Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release
Abstract
:1. Introduction
2. Materials and Methods
2.1. Reagents
2.2. U937 Cells
2.3. Human Peripheral Blood Mononuclear Cells (PBMCs)
2.4. Human Plasma Samples of Patients Undergoing Major Surgery
2.5. Cell Viability and Cytokine Measurements
2.6. Human P2X7R Expressing HEK293 Cell Line
2.7. Whole-Cell Patch-Clamp Recordings
2.8. Measurements of Intracellular Ca2+
2.9. Statistical Analyses and Data Processing
3. Results
3.1. Amyloid Beta Peptide (Aβ1-42) Attenuates the Inhibitory Effect of Acetylcholine (ACh) and Nicotine (Nic) on BzATP-Induced Relase of IL-1β by Human Monocytic U937 Cells
3.2. Aβ1-42 Attenuates the Inhibitory Effect of Non-Canonical Nicotinic Agonists on BzATP-Induced IL-1β Release by Human Monocytic U937 Cells
3.3. Aβ1-42 Attenuates the Inhibitory Effect of PC on BzATP-Induced IL-1β Release by Human PBMCs
3.4. Aβ1-42 Has No Impact on the Ion Channel Activity of the Human P2X7R
3.5. Aβ1-42 and IL-1β Concentrations in Human Plasma of Patients Undergoing Major Surgery
4. Discussion
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Acknowledgments
Conflicts of Interest
References
- Dinarello, C.A.; Simon, A.; van der Meer, J.W.M. Treating inflammation by blocking interleukin-1 in a broad spectrum of diseases. Nat. Rev. Drug Discov. 2012, 11, 633–652. [Google Scholar] [CrossRef] [Green Version]
- Broz, P.; Dixit, V.M. Inflammasomes: Mechanism of assembly, regulation and signalling. Nat. Rev. Immunol. 2016, 16, 407–420. [Google Scholar] [CrossRef]
- Bortolotti, P.; Faure, E.; Kipnis, E. Inflammasomes in tissue damages and immune disorders after trauma. Front. Immunol. 2018, 9, 1900. [Google Scholar] [CrossRef] [Green Version]
- Dinarello, C.A. Overview of the IL-1 family in innate inflammation and acquired immunity. Immunol. Rev. 2018, 281, 8–27. [Google Scholar] [CrossRef]
- Grau, V.; Richter, K.; Hone, A.J.; McIntosh, J.M. Conopeptides V11L.; V16DArIB and RgIA4: Powerful tools for the identification of novel nicotinic acetylcholine receptors in monocytes. Front. Pharmacol. 2018, 9, 1499. [Google Scholar] [CrossRef]
- Hecker, A.; Küllmar, M.; Wilker, S.; Richter, K.; Zakrzewicz, A.; Atanasova, S.; Mathes, V.; Timm, T.; Lerner, S.; Klein, J.; et al. Phosphocholine-modified macromolecules and canonical nicotinic agonists inhibit ATP-induced IL-1β release. J. Immunol. 2015, 195, 2325–2334. [Google Scholar] [CrossRef] [PubMed]
- Richter, K.; Mathes, V.; Fronius, M.; Althaus, M.; Hecker, A.; Krasteva-Christ, G.; Padberg, W.; Hone, A.J.; McIntosh, J.M.; Zakrzewicz, A.; et al. Phosphocholine—An agonist of metabotropic but not of ionotropic functions of α9-containing nicotinic acetylcholine receptors. Sci. Rep. 2016, 6, 28660. [Google Scholar] [CrossRef] [PubMed]
