Nutraceutical Aid for Allergies – Strategies for Down-Regulating Mast Cell Degranulation

References

• Dahlin JS, Maurer M, Metcalfe DD, Pejler G, Sagi-Eisenberg R, Nilsson G. The ingenious mast cell: contemporary insights into mast cell behavior and function. Allergy Eur J Allergy Clin Immunol. 2021. doi:10.1111/all.14881
   Web of Science ®Google Scholar
• Varricchi G, Marone G. Mast cells: fascinating but still elusive after 140 years from their discovery. Int J Mol Sci. 2020;21(464):464. doi:10.3390/ijms21020464
   Web of Science ®Google Scholar
• Giannetti A, Filice E, Caffarelli C, Ricci G, Pession A. Mast cell activation disorders. Med. 2021;57:124. doi:10.3390/medicina57020124
   Web of Science ®Google Scholar
• Theoharides TC, Valent P, Akin C. Mast cells, mastocytosis, and related disorders. N Engl J Med. 2015;373(2):163–172. doi:10.1056/NEJMRA1409760
   PubMed Web of Science ®Google Scholar
• Dvorak A. Piecemeal degranulation of basophils and mast cells is effected by vesicular transport of stored secretory granule contents. Chem Immunol Allergy. 2005;85:135–184. doi:10.1159/000086516
   PubMedGoogle Scholar
• Metcalfe D, Peavy R, Gilfillan A. Mechanisms of mast cell signaling in anaphylaxis. J Allergy Clin Immunol. 2009;124(4):639–646. doi:10.1016/J.JACI.2009.08.035
   Web of Science ®Google Scholar
• Blank U, Huang H, Kawakami T. The high affinity IgE receptor: a signaling update. Curr Opin Immunol. 2021;72:51–58. doi:10.1016/J.COI.2021.03.015
   Web of Science ®Google Scholar
• Inoue T, Suzuki Y, Yoshimaru T, Ra C. Reactive oxygen species produced up- or downstream of calcium influx regulate proinflammatory mediator release from mast cells: role of NADPH oxidase and mitochondria. Biochim Biophys Acta Mol Cell Res. 2008;1783(5):789–802. doi:10.1016/J.BBAMCR.2007.12.004
   Web of Science ®Google Scholar
• Costello PS, Turner M, Walters AE, et al. Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. Oncogene. 1996;13(12):2595–2605.
   PubMed Web of Science ®Google Scholar
• Shao Y, Zhang S, Zhang Y, Liu Z. Recent advance of spleen tyrosine kinase in diseases and drugs. Int Immunopharmacol. 2021;90:107168. doi:10.1016/J.INTIMP.2020.107168
   Web of Science ®Google Scholar
• Nakata K, Yoshimaru T, Suzuki Y, et al. Positive and negative regulation of high affinity ige receptor signaling by src homology region 2 domain-containing phosphatase 1. J Immunol. 2008;181(8):5414–5424. doi:10.4049/JIMMUNOL.181.8.5414
   Web of Science ®Google Scholar
• Gilfillan AM, Rivera J. The tyrosine kinase network regulating mast cell activation. Immunol Rev. 2009;228(1):149–169. doi:10.1111/J.1600-065X.2008.00742.X
   PubMed Web of Science ®Google Scholar
• Mahajan A, Barua D, Cutler P, et al. Optimal aggregation of FcεRI with a structurally defined trivalent ligand overrides negative regulation driven by phosphatases. ACS Chem Biol. 2014;9(7):1508–1519. doi:10.1021/CB500134T
   Web of Science ®Google Scholar
• Deng Y, Jin F, Li X, et al. Sauchinone suppresses FcεRI-mediated mast cell signaling and anaphylaxis through regulation of LKB1/AMPK axis and SHP-1-Syk signaling module. Int Immunopharmacol. 2019;74:105702. doi:10.1016/J.INTIMP.2019.105702
   PubMed Web of Science ®Google Scholar
• Cunnick JM, Dorsey JF, Mei L, Wu J. Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation. IUBMB Life. 1998;45(5):887–894. doi:10.1002/IUB.7510450506
   Google Scholar
• Weibrecht I, Böhmer SA, Dagnell M, Kappert K, Östman A, Böhmer FD. Oxidation sensitivity of the catalytic cysteine of the protein-tyrosine phosphatases SHP-1 and SHP-2. Free Radic Biol Med. 2007;43(1):100–110. doi:10.1016/J.FREERADBIOMED.2007.03.021
   Web of Science ®Google Scholar
• Chen C-Y, Willard D, Rudolph J. Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines. Biochemistry. 2009;48(6):1399–1409. doi:10.1021/BI801973Z
   Web of Science ®Google Scholar
