Therapeutic Potential of Hispidin—Fungal and Plant Polyketide
Abstract
:1. Introduction
2. Cytotoxic Effect of Hispidin on Cancer Cells
3. The Effect of Hispidin on the Metabolic Syndrome
4. Hispidin as a Potential Cardiovascular Protector
5. Potential Neuroprotective Effect of Hispidin
6. Antiviral Effects of Hispidin
7. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Hobbs, C. Medicinal Mushrooms: An Exploration of Tradition, Healing, and Culture; Botanica Press: Summertown, TN, USA, 2002; ISBN 9781570679506. [Google Scholar]
- Chen, H.; Tian, T.; Miao, H.; Zhao, Y.-Y. Traditional uses, fermentation, phytochemistry and pharmacology of Phellinus linteus: A review. Fitoterapia 2016, 113, 6–26. [Google Scholar] [CrossRef]
- Lee, I.-K.; Yun, B.-S. Styrylpyrone-class compounds from medicinal fungi Phellinus and Inonotus spp., and their medicinal importance. J. Antibiot. 2011, 64, 349–359. [Google Scholar] [CrossRef] [PubMed]
- He, P.; Zhang, Y.; Li, N. The phytochemistry and pharmacology of medicinal fungi of the genus Phellinus: A review. Food Funct. 2021, 12, 1856–1881. [Google Scholar] [CrossRef] [PubMed]
- Edwards, R.L.; Lewis, D.G.; Wilson, D.V. 983. Constituents of the higher fungi. Part I. Hispidin, a new 4-hydroxy-6-styryl-2-pyrone from polyporus hispidus (Bull.) Fr. J. Chem. Soc. 1961, 4995–5002. [Google Scholar] [CrossRef]
- Edwards, R.L.; Wilson, D.V. 984. Constituents of the higher fungi. Part II. The synthesis of hispidin. J. Chem. Soc. (Resumed) 1961, 5003–5004. [Google Scholar] [CrossRef]
- Li, I.-C.; Chen, C.C.; Sheu, S.-J.; Huang, I.-H.; Chen, C.-C. Optimized production and safety evaluation of hispidin-enriched Sanghuangporus sanghuang mycelia. Food Sci. Nutr. 2020, 8, 1864–1873. [Google Scholar] [CrossRef] [Green Version]
- Watling, R.; Gill, M.; Giménez, A.; May, T.W. A new styrylpyrone-containing Cortinarius from Australia. Mycol. Res. 1992, 96, 743–748. [Google Scholar] [CrossRef]
- Kotlobay, A.A.; Sarkisyan, K.S.; Mokrushina, Y.A.; Marcet-Houben, M.; Serebrovskaya, E.O.; Markina, N.M.; Gonzalez Somermeyer, L.; Gorokhovatsky, A.Y.; Vvedensky, A.; Purtov, K.V.; et al. Genetically encodable bioluminescent system from fungi. Proc. Natl. Acad. Sci. USA 2018, 115, 12728–12732. [Google Scholar] [CrossRef] [Green Version]
- Beckert, C.; Horn, C.; Schnitzler, J.-P.; Lehning, A.; Heller, W.; Veit, M. Styrylpyrone biosynthesis in Equisetum arvense. Phytochemistry 1997, 44, 275–283. [Google Scholar] [CrossRef]
- Pluskal, T.; Torrens-Spence, M.P.; Fallon, T.R.; De Abreu, A.; Shi, C.H.; Weng, J.-K. The biosynthetic origin of psychoactive kavalactones in kava. Nat. Plants 2019, 5, 867–878. [Google Scholar] [CrossRef] [Green Version]
- Tian, L.-W.; Feng, Y.; Tran, T.D.; Shimizu, Y.; Pfeifer, T.; Vu, H.T.; Quinn, R.J. Achyrodimer F, a tyrosyl-DNA phosphodiesterase I inhibitor from an Australian fungus of the family Cortinariaceae. Bioorg. Med. Chem. Lett. 2017, 27, 4007–4010. [Google Scholar] [CrossRef]
- Yousfi, M.; Djeridane, A.; Bombarda, I.; Chahrazed-Hamia; Duhem, B.; Gaydou, E.M. Isolation and characterization of a new hispolone derivative from antioxidant extracts ofPistacia atlantica. Phytother. Res. 2009, 23, 1237–1242. [Google Scholar] [CrossRef]
- Jung, J.-Y.; Lee, I.-K.; Seok, S.-J.; Lee, H.-J.; Kim, Y.-H.; Yun, B.-S. Antioxidant polyphenols from the mycelial culture of the medicinal fungi Inonotus xeranticus and Phellinus linteus. J. Appl. Microbiol. 2008, 104, 1824–1832. [Google Scholar] [CrossRef]