- Zakrzewicz, A.; Richter, K.; Agné, A.; Wilker, S.; Siebers, K.; Fink, B.; Krasteva-Christ, G.; Althaus, M.; Padberg, W.; Hone, A.J.; et al. Canonical and novel non-canonical cholinergic agonists inhibit ATP-induced release of monocytic interleukin-1β via different combinations of nicotinic acetylcholine receptor subunits α7, α9 and α10. Front. Cell. Neurosci. 2017, 11, 491. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Pepys, M.B.; Hirschfield, G.M.; Tennent, G.A.; Gallimore, J.R.; Kahan, M.C.; Bellotti, V.; Hawkins, P.N.; Myers, R.M.; Smith, M.D.; Polara, A.; et al. Targeting C-reactive protein for the treatment of cardiovascular disease. Nature 2006, 440, 1217–1221. [Google Scholar] [CrossRef] [Green Version]
- Mantovani, A.; Garlanda, C.; Doni, A.; Bottazzi, B. Pentraxins in innate immunity: From C-reactive protein to the long pentraxin PTX3. J. Clin. Immunol. 2008, 28, 1–13. [Google Scholar] [CrossRef]
- Richter, K.; Sagawe, S.; Hecker, A.; Küllmar, M.; Askevold, I.; Damm, J.; Heldmann, S.; Pöhlmann, M.; Ruhrmann, S.; Sander, M.; et al. C-reactive protein stimulates nicotinic acetylcholine receptors to control ATP-mediated monocytic inflammasome activation. Front. Immunol. 2018, 9, 1604. [Google Scholar] [CrossRef] [PubMed]
- Backhaus, S.; Zakrzewicz, A.; Richter, K.; Damm, J.; Wilker, S.; Fuchs-Moll, G.; Küllmar, M.; Hecker, A.; Manzini, I.; Ruppert, C.; et al. Surfactant inhibits ATP-induced release of interleukin-1β via nicotinic acetylcholine receptors. J. Lipid Res. 2017, 58, 1055–1066. [Google Scholar] [CrossRef] [Green Version]
- Nagele, R.G.; D’Andrea, M.R.; Anderson, W.J.; Wang, H.-Y. Intracellular accumulation of β-amyloid1–42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer’s disease. Neuroscience 2002, 110, 199–211. [Google Scholar] [CrossRef]
- Lee, D.H.S.; Wang, H.-Y. Differential physiologic responses of alpha7 nicotinic acetylcholine receptors to beta-amyloid1-40 and beta-amyloid1-42. J. Neurobiol. 2003, 55, 25–30. [Google Scholar] [CrossRef] [PubMed]
- Parri, R.H.; Dineley, T.K. Nicotinic acetylcholine receptor interaction with beta-amyloid: Molecular, cellular, and physiological consequences. Curr. Alzheimer Res. 2010, 7, 27–39. [Google Scholar] [CrossRef]
- Sadigh-Eteghad, S.; Talebi, M.; Farhoudi, M.; Golzari, S.E.J.; Sabermarouf, B.; Mahmoudi, J. Beta-amyloid exhibits antagonistic effects on alpha 7 nicotinic acetylcholine receptors in orchestrated manner. J. Med. Hypotheses Ideas 2014, 8, 49–52. [Google Scholar] [CrossRef] [Green Version]
- Barykin, E.P.; Garifulina, A.I.; Kruykova, E.V.; Spirova, E.N.; Anashkina, A.A.; Adzhubei, A.A.; Shelukhina, I.V.; Kasheverov, I.E.; Mitkevich, V.A.; Kozin, S.A.; et al. Isomerization of Asp7 in beta-amyloid enhances inhibition of the α7 nicotinic receptor and promotes neurotoxicity. Cells 2019, 8, 771. [Google Scholar] [CrossRef] [Green Version]
- Lasala, M.; Fabiani, C.; Corradi, J.; Antollini, S.; Bouzat, C. Molecular modulation of human α7 nicotinic receptor by amyloid-β peptides. Front. Cell. Neurosci. 2019, 13, 37. [Google Scholar] [CrossRef]
- Li, M.D. (Ed.) Nicotinic Acetylcholine Receptor Technologies; Springer: New York, NY, USA, 2016; ISBN 978-1-4939-3768-4. [Google Scholar]
- Puig, K.L.; Combs, C.K. Expression and function of APP and its metabolites outside the central nervous system. Exp. Gerontol. 2013, 48, 608–611. [Google Scholar] [CrossRef] [Green Version]