• Heneberg P, Dráberová L, Bambousková M, Pompach P, Dráber P. Down-regulation of protein-tyrosine phosphatases activates an immune receptor in the absence of its translocation into lipid rafts. J Biol Chem. 2010;285(17):12787–12802. doi:10.1074/JBC.M109.052555
   Web of Science ®Google Scholar
• Tanner JJ, Parsons ZD, Cummings AH, Zhou H, Gates KS. Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid Redox Signal. 2011;15(1):77–97. doi:10.1089/ARS.2010.3611
   Web of Science ®Google Scholar
• Lo Conte M, Carroll KS. The redox biochemistry of protein sulfenylation and sulfinylation. J Biol Chem. 2013;288(37):26480–26488. doi:10.1074/JBC.R113.467738
   PubMed Web of Science ®Google Scholar
• Li ZY, Jiang WY, Cui ZJ. An essential role of NAD(P)H oxidase 2 in UVA-induced calcium oscillations in mast cells. Photochem Photobiol Sci. 2015;14(2):414–428. doi:10.1039/C4PP00304G
   Web of Science ®Google Scholar
• Min A, Lee YA, Kim KA, Shin MH. BLT1-mediated O-GlcNAcylation is required for NOX2-dependent migration, exocytotic degranulation and IL-8 release of human mast cell induced by Trichomonas vaginalis-secreted LTB4. Microbes Infect. 2018;20(6):376–384. doi:10.1016/J.MICINF.2018.05.005
   Web of Science ®Google Scholar
• Kuehn HS, Rådinger M, Brown JM, et al. Btk-dependent Rac activation and actin rearrangement following FcεRI aggregation promotes enhanced chemotactic responses of mast cells. J Cell Sci. 2010;123(15):2576–2585. doi:10.1242/JCS.071043
   Web of Science ®Google Scholar
• Rastogi R, Geng X, Li F, Ding Y. NOX activation by subunit interaction and underlying mechanisms in disease. Front Cell Neurosci. 2017;301. doi:10.3389/FNCEL.2016.00301
   Web of Science ®Google Scholar
• Takamiya R, Murakami M, Kajimura M, et al. Stabilization of mast cells by heme oxygenase-1: an anti-inflammatory role. Am J Physiol Hear Circ Physiol. 2002;283(3):H861–H870. doi:10.1152/AJPHEART.00740.2001
   Web of Science ®Google Scholar
• Yasui Y, Nakamura M, Onda T, et al. Heme oxygenase-1 inhibits cytokine production by activated mast cells. Biochem Biophys Res Commun. 2007;354(2):485–490. doi:10.1016/J.BBRC.2006.12.228
   Web of Science ®Google Scholar
• Matsushima M, Takagi K, Ogawa M, et al. Heme oxygenase-1 mediates the anti-allergic actions of quercetin in rodent mast cells. Inflamm Res. 2009;58(10):705–715. doi:10.1007/S00011-009-0039-1
   PubMed Web of Science ®Google Scholar
• Ma Y, Yang M, Wang C, Ding J, Li J. Inhibiting mast cell degranulation by HO-1 affects dendritic cell maturation in vitro. Inflamm Res. 2014;63(7):527–537. doi:10.1007/S00011-014-0722-8
   Web of Science ®Google Scholar
• Lanone S, Bloc S, Foresti R, et al. Bilirubin decreases NOS2 expression via inhibition of NAD(P)H oxidase: implications for protection against endotoxic shock in rats. FASEB J. 2005;19(13):1890–1892. doi:10.1096/FJ.04-2368FJE
   PubMed Web of Science ®Google Scholar
• Matsumoto H, Ishikawa K, Itabe H, Maruyama Y. Carbon monoxide and bilirubin from heme oxygenase-1 suppresses reactive oxygen species generation and plasminogen activator inhibitor-1 induction. Mol Cell Biochem. 2006;291(1):21–28. doi:10.1007/S11010-006-9190-Y
   Web of Science ®Google Scholar
• Jiang F, Roberts SJ, Datla S, Dusting GJ. NO modulates NADPH oxidase function via heme oxygenase-1 in human endothelial cells. Hypertension. 2006;48(5):950–957. doi:10.1161/01.HYP.0000242336.58387.1F
   PubMed Web of Science ®Google Scholar
• Datla SR, Dusting GJ, Mori TA, Taylor CJ, Croft KD, Jiang F. Induction of heme oxygenase-1 in vivo suppresses NADPH oxidase–derived oxidative stress. Hypertension. 2007;50(4):636–642. doi:10.1161/HYPERTENSIONAHA.107.092296
   PubMed Web of Science ®Google Scholar
• Hwang SL, Li X, Lu Y, et al. AMP-activated protein kinase negatively regulates FcεRI-mediated mast cell signaling and anaphylaxis in mice. J Allergy Clin Immunol. 2013;132(3):729–736.e12. doi:10.1016/J.JACI.2013.02.018
   PubMed Web of Science ®Google Scholar
