Overview of the Role of Vanillin in Neurodegenerative Diseases and Neuropathophysiological Conditions
Abstract
:1. Introduction
2. Protective Effects of Vanillin on Neurological Diseases
2.1. Neurodegenerative Diseases
2.1.1. Alzheimer’s Disease
2.1.2. Parkinson’s Disease
2.1.3. Huntington’s Disease
2.2. Other Neurological Diseases
Spinal Cord Injury
3. Protective Effects of Vanillin in Neuropathophysiological Conditions
3.1. Hypoxic-Ischemic Brain Injuries
3.2. Brain Toxins
3.3. Microglial Activation—Neuroinflammation
4. Conclusions
Author Contributions
Funding
Data Availability Statement
Conflicts of Interest
References
- Arya, S.S.; Rookes, J.E.; Cahill, D.M.; Sangram, K.L. Vanillin: A review on the therapeutic prospects of a popular flavouring molecule. Adv. Trad. Med. (ADTM) 2021, 21, 1–17. [Google Scholar] [CrossRef]
- Bezerra-Filho, C.S.M.; Barboza, J.N.; Souza, M.T.S.; Sabry, P.; Ismail, N.S.M.; de Sousa, D.P. Therapeutic Potential of Vanillin and its Main Metabolites to Regulate the Inflammatory Response and Oxidative Stress. Mini Rev. Med. Chem. 2019, 19, 1681–1693. [Google Scholar] [CrossRef] [PubMed]
- Bezerra, D.P.; Soares, A.K.N.; de Sousa, D.P. Overview of the role of vanillin on redox status and cancer development. Oxid. Med. Cell Longev. 2016, 2016, 9734816. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, J.M.; Lee, Y.C.; Li, C.C.; Lo, H.Y.; Chen, F.Y.; Chen, Y.S.; Hsiang, C.Y.; Ho, T.Y. Vanillin-ameliorated development of azoxymethane/dextran sodium sulfate-induced murine colorectal cancer: The involvement of proteasome/nuclear factor-κB/mitogen-activated protein kinase pathways. J. Agric. Food Chem. 2018, 66, 5563–5573. [Google Scholar] [CrossRef] [PubMed]
- Rakoczy, K.; Szlasa, W.M.; Saczko, J.; Kulbacka, J. Therapeutic role of vanillin receptors in cancer. Adv. Clin. Exp. Med. 2021, 30, 1293–1301. [Google Scholar] [CrossRef]
- Yadav, R.; Saini, D.; Yadav, D. Synthesis and Evaluation of Vanillin Derivatives as Antimicrobial Agents. Turk. J. Pharm. Sci. 2018, 15, 57–62. [Google Scholar] [CrossRef]
- Cava-Roda, R.; Taboada-Rodríguez, A.; López-Gómez, A.; Martínez-Hernández, G.B.; Marín-Iniesta, F. Synergistic Antimicrobial Activities of Combinations of Vanillin and Essential Oils of Cinnamon Bark, Cinnamon Leaves, and Cloves. Foods 2021, 10, 1406. [Google Scholar] [CrossRef]
- Deryabin, D.; Inchagova, K.; Rusakova, E.; Duskaev, G. Coumarin’s Anti-Quorum Sensing Activity Can Be Enhanced When Combined with Other Plant-Derived Small Molecules. Molecules 2021, 26, 208. [Google Scholar] [CrossRef]
- Wang, Y.J.; Pan, M.H.; Cheng, A.L.; Lin, L.I.; Ho, Y.S.; Hsieh, C.Y.; Lin, J.K. Stability of curcumin in buffer solutions and characterization of its degradation products. J. Pharm. Biomed. Anal. 1997, 15, 1867–1876. [Google Scholar] [CrossRef]
- Shen, L.; Ji, H.F. Contribution of degradation products to the anticancer activity of curcumin. Clin. Cancer Res. 2009, 15, 7108–7109. [Google Scholar] [CrossRef]