- Thinakaran, G.; Koo, E.H. Amyloid precursor protein trafficking, processing, and function. J. Biol. Chem. 2008, 283, 29615–29619. [Google Scholar] [CrossRef] [Green Version]
- Mattson, M.P. Pathways towards and away from Alzheimer’s disease. Nature 2004, 430, 631–639. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sinha, S.; Lieberburg, I. Cellular mechanisms of beta-amyloid production and secretion. Proc. Natl. Acad. Sci. USA 1999, 96, 11049–11053. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Selkoe, D.J. Normal and abnormal biology of the beta-amyloid precursor protein. Annu. Rev. Neurosci. 1994, 17, 489–517. [Google Scholar] [CrossRef] [PubMed]
- Solfrizzi, V.; D’Introno, A.; Colacicco, A.M.; Capurso, C.; Todarello, O.; Pellicani, V.; Capurso, S.A.; Pietrarossa, G.; Santamato, V.; Capurso, A.; et al. Circulating biomarkers of cognitive decline and dementia. Clin. Chim. Acta 2006, 364, 91–112. [Google Scholar] [CrossRef]
- Karran, E.; Mercken, M.; de Strooper, B. The amyloid cascade hypothesis for Alzheimer’s disease: An appraisal for the development of therapeutics. Nat. Rev. Drug Discov. 2011, 10, 698–712. [Google Scholar] [CrossRef]
- Kametani, F.; Hasegawa, M. Reconsideration of Amyloid hypothesis and tau hypothesis in Alzheimer’s disease. Front. Neurosci. 2018, 12, 25. [Google Scholar] [CrossRef] [Green Version]
- Godoy, P.A.; Ramírez-Molina, O.; Fuentealba, J. Exploring the role of P2X receptors in Alzheimer’s disease. Front. Pharmacol. 2019, 10, 1330. [Google Scholar] [CrossRef] [Green Version]
- Dong, Y.; Li, X.; Cheng, J.; Hou, L. Drug development for Alzheimer’s disease: Microglia induced neuroinflammation as a target? Int. J. Mol. Sci. 2019, 20, 558. [Google Scholar] [CrossRef] [Green Version]
- Heneka, M.T.; Carson, M.J.; Khoury, J.E.; Landreth, G.E.; Brosseron, F.; Feinstein, D.L.; Jacobs, A.H.; Wyss-Coray, T.; Vitorica, J.; Ransohoff, R.M.; et al. Neuroinflammation in Alzheimer’s disease. Lancet Neurol. 2015, 14, 388–405. [Google Scholar] [CrossRef] [Green Version]
- Han, S.-H.; Park, J.-C.; Mook-Jung, I. Amyloid β-interacting partners in Alzheimer’s disease: From accomplices to possible therapeutic targets. Prog. Neurobiol. 2016, 137, 17–38. [Google Scholar] [CrossRef]
- Müller, U.C.; Deller, T.; Korte, M. Not just amyloid: Physiological functions of the amyloid precursor protein family. Nat. Rev. Neurosci. 2017, 18, 281–298. [Google Scholar] [CrossRef] [PubMed]
- El Khoury, J.; Hickman, S.E.; Thomas, C.A.; Cao, L.; Silverstein, S.C.; Loike, J.D. Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils. Nature 1996, 382, 716–719. [Google Scholar] [CrossRef] [PubMed]
- Du Yan, S.; Zhu, H.; Fu, J.; Yan, S.F.; Roher, A.; Tourtellotte, W.W.; Rajavashisth, T.; Chen, X.; Godman, G.C.; Stern, D.; et al. Amyloid-beta peptide-receptor for advanced glycation endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: A proinflammatory pathway in Alzheimer disease. Proc. Natl. Acad. Sci. USA 1997, 94, 5296–5301. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Herzog, V.; Kirfel, G.; Siemes, C.; Schmitz, A. Biological roles of APP in the epidermis. Eur. J. Cell Biol. 2004, 83, 613–624. [Google Scholar] [CrossRef]