• Hwang SL, Lu Y, Li X, et al. ERK1/2 antagonize AMPK-dependent regulation of FcεRI-mediated mast cell activation and anaphylaxis. J Allergy Clin Immunol. 2014;134(3):714–721.e7. doi:10.1016/J.JACI.2014.05.001
   Web of Science ®Google Scholar
• Li X, Park SJ, Jin F, et al. Tanshinone IIA suppresses FcεRI-mediated mast cell signaling and anaphylaxis by activation of the Sirt1/LKB1/AMPK pathway. Biochem Pharmacol. 2018;152:362–372. doi:10.1016/J.BCP.2018.04.015
   PubMed Web of Science ®Google Scholar
• Wang C, Li L, Jiang J, et al. Pterostilbene inhibits FcεRI signaling through activation of the LKB1/AMPK pathway in allergic response. J Agric Food Chem. 2020;68(11):3456–3465. doi:10.1021/ACS.JAFC.9B07126
   PubMed Web of Science ®Google Scholar
• Masini E, Mannaioni PF, Pistelli A, Salvemini D, Vane J. Impairment of the L-arginine-nitric oxide pathway in mast cells from spontaneously hypertensive rats. Biochem Biophys Res Commun. 1991;177(3):1178–1182. doi:10.1016/0006-291X(91)90664-S
   Web of Science ®Google Scholar
• Yip KH, Huang Y, Leung FP, Lau HYA. Cyclic guanosine monophosphate dependent pathway contributes to human mast cell inhibitory actions of the nitric oxide donor, diethylamine NONOate. Eur J Pharmacol. 2010;632(1–3):86–92. doi:10.1016/J.EJPHAR.2010.01.007
   Web of Science ®Google Scholar
• El-Awady MS, Eman S. Vardenafil ameliorates immunologic- and non-immunologic-induced allergic reactions. Can J Physiol Pharmacol. 2014;92(3):175–180. doi:10.1139/CJPP-2013-0316
   Web of Science ®Google Scholar
• Liu Y-H, Lu M, Xie Z-Z. Hydrogen sulfide prevents heart failure development via inhibition of renin release from mast cells in isoproterenol-treated rats. Antioxid Redox Signal. 2014;20(5):759–769. doi:10.1089/ARS.2012.4888
   PubMed Web of Science ®Google Scholar
• Roviezzo F, Bertolino A, Sorrentino R, et al. Hydrogen sulfide inhalation ameliorates allergen induced airway hyperreactivity by modulating mast cell activation. Pharmacol Res. 2015;100:85–92. doi:10.1016/J.PHRS.2015.07.032
   PubMed Web of Science ®Google Scholar
• Marino A, Martelli A, Citi V, et al. The novel H2S donor 4-carboxy-phenyl isothiocyanate inhibits mast cell degranulation and renin release by decreasing intracellular calcium. Br J Pharmacol. 2016;173(22):3222–3234. doi:10.1111/BPH.13583
   PubMed Web of Science ®Google Scholar
• Rodrigues L, Ekundi-Valentim E, Florenzano J, et al. Protective effects of exogenous and endogenous hydrogen sulfide in mast cell-mediated pruritus and cutaneous acute inflammation in mice. Pharmacol Res. 2017;115:255–266. doi:10.1016/J.PHRS.2016.11.006
   PubMed Web of Science ®Google Scholar
• Lin K-C, Huang D-Y, Huang D-W, Tzeng S-J, Lin -W-W. Inhibition of AMPK through Lyn-Syk-Akt enhances FcεRI signal pathways for allergic response. J Mol Med. 2015;94(2):183–194. doi:10.1007/S00109-015-1339-2
   Web of Science ®Google Scholar
• Rangaswami H, Schwappacher R, Marathe N, et al. Cyclic GMP and protein kinase G control a Src-containing mechanosome in osteoblasts. Sci Signal. 2010;3(153):ra91–ra91. doi:10.1126/SCISIGNAL.2001423
   Web of Science ®Google Scholar
• Brüne B, Schmidt K-U, Ullrich V. Activation of soluble guanylate cyclase by carbon monoxide and inhibition by superoxide anion. Eur J Biochem. 1990;192(3):683–688. doi:10.1111/J.1432-1033.1990.TB19276.X
   Google Scholar
• Siow RCM, Sato H, Mann GE. Heme oxygenase–carbon monoxide signalling pathway in atherosclerosis: anti-atherogenic actions of bilirubin and carbon monoxide? Cardiovasc Res. 1999;41(2):385–394. doi:10.1016/S0008-6363(98)00278-8
   Web of Science ®Google Scholar
• Lee HJ, Mariappan MM, Feliers D, et al. Hydrogen sulfide inhibits high glucose-induced matrix protein synthesis by activating AMP-activated protein kinase in renal epithelial cells. J Biol Chem. 2012;287(7):4451–4461. doi:10.1074/JBC.M111.278325
   PubMed Web of Science ®Google Scholar