- Shen, L.; Jiang, H.H.; Ji, H.F. Is boiled food spice curcumin still biologically active? An experimental exploration. Food Nutr. Res. 2018, 62. [Google Scholar] [CrossRef] [Green Version]
- Tai, A.; Sawano, T.; Yazama, F.; Ito, H. Evaluation of antioxidant activity of vanillin by using multiple antioxidant assays. Biochim. Biophys. Acta 2011, 1810, 170–177. [Google Scholar] [CrossRef]
- Lim, E.J.; Kang, H.J.; Jung, H.J.; Song, Y.S.; Lim, C.J.; Park, E.H. Anti-angiogenic, anti-inflammatory and anti-nociceptive activities of vanillin in ICR mice. Biomol. Ther. 2008, 16, 132–136. [Google Scholar] [CrossRef] [Green Version]
- Ho, K.; Yazan, L.S.; Ismail, N.; Ismail, M. Toxicology study of vanillin on rats via oral and intra-peritoneal administration. Food Chem. Toxicol. 2011, 49, 25–30. [Google Scholar] [CrossRef]
- Guo, T.; Zhang, D.; Zeng, Y.; Huang, T.Y.; Xu, H.; Zhao, Y. Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease. Mol. Neurodegener. 2020, 15, 40. [Google Scholar] [CrossRef]
- Sung, P.S.; Lin, P.Y.; Liu, C.H.; Su, H.C.; Tsai, K.J. Neuroinflammation and Neurogenesis in Alzheimer’s Disease and Potential Therapeutic Approaches. Int. J. Mol. Sci. 2020, 21, 701. [Google Scholar] [CrossRef] [Green Version]
- Butterfield, D.A.; Halliwell, B. Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease. Nat. Rev. Neurosci. 2019, 20, 148–160. [Google Scholar] [CrossRef]
- Perry, E.K.; Perry, R.H.; Blessed, G.; Tomlinson, B.E. Changes in brain cholinesterases in senile dementia of Alzheimer type. Neuropathol. Appl. Neurobiol. 1978, 4, 273–277. [Google Scholar] [CrossRef]
- Geula, C.; Mesulam, M. Special properties of cholinesterases in the cerebral cortex of Alzheimer’s disease. Brain Res. 1989, 498, 185–189. [Google Scholar] [CrossRef]
- Sharma, K. Cholinesterase inhibitors as Alzheimer’s therapeutics (Review). Mol. Med. Rep. 2019, 20, 1479–1487. [Google Scholar] [CrossRef]
- Akıncıoğlu, H.; Gülçin, İ. Potent Acetylcholinesterase Inhibitors: Potential Drugs for Alzheimer’s Disease. Mini Rev. Med. Chem. 2020, 20, 703–715. [Google Scholar] [CrossRef] [PubMed]
- Ravi, S.K.; Narasingappa, R.B.; Vincent, B. Neuro-nutrients as anti-alzheimer’s disease agents: A critical review. Crit. Rev. Food Sci. Nutr. 2019, 59, 2999–3018. [Google Scholar] [CrossRef] [PubMed]
- Chauhan, P.S.; Yadav, D. Dietary Nutrients and Prevention of Alzheimer’s disease. CNS Neurol. Disord. Drug Targets 2022, 21, 217–227. [Google Scholar] [CrossRef] [PubMed]
- Cremonini, A.L.; Caffa, I.; Cea, M.; Nencioni, A.; Odetti, P.; Monacelli, F. Nutrients in the Prevention of Alzheimer’s Disease. Oxid. Med. Cell. Longev. 2019, 2019, 9874159. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ahammed, S.; Afrin, R.; Uddin, N.; Al-Amin, Y.; Hasan, K.; Haque, U.; Islam, K.M.M.; Alam, A.H.M.K.M.; Tanaka, T.; Sadik, G. Acetylcholinesterase Inhibitory and Antioxidant Activity of the Compounds Isolated from Vanda roxburghii. Adv. Pharmacol. Pharm. Sci. 2021, 2021, 5569054. [Google Scholar] [CrossRef]