- Puig, K.L.; Swigost, A.J.; Zhou, X.; Sens, M.A.; Combs, C.K. Amyloid precursor protein expression modulates intestine immune phenotype. J. Neuroimmune Pharmacol. 2012, 7, 215–230. [Google Scholar] [CrossRef] [Green Version]
- François, A.; Julian, A.; Ragot, S.; Dugast, E.; Blanchard, L.; Brishoual, S.; Terro, F.; Chassaing, D.; Page, G.; Paccalin, M. Inflammatory stress on autophagy in peripheral blood mononuclear cells from patients with Alzheimer’s disease during 24 months of follow-up. PLoS ONE 2015, 10, e0138326. [Google Scholar] [CrossRef] [Green Version]
- Gold, M.; El Khoury, J. β-amyloid, microglia, and the inflammasome in Alzheimer’s disease. Semin. Immunopathol. 2015, 37, 607–611. [Google Scholar] [CrossRef] [Green Version]
- Rosenberg, P.B. Clinical aspects of inflammation in Alzheimer’s disease. Int. Rev. Psychiatry 2005, 17, 503–514. [Google Scholar] [CrossRef]
- Reale, M.; Kamal, M.A.; Velluto, L.; Gambi, D.; Di Nicola, M.; Greig, N.H. Relationship between inflammatory mediators, Aβ levels and ApoE genotype in Alzheimer disease. Curr. Alzheimer Res. 2012, 9, 447–457. [Google Scholar] [CrossRef]
- Fiala, M.; Zhang, L.; Gan, X.; Sherry, B.; Taub, D.; Graves, M.C.; Hama, S.; Way, D.; Weinand, M.; Witte, M.; et al. Amyloid-beta induces chemokine secretion and monocyte migration across a human blood—Brain barrier model. Mol. Med. 1998, 4, 480–489. [Google Scholar] [CrossRef] [Green Version]
- Kaplin, A.; Carroll, K.A.L.; Cheng, J.; Allie, R.; Lyketsos, C.G.; Calabresi, P.; Rosenberg, P.B. IL-6 release by LPS-stimulated peripheral blood mononuclear cells as a potential biomarker in Alzheimer’s disease. Int. Psychogeriatr. 2009, 21, 413–414. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ramarao, M.K.; Cohen, J.B. Mechanism of nicotinic acetylcholine receptor cluster formation by rapsyn. Proc. Natl. Acad. Sci. USA 1998, 95, 4007–4012. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Innocent, N.; Livingstone, P.D.; Hone, A.; Kimura, A.; Young, T.; Whiteaker, P.; McIntosh, J.M.; Wonnacott, S. Alpha-conotoxin Arenatus IBV11L, V16D corrected is a potent and selective antagonist at rat and human native alpha7 nicotinic acetylcholine receptors. J. Pharmacol. Exp. Ther. 2008, 327, 529–537. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Romero, H.K.; Christensen, S.B.; Di Cesare Mannelli, L.; Gajewiak, J.; Ramachandra, R.; Elmslie, K.S.; Vetter, D.E.; Ghelardini, C.; Iadonato, S.P.; Mercado, J.L.; et al. Inhibition of α9α10 nicotinic acetylcholine receptors prevents chemotherapy-induced neuropathic pain. Proc. Natl. Acad. Sci. USA 2017, 114, E1825–E1832. [Google Scholar] [CrossRef] [Green Version]
- Klapperstück, M.; Büttner, C.; Schmalzing, G.; Markwardt, F. Functional evidence of distinct ATP activation sites at the human P2X(7) receptor. J. Physiol. 2001, 534, 25–35. [Google Scholar] [CrossRef]