• Chen X, Zhao X, Lan F, et al. Hydrogen sulphide treatment increases insulin sensitivity and improves oxidant metabolism through the CaMKKbeta-AMPK pathway in PA-induced IR C2C12 cells. Sci Rep. 2017;7(1):1–13. doi:10.1038/s41598-017-13251-0
   PubMed Web of Science ®Google Scholar
• Chen X, Zhao X, Cai H, et al. The role of sodium hydrosulfide in attenuating the aging process via PI3K/AKT and CaMKKβ/AMPK pathways. Redox Biol. 2017;12:987–1003. doi:10.1016/J.REDOX.2017.04.031
   Web of Science ®Google Scholar
• Zhou X, Cao Y, Ao G, et al. CaMKKβ-dependent activation of AMP-activated protein kinase is critical to suppressive effects of hydrogen sulfide on neuroinflammation. Antioxid Redox Signal. 2014;21(12):1741–1758. doi:10.1089/ARS.2013.5587
   PubMed Web of Science ®Google Scholar
• Hourihan JM, Kenna JG, Hayes JD. The gasotransmitter hydrogen sulfide induces Nrf2-target genes by inactivating the Keap1 ubiquitin ligase substrate adaptor through formation of a disulfide bond between Cys-226 and Cys-613. Antioxid Redox Signal. 2013;19(5):465–481. doi:10.1089/ARS.2012.4944
   Web of Science ®Google Scholar
• Yang G, Zhao K, Ju Y, et al. Hydrogen sulfide protects against cellular senescence via S-sulfhydration of Keap1 and activation of Nrf2. Antioxid Redox Signal. 2013;18(15):1906–1919. doi:10.1089/ARS.2012.4645
   PubMed Web of Science ®Google Scholar
• Yang H, Mao Y, Tan B, Luo S, Zhu Y. The protective effects of endogenous hydrogen sulfide modulator, S-propargyl-cysteine, on high glucose-induced apoptosis in cardiomyocytes: a novel mechanism mediated by the activation of Nrf2. Eur J Pharmacol. 2015;761:135–143. doi:10.1016/J.EJPHAR.2015.05.001
   Web of Science ®Google Scholar
• Xie L, Gu Y, Wen M, et al. Hydrogen sulfide induces Keap1 S-sulfhydration and suppresses diabetes-accelerated atherosclerosis via Nrf2 activation. Diabetes. 2016;65(10):3171–3184. doi:10.2337/DB16-0020
   PubMed Web of Science ®Google Scholar
• Szabo C. Hydrogen sulfide, an enhancer of vascular nitric oxide signaling: mechanisms and implications. Am J Physiol Cell Physiol. 2017;312(1):C3–C15. doi:10.1152/AJPCELL.00282.2016
   PubMed Web of Science ®Google Scholar
• Nalli AD, Bhattacharya S, Wang H, Kendig DM, Grider JR, Murthy KS. Augmentation of cGMP/PKG pathway and colonic motility by hydrogen sulfide. Am J Physiol Gastrointest Liver Physiol. 2017;313(4):G330–G341. doi:10.1152/AJPGI.00161.2017
   Web of Science ®Google Scholar
• Zhou Z, Martin E, Sharina I, et al. Regulation of soluble guanylyl cyclase redox state by hydrogen sulfide. Pharmacol Res. 2016;111:556–562. doi:10.1016/J.PHRS.2016.06.029
   PubMed Web of Science ®Google Scholar
• Liang Y, Xu X, Yin M, et al. Effects of berberine on blood glucose in patients with type 2 diabetes mellitus: a systematic literature review and a meta-analysis. Endocr J. 2019;66(1):51–63. doi:10.1507/ENDOCRJ.EJ18-0109
   PubMed Web of Science ®Google Scholar
• Ju J, Li J, Lin Q, Xu H. Efficacy and safety of berberine for dyslipidaemias: a systematic review and meta-analysis of randomized clinical trials. Phytomedicine. 2018;50:25–34. doi:10.1016/J.PHYMED.2018.09.212
   Web of Science ®Google Scholar
• Ye Y, Liu X, Wu N, et al. Efficacy and safety of berberine alone for several metabolic disorders: a systematic review and meta-analysis of randomized clinical trials. Front Pharmacol. 2021;12. doi:10.3389/FPHAR.2021.653887
   Web of Science ®Google Scholar
• Lee YS, Kim WS, Kim KH, et al. Berberine, a natural plant product, activates AMP-activated protein kinase with beneficial metabolic effects in diabetic and insulin-resistant states. Diabetes. 2006;55(8):2256–2264. doi:10.2337/DB06-0006
   PubMed Web of Science ®Google Scholar
• Turner N, Li J-Y, Gosby A, et al. Berberine and its more biologically available derivative, dihydroberberine, inhibit mitochondrial respiratory complex I. Diabetes. 2008;57(5):1414–1418. doi:10.2337/DB07-1552
   PubMed Web of Science ®Google Scholar
