author(s):  
Jon M. Lindstrom
Keyword(s):  
Monoclonal Antibodies ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Electric Organ ◽  
Structure And Function ◽  
Nicotinic Acetylcholine ◽  
And Function

scholarly journals Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3373
Author(s):  
Ayaulym Bekbossynova ◽  
Albina Zharylgap ◽  
Olena Filchakova
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Cholinergic System ◽  
Acetylcholine Receptors ◽  
Structure And Function ◽  
Structural Determinants ◽  
Nicotinic Acetylcholine ◽  
High Affinity ◽  
Marine Snails ◽  
And Function ◽  
Proteins And Peptides

Acetylcholine was the first neurotransmitter described. The receptors targeted by acetylcholine are found within organisms spanning different phyla and position themselves as very attractive targets for predation, as well as for defense. Venoms of snakes within the Elapidae family, as well as those of marine snails within the Conus genus, are particularly rich in proteins and peptides that target nicotinic acetylcholine receptors (nAChRs). Such compounds are invaluable tools for research seeking to understand the structure and function of the cholinergic system. Proteins and peptides of venomous origin targeting nAChR demonstrate high affinity and good selectivity. This review aims at providing an overview of the toxins targeting nAChRs found within venoms of different animals, as well as their activities and the structural determinants important for receptor binding.

scholarly journals Interactions of Nereistoxin and Its Analogs with Vertebrate Nicotinic Acetylcholine Receptors and Molluscan ACh Binding Proteins

Marine Drugs ◽  
2022 ◽  
Vol 20 (1) ◽  
pp. 49
Author(s):  
William Kem ◽  
Kristin Andrud ◽  
Galen Bruno ◽  
Hong Xing ◽  
Ferenc Soti ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Specific Radioactivity ◽  
Electric Organ ◽  
Binding Affinities ◽  
Nicotinic Acetylcholine ◽  
High Affinity ◽  
High Specific Radioactivity ◽  
Alpha Bungarotoxin

Nereistoxin (NTX) is a marine toxin isolated from an annelid worm that lives along the coasts of Japan. Its insecticidal properties were discovered decades ago and this stimulated the development of a variety of insecticides such as Cartap that are readily transformed into NTX. One unusual feature of NTX is that it is a small cyclic molecule that contains a disulfide bond. In spite of its size, it acts as an antagonist at insect and mammalian nicotinic acetylcholine receptors (nAChRs). The functional importance of the disulfide bond was assessed by determining the effects of inserting a methylene group between the two sulfur atoms, creating dimethylaminodithiane (DMA-DT). We also assessed the effect of methylating the NTX and DMA-DT dimethylamino groups on binding to three vertebrate nAChRs. Radioligand receptor binding experiments were carried out using washed membranes from rat brain and fish (Torpedo) electric organ; [3H]-cytisine displacement was used to assess binding to the predominantly high affinity alpha4beta2 nAChRs and [125I]-alpha-bungarotoxin displacement was used to measure binding of NTX and analogs to the alpha7 and skeletal muscle type nAChRs. While the two quaternary nitrogen analogs, relative to their respective tertiary amines, displayed lower α4β2 nAChR binding affinities, both displayed much higher affinities for the Torpedo muscle nAChR and rat alpha7 brain receptors than their respective tertiary amine forms. The binding affinities of DMA-DT for the three nAChRs were lower than those of NTX and MeNTX. An AChBP mutant lacking the C loop disulfide bond that would potentially react with the NTX disulfide bond displayed an NTX affinity very similar to the parent AChBP. Inhibition of [3H]-epibatidine binding to the AChBPs was not affected by exposure to NTX or MeNTX for up to 24 hr prior to addition of the radioligand. Thus, the disulfide bond of NTX is not required to react with the vicinal disulfide in the AChBP C loop for inhibition of [3H]-epibatidine binding. However, a reversible disulfide interchange reaction of NTX with nAChRs might still occur, especially under reducing conditions. Labeled MeNTX, because it can be readily prepared with high specific radioactivity and possesses relatively high affinity for the nAChR-rich Torpedo nAChR, would be a useful probe to detect and identify any nereistoxin adducts.

Interactions of charatoxins and nereistoxin with the nicotinic acetylcholine receptors of insect cns andTorpedo electric organ

1986 ◽  
Vol 3 (5) ◽  
pp. 431-445 ◽  
Author(s):  
Shebl M. Sherby ◽  
Amira T. Eldefrawi ◽  
Jonathan A. David ◽  
David B. Sattelle ◽  
Mohyee E. Eldefrawi
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Electric Organ ◽  
Nicotinic Acetylcholine ◽  
Insect Cns
Sign in / Sign up

Export Citation Format

Share Document