- Park, I.-H.; Chung, S.-K.; Lee, K.-B.; Yoo, Y.-C.; Kim, S.-K.; Kim, G.-S.; Song, K.-S. An antioxidant hispidin from the mycelial cultures of Phellinus linteus. Arch. Pharm. Res. 2004, 27, 615–618. [Google Scholar] [CrossRef]
- El Hassane, A.; Shah, S.A.A.; Hassan, N.B.; El Moussaoui, N.; Ahmad, R.; Zulkefeli, M.; Weber, J.-F.F. Antioxidant activity of hispidin oligomers from medicinal fungi: A DFT study. Molecules 2014, 19, 3489–3507. [Google Scholar] [PubMed] [Green Version]
- Zan, L.-F.; Qin, J.-C.; Zhang, Y.-M.; Yao, Y.-H.; Bao, H.-Y.; Li, X. Antioxidant hispidin derivatives from medicinal mushroom Inonotus hispidus. Chem. Pharm. Bull. 2011, 59, 770–772. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Zhang, H.; Chen, R.; Zhang, J.; Bu, Q.; Wang, W.; Liu, Y.; Li, Q.; Guo, Y.; Zhang, L.; Yang, Y. The integration of metabolome and proteome reveals bioactive polyphenols and hispidin in ARTP mutagenized Phellinus baumii. Sci. Rep. 2019, 9, 16172. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gonindard, C.; Bergonzi, C.; Denier, C.; Sergheraert, C.; Klaebe, A.; Chavant, L.; Hollande, E. Synthetic hispidin, a PKC inhibitor, is more cytotoxic toward cancer cells than normal cells in vitro. Cell Biol. Toxicol. 1997, 13, 141–153. [Google Scholar] [CrossRef]
- Lee, Y.S.; Kang, Y.-H.; Jung, J.-Y.; Kang, I.-J.; Han, S.-N.; Chung, J.-S.; Shin, H.-K.; Lim, S.S. Inhibitory constituents of aldose reductase in the fruiting body of Phellinus linteus. Biol. Pharm. Bull. 2008, 31, 765–768. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wangun, H.V.K.; Härtl, A.; Tam Kiet, T.; Hertweck, C. Inotilone and related phenylpropanoid polyketides from Inonotus sp. and their identification as potent COX and XO inhibitors. Org. Biomol. Chem. 2006, 4, 2545–2548. [Google Scholar] [CrossRef]
- Ali, N.A.A.; Awadh Ali, N.A.; Mothana, R.A.A.; Lesnau, A.; Pilgrim, H.; Lindequist, U. Antiviral activity of Inonotus hispidus. Fitoterapia 2003, 74, 483–485. [Google Scholar]
- Park, I.-H.; Jeon, S.-Y.; Lee, H.-J.; Kim, S.-I.; Song, K.-S. A beta-secretase (BACE1) inhibitor hispidin from the mycelial cultures of Phellinus linteus. Planta Med. 2004, 70, 143–146. [Google Scholar]
- WHO. Key Facts about Cancer; WHO: Geneva, Switzerland, 2018. [Google Scholar]
- Roy, P.S.; Saikia, B.J. Cancer and cure: A critical analysis. Indian J. Cancer 2016, 53, 441–442. [Google Scholar]
- Joseph, T.P.; Chanda, W.; Padhiar, A.A.; Batool, S.; LiQun, S.; Zhong, M.; Huang, M. A Preclinical Evaluation of the Antitumor Activities of Edible and Medicinal Mushrooms: A Molecular Insight. Integr. Cancer Ther. 2018, 17, 200–209. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chen, W.; Tan, H.; Liu, Q.; Zheng, X.; Zhang, H.; Liu, Y.; Xu, L. A Review: The Bioactivities and Pharmacological Applications of Phellinus linteus. Molecules 2019, 24, 1888. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lim, J.-H.; Lee, Y.-M.; Park, S.R.; Kim, D.H.; Lim, B.O. Anticancer activity of hispidin via reactive oxygen species-mediated apoptosis in colon cancer cells. Anticancer Res. 2014, 34, 4087–4093. [Google Scholar] [PubMed]
- Nguyen, B.C.Q.; Taira, N.; Maruta, H.; Tawata, S. Artepillin C and other herbal PAK1-blockers: Effects on hair cell proliferation and related PAK1-dependent biological function in cell culture. Phytother. Res. 2016, 30, 120–127. [Google Scholar] [CrossRef]