• Song Y, Qu C, Srivastava K, et al. Food allergy herbal formula 2 protection against peanut anaphylactic reaction is via inhibition of mast cells and basophils. J Allergy Clin Immunol. 2010;126(6):1208–1217.e3. doi:10.1016/J.JACI.2010.09.013
   Web of Science ®Google Scholar
• Fu S, Ni S, Wang D, Fu M, Hong T. Berberine suppresses mast cell-mediated allergic responses via regulating FcɛRI-mediated and MAPK signaling. Int Immunopharmacol. 2019;71:1–6. doi:10.1016/J.INTIMP.2019.02.041
   Web of Science ®Google Scholar
• Kim BY, Park HR, Jeong HG, Kim SW. Berberine reduce allergic inflammation in a house dust mite allergic rhinitis mouse model. Rhinol J. 2015;53(4):353–358. doi:10.4193/RHIN15.028
   Web of Science ®Google Scholar
• Sakat MS, Kilic K, Kandemir FM, et al. The ameliorative effect of berberine and coenzyme Q10 in an ovalbumin-induced allergic rhinitis model. Eur Arch Otorhinolaryngol. 2018;275(10):2495–2505. doi:10.1007/S00405-018-5104-3
   PubMed Web of Science ®Google Scholar
• Koriyama Y, Nakayama Y, Matsugo S, Kato S. Protective effect of lipoic acid against oxidative stress is mediated by Keap1/Nrf2-dependent heme oxygenase-1 induction in the RGC-5 cellline. Brain Res. 2013;1499:145–157. doi:10.1016/J.BRAINRES.2012.12.041
   PubMed Web of Science ®Google Scholar
• Kyung S, Lim Joo W, Kim H. α-Lipoic acid inhibits IL-8 expression by activating Nrf2 signaling in helicobacter pylori-infected gastric epithelial cells. Nutrients. 2019;11(10):2524. doi:10.3390/NU11102524
   Web of Science ®Google Scholar
• Jeffrey S, Samraj P, Raj B. The role of alpha-lipoic acid supplementation in the prevention of diabetes complications: a comprehensive review of clinical trials. Curr Diabetes Rev. 2021;17. doi:10.2174/1573399817666210118145550
   Web of Science ®Google Scholar
• Kensler TW, Egner PA, Agyeman AS, et al. Keap1-nrf2 signaling: a target for cancer prevention by sulforaphane. Top Curr Chem. 2013;329:163–177. doi:10.1007/128_2012_339
   PubMed Web of Science ®Google Scholar
• Riedl MA, Saxon A, Diaz-Sanchez D. Oral sulforaphane increases phase II antioxidant enzymes in the human upper airway. Clin Immunol. 2009;130(3):244–251. doi:10.1016/J.CLIM.2008.10.007
   PubMed Web of Science ®Google Scholar
• Choi YH, Chai OH, Han E-H, Choi S-Y, Kim HT, Song CH. Lipoic acid suppresses compound 48/80-induced anaphylaxis-like reaction. Anat Cell Biol. 2010;43(4):317. doi:10.5115/ACB.2010.43.4.317
   Google Scholar
• Ma X, He P, Sun P, Han P. Lipoic acid: an immunomodulator that attenuates glycinin-induced anaphylactic reactions in a rat model. J Agric Food Chem. 2010;58(8):5086–5092. doi:10.1021/JF904403U
   PubMed Web of Science ®Google Scholar
• Van Nguyen T, Piao CH, Fan YJ, et al. Anti-allergic rhinitis activity of α-lipoic acid via balancing Th17/Treg expression and enhancing Nrf2/HO-1 pathway signaling. Sci Rep. 2020;10(1):1–13. doi:10.1038/s41598-020-69234-1
   Web of Science ®Google Scholar
• Yusin J, Wang V, Henning SM, et al. The effect of broccoli sprout extract on seasonal grass pollen-induced allergic rhinitis. Nutrients. 2021;13(4):1337. doi:10.3390/NU13041337
   Web of Science ®Google Scholar
• David H, Zhaoping L, Maria G-L, et al. Sulforaphane-rich broccoli sprout extract attenuates nasal allergic response to diesel exhaust particles. Food Funct. 2013;5(1):35–41. doi:10.1039/C3FO60277J
   Web of Science ®Google Scholar
• Fang J, Yan Y, Teng X, et al. Melatonin prevents senescence of canine adipose-derived mesenchymal stem cells through activating NRF2 and inhibiting ER stress. Aging (Albany NY). 2018;10(10):2954. doi:10.18632/AGING.101602
   PubMedGoogle Scholar
• Hardeland R. Melatonin and inflammation—story of a double-edged blade. J Pineal Res. 2018;65(4):e12525. doi:10.1111/JPI.12525
   PubMed Web of Science ®Google Scholar
• Merlo S, Luaces JP, Spampinato SF, et al. SIRT1 mediates melatonin’s effects on microglial activation in hypoxia: in vitro and in vivo evidence. Biomolecules. 2020;10(3):364. doi:10.3390/BIOM10030364
   Web of Science ®Google Scholar
