The Modulatory Influence of Plant-Derived Compounds on Human Keratinocyte Function
Abstract
:1. Introduction
2. Criteria for Paper Selection
3. Plant Secondary Metabolites
4. Keratinocyte Characteristics
5. Modulatory Effect of Plant Secondary Metabolites on Keratinocytes Exposed to ROS
6. The Modulatory Effect of Plant Secondary Metabolites on Keratinocytes Involved in the Inflammation Process Triggered by Physical, Chemical or Biological Agents
7. The Effect of Plant Secondary Metabolite Treatment on Keratinocytes Exposed to UV-Radiation
8. Modulatory Effect of Plant Secondary Metabolites on Keratinocytes Involved in the Wound Healing Process Triggered by Disruption of the Epidermal Barrier
9. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Erb, M.; Kliebenstein, D.J. Plant Secondary Metabolites as Defenses, Regulators, and Primary Metabolites: The Blurred Functional Trichotomy. Plant Physiol. 2020, 184, 39–52. [Google Scholar] [CrossRef] [PubMed]
- Wickett, R.R.; Visscher, M.O. Structure and function of the epidermal barrier. Am. J. Infect. Control 2006, 34, S98–S110. [Google Scholar] [CrossRef]
- Kasote, D.M.; Katyare, S.S.; Hegde, M.V.; Bae, H. Significance of antioxidant potential of plants and its relevance to therapeutic applications. Int. J. Biol. Sci. 2015, 11, 982–991. [Google Scholar] [CrossRef] [Green Version]
- Nunes, C.R.; Arantes, M.B.; de Faria Pereira, S.M.; da Cruz, L.L.; de Souza Passos, M.; de Moraes, L.P.; Vieira, I.J.C.; de Oliveira, D.B. Plants as Sources of Anti-Inflammatory Agents. Molecules 2020, 25, 3726. [Google Scholar] [CrossRef]
- De Jager, T.L.; Cockrell, A.E.; Du Plessis, S.S. Ultraviolet light induced generation of reactive oxygen species. Adv. Exp. Med. Biol. 2017, 996, 15–23. [Google Scholar] [CrossRef] [PubMed]
- Ciążyńska, M.; Olejniczak-Staruch, I.; Sobolewska-Sztychny, D.; Narbutt, J.; Skibińska, M.; Lesiak, A. Ultraviolet radiation and chronic inflammation-molecules and mechanisms involved in skin carcinogenesis: A narrative review. Life 2021, 11, 326. [Google Scholar] [CrossRef]
- Pastar, I.; Stojadinovic, O.; Tomic-Canic, M. Role of keratinocytes in healing of chronic wounds. Surg. Technol. Int. 2008, 17, 105–112. [Google Scholar]
- Teoh, E.S. Secondary Metabolites of Plants. In Medicinal Orchids of Asia; Springer: Berlin/Heidelberg, Germany, 2016; pp. 59–73. [Google Scholar] [CrossRef]
- Hussein, A.R.; El-Anssary, A.A. Plants Secondary Metabolites: The Key Drivers of the Pharmacological Actions of Medicinal Plants. In Herbal Medicine; IntechOpen Limited: London, UK, 2019. [Google Scholar]
- Merecz-Sadowska, A.; Sitarek, P.; Kucharska, E.; Kowalczyk, T.; Zajdel, K.; Cegliński, T.; Zajdel, R. Antioxidant properties of plant-derived phenolic compounds and their effect on skin fibroblast cells. Antioxidants 2021, 10, 726. [Google Scholar] [CrossRef]
- Merecz-Sadowska, A.; Sitarek, P.; Śliwiński, T.; Zajdel, R. Anti-inflammatory activity of extracts and pure compounds derived from plants via modulation of signaling pathways, especially PI3K/akt in macrophages. Int. J. Mol. Sci. 2020, 21, 9605. [Google Scholar] [CrossRef]
- Sitarek, P.; Merecz-Sadowska, A.; Śliwiński, T.; Zajdel, R.; Kowalczyk, T. An in vitro evaluation of the molecular mechanisms of action of medical plants from the lamiaceae family as effective sources of active compounds against human cancer cell lines. Cancers 2020, 12, 2957. [Google Scholar] [CrossRef] [PubMed]