- Lv, L.-X.; Zhou, Z.-X.; Zhou, Z.; Zhang, L.-J.; Yan, R.; Zhao, Z.; Yang, L.-Y.; Bian, X.-Y.; Jiang, H.-Y.; Li, Y.-D.; et al. Hispidin induces autophagic and necrotic death in SGC-7901 gastric cancer cells through lysosomal membrane permeabilization by inhibiting tubulin polymerization. Oncotarget 2017, 8, 26992–27006. [Google Scholar] [CrossRef]
- Chandimali, N.; Huynh, D.O.L.; Jin, W.Y.; Kwon, T. Combination Effects of Hispidin and Gemcitabine via Inhibition of Stemness in Pancreatic Cancer Stem Cells. Anticancer Res. 2018, 38, 3967–3975. [Google Scholar] [CrossRef]
- Isakov, N. Protein kinase C (PKC) isoforms in cancer, tumor promotion and tumor suppression. Semin. Cancer Biol. 2018, 48, 36–52. [Google Scholar] [CrossRef]
- Pellicano, F.; Copland, M.; Jorgensen, H.G.; Mountford, J.; Leber, B.; Holyoake, T.L. BMS-214662 induces mitochondrial apoptosis in chronic myeloid leukemia (CML) stem/progenitor cells, including CD34 38−cells, through activation of protein kinase Cβ. Blood 2009, 114, 4186–4196. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Grosso, S.; Volta, V.; Sala, L.A.; Vietri, M.; Marchisio, P.C.; Ron, D.; Biffo, S. PKCβII modulates translation independently from mTOR and through RACK1. Biochem. J. 2008, 415, 77–85. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hernández-Méndez, A.; Alcántara-Hernández, R.; Acosta-Cervantes, G.C.; Martínez-Ortiz, J.; Avendaño-Vázquez, S.E.; García-Sáinz, J.A. Conventional protein kinase C isoforms mediate phorbol ester-induced lysophosphatidic acid LPA1 receptor phosphorylation. Eur. J. Pharmacol. 2014, 723, 124–130. [Google Scholar] [CrossRef] [PubMed]
- Piao, S.; Amaravadi, R.K. Targeting the lysosome in cancer. Ann. N. Y. Acad. Sci. 2016, 1371, 45–54. [Google Scholar] [CrossRef] [Green Version]
- Tu, P.T.B.; Chompoo, J.; Tawata, S. Hispidin and related herbal compounds from Alpinia zerumbet inhibit both PAK1-dependent melanogenesis in melanocytes and reactive oxygen species (ROS) production in adipocytes. Drug Discov. Ther. 2015, 9, 197–204. [Google Scholar]
- Park, J.M.; Lee, J.S.; Song, J.E.; Sim, Y.C.; Ha, S.-J.; Hong, E.K. Cytoprotective effect of hispidin against palmitate-induced lipotoxicity in C2C12 myotubes. Molecules 2015, 20, 5456–5467. [Google Scholar] [CrossRef] [PubMed]
- Jang, J.S.; Lee, J.S.; Lee, J.H.; Kwon, D.S.; Lee, K.E.; Lee, S.Y.; Hong, E.K. Hispidin produced from Phellinus linteus protects pancreatic β-cells from damage by hydrogen peroxide. Arch. Pharm. Res. 2010, 33, 853–861. [Google Scholar] [CrossRef] [PubMed]
- Song, T.-Y.; Yang, N.-C.; Chen, C.-L.; Thi, T.L.V. Protective Effects and Possible Mechanisms of Ergothioneine and Hispidin against Methylglyoxal-Induced Injuries in Rat Pheochromocytoma Cells. Oxid. Med. Cell. Longev. 2017, 2017, 4824371. [Google Scholar] [CrossRef] [Green Version]
- Lee, J.H.; Lee, J.S.; Kim, Y.R.; Jung, W.C.; Lee, K.E.; Lee, S.Y.; Hong, E.K. Hispidin Isolated from Phellinus linteus Protects Against Hydrogen Peroxide–Induced Oxidative Stress in Pancreatic MIN6N β-Cells. J. Med. Food 2011, 14, 1431–1438. [Google Scholar] [CrossRef]