• Cakir Cetin A, Ecevit MC, Gumustekin M, et al. Therapeutic effects of melatonin on an ovalbumin-induced allergic rhinitis model in rats. Auris Nasus Larynx. 2021;48(6):1109–1119. doi:10.1016/J.ANL.2021.04.010
   Web of Science ®Google Scholar
• Çikler E, Ercan F, Çetinel Ş, Contuk G, Şener G. The protective effects of melatonin against water avoidance stress-induced mast cell degranulation in dermis. Acta Histochem. 2005;106(6):467–475. doi:10.1016/J.ACTHIS.2004.10.001
   Web of Science ®Google Scholar
• Maldonado MD, García-Moreno H, González-Yanes C, Calvo JR. Possible involvement of the inhibition of NF-κB factor in anti-inflammatory actions that melatonin exerts on mast cells. J Cell Biochem. 2016;117(8):1926–1933. doi:10.1002/JCB.25491
   PubMed Web of Science ®Google Scholar
• Wang J, Zhang Y, Hu S, Ge S, Jia M, Wang N. Resveratrol inhibits MRGPRX2-mediated mast cell activation via Nrf2 pathway. Int Immunopharmacol. 2021;93:107426. doi:10.1016/J.INTIMP.2021.107426
   PubMed Web of Science ®Google Scholar
• Zhang Y, Hu S, Ge S, Wang J, He L. Paeoniflorin inhibits IgE-mediated allergic reactions by suppressing the degranulation of mast cells though binding with FcϵRI alpha subunits. Eur J Pharmacol. 2020;886:173415. doi:10.1016/J.EJPHAR.2020.173415
   Web of Science ®Google Scholar
• Wang G, Cheng N. Paeoniflorin inhibits mast cell–mediated allergic inflammation in allergic rhinitis. J Cell Biochem. 2018;119(10):8636–8642. doi:10.1002/JCB.27135
   PubMed Web of Science ®Google Scholar
• Wang J, Zhang Y, Wang J, et al. Paeoniflorin inhibits MRGPRX2-mediated pseudo-allergic reaction via calcium signaling pathway. Phyther Res. 2020;34(2):401–408. doi:10.1002/PTR.6531
   PubMed Web of Science ®Google Scholar
• Zhao Y, Li X, Chu J, et al. Inhibitory effect of paeoniflorin on IgE-dependent and IgE-independent mast cell degranulation: in vitro and vivo. Food Funct. 2021;12(16):7448–7468. doi:10.1039/D1FO01421H
   Web of Science ®Google Scholar
• Terry MJ, Maines MD, Lagarias JC. Inactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase. J Biol Chem. 1993;268(35):26099–26106. doi:10.1016/S0021-9258(19)74286-0
   Web of Science ®Google Scholar
• McCarty MF. Clinical potential of spirulina as a source of phycocyanobilin. J Med Food. 2007;10(4):566–570. doi:10.1089/JMF.2007.621
   PubMed Web of Science ®Google Scholar
• Zheng J, Inoguchi T, Sasaki S, et al. Phycocyanin and phycocyanobilin from Spirulina platensis protect against diabetic nephropathy by inhibiting oxidative stress. Am J Physiol Regul Integr Comp Physiol. 2013;304(2):R110–R120. doi:10.1152/AJPREGU.00648.2011
   PubMed Web of Science ®Google Scholar
• Liu Q, Huang Y, Zhang R, Cai T, Cai Y. Medical application of spirulina platensis derived C-phycocyanin. Evid Based Complement Altern Med. 2016;2016. doi:10.1155/2016/7803846
   Web of Science ®Google Scholar
• Wu Q, Liu L, Miron A, Klímová B, Wan D, Kuča K. The antioxidant, immunomodulatory, and anti-inflammatory activities of spirulina: an overview. Arch Toxicol. 2016;90(8):1817–1840. doi:10.1007/S00204-016-1744-5
   PubMed Web of Science ®Google Scholar
• Yang H-N, Lee E-H, Kim H-M. Spirulina platensis inhibits anaphylactic reaction. Life Sci. 1997;61(13):1237–1244. doi:10.1016/S0024-3205(97)00668-1
   PubMed Web of Science ®Google Scholar
• Kim HM, Lee EH, Cho HH, Moon YH. Inhibitory effect of mast cell-mediated immediate-type allergic reactions in rats by spirulina. Biochem Pharmacol. 1998;55(7):1071–1076. doi:10.1016/S0006-2952(97)00678-3
   Web of Science ®Google Scholar
• Remirez D, Ledón N, González R. Role of histamine in the inhibitory effects of phycocyanin in experimental models of allergic inflammatory response. Mediators Inflamm. 2002;11(2):81–85. doi:10.1080/09629350220131926
   PubMed Web of Science ®Google Scholar
• Chen LL, Zhang SF, Huang DN, Tan JQ, He SH. Experimental study of spirulina platensis in treating allergic rhinitis in rats. J Cent South Univ). 2005;30(1):96–98.
