Studies on the role of alpha 7 nicotinic acetylcholine receptors in K562 cell proliferation and signaling

2021 ◽  
Author(s):  
Gözde Önder Narin ◽  
Banu Aydın ◽  
Hülya Cabadak
Keyword(s):  
Cell Proliferation ◽  
Nicotinic Acetylcholine Receptors ◽  
K562 Cell ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
Alpha 7

Role of nicotinic acetylcholine receptors in cell proliferation and tumour invasion in broncho-pulmonary carcinomas

Lung Cancer ◽  
2015 ◽  
Vol 87 (3) ◽  
pp. 258-264 ◽  
Author(s):  
Kahina Medjber ◽  
Mohamed Lamine Freidja ◽  
Simon Grelet ◽  
Marianne Lorenzato ◽  
Kamel Maouche ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Tumour Invasion ◽  
Nicotinic Acetylcholine

scholarly journals Novel Three-Finger Neurotoxins from Naja melanoleuca Cobra Venom Interact with GABAA and Nicotinic Acetylcholine Receptors

Toxins ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 164
Author(s):  
Lina Son ◽  
Elena Kryukova ◽  
Rustam Ziganshin ◽  
Tatyana Andreeva ◽  
Denis Kudryavtsev ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Gabaa Receptors ◽  
Binding Sites ◽  
Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
High Affinity ◽  
Central Loop ◽  
Acetylcholine Binding Proteins ◽  
Α7 Nachrs

Cobra venoms contain three-finger toxins (TFT) including α-neurotoxins efficiently binding nicotinic acetylcholine receptors (nAChRs). As shown recently, several TFTs block GABAA receptors (GABAARs) with different efficacy, an important role of the TFTs central loop in binding to these receptors being demonstrated. We supposed that the positive charge (Arg36) in this loop of α-cobratoxin may explain its high affinity to GABAAR and here studied α-neurotoxins from African cobra N. melanoleuca venom for their ability to interact with GABAARs and nAChRs. Three α-neurotoxins, close homologues of the known N. melanoleuca long neurotoxins 1 and 2, were isolated and sequenced. Their analysis on Torpedocalifornica and α7 nAChRs, as well as on acetylcholine binding proteins and on several subtypes of GABAARs, showed that all toxins interacted with the GABAAR much weaker than with the nAChR: one neurotoxin was almost as active as α-cobratoxin, while others manifested lower activity. The earlier hypothesis about the essential role of Arg36 as the determinant of high affinity to GABAAR was not confirmed, but the results obtained suggest that the toxin loop III may contribute to the efficient interaction of some long-chain neurotoxins with GABAAR. One of isolated toxins manifested different affinity to two binding sites on Torpedo nAChR.

Pathologic role of neuronal nicotinic acetylcholine receptors in epileptic disorders: implication for pharmacological interventions

2015 ◽  
Vol 26 (2) ◽  
Author(s):  
Mehdi Ghasemi ◽  
Arash Hadipour-Niktarash
Keyword(s):  
Animal Models ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Neurological Diseases ◽  
Juvenile Myoclonic Epilepsy ◽  
Neuronal Nicotinic Acetylcholine Receptors ◽  
Pharmacological Interventions ◽  
Nicotinic Acetylcholine ◽  
Neuronal Nachr

AbstractAccumulating evidence suggests that neuronal nicotinic acetylcholine receptors (nAChRs) may play a key role in the pathophysiology of some neurological diseases such as epilepsy. Based on genetic studies in patients with epileptic disorders worldwide and animal models of seizure, it has been demonstrated that nAChR activity is altered in some specific types of epilepsy, including autosomal dominant nocturnal frontal lobe epilepsy (ADNFLE) and juvenile myoclonic epilepsy (JME). Neuronal nAChR antagonists also have antiepileptic effects in pre-clinical studies. There is some evidence that conventional antiepileptic drugs may affect neuronal nAChR function. In this review, we re-examine the evidence for the involvement of nAChRs in the pathophysiology of some epileptic disorders, especially ADNFLE and JME, and provide an overview of nAChR antagonists that have been evaluated in animal models of seizure.

scholarly journals Role of the Cys Loop and Transmembrane Domain in the Allosteric Modulation of α4β2 Nicotinic Acetylcholine Receptors

2016 ◽  
Vol 292 (2) ◽  
pp. 551-562 ◽  
Author(s):  
Constanza Alcaino ◽  
Maria Musgaard ◽  
Teresa Minguez ◽  
Simone Mazzaferro ◽  
Manuel Faundez ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Transmembrane Domain ◽  
Allosteric Modulation ◽  
Nicotinic Acetylcholine
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