- Arlt, A.; Gehrz, A.; Müerköster, S.; Vorndamm, J.; Kruse, M.-L.; Fölsch, U.R.; Schäfer, H. Role of NF-κB and Akt/PI3K in the resistance of pancreatic carcinoma cell lines against gemcitabine-induced cell death. Oncogene 2003, 22, 3243–3251. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Xie, C.; Liu, D.; Chen, Q.; Yang, C.; Wang, B.; Wu, H. Soluble B7-H3 promotes the invasion and metastasis of pancreatic carcinoma cells through the TLR4/NF-κB pathway. Sci. Rep. 2016, 6, 27528. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Smolskaite, L.; Slapšyte, G.; Mierauskiene, J.; Dedonyte, V.; Venskutonis, P.R. Antioxidant and Genotoxic Properties of Hispidin Isolated from the Velvet-Top Mushroom, Phaeolus schweinitzii (Agaricomycetes). Int. J. Med. Mushrooms 2017, 19, 967–980. [Google Scholar] [CrossRef]
- Zhao, H.; Duan, Q.; Zhang, Z.; Li, H.; Wu, H.; Shen, Q.; Wang, C.; Yin, T. Up-regulation of glycolysis promotes the stemness and EMT phenotypes in gemcitabine-resistant pancreatic cancer cells. J. Cell. Mol. Med. 2017, 21, 2055–2067. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Saklayen, M.G. The Global Epidemic of the Metabolic Syndrome. Curr. Hypertens. Rep. 2018, 20, 12. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- McCracken, E.; Monaghan, M.; Sreenivasan, S. Pathophysiology of the metabolic syndrome. Clin. Dermatol. 2018, 36, 14–20. [Google Scholar] [CrossRef]
- Yazıcı, D.; Sezer, H. Insulin Resistance, Obesity and Lipotoxicity. In Obesity and Lipotoxicity; Engin, A.B., Engin, A., Eds.; Springer International Publishing: Cham, Switzerland, 2017; pp. 277–304. ISBN 9783319483825. [Google Scholar]
- Wang, Y.W.; Jones, P.J.H. Conjugated linoleic acid and obesity control: Efficacy and mechanisms. Int. J. Obes. Relat. Metab. Disord. 2004, 28, 941–955. [Google Scholar] [CrossRef] [Green Version]
- Liu, T.-T.; Liu, X.-T.; Chen, Q.-X.; Shi, Y. Lipase Inhibitors for Obesity: A Review. Biomed. Pharmacother. 2020, 128, 110314. [Google Scholar] [CrossRef]
- Tu, P.T.B.; Tawata, S. Anti-obesity effects of hispidin and Alpinia zerumbet bioactives in 3T3-L1 adipocytes. Molecules 2014, 19, 16656–16671. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Holm, C.; Osterlund, T.; Laurell, H.; Contreras, J.A. Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Annu. Rev. Nutr. 2000, 20, 365–393. [Google Scholar] [CrossRef] [Green Version]
- De Luca, C.; Olefsky, J.M. Inflammation and insulin resistance. FEBS Lett. 2008, 582, 97–105. [Google Scholar] [CrossRef] [Green Version]
- Björnholm, M.; Zierath, J.R. Insulin signal transduction in human skeletal muscle: Identifying the defects in Type II diabetes. Biochem. Soc. Trans. 2005, 33, 354–357. [Google Scholar] [CrossRef] [Green Version]
- Wei, Y.; Chen, K.; Whaley-Connell, A.T.; Stump, C.S.; Ibdah, J.A.; Sowers, J.R. Skeletal muscle insulin resistance: Role of inflammatory cytokines and reactive oxygen species. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2008, 294, R673–R680. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Giardino, I.; Edelstein, D.; Brownlee, M. BCL-2 expression or antioxidants prevent hyperglycemia-induced formation of intracellular advanced glycation endproducts in bovine endothelial cells. J. Clin. Investig. 1996, 97, 1422–1428. [Google Scholar] [CrossRef]
- Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 414, 813–820. [Google Scholar] [CrossRef] [PubMed]