- Kopp, R.; Krautloher, A.; Ramírez-Fernández, A.; Nicke, A. P2X7 Interactions and signaling—Making head or tail of it. Front. Mol. Neurosci. 2019, 12, 183. [Google Scholar] [CrossRef]
- Le Novère, N.; Changeux, J.P. Molecular evolution of the nicotinic acetylcholine receptor: An example of multigene family in excitable cells. J. Mol. Evol. 1995, 40, 155–172. [Google Scholar] [CrossRef]
- Franchini, L.F.; Elgoyhen, A.B. Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility. Mol. Phylogenet. Evol. 2006, 41, 622–635. [Google Scholar] [CrossRef]
- d’Uscio, L.V.; He, T.; Katusic, Z.S. Expression and processing of amyloid precursor protein in vascular endothelium. Physiology 2017, 32, 20–32. [Google Scholar] [CrossRef]
- Fabiani, C.; Antollini, S.S. Alzheimer’s disease as a membrane disorder: Spatial cross-talk among beta-amyloid peptides, nicotinic acetylcholine receptors and lipid rafts. Front. Cell. Neurosci. 2019, 13, 309. [Google Scholar] [CrossRef] [Green Version]
- Lombardo, S.; Maskos, U. Role of the nicotinic acetylcholine receptor in Alzheimer’s disease pathology and treatment. Neuropharmacology 2015, 96, 255–262. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Roher, A.E.; Esh, C.L.; Kokjohn, T.A.; Castaño, E.M.; van Vickle, G.D.; Kalback, W.M.; Patton, R.L.; Luehrs, D.C.; Daugs, I.D.; Kuo, Y.-M.; et al. Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer’s disease. Alzheimer’s Dement. 2009, 5, 18–29. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, Q.X.; Fuller, S.J.; Beyreuther, K.; Masters, C.L. The amyloid precursor protein of Alzheimer disease in human brain and blood. J. Leukoc. Biol. 1999, 66, 567–574. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Marksteiner, J.; Humpel, C. Platelet-derived secreted amyloid-precursor protein-β as a marker for diagnosing Alzheimer’s disease. Curr. Neurovasc. Res. 2013, 10, 297–303. [Google Scholar] [CrossRef] [PubMed]
- Mestas, J.; Ley, K. Monocyte-endothelial cell interactions in the development of atherosclerosis. Trends Cardiovasc. Med. 2008, 18, 228–232. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lam, F.W.; Vijayan, K.V.; Rumbaut, R.E. Platelets and their interactions with other immune cells. Compr. Physiol. 2015, 5, 1265–1280. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sanz, J.M.; Chiozzi, P.; Ferrari, D.; Colaianna, M.; Idzko, M.; Falzoni, S.; Fellin, R.; Trabace, L.; Di Virgilio, F. Activation of microglia by amyloid β requires P2X7 receptor expression. J. Immunol. 2009, 182, 4378–4385. [Google Scholar] [CrossRef] [Green Version]
- Wang, H.Y.; Lee, D.H.; D’Andrea, M.R.; Peterson, P.A.; Shank, R.P.; Reitz, A.B. beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer’s disease pathology. J. Biol. Chem. 2000, 275, 5626–5632. [Google Scholar] [CrossRef] [Green Version]
- Wang, H.Y.; Lee, D.H.; Davis, C.B.; Shank, R.P. Amyloid peptide Abeta(1-42) binds selectively and with picomolar affinity to alpha7 nicotinic acetylcholine receptors. J. Neurochem. 2000, 75, 1155–1161. [Google Scholar] [CrossRef]