   Google Scholar
• Cingi C, Conk-Dalay M, Cakli H, Bal C. The effects of spirulina on allergic rhinitis. Eur Arch Otorhinolaryngol. 2008;265(10):1219–1223. doi:10.1007/S00405-008-0642-8
   PubMed Web of Science ®Google Scholar
• Nourollahian M, Rasoulian B, Gafari A, Anoushiravani M, Jabari F, Bakhshaee M. Clinical comparison of the efficacy of spirulina platensis and cetirizine for treatment of allergic rhinitis. Acta Otorhinolaryngol Ital. 2020;40(3):224–229. doi:10.14639/0392-100X-N0139
   Web of Science ®Google Scholar
• Mao TK, Van De Water J, Gershwin ME. Effects of a Spirulina-based dietary supplement on cytokine production from allergic rhinitis patients. J Med Food. 2005;8(1):27–30. doi:10.1089/JMF.2005.8.27
   PubMed Web of Science ®Google Scholar
• Vesely D. Biotin enhances guanylate cyclase activity. Science. 1982;216(4552):1329–1330. doi:10.1126/SCIENCE.6123152
   PubMed Web of Science ®Google Scholar
• Watanabe-Kamiyama M, Kamiyama S, Horiuchi K, et al. Antihypertensive effect of biotin in stroke-prone spontaneously hypertensive rats. Br J Nutr. 2008;99(4):756–763. doi:10.1017/S0007114507841122
   PubMed Web of Science ®Google Scholar
• McCarty MF, DiNicolantonio JJ. Neuroprotective potential of high-dose biotin. Med Hypotheses. 2017;109:145–149. doi:10.1016/J.MEHY.2017.10.012
   PubMed Web of Science ®Google Scholar
• Ezeriņa D, Takano Y, Hanaoka K, Urano Y, Dick TP. N-acetyl cysteine functions as a fast-acting antioxidant by triggering intracellular H 2 S and sulfane sulfur production. Cell Chem Biol. 2018;25(4):447–459.e4. doi:10.1016/J.CHEMBIOL.2018.01.011
   PubMed Web of Science ®Google Scholar
• Dinicolantonio JJ, Okeefe JH, McCarty MF. Boosting endogenous production of vasoprotective hydrogen sulfide via supplementation with taurine and N-acetylcysteine: a novel way to promote cardiovascular health. Open Heart. 2017;4(1):e000600. doi:10.1136/OPENHRT-2017-000600
   Web of Science ®Google Scholar
• Zuhra K, Tomé CS, Masi L, et al. N-acetylcysteine serves as substrate of 3-mercaptopyruvate sulfurtransferase and stimulates sulfide metabolism in colon cancer cells. Cells. 2019;8(8):828. doi:10.3390/CELLS8080828
   Web of Science ®Google Scholar
• Bourgonje AR, Offringa AK, van Eijk LE, et al. N-acetylcysteine and hydrogen sulfide in coronavirus disease 2019. Antioxid Redox Signal. 2021. doi:10.1089/ARS.2020.8247
   Web of Science ®Google Scholar
• Atkuri KR, Mantovani JJ, Herzenberg LA, Herzenberg LA. N-acetylcysteine-a safe antidote for cysteine/glutathione deficiency. Curr Opin Pharmacol. 2007;7(4):355–359. doi:10.1016/J.COPH.2007.04.005
   PubMed Web of Science ®Google Scholar
• Dodd S, Dean O, Copolov DL, Malhi GS, Berk M. N-acetylcysteine for antioxidant therapy: pharmacology and clinical utility. Expert Opin Biol Ther. 2008;8(12):1955–1962. doi:10.1517/14728220802517901
   PubMed Web of Science ®Google Scholar
• Sun Q, Wang B, Li Y, et al. Taurine supplementation lowers blood pressure and improves vascular function in prehypertension: Randomized, Double-Blind, Placebo-Controlled Study. Hypertension. 2016;67(3):541–549. doi:10.1161/HYPERTENSIONAHA.115.06624
   PubMed Web of Science ®Google Scholar
• Guizoni DM, Freitas IN, Victorio JA, et al. Taurine treatment reverses protein malnutrition-induced endothelial dysfunction of the pancreatic vasculature: the role of hydrogen sulfide. Metabolism. 2021;116:154701. doi:10.1016/J.METABOL.2021.154701
   Web of Science ®Google Scholar
• Nam SY, Kim HM, Jeong HJ. The potential protective role of taurine against experimental allergic inflammation. Life Sci. 2017;184:18–24. doi:10.1016/J.LFS.2017.07.007
   Web of Science ®Google Scholar
• Zhou J, Lu Y, Li F, Wu W, Xie D, Feng Y. In vitro and in vivo antiallergic effects of taurine on allergic rhinitis. Int Arch Allergy Immunol. 2020;181(6):404–416. doi:10.1159/000505209
   Web of Science ®Google Scholar