- Stern, D.; Yan, S.D.; Yan, S.F.; Schmidt, A.M. Receptor for advanced glycation endproducts: A multiligand receptor magnifying cell stress in diverse pathologic settings. Adv. Drug Deliv. Rev. 2002, 54, 1615–1625. [Google Scholar] [CrossRef]
- Lee, Y.S.; Kang, Y.-H.; Jung, J.-Y.; Lee, S.; Ohuchi, K.; Shin, K.H.; Kang, I.-J.; Park, J.H.Y.; Shin, H.-K.; Lim, S.S. Protein glycation inhibitors from the fruiting body of Phellinus linteus. Biol. Pharm. Bull. 2008, 31, 1968–1972. [Google Scholar] [CrossRef] [Green Version]
- Reddy, V.P.; Prakash Reddy, V.; Beyaz, A. Inhibitors of the Maillard reaction and AGE breakers as therapeutics for multiple diseases. Drug Discov. Today 2006, 11, 646–654. [Google Scholar] [CrossRef]
- Johnson, T.O.; Ermolieff, J.; Jirousek, M.R. Protein tyrosine phosphatase 1B inhibitors for diabetes. Nat. Rev. Drug Discov. 2002, 1, 696–709. [Google Scholar] [CrossRef]
- Liu, G.; Trevillyan, J.M. Protein tyrosine phosphatase 1B as a target for the treatment of impaired glucose tolerance and type II diabetes. Curr. Opin. Investig. Drugs 2002, 3, 1608–1616. [Google Scholar]
- Taylor, S.D.; Hill, B. Recent advances in protein tyrosine phosphatase 1B inhibitors. Expert Opin. Investig. Drugs 2004, 13, 199–214. [Google Scholar] [CrossRef]
- Cho, S.-Y.; Ahn, J.-H.; Ha, J.-D.; Kang, S.-K.; Baek, J.-Y.; Han, S.-S.; Shin, E.-Y.; Kim, S.-S.; Kim, K.-R.; Cheon, H.-G.; et al. Protein Tyrosine Phosphatase 1B Inhibitors: Heterocyclic Carboxylic Acids. Bull. Korean Chem. Soc. 2003, 24, 1455–1464. [Google Scholar] [CrossRef]
- Lee, Y.S.; Kang, I.-J.; Won, M.H.; Lee, J.-Y.; Kim, J.K.; Lim, S.S. Inhibition of Protein Tyrosine Phosphatase 1β by Hispidin Derivatives Isolated from the Fruiting Body of Phellinus linteus. Nat. Prod. Commun. 2010, 5. [Google Scholar] [CrossRef] [Green Version]
- Remedi, M.S.; Emfinger, C. Pancreatic β-cell identity in diabetes. Diabetes Obes. Metab. 2016, 18, 110–116. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Rolo, A.P.; Palmeira, C.M. Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress. Toxicol. Appl. Pharmacol. 2006, 212, 167–178. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Incalza, M.A.; D’Oria, R.; Natalicchio, A.; Perrini, S.; Laviola, L.; Giorgino, F. Oxidative stress and reactive oxygen species in endothelial dysfunction associated with cardiovascular and metabolic diseases. Vasc. Pharmacol. 2018, 100, 1–19. [Google Scholar] [CrossRef]
- Takano, H.; Zou, Y.; Hasegawa, H.; Akazawa, H.; Nagai, T.; Komuro, I. Oxidative stress-induced signal transduction pathways in cardiac myocytes: Involvement of ROS in heart diseases. Antioxid. Redox Signal. 2003, 5, 789–794. [Google Scholar] [CrossRef]
- Endemann, D.H.; Schiffrin, E.L. Endothelial dysfunction. J. Am. Soc. Nephrol. 2004, 15, 1983–1992. [Google Scholar] [CrossRef]
- Kim, D.-E.; Kim, B.; Shin, H.-S.; Kwon, H.J.; Park, E.-S. The protective effect of hispidin against hydrogen peroxide-induced apoptosis in H9c2 cardiomyoblast cells through Akt/GSK-3β and ERK1/2 signaling pathway. Exp. Cell Res. 2014, 327, 264–275. [Google Scholar] [CrossRef]
- Amaravadi, R.; Thompson, C.B. The survival kinases Akt and Pim as potential pharmacological targets. J. Clin. Investig. 2005, 115, 2618–2624. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Yamaguchi, H.; Wang, H.G. The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change. Oncogene 2001, 20, 7779–7786. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Weston, C.R.; Balmanno, K.; Chalmers, C.; Hadfield, K.; Molton, S.A.; Ley, R.; Wagner, E.F.; Cook, S.J. Activation of ERK1/2 by ΔRaf-1: ER* represses Bim expression independently of the JNK or PI3K pathways. Oncogene 2003, 22, 1281–1293. [Google Scholar] [CrossRef] [Green Version]