- Wu, J.; Kuo, Y.-P.; George, A.A.; Xu, L.; Hu, J.; Lukas, R.J. beta-Amyloid directly inhibits human alpha4beta2-nicotinic acetylcholine receptors heterologously expressed in human SH-EP1 cells. J. Biol. Chem. 2004, 279, 37842–37851. [Google Scholar] [CrossRef] [Green Version]
- Lamb, P.W.; Melton, M.A.; Yakel, J.L. Inhibition of neuronal nicotinic acetylcholine receptor channels expressed in Xenopus oocytes by β-amyloid1-42 peptide. JMN 2005, 27, 13–22. [Google Scholar] [CrossRef]
- Karlin, A. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 2002, 3, 102–114. [Google Scholar] [CrossRef] [PubMed]
- Papke, R.L. Merging old and new perspectives on nicotinic acetylcholine receptors. Biochem. Pharmacol. 2014, 89, 1–11. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gotti, C.; Zoli, M.; Clementi, F. Brain nicotinic acetylcholine receptors: Native subtypes and their relevance. Trends Pharmacol. Sci. 2006, 27, 482–491. [Google Scholar] [CrossRef] [PubMed]
- Pettit, D.L.; Shao, Z.; Yakel, J.L. beta-Amyloid(1-42) peptide directly modulates nicotinic receptors in the rat hippocampal slice. J. Neurosci. 2001, 21, RC120. [Google Scholar] [CrossRef] [Green Version]
- Dougherty, J.J.; Wu, J.; Nichols, R.A. β-Amyloid regulation of presynaptic nicotinic receptors in rat hippocampus and neocortex. J. Neurosci. 2003, 23, 6740–6747. [Google Scholar] [CrossRef]
- Liu, Q.; Kawai, H.; Berg, D.K. beta-Amyloid peptide blocks the response of alpha 7-containing nicotinic receptors on hippocampal neurons. Proc. Natl. Acad. Sci. USA 2001, 98, 4734–4739. [Google Scholar] [CrossRef] [Green Version]
- Dineley, K.T.; Bell, K.A.; Bui, D.; Sweatt, J.D. Beta-Amyloid peptide activates alpha 7 nicotinic acetylcholine receptors expressed in Xenopus oocytes. J. Biol. Chem. 2002, 277, 25056–25061. [Google Scholar] [CrossRef] [Green Version]
- Sondag, C.M.; Combs, C.K. Amyloid precursor protein cross-linking stimulates beta amyloid production and pro-inflammatory cytokine release in monocytic lineage cells. J. Neurochem. 2006, 97, 449–461. [Google Scholar] [CrossRef]
- Wang, H.-Y.; Stucky, A.; Liu, J.; Shen, C.; Trocme-Thibierge, C.; Morain, P. Dissociating beta-amyloid from alpha 7 nicotinic acetylcholine receptor by a novel therapeutic agent, S 24795, normalizes alpha 7 nicotinic acetylcholine and NMDA receptor function in Alzheimer’s disease brain. J. Neurosci. 2009, 29, 10961–10973. [Google Scholar] [CrossRef]
- Peng, H.; Ferris, R.L.; Matthews, T.; Hiel, H.; Lopez-Albaitero, A.; Lustig, L.R. Characterization of the human nicotinic acetylcholine receptor subunit alpha (alpha) 9 (CHRNA9) and alpha (alpha) 10 (CHRNA10) in lymphocytes. Life Sci. 2004, 76, 263–280. [Google Scholar] [CrossRef] [PubMed]
- Razani-Boroujerdi, S.; Boyd, R.T.; Dávila-García, M.I.; Nandi, J.S.; Mishra, N.C.; Singh, S.P.; Pena-Philippides, J.C.; Langley, R.; Sopori, M.L. T cells express alpha7-nicotinic acetylcholine receptor subunits that require a functional TCR and leukocyte-specific protein tyrosine kinase for nicotine-induced Ca2+ response. J. Immunol. 2007, 179, 2889–2898. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hecker, A.; Mikulski, Z.; Lips, K.S.; Pfeil, U.; Zakrzewicz, A.; Wilker, S.; Hartmann, P.; Padberg, W.; Wessler, I.; Kummer, W.; et al. Pivotal advance: Up-regulation of acetylcholine synthesis and paracrine cholinergic signaling in intravascular transplant leukocytes during rejection of rat renal allografts. J. Leukoc. Biol. 2009, 86, 13–22. [Google Scholar] [CrossRef] [PubMed]