- Josiah, A.J.; Twilley, D.; Pillai, S.K.; Ray, S.S.; Lall, N. Pathogenesis of Keratinocyte Carcinomas and the Therapeutic Potential of Medicinal Plants and Phytochemicals. Molecules 2021, 26, 1979. [Google Scholar] [CrossRef]
- Sitarek, P.; Merecz-Sadowska, A.; Kowalczyk, T.; Wieczfinska, J.; Zajdel, R.; Śliwiński, T. Potential synergistic action of bioactive compounds from plant extracts against skin infecting microorganisms. Int. J. Mol. Sci. 2020, 21, 5105. [Google Scholar] [CrossRef]
- Sitarek, P.; Kowalczyk, T.; Wieczfinska, J.; Merecz-Sadowska, A.; Górski, K.; Śliwiński, T.; Skała, E. Plant extracts as a natural source of bioactive compounds and potential remedy for the treatment of certain skin diseases. Curr. Pharm. Des. 2020, 26, 2859–2875. [Google Scholar] [CrossRef]
- Zielinska-Blizniewska, H.; Sitarek, P.; Merecz-Sadowska, A.; Malinowska, K.; Zajdel, K.; Jablonska, M.; Sliwinski, T.; Zajdel, R. Plant extracts and reactive oxygen species as two counteracting agents with anti- and pro-obesity properties. Int. J. Mol. Sci. 2019, 20, 4556. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Chiocchio, I.; Mandrone, M.; Tomasi, P.; Marincich, L.; Poli, F. Plant secondary metabolites: An opportunity for circular economy. Molecules 2021, 26, 495. [Google Scholar] [CrossRef]
- Ekor, M. The growing use of herbal medicines: Issues relating to adverse reactions and challenges in monitoring safety. Front. Neurol. 2014, 4, 177. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Abubakar, A.R.; Haque, M. Preparation of medicinal plants: Basic extraction and fractionation procedures for experimental purposes. J. Pharm. Bioallied Sci. 2020, 12, 1–10. [Google Scholar] [CrossRef]
- Atanasov, A.G.; Waltenberger, B.; Pferschy-Wenzig, E.M.; Linder, T.; Wawrosch, C.; Uhrin, P.; Temml, V.; Wang, L.; Schwaiger, S.; Heiss, E.H.; et al. Discovery and resupply of pharmacologically active plant-derived natural products: A review. Biotechnol. Adv. 2015, 33, 1582–1614. [Google Scholar] [CrossRef] [Green Version]
- Abdo, J.M.; Sopko, N.A.; Milner, S.M. The applied anatomy of human skin: A model for regeneration. Wound Med. 2020, 28, 100179. [Google Scholar] [CrossRef]
- Apalla, Z.; Nashan, D.; Weller, R.B.; Castellsagué, X. Skin Cancer: Epidemiology, Disease Burden, Pathophysiology, Diagnosis, and Therapeutic Approaches. Dermatol. Ther. 2017, 7 (Suppl. 1), 5–19. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Botchkarev, V.A.; Gdula, M.R.; Mardaryev, A.N.; Sharov, A.A.; Fessing, M.Y. Epigenetic regulation of gene expression in keratinocytes. J. Investig. Dermatol. 2012, 132, 2505–2521. [Google Scholar] [CrossRef] [Green Version]
- Tomic-Canic, M.; Komine, M.; Freedberg, I.M.; Blumenberg, M. Epidermal signal transduction and transcription factor activation in activated keratinocytes. J. Dermatol. Sci. 1998, 17, 167–181. [Google Scholar] [CrossRef]
- Jost, M.; Huggett, T.M.; Kari, C.; Rodeck, U. Matrix-independent survival of human keratinocytes through an EGF receptor/MAPK-kinase-dependent pathway. Mol. Biol. Cell. 2001, 12, 1519–1527. [Google Scholar] [CrossRef] [Green Version]
- Deucher, A.; Efimova, T.; Eckert, R.L. Calcium-dependent involucrin expression is inversely regulated by protein kinase C (PKC)α and PKCδ. J. Biol. Chem. 2002, 277, 17032–17040. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Meng, X.; Qiu, L.; Song, H.; Dang, N. MAPK pathway involved in epidermal terminal differentiation of normal human epidermal keratinocytes. Open Med. 2018, 13, 189–195. [Google Scholar] [CrossRef]