- Naruse, K.; Rask-Madsen, C.; Takahara, N.; Ha, S.-W.; Suzuma, K.; Way, K.J.; Jacobs, J.R.C.; Clermont, A.C.; Ueki, K.; Ohshiro, Y.; et al. Activation of Vascular Protein Kinase C- Inhibits Akt-Dependent Endothelial Nitric Oxide Synthase Function in Obesity-Associated Insulin Resistance. Diabetes 2006, 55, 691–698. [Google Scholar] [CrossRef] [Green Version]
- Li, D.; Liu, L.; Chen, H.; Sawamura, T.; Ranganathan, S.; Mehta, J.L. LOX-1 mediates oxidized low-density lipoprotein-induced expression of matrix metalloproteinases in human coronary artery endothelial cells. Circulation 2003, 107, 612–617. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, Y.-B.; Zhang, Q.-H.; Chen, Z.; He, Z.-J.; Yi, G.-H. Oxidized low-density lipoprotein attenuated desmoglein 1 and desmocollin 2 expression via LOX-1/Ca(2+)/PKC-β signal in human umbilical vein endothelial cells. Biochem. Biophys. Res. Commun. 2015, 468, 380–386. [Google Scholar] [CrossRef] [PubMed]
- Yuan, S.Y.; Ustinova, E.E.; Wu, M.H.; Tinsley, J.H.; Xu, W.; Korompai, F.L.; Taulman, A.C. Protein kinase C activation contributes to microvascular barrier dysfunction in the heart at early stages of diabetes. Circ. Res. 2000, 87, 412–417. [Google Scholar] [CrossRef] [Green Version]
- Curigliano, G.; Cardinale, D.; Dent, S.; Criscitiello, C.; Aseyev, O.; Lenihan, D.; Cipolla, C.M. Cardiotoxicity of anticancer treatments: Epidemiology, detection, and management. CA Cancer J. Clin. 2016, 66, 309–325. [Google Scholar] [CrossRef] [Green Version]
- Carvalho, F.S.; Burgeiro, A.; Garcia, R.; Moreno, A.J.; Carvalho, R.A.; Oliveira, P.J. Doxorubicin-Induced Cardiotoxicity: From Bioenergetic Failure and Cell Death to Cardiomyopathy. Med. Res. Rev. 2014, 34, 106–135. [Google Scholar] [CrossRef]
- Sampaio, S.F.; Branco, A.F.; Wojtala, A.; Vega-Naredo, I.; Wieckowski, M.R.; Oliveira, P.J. p66Shc signaling is involved in stress responses elicited by anthracycline treatment of rat cardiomyoblasts. Arch. Toxicol. 2016, 90, 1669–1684. [Google Scholar] [CrossRef]
- Pinton, P.; Rizzuto, R. p66Shc, oxidative stress and aging: Importing a lifespan determinant into mitochondria. Cell Cycle 2008, 7, 304–308. [Google Scholar] [CrossRef] [Green Version]
- Moreira, A.C.; Branco, A.F.; Sampaio, S.F.; Cunha-Oliveira, T.; Martins, T.R.; Holy, J.; Oliveira, P.J.; Sardão, V.A. Mitochondrial apoptosis-inducing factor is involved in doxorubicin-induced toxicity on H9c2 cardiomyoblasts. Biochim. Biophys. Acta 2014, 1842, 2468–2478. [Google Scholar] [CrossRef] [Green Version]
- Wojtala, A.; Karkucinska-Wieckowska, A.; Sardao, V.A.; Szczepanowska, J.; Kowalski, P.; Pronicki, M.; Duszynski, J.; Wieckowski, M.R. Modulation of mitochondrial dysfunction-related oxidative stress in fibroblasts of patients with Leigh syndrome by inhibition of prooxidative p66Shc pathway. Mitochondrion 2017, 37, 62–79. [Google Scholar] [CrossRef]
- Dugger, B.N.; Dickson, D.W. Pathology of Neurodegenerative Diseases. Cold Spring Harb. Perspect. Biol. 2017, 9, a028035. [Google Scholar] [CrossRef]
- Lin, M.T.; Beal, M.F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006, 443, 787–795. [Google Scholar] [CrossRef]