- Mikulski, Z.; Hartmann, P.; Jositsch, G.; Zasłona, Z.; Lips, K.S.; Pfeil, U.; Kurzen, H.; Lohmeyer, J.; Clauss, W.G.; Grau, V.; et al. Nicotinic receptors on rat alveolar macrophages dampen ATP-induced increase in cytosolic calcium concentration. Respir. Res. 2010, 11, 133. [Google Scholar] [CrossRef] [Green Version]
- Mishra, N.C.; Rir-sima-ah, J.; Boyd, R.T.; Singh, S.P.; Gundavarapu, S.; Langley, R.J.; Razani-Boroujerdi, S.; Sopori, M.L. Nicotine inhibits Fc epsilon RI-induced cysteinyl leukotrienes and cytokine production without affecting mast cell degranulation through alpha 7/alpha 9/alpha 10-nicotinic receptors. J. Immunol. 2010, 185, 588–596. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Valbuena, S.; Lerma, J. Non-canonical signaling, the hidden life of ligand-gated ion channels. Neuron 2016, 92, 316–329. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Godin, J.-R.; Roy, P.; Quadri, M.; Bagdas, D.; Toma, W.; Narendrula-Kotha, R.; Kishta, O.A.; Damaj, M.I.; Horenstein, N.A.; Papke, R.L.; et al. A silent agonist of α7 nicotinic acetylcholine receptors modulates inflammation ex vivo and attenuates EAE. Brain Behav. Immun. 2019. [Google Scholar] [CrossRef] [PubMed]
- Báez-Pagán, C.A.; Delgado-Vélez, M.; Lasalde-Dominicci, J.A. Activation of the macrophage α7 nicotinic acetylcholine receptor and control of inflammation. J. Neuroimmune Pharmacol. 2015, 10, 468–476. [Google Scholar] [CrossRef] [Green Version]
- Siniavin, A.E.; Streltsova, M.A.; Kudryavtsev, D.S.; Shelukhina, I.V.; Utkin, Y.N.; Tsetlin, V.I. Activation of α7 nicotinic acetylcholine receptor upregulates HLA-DR and macrophage receptors: Potential role in adaptive immunity and in preventing immunosuppression. Biomolecules 2020, 10, 507. [Google Scholar] [CrossRef] [Green Version]
- Rocha, N.P.; Teixeira, A.L.; Coelho, F.M.; Caramelli, P.; Guimarães, H.C.; Barbosa, I.G.; da Silva, T.A.; Mukhamedyarov, M.A.; Zefirov, A.L.; Rizvanov, A.A.; et al. Peripheral blood mono-nuclear cells derived from Alzheimer’s disease patients show elevated baseline levels of secreted cytokines but resist stimulation with β-amyloid peptide. Mol. Cell. Neurosci. 2012, 49, 77–84. [Google Scholar] [CrossRef]
- Reale, M.; Di Nicola, M.; Velluto, L.; D’Angelo, C.; Costantini, E.; Lahiri, D.K.; Kamal, M.A.; Yu, Q.-S.; Greig, N.H. Selective acetyl- and butyrylcholinesterase inhibitors reduce amyloid-β ex vivo activation of peripheral chemo-cytokines from Alzheimer’s disease subjects: Exploring the cholinergic anti-inflammatory pathway. Curr. Alzheimer Res. 2014, 11, 608–622. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Udan, M.L.D.; Ajit, D.; Crouse, N.R.; Nichols, M.R. Toll-like receptors 2 and 4 mediate Abeta(1-42) activation of the innate immune response in a human monocytic cell line. J. Neurochem. 2008, 104, 524–533. [Google Scholar] [CrossRef] [PubMed]