- Yano, S.; Komine, M.; Fujimoto, M.; Okochi, H.; Tamaki, K. Mechanical stretching in vitro regulates signal transduction pathways and cellular proliferation in human epidermal keratinocytes. J. Investig. Dermatol. 2004, 122, 783–790. [Google Scholar] [CrossRef] [Green Version]
- El Darzi, E.; Bazzi, S.; Daoud, S.; Echtay, K.S.; Bahr, G.M. Differential regulation of surface receptor expression, proliferation, and apoptosis in HaCaT cells stimulated with interferon-3, interleukin-4, tumor necrosis factor-α, or muramyl dipeptide. Int. J. Immunopathol. Pharmacol. 2017, 30, 130–145. [Google Scholar] [CrossRef] [Green Version]
- Mitev, V.; Miteva, L. Signal transduction in keratinocytes. Exp. Dermatol. 1999, 8, 96–108. [Google Scholar] [CrossRef] [Green Version]
- Sun, L.R.; Zhou, W.; Zhang, H.M.; Guo, Q.S.; Yang, W.; Li, B.J.; Sun, Z.H.; Gao, S.H.; Cui, R.J. Modulation of Multiple Signaling Pathways of the Plant-Derived Natural Products in Cancer. Front. Oncol. 2019, 9, 1153. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Gupta, A.; Rosenberger, S.F.; Bowden, G.T. Increased ROS levels contribute to elevated transcription factor and MAP kinase activities in malignantly progressed mouse keratinocyte cell lines. Carcinogenesis 1999, 20, 2063–2073. [Google Scholar] [CrossRef] [Green Version]
- Bito, T.; Nishigori, C. Impact of reactive oxygen species on keratinocyte signaling pathways. J. Dermatol. Sci. 2012, 68, 3–8. [Google Scholar] [CrossRef] [PubMed]
- Leopoldini, M.; Marino, T.; Russo, N.; Toscano, M. Antioxidant properties of phenolic compounds: H-atom versus electron transfer mechanism. J. Phys. Chem. A 2004, 108, 4916–4922. [Google Scholar] [CrossRef]
- Dangles, O. Antioxidant Activity of Plant Phenols: Chemical Mechanisms and Biological Significance. Curr. Org. Chem. 2012, 16, 692–714. [Google Scholar] [CrossRef]
- Minatel, I.O.; Borges, C.V.; Ferreira, M.I.; Gomez, H.A.G.; Chen, C.-Y.O.; Lima, G.P.P. Phenolic Compounds: Functional Properties, Impact of Processing and Bioavailability. In Phenolic Compounds—Biological Activity; IntechOpen Limited: London, UK, 2017. [Google Scholar]
- Mussard, E.; Jousselin, S.; Cesaro, A.; Legrain, B.; Lespessailles, E.; Esteve, E.; Berteina-raboin, S.; Toumi, H. Andrographis paniculata and its bioactive diterpenoids against inflammation and oxidative stress in keratinocytes. Antioxidants 2020, 9, 530. [Google Scholar] [CrossRef]
- Liu, C.; Guo, H.; Dain, J.A.; Wan, Y.; Gao, X.H.; Chen, H.D.; Seeram, N.P.; Ma, H. Cytoprotective effects of a proprietary red maple leaf extract and its major polyphenol, ginnalin A, against hydrogen peroxide and methylglyoxal induced oxidative stress in human keratinocytes. Food Funct. 2020, 11, 5105–5114. [Google Scholar] [CrossRef]
- Zhou, Y.; Yang, W.; Li, Z.; Luo, D.; Li, W.; Zhang, Y.; Wang, X.; Fang, M.; Chen, Q.; Jin, X. Moringa oleifera stem extract protect skin keratinocytes against oxidative stress injury by enhancement of antioxidant defense systems and activation of PPARα. Biomed. Pharmacother. 2018, 107, 44–53. [Google Scholar] [CrossRef]
- Kolakul, P.; Sripanidkulchai, B. Phytochemicals and anti-aging potentials of the extracts from Lagerstroemia speciosa and Lagerstroemia floribunda. Ind. Crops Prod. 2017, 109, 707–716. [Google Scholar] [CrossRef]