- Golpich, M.; Amini, E.; Mohamed, Z.; Azman Ali, R.; Mohamed Ibrahim, N.; Ahmadiani, A. Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment. CNS Neurosci. Ther. 2017, 23, 5–22. [Google Scholar] [CrossRef] [PubMed]
- Khandhadia, S.; Lotery, A. Oxidation and age-related macular degeneration: Insights from molecular biology. Expert Rev. Mol. Med. 2010, 12, e34. [Google Scholar] [CrossRef]
- Huang, S.-Y.; Chang, S.-F.; Chau, S.-F.; Chiu, S.-C. The Protective Effect of Hispidin against Hydrogen Peroxide-Induced Oxidative Stress in ARPE-19 Cells via Nrf2 Signaling Pathway. Biomolecules 2019, 9, 380. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lebiedzinska, M.; Karkucinska-Wieckowska, A.; Giorgi, C.; Karczmarewicz, E.; Pronicka, E.; Pinton, P.; Duszynski, J.; Pronicki, M.; Wieckowski, M.R. Oxidative stress-dependent p66Shc phosphorylation in skin fibroblasts of children with mitochondrial disorders. Biochim. Biophys. Acta 2010, 1797, 952–960. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sherer, T.B.; Betarbet, R.; Greenamyre, J.T. Pathogenesis of Parkinson’s disease. Curr. Opin. Investig. Drugs 2001, 2, 657–662. [Google Scholar]
- Yamamori, T.; Mizobata, A.; Saito, Y.; Urano, Y.; Inanami, O.; Irani, K.; Noguchi, N. Phosphorylation of p66shc mediates 6-hydroxydopamine cytotoxicity. Free Radic. Res. 2011, 45, 342–350. [Google Scholar] [CrossRef]
- Citron, M. Alzheimer’s disease: Treatments in discovery and development. Nat. Neurosci. 2002, 5, 1055–1057. [Google Scholar] [CrossRef]
- Bennett, L.; Sheean, P.; Zabaras, D.; Head, R. Heat-stable components of wood ear mushroom, Auricularia polytricha (higher Basidiomycetes), inhibit in vitro activity of beta secretase (BACE1). Int. J. Med. Mushrooms 2013, 15, 233–249. [Google Scholar] [CrossRef]
- Ischiropoulos, H.; Beckman, J.S. Oxidative stress and nitration in neurodegeneration: Cause, effect, or association? J. Clin. Investig. 2003, 111, 163–169. [Google Scholar] [CrossRef] [Green Version]
- Szabó, C. Multiple pathways of peroxynitrite cytotoxicity. Toxicol. Lett. 2003, 140–141, 105–112. [Google Scholar] [CrossRef]
- Chen, W.; Feng, L.; Huang, Z.; Su, H. Hispidin produced from Phellinus linteus protects against peroxynitrite-mediated DNA damage and hydroxyl radical generation. Chem. Biol. Interact. 2012, 199, 137–142. [Google Scholar] [CrossRef]
- Shin, E.-J.; Duong, C.X.; Nguyen, X.-K.T.; Li, Z.; Bing, G.; Bach, J.-H.; Park, D.H.; Nakayama, K.; Ali, S.F.; Kanthasamy, A.G.; et al. Role of oxidative stress in methamphetamine-induced dopaminergic toxicity mediated by protein kinase Cδ. Behav. Brain Res. 2012, 232, 98–113. [Google Scholar] [CrossRef] [Green Version]
- Hwang, B.S.; Lee, I.-K.; Choi, H.J.; Yun, B.-S. Anti-influenza activities of polyphenols from the medicinal mushroom Phellinus baumii. Bioorg. Med. Chem. Lett. 2015, 25, 3256–3260. [Google Scholar] [CrossRef] [PubMed]
- Yeom, J.-H.; Lee, I.-K.; Ki, D.-W.; Lee, M.-S.; Seok, S.-J.; Yun, B.-S. Neuraminidase Inhibitors from the Culture Broth of Phellinus linteus. Mycobiology 2012, 40, 142–144. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Serseg, T.; Benarous, K.; Yousfi, M. Hispidin and Lepidine E: Two Natural Compounds and Folic acid as Potential Inhibitors of 2019-novel coronavirus Main Protease (2019-nCoVMpro), molecular docking and SAR study. Curr. Comput. Aided Drug Des. 2020, 16, 1–14. [Google Scholar] [CrossRef] [PubMed]