- Kundu, A.; Mitra, A. Flavoring extracts of Hemidesmus indicus roots and Vanilla planifolia pods exhibit in vitro acetylcholinesterase inhibitory activities. Plant Foods Hum. Nutr. 2013, 68, 247–253. [Google Scholar] [CrossRef]
- Salau, V.F.; Erukainure, O.L.; Ibeji, C.U.; Olasehinde, T.A.; Koorbanally, N.A.; Islam, M.S. Vanillin and vanillic acid modulate antioxidant defense system via amelioration of metabolic complications linked to Fe2+-induced brain tissues damage. Metab. Brain Dis. 2020, 35, 727–738. [Google Scholar] [CrossRef]
- Blaikie, L.; Kay, G.; Kong Thoo Lin, P. Synthesis and in vitro evaluation of vanillin derivatives as multi-target therapeutics for the treatment of Alzheimer’s disease. Bioorg. Med. Chem. Lett. 2020, 30, 127505. [Google Scholar] [CrossRef]
- Scipioni, M.; Kay, G.; Megson, I.L.; Kong Thoo Lin, P. Synthesis of novel vanillin derivatives: Novel multi-targeted scaffold ligands against Alzheimer’s disease. Medchemcomm 2019, 10, 764–777. [Google Scholar] [CrossRef]
- Abuhamdah, S.; Duaa, T.; Naji, A.; Anas, B.; Izzeddin, S.; Amjad, A. Behavioral and Neurochemical Alterations Induced by Vanillin in a Mouse Model of Alzheimer’s Disease. Int. J. Pharmacol. 2017, 13, 573–582. [Google Scholar] [CrossRef]
- Jayant, S.; Sharma, B.M.; Sharma, B. Protective effect of transient receptor potential vanilloid subtype 1 (TRPV1) modulator, against behavioral, biochemical and structural damage in experimental models of Alzheimer’s disease. Brain Res. 2016, 1642, 397–408. [Google Scholar] [CrossRef]
- Zhong, L.; Tong, Y.; Chuan, J.; Bai, L.; Shi, J.; Zhu, Y. Protective effect of ethyl vanillin against Aβ induced neurotoxicity in PC12 cells via the reduction of oxidative stress and apoptosis. Exp. Ther. Med. 2019, 17, 2666–2674. [Google Scholar] [CrossRef] [Green Version]
- Zhou, C.; Huang, Y.; Przedborski, S. Oxidative stress in Parkinson’s disease: A mechanism of pathogenic and therapeutic significance. Ann. N. Y. Acad. Sci. 2008, 1147, 93–104. [Google Scholar] [CrossRef]
- Raza, C.; Anjum, R.; Shakeel, N.U.A. Parkinson’s disease: Mechanisms, translational models and management strategies. Life Sci. 2019, 226, 77–90. [Google Scholar] [CrossRef]
- Tansey, M.G.; Goldberg, M.S. Neuroinflammation in Parkinson’s disease: Its role in neuronal death and implications for therapeutic intervention. Neurobiol. Dis. 2010, 37, 510–518. [Google Scholar] [CrossRef] [Green Version]
- Dhanalakshmi, C.; Manivasagam, T.; Nataraj, J.; Justin Thenmozhi, A.; Essa, M.M. Neurosupportive Role of Vanillin, a Natural Phenolic Compound, on Rotenone Induced Neurotoxicity in SH-SY5Y Neuroblastoma Cells. Evid. Based Complement Alternat. Med. 2015, 2015, 626028. [Google Scholar] [CrossRef] [Green Version]
- Klintworth, H.; Newhouse, K.; Li, T.; Choi, W.S.; Faigle, R.; Xia, Z. Activation of c-Jun N-Terminal Protein Kinase Is a Common Mechanism Underlying Paraquat- and Rotenone-Induced Dopaminergic Cell Apoptosis. Toxicol. Sci. 2007, 97, 149–162. [Google Scholar] [CrossRef] [Green Version]