- Liu, C.; Guo, H.; DaSilva, N.A.; Li, D.; Zhang, K.; Wan, Y.; Gao, X.H.; Chen, H.D.; Seeram, N.P.; Ma, H. Pomegranate (Punica granatum) phenolics ameliorate hydrogen peroxide-induced oxidative stress and cytotoxicity in human keratinocytes. J. Funct. Foods 2019, 54, 559–567. [Google Scholar] [CrossRef]
- Squillaci, G.; Apone, F.; Sena, L.M.; Carola, A.; Tito, A.; Bimonte, M.; Lucia, A.D.; Colucci, G.; Cara, F.L.; Morana, A. Chestnut (Castanea sativa Mill.) industrial wastes as a valued bioresource for the production of active ingredients. Process Biochem. 2018, 64, 228–236. [Google Scholar] [CrossRef]
- Lee, S.Y.; Kim, C.H.; Hwang, B.S.; Choi, K.M.; Yang, I.J.; Kim, G.Y.; Choi, Y.H.; Park, C.; Jeong, J.W. Protective effects of Oenothera biennis against hydrogen peroxide-induced oxidative stress and cell death in skin keratinocytes. Life 2020, 10, 255. [Google Scholar] [CrossRef] [PubMed]
- Bazzicalupo, M.; Burlando, B.; Denaro, M.; Barreca, D.; Trombetta, D.; Smeriglio, A.; Cornara, L. Polyphenol characterization and skin-preserving properties of hydroalcoholic flower extract from Himantoglossum robertianum (Orchidaceae). Plants 2019, 8, 502. [Google Scholar] [CrossRef] [Green Version]
- Do, N.Q.; Zheng, S.; Park, B.; Nguyen, Q.T.N.; Choi, B.R.; Fang, M.; Kim, M.; Jeong, J.; Choi, J.; Yang, S.J.; et al. Camu-camu fruit extract inhibits oxidative stress and inflammatory responses by regulating NFAT and Nrf2 signaling pathways in high glucose-induced human keratinocytes. Molecules 2021, 26, 3174. [Google Scholar] [CrossRef]
- Zakaria, N.N.A.; Okello, E.J.; Howes, M.J.; Birch-Machin, M.A.; Bowman, A. In vitro protective effects of an aqueous extract of Clitoria ternatea L. flower against hydrogen peroxide-induced cytotoxicity and UV-induced mtDNA damage in human keratinocytes. Phyther. Res. 2018, 32, 1064–1072. [Google Scholar] [CrossRef] [Green Version]
- Pastore, S.; Mascia, F.; Mariani, V.; Girolomoni, G. Keratinocytes in skin inflammation. Expert Rev. Dermatol. 2006, 1, 279–291. [Google Scholar] [CrossRef]
- Ćabrijan, L.; Lipozenćić, J. Adhesion molecules in keratinocytes. Clin. Dermatol. 2011, 29, 427–431. [Google Scholar] [CrossRef] [PubMed]
- Bernard, F.-X.; Morel, F.; Camus, M.; Pedretti, N.; Barrault, C.; Garnier, J.; Lecron, J.-C. Keratinocytes under Fire of Proinflammatory Cytokines: Bona Fide Innate Immune Cells Involved in the Physiopathology of Chronic Atopic Dermatitis and Psoriasis. J. Allergy 2012, 2012, 718725. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lebre, M.C.; Van Der Aar, A.M.G.; Van Baarsen, L.; Van Capel, T.M.M.; Schuitemaker, J.H.N.; Kapsenberg, M.L.; De Jong, E.C. Human keratinocytes express functional toll-like receptor 3, 4, 5, and 9. J. Investig. Dermatol. 2007, 127, 331–341. [Google Scholar] [CrossRef] [Green Version]
- Miller, L.S. Toll-Like Receptors in Skin. Adv. Dermatol. 2008, 24, 71–87. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Li, Z.J.; Sohn, K.C.; Choi, D.K.; Shi, G.; Hong, D.; Lee, H.E.; Whang, K.U.; Lee, Y.H.; Im, M.; Lee, Y.; et al. Roles of TLR7 in Activation of NF-κB Signaling of Keratinocytes by Imiquimod. PLoS ONE 2013, 8, e77159. [Google Scholar] [CrossRef] [Green Version]
- Pivarcsi, A.; Bodai, L.; Réthi, B.; Kenderessy-Szabó, A.; Koreck, A.; Széll, M.; Beer, Z.; Bata-Csörgo, Z.; Magócsi, M.; Rajnavölgyi, E.; et al. Expression and function of Toll-like receptors 2 and 4 in human keratinocytes. Int. Immunol. 2