- Lehrer, S.; Rheinstein, P.H. Ivermectin Docks to the SARS-CoV-2 Spike Receptor-binding Domain Attached to ACE2. In Vivo 2020, 34, 3023–3026. [Google Scholar] [CrossRef]
- Maddu, N. Diseases Related to Types of Free Radicals. In Antioxidants; Shalaby, E., Ed.; IntechOpen: Rijeka, Croatia, 2019. [Google Scholar]
- Kozlowski, D.; Marsal, P.; Steel, M.; Mokrini, R.; Duroux, J.-L.; Lazzaroni, R.; Trouillas, P. Theoretical investigation of the formation of a new series of antioxidant depsides from the radiolysis of flavonoid compounds. Radiat. Res. 2007, 168, 243–252. [Google Scholar] [CrossRef]
- Priyadarsini, K.I.; Indira Priyadarsini, K.; Maity, D.K.; Naik, G.H.; Sudheer Kumar, M.; Unnikrishnan, M.K.; Satav, J.G.; Mohan, H. Role of phenolic O-H and methylene hydrogen on the free radical reactions and antioxidant activity of curcumin. Free Radic. Biol. Med. 2003, 35, 475–484. [Google Scholar] [CrossRef]
- Tamrakar, S.; Fukami, K.; Parajuli, G.P.; Shimizu, K. Antiallergic Activity of the Wild Mushrooms of Nepal and the Pure Compound Hispidin. J. Med. Food 2019, 22, 225–227. [Google Scholar] [CrossRef] [PubMed]
Cell Line | Approximate Semilethal Hispidin Dose, mol/L |
---|---|
Skin squamous cell carcinoma SCL-1 [19] | 1 × 10−4 |
Pancreatic ductal adenocarcinoma Capan-1 [19] | Between 1 × 10−4 and 1 × 10−3 |
Rectal carcinoma CMT-93 [28] | 7 ± 1 × 10−4 |
Colorectal carcinoma HCT 116 [28] | 7 ± 1 × 10−4 |
Lung carcinoma A549 [29] | 2.5 × 10−4 |
Endocervical adenocarcinoma SGC-7901 [30] | 6.1 ± 1.1 × 10−3 |
Pancreatic ductal adenocarcinoma BxPC-3 [31] | 1 × 10−4 |
Pancreatic ductal adenocarcinoma AsPC-1 [31] | 2 × 10−4 |
Bioactive Property of Hispidin | Cytotoxic Effect | The Effect on Carbohydrate and Lipid Metabolism | Possible Neuroprotective Effect | Possible Cardioprotective Effect | Antiviral Effect |
---|---|---|---|---|---|
Free radical scavenger | Direct antioxidant activity and reduction of oxidative stress | ||||
↓PAK1 and NF-kB signaling—anti-inflammatory activity | |||||
↑Gene expression of antioxidant enzymes that (but not only) control apoptosis | |||||
Inhibitor of activities of proteins | ↓Protein kinase C | ↓Caspase-3 ↓Caspase-9 | ↓Neuraminidases | ||
↓Aldose reductase ↓GPDH ↓PTP1β | ↓p66Shc | ||||
↓BACE1 | |||||
Regulator of pro- and anti-apoptotic proteins interplay | Tumor cell death | Survival of myoblasts | Survival of cardiomyoblasts | ||
Anti-apoptotic proteins levels | ↓ | ↑ | ↑ | ||
Pro-apoptotic proteins levels | ↑ | ↓ | ↓ |
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. |
© 2021 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
Palkina, K.A.; Ipatova, D.A.; Shakhova, E.S.; Balakireva, A.V.; Markina, N.M. Therapeutic Potential of Hispidin—Fungal and Plant Polyketide. J. Fungi 2021, 7, 323. https://doi.org/10.3390/jof7050323
Palkina KA, Ipatova DA, Shakhova ES, Balakireva AV, Markina NM. Therapeutic Potential of Hispidin—Fungal and Plant Polyketide. Journal of Fungi. 2021; 7(5):323. https://doi.org/10.3390/jof7050323
Chicago/Turabian StylePalkina, Kseniia A., Daria A. Ipatova, Ekaterina S. Shakhova, Anastasia V. Balakireva, and Nadezhda M. Markina. 2021. "Therapeutic Potential of Hispidin—Fungal and Plant Polyketide" Journal of Fungi 7, no. 5: 323. https://doi.org/10.3390/jof7050323