• Maeda Yamamoto M, Ema K, Monobe M, Tokuda Y, Tachibana H. Epicatechin-3-O-(3″-O-methyl)-gallate content in various tea cultivars (Camellia sinensis L.) and its in vitro inhibitory effect on histamine release. J Agric Food Chem. 2012;60(9):2165–2170. doi:10.1021/JF204497B
   Web of Science ®Google Scholar
• Masuda S, Maeda-Yamamoto M, Usui S, Fujisawa T. “Benifuuki” green tea containing O-methylated catechin reduces symptoms of Japanese cedar pollinosis: a randomized, double- blind, placebo-controlled trial. Allergol Int. 2014;63(2):211–217. doi:10.2332/ALLERGOLINT.13-OA-0620
   Web of Science ®Google Scholar
• Maeda-Yamamoto M, Ema K, Monobe M, et al. The efficacy of early treatment of seasonal allergic rhinitis with benifuuki green tea containing O-methylated catechin before pollen exposure: an Open Randomized Study. Allergol Int. 2009;58(3):437–444. doi:10.2332/ALLERGOLINT.08-OA-0066
   Google Scholar
• Oritani Y, Setoguchi Y, Ito R, Maruki-Uchida H, Ichiyanagi T, Ito T. Comparison of (−)-epigallocatechin-3-O-gallate (EGCG) and O-methyl EGCG bioavailability in rats. Biol Pharm Bull. 2013;36(10):1577–1582. doi:10.1248/BPB.B13-00349
   PubMed Web of Science ®Google Scholar
• Maeda-Yamamoto M, Ema K, Tokuda Y, et al. Effect of green tea powder (Camellia sinensis L. cv. Benifuuki) particle size on O-methylated EGCG absorption in rats; the Kakegawa Study. Cytotechnology. 2011;63(2):171–179. doi:10.1007/S10616-010-9331-8
   Web of Science ®Google Scholar
• Inoue T, Suzuki Y, Ra C. Epigallocatechin-3-gallate inhibits mast cell degranulation, leukotriene C4 secretion, and calcium influx via mitochondrial calcium dysfunction. Free Radic Biol Med. 2010;49(4):632–640. doi:10.1016/J.FREERADBIOMED.2010.05.015
   Web of Science ®Google Scholar
• Yamashita K, Suzuki Y, Matsui T, et al. Epigallocatechin gallate inhibits histamine release from rat basophilic leukemia (RBL-2H3) cells: role of tyrosine phosphorylation pathway. Biochem Biophys Res Commun. 2000;274(3):603–608. doi:10.1006/BBRC.2000.3200
   Web of Science ®Google Scholar
• Fujimura Y, Tachibana H, Maeda-Yamamoto M, Miyase T, Sano M, Yamada K. Antiallergic tea catechin, (-)-epigallocatechin-3-O-(3-O-methyl)-gallate, suppresses FcεRl expression in human basophilic KU812 cells. J Agric Food Chem. 2002;50(20):5729–5734. doi:10.1021/JF025680Z
   Web of Science ®Google Scholar
• Nishikawa H, Wakano K, Kitani S. Inhibition of NADPH oxidase subunits translocation by tea catechin EGCG in mast cell. Biochem Biophys Res Commun. 2007;362(2):504–509. doi:10.1016/J.BBRC.2007.08.015
   Web of Science ®Google Scholar
• Fujimura Y, Sumida M, Sugihara K, Tsukamoto S, Yamada K, Tachibana H. Green tea polyphenol EGCG sensing motif on the 67-kDa laminin receptor. PLoS One. 2012;7(5):5. doi:10.1371/JOURNAL.PONE.0037942
   Web of Science ®Google Scholar
• Fujimura Y, Yamada K, Tachibana H. A lipid raft-associated 67 kDa laminin receptor mediates suppressive effect of epigallocatechin-3-O-gallate on FcεRI expression. Biochem Biophys Res Commun. 2005;336(2):674–681. doi:10.1016/J.BBRC.2005.08.146
   PubMed Web of Science ®Google Scholar
• Fujimura Y, Umeda D, Kiyohara Y, Sunada Y, Yamada K, Tachibana H. The involvement of the 67 kDa laminin receptor-mediated modulation of cytoskeleton in the degranulation inhibition induced by epigallocatechin-3-O-gallate. Biochem Biophys Res Commun. 2006;348(2):524–531. doi:10.1016/J.BBRC.2006.07.086
   Web of Science ®Google Scholar
• Fujimura Y, Umeda D, Yano S, Maeda-Yamamoto M, Yamada K, Tachibana H. The 67 kDa laminin receptor as a primary determinant of anti-allergic effects of O-methylated EGCG. Biochem Biophys Res Commun. 2007;364(1):79–85. doi:10.1016/J.BBRC.2007.09.095
   Web of Science ®Google Scholar
• Adachi S, Nagao T, To S, et al. (-)-Epigallocatechin gallate causes internalization of the epidermal growth factor receptor in human colon cancer cells. Carcinogenesis. 2008;29(10):1986–1993. doi:10.1093/CARCIN/BGN128
   PubMed Web of Science ®Google Scholar