- Junn, E.; Mouradian, M.M. Apoptotic signaling in dopamine-induced cell death: The role of oxidative stress, p38 mitogen-activated protein kinase, cytochrome c and caspases. J. Neurochem. 2001, 78, 374–383. [Google Scholar] [CrossRef] [Green Version]
- Dhanalakshmi, C.; Janakiraman, U.; Manivasagam, T.; Justin Thenmozhi, A.; Essa, M.M.; Kalandar, A.; Khan, M.A.; Guillemin, G.J. Vanillin Attenuated Behavioural Impairments, Neurochemical Deficts, Oxidative Stress and Apoptosis Against Rotenone Induced Rat Model of Parkinson’s Disease. Neurochem. Res. 2016, 41, 1899–1910. [Google Scholar] [CrossRef]
- Abuthawabeh, R.; Abuirmeileh, A.N.; Alzoubi, K.H. The beneficial effect of vanillin on 6-hydroxydopamine rat model of Parkinson’s disease. Restor. Neurol. Neurosci. 2020, 38, 369–373. [Google Scholar] [CrossRef]
- Vijitruth, R.; Liu, M.; Choi, D.Y.; Nguyen, X.V.; Hunter, R.L.; Bing, G. Cyclooxygenase-2 mediates microglial activation and secondary dopaminergic cell death in the mouse MPTP model of Parkinson’s disease. J. Neuroinflamm. 2006, 3, 6. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Shao, W.; Zhang, S.Z.; Tang, M.; Zhang, X.H.; Zhou, Z.; Yin, Y.Q.; Zhou, Q.B.; Huang, Y.Y.; Liu, Y.J.; Wawrousek, E. Suppression of neuroinflammation by astrocytic dopamine D2 receptors via αB-crystallin. Nature 2013, 494, 90–94. [Google Scholar] [CrossRef] [PubMed]
- Appel, S.H. Inflammation in Parkinson’s disease: Cause or consequence? Mov. Disord. 2012, 27, 1075–1077. [Google Scholar] [CrossRef] [PubMed]
- Yan, X.; Liu, D.F.; Zhang, X.Y.; Liu, D.; Xu, S.Y.; Chen, G.X.; Huang, B.X.; Ren, W.Z.; Wang, W.; Fu, S.P.; et al. Vanillin Protects Dopaminergic Neurons against Inflammation-Mediated Cell Death by Inhibiting ERK1/2, P38 and the NF-κB Signaling Pathway. Int. J. Mol. Sci. 2017, 18, 389. [Google Scholar] [CrossRef]
- Tabrizi, S.J.; Flower, M.D.; Ross, C.A.; Wild, E.J. Huntington disease: New insights into molecular pathogenesis and therapeutic opportunities. Nat. Rev. Neurol. 2020, 16, 529–546. [Google Scholar] [CrossRef]
- Bhateja, D.K.; Dhull, D.K.; Gill, A.; Sidhu, A.; Sharma, S.; Reddy, B.V.K.; Padi, S.V. Peroxisome proliferator-activated receptor-α activation attenuates 3-nitropropionic acid induced behavioral and biochemical alterations in rats: Possible neuroprotective mechanisms. Eur. J. Pharmacol. 2012, 674, 33–43. [Google Scholar] [CrossRef]
- Gupta, S.; Sharma, B. Pharmacological benefits of agomelatine and vanillin in experimental model of Huntington’s disease. Pharmacol. Biochem. Behav. 2014, 122, 122–135. [Google Scholar] [CrossRef]
- Pecze, L.; Blum, W.; Schwaller, B. Mechanism of capsaicin receptor TRPV1-mediated toxicity in pain-sensing neurons focusing on the effects of Na(+)/Ca(2+) fluxes and the Ca(2+)-binding protein calretinin. Biochim. Biophys. Acta. 2013, 1833, 1680–1691. [Google Scholar] [CrossRef] [Green Version]
- Fernández-Ruiz, J.; Gonzáles, S. Cannabinoid control of motor function at the basal ganglia. Handb. Exp. Pharmacol. 2005, 168, 479–507. [Google Scholar] [CrossRef]
