Spike protein (inc vax) induced immunodeficiency & carcinogenesis megathread #13: interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors
Spike protein (inc vax) induced immunodeficiency & carcinogenesis megathread #13: interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors
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Any extracts used in the following article are for non commercial research and educational purposes only and may be subject to copyright from their respective owners.
Nicotinic acetylcholine receptors and cancer (2016)
…Nicotine can cause Ca2+ influx into lung cancer cells by binding to α7nAChR and triggering membrane depolarization, which activates voltage-gated Ca2+ channels and subsequently activates the MAPK pathway, which may result in increased expression of the B-cell lymphoma-2 protein and downregulation of apoptosis (23). Subsequently, the MAPK pathway activates the transcription factor nuclear factor-κB (NF-κB) and promotes cancer cell proliferation.
4. Conclusion
Taken together, the obtained results provide new insight into the molecular mechanisms of nAChR-mediated oncogenic effects on types of human cancer. It is clear that nAChRs has significant roles in the pathogenesis of cancers. Further analyses of nAChRs may contribute to clinical applications in the future. More in vivo studies are required to confirm their oncogenic effects.
You know what else binds with nAChRs? Take a wild guess:
Simulations support the interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors (preprint, 2020)
Abstract
Changeux et al. recently suggested that the SARS-CoV-2 spike (S) protein may interact with nicotinic acetylcholine receptors (nAChRs). Such interactions may be involved in pathology and infectivity. Here, we use molecular simulations of validated atomically detailed structures of nAChRs, and of the S protein, to investigate this ‘nicotinic hypothesis’. We examine the binding of the Y674-R685 loop of the S protein to three nAChRs, namely the human α4β2 and α7 subtypes and the muscle-like αβγδ receptor from Tetronarce californica. Our results indicate that Y674-R685 has affinity for nAChRs and the region responsible for binding contains the PRRA motif, a four-residue insertion not found in other SARS-like coronaviruses.
Spike protein (inc vax) induced immunodeficiency & carcinogenesis megathread #13: interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors
Spike protein (inc vax) induced immunodeficiency & carcinogenesis megathread #13: interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors
Spike protein (inc vax) induced immunodeficiency & carcinogenesis megathread #13: interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors
Any extracts used in the following article are for non commercial research and educational purposes only and may be subject to copyright from their respective owners.
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Nicotinic acetylcholine receptors and cancer (2016)
…Nicotine can cause Ca2+ influx into lung cancer cells by binding to α7nAChR and triggering membrane depolarization, which activates voltage-gated Ca2+ channels and subsequently activates the MAPK pathway, which may result in increased expression of the B-cell lymphoma-2 protein and downregulation of apoptosis (23). Subsequently, the MAPK pathway activates the transcription factor nuclear factor-κB (NF-κB) and promotes cancer cell proliferation.
4. Conclusion
Taken together, the obtained results provide new insight into the molecular mechanisms of nAChR-mediated oncogenic effects on types of human cancer. It is clear that nAChRs has significant roles in the pathogenesis of cancers. Further analyses of nAChRs may contribute to clinical applications in the future. More in vivo studies are required to confirm their oncogenic effects.
Full paper:
https://www.ncbi.nlm.nih.gov/labs/pmc/articles/PMC4840641/
You know what else binds with nAChRs? Take a wild guess:
Simulations support the interaction of the SARS-CoV-2 spike protein with nicotinic acetylcholine receptors (preprint, 2020)
Abstract
Changeux et al. recently suggested that the SARS-CoV-2 spike (S) protein may interact with nicotinic acetylcholine receptors (nAChRs). Such interactions may be involved in pathology and infectivity. Here, we use molecular simulations of validated atomically detailed structures of nAChRs, and of the S protein, to investigate this ‘nicotinic hypothesis’. We examine the binding of the Y674-R685 loop of the S protein to three nAChRs, namely the human α4β2 and α7 subtypes and the muscle-like αβγδ receptor from Tetronarce californica. Our results indicate that Y674-R685 has affinity for nAChRs and the region responsible for binding contains the PRRA motif, a four-residue insertion not found in other SARS-like coronaviruses.
https://www.ncbi.nlm.nih.gov/labs/pmc/articles/PMC7386492/
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