- Ebrahimi, T.; Rust, M.; Kaiser, S.N.; Slowik, A.; Beyer, C.; Koczulla, A.R.; Schulz, J.B.; Habib, P.; Bach, J.P. α1-antitrypsin mitigates NLRP3-inflammasome activation in amyloid β1-42-stimulated murine astrocytes. J. Neuroinflamm. 2018, 15, 282. [Google Scholar] [CrossRef] [PubMed]
- Halle, A.; Hornung, V.; Petzold, G.C.; Stewart, C.R.; Monks, B.G.; Reinheckel, T.; Fitzgerald, K.A.; Latz, E.; Moore, K.J.; Golenbock, D.T. The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat. Immunol. 2008, 9, 857–865. [Google Scholar] [CrossRef] [Green Version]
- El Khoury, J.B.; Moore, K.J.; Means, T.K.; Leung, J.; Terada, K.; Toft, M.; Freeman, M.W.; Luster, A.D. CD36 mediates the innate host response to beta-amyloid. J. Exp. Med. 2003, 197, 1657–1666. [Google Scholar] [CrossRef] [Green Version]
- Sheedy, F.J.; Grebe, A.; Rayner, K.J.; Kalantari, P.; Ramkhelawon, B.; Carpenter, S.B.; Becker, C.E.; Ediriweera, H.N.; Mullick, A.E.; Golenbock, D.T.; et al. CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation. Nat. Immunol. 2013, 14, 812–820. [Google Scholar] [CrossRef] [Green Version]
- Kudo, S.; Mizuno, K.; Hirai, Y.; Shimizu, T. Clearance and tissue distribution of recombinant human interleukin 1 beta in rats. Cancer Res. 1990, 50, 5751–5755. [Google Scholar]
- Lopez-Castejon, G.; Brough, D. Understanding the mechanism of IL-1β secretion. Cytokine Growth Factor Rev. 2011, 22, 189–195. [Google Scholar] [CrossRef]
- Schmidt, J.; Barthel, K.; Wrede, A.; Salajegheh, M.; Bähr, M.; Dalakas, M.C. Interrelation of inflammation and APP in sIBM: IL-1 beta induces accumulation of beta-amyloid in skeletal muscle. Brain 2008, 131, 1228–1240. [Google Scholar] [CrossRef] [Green Version]
- Alasmari, F.; Alshammari, M.A.; Alasmari, A.F.; Alanazi, W.A.; Alhazzani, K. Neuroinflammatory cytokines induce amyloid beta neurotoxicity through modulating amyloid precursor protein levels/metabolism. BioMed Res. Int. 2018, 2018, 3087475. [Google Scholar] [CrossRef]
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Richter, K.; Ogiemwonyi-Schaefer, R.; Wilker, S.; Chaveiro, A.I.; Agné, A.; Hecker, M.; Reichert, M.; Amati, A.-L.; Schlüter, K.-D.; Manzini, I.; et al. Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release. J. Clin. Med. 2020, 9, 2887. https://doi.org/10.3390/jcm9092887
Richter K, Ogiemwonyi-Schaefer R, Wilker S, Chaveiro AI, Agné A, Hecker M, Reichert M, Amati A-L, Schlüter K-D, Manzini I, et al. Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release. Journal of Clinical Medicine. 2020; 9(9):2887. https://doi.org/10.3390/jcm9092887
Chicago/Turabian StyleRichter, Katrin, Raymond Ogiemwonyi-Schaefer, Sigrid Wilker, Anna I. Chaveiro, Alisa Agné, Matthias Hecker, Martin Reichert, Anca-Laura Amati, Klaus-Dieter Schlüter, Ivan Manzini, and et al. 2020. "Amyloid Beta Peptide (Aβ1-42) Reverses the Cholinergic Control of Monocytic IL-1β Release" Journal of Clinical Medicine 9, no. 9: 2887. https://doi.org/10.3390/jcm9092887