- McKinley, W.O.; Jackson, A.B.; Cardenas, D.D.; DeVivo, M.J. Long-term medical complications after traumatic spinal cord injury: A regional model systems analysis. Arch. Phys. Med. Rehabil. 1999, 80, 1402–1410. [Google Scholar] [CrossRef]
- Hirose, K.; Okajima, K.; Uchiba, M.; Nakano, K.Y.; Utoh, J.; Kitamura, N. Antithrombin reduces the ischemia/reperfusion-induced spinal cord injury in rats by attenuating inflammatory responses. Thromb. Haemost. 2004, 91, 162–170. [Google Scholar] [CrossRef] [Green Version]
- Kasahara, A.; Scorrano, L. Mitochondria: From cell death executioners to regulators of cell differentiation. Trends. Cell Biol. 2014, 24, 761–770. [Google Scholar] [CrossRef]
- Klecker, T.; Böckler, S.; Westermann, B. Making connections: Interorganelle contacts orchestrate mitochondrial behavior. Trends Cell Biol. 2014, 24, 537–545. [Google Scholar] [CrossRef]
- Chen, M.H.; Ren, Q.X.; Yang, W.F.; Chen, X.L.; Lu, C.; Sun, J. Influences of HIF-lα on Bax/Bcl-2 and VEGF expressions in rats with spinal cord injury. Int. J. Clin. Exp. Pathol. 2013, 6, 2312–2322. [Google Scholar]
- Lawn, J.E.; Cousens, S.; Zupan, J. 4 Million Neonatal Deaths: When? Where? Why? Lancet 2005, 365, 891–900. [Google Scholar] [CrossRef]
- Mohsenpour, H.; Pesce, M.; Patruno, A.; Bahrami, A.; Pour, P.M.; Farzaei, M.H. A Review of Plant Extracts and Plant-Derived Natural Compounds in the Prevention/Treatment of Neonatal Hypoxic-Ischemic Brain Injury. Int. J. Mol. Sci. 2021, 22, 833. [Google Scholar] [CrossRef]
- Albrecht, M.; Zitta, K.; Groenendaal, F.; Van Bel, F.; Peeters-Scholte, C. Neuroprotective Strategies Following Perinatal Hypoxia Ischemia: Taking Aim at NOS. Free Radic. Biol. Med. 2019, 142, 123–131. [Google Scholar] [CrossRef]
- Lan, X.B.; Wang, Q.; Yang, J.M.; Ma, L.; Zhang, W.J.; Zheng, P.; Sun, T.; Niu, J.G.; Liu, N.; Yu, J.Q. Neuroprotective effect of Vanillin on hypoxic-ischemic brain damage in neonatal rats. Biomed. Pharmacother. 2019, 118, 109196. [Google Scholar] [CrossRef]
- Kim, H.J.; Hwang, I.K.; Won, M.H. Vanillin, 4-hydroxybenzyl aldehyde and 4-hydroxybenzyl alcohol prevent hippocampal CA1 cell death following global ischemia. Brain Res. 2007, 1181, 130–141. [Google Scholar] [CrossRef]
- Deng, Y.; Liu, K.; Pan, Y.; Ren, J.; Shang, J.; Chen, L.; Liu, H. TLR2 antagonism attenuates the hippocampal neuronal damage in a murine model of sleep apnea via inhibiting neuroinflammation and oxidative stress. Sleep Breath 2020, 24, 1613–1621. [Google Scholar] [CrossRef]
- Ben Amara, I.; Ben Saad, H.; Cherif, B.; Elwej, A.; Lassoued, S.; Kallel, C.; Zeghal, N. Methyl-thiophanate increases reactive oxygen species production and induces genotoxicity in rat peripheral blood. Toxicol. Mech. Methods 2014, 24, 679–687. [Google Scholar] [CrossRef] [PubMed]
- Ben Amara, I.; Ben Saad, H.; Hamdaoui, L.; Karray, A.; Boudawara, T.; Ben Ali, Y.; Zeghal, N. Maneb disturbs expression of superoxide dismutase and glutathione peroxidase, increases reactive oxygen species production, and induces genotoxicity in liver of adult mice. Environ. Sci. Pollut. Res. Int. 2015, 22, 12309–12322. [Google Scholar] [CrossRef] [PubMed]
- Ben Saad, H.; Kharrat, N.; Driss, D.; Gargouri, M.; Marrakchi, R.; Jammoussi, K.; Magné, C.; Boudawara, T.; Ellouz Chaabouni, S.; Zeghal, K.M.; et al. Effects of vanillin on potassium bromate-induced neurotoxicity in adult mice: Impact on behavior, oxidative stress, genes expression, inflammation and fatty acid composition. Arch. Physiol. Biochem. 2017, 123, 165–174. [Google Scholar] [CrossRef] [PubMed]
- Hidalgo, C.; Núñez, M.T. Calcium, iron and neuronal function. IUBMB Life 2007, 59, 280–285. [Google Scholar] [CrossRef] [PubMed]
- Latunde-Dada, G.O. Ferroptosis: Role of lipid peroxidation, iron and ferritinophagy. Biochim. Biophys. Acta Gen. Subj. 2017, 1861, 1893–1900. [Google Scholar] [CrossRef] [Green Version]
- Makni, M.; Chtourou, Y.; Barkallah, M.; Fetoui, H. Protective effect of vanillin against carbon tetrachloride (CCl4)-induced oxidative brain injury in rats. Toxicol. Ind. Health 2012, 28, 655–662. [Google Scholar] [CrossRef]
- Kim, H.J.; Odend’hal, S.; Bruckner, J.V. Effect of oral dosing vehicles on the acute hepatotoxicity of carbon tetrachloride in rats. Toxicol. Appl. Pharmacol. 1990, 102, 34–49. [Google Scholar] [CrossRef]
- McGregor, D.; Lang, M. Carbon tetrachloride: Genetic effects and other modes of action. Mutat. Res. 1996, 366, 181–195. [Google Scholar] [CrossRef]
- Jana, A.K.; Batkulwar, K.B.; Kulkarni, M.J.; Sengupta, N. Glycation induces conformational changes in the amyloid-β peptide and enhances its aggregation propensity: Molecular insights. Phys. Chem. Chem. Phys. 2016, 18, 31446–31458. [Google Scholar] [CrossRef]
- Ledesma, M.D.; Pérez, M.; Colaco, C.; Avila, J. Tau glycation is involved in aggregation of the protein but not in the formation of filaments. Cell Mol. Biol. (Noisy-le-grand) 1998, 44, 1111–1116. [Google Scholar]
- Necula, M.; Kuret, J. Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro. J. Biol. Chem. 2004, 279, 49694–49703. [Google Scholar] [CrossRef] [Green Version]
- Shuvaev, V.V.; Laffont, I.; Serot, J.M.; Fujii, J.; Taniguchi, N.; Siest, G. Increased protein glycation in cerebrospinal fluid of Alzheimer’s disease. Neurobiol. Aging 2001, 22, 397–402. [Google Scholar] [CrossRef]
- Iannuzzi, C.; Borriello, M.; Irace, G.; Cammarota, M.; Di Maro, A.; Sirangelo, I. Vanillin affects amyloid aggregation and non-enzymatic glycation in human insulin. Sci. Rep. 2017, 7, 15086. [Google Scholar] [CrossRef] [Green Version]
- Chen, L.; Mo, M.; Li, G.; Cen, L.; Wei, L.; Xiao, Y.; Chen, X.; Li, S.; Yang, X.; Qu, S.; et al. The biomarkers of immune dysregulation and inflammation response in Parkinson disease. Transl. Neurodegener. 2016, 5, 16. [Google Scholar] [CrossRef] [Green Version]
- Shih, R.H.; Wang, C.Y.; Yang, C.M. NF-kappaB Signaling Pathways in Neurological Inflammation: A Mini Review. Front. Mol. Neurosci. 2015, 8, 77. [Google Scholar] [CrossRef] [Green Version]
- Plastira, I.; Bernhart, E.; Joshi, L.; Koyani, C.N.; Strohmaier, H.; Reicher, H.; Malle, E.; Sattler, W. MAPK signaling determines lysophosphatidic acid (LPA)-induced inflammation in microglia. J. Neuroinflam. 2020, 17, 127. [Google Scholar] [CrossRef]
- Kim, M.E.; Na, J.Y.; Park, Y.D.; Lee, J.S. Anti-Neuroinflammatory Effects of Vanillin through the Regulation of Inflammatory Factors and NF-κB Signaling in LPS-Stimulated Microglia. Appl. Biochem. Biotechnol. 2019, 187, 884–893. [Google Scholar] [CrossRef]
- Ullah, R.; Ikram, M.; Park, T.J.; Ahmad, R.; Saeed, K.; Alam, S.I.; Rehman, I.U.; Khan, A.; Khan, I.; Jo, M.G.; et al. Vanillic Acid, a Bioactive Phenolic Compound, Counteracts LPS-Induced Neurotoxicity by Regulating c-Jun N-Terminal Kinase in Mouse Brain. Int. J. Mol. Sci. 2020, 22, 361. [Google Scholar] [CrossRef]
- Badie, B.; Schartner, J. Role of microglia in glioma biology. Microsc. Res. Tech. 2001, 54, 106–113. [Google Scholar] [CrossRef]
- Hambardzumyan, D.; Gutmann, D.H.; Kettenmann, H. The role of microglia and macrophages in glioma maintenance and progression. Nat. Neurosci. 2016, 19, 20–27. [Google Scholar] [CrossRef] [Green Version]
- Vinnakota, K.; Hu, F.; Ku, M.C.; Georgieva, P.B.; Szulzewsky, F.; Pohlmann, A.; Waiczies, S.; Waiczies, H.; Niendorf, T.; Lehnardt, S.; et al. Toll-like receptor 2 mediates microglia/brain macrophage MT1-MMP expression and glioma expansion. Neuro Oncol. 2013, 15, 1457–1468. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Triller, P.; Bachorz, J.; Synowitz, M.; Kettenmann, H.; Markovic, D. O-Vanillin Attenuates the TLR2 Mediated Tumor-Promoting Phenotype of Microglia. Int. J. Mol. Sci. 2020, 21, 2959. [Google Scholar] [CrossRef]
- Markovic, D.S.; Glass, R.; Synowitz, M.; Rooijen, N.; Kettenmann, H. Microglia stimulate the invasiveness of glioma cells by increasing the activity of metalloprotease-2. J. Neuropathol. Exp. Neurol. 2005, 64, 754–762. [Google Scholar] [CrossRef]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. |
© 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Iannuzzi, C.; Liccardo, M.; Sirangelo, I. Overview of the Role of Vanillin in Neurodegenerative Diseases and Neuropathophysiological Conditions. Int. J. Mol. Sci. 2023, 24, 1817. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms24031817
Iannuzzi C, Liccardo M, Sirangelo I. Overview of the Role of Vanillin in Neurodegenerative Diseases and Neuropathophysiological Conditions. International Journal of Molecular Sciences. 2023; 24(3):1817. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms24031817
Chicago/Turabian StyleIannuzzi, Clara, Maria Liccardo, and Ivana Sirangelo. 2023. "Overview of the Role of Vanillin in Neurodegenerative Diseases and Neuropathophysiological Conditions" International Journal of Molecular Sciences 24, no. 3: 1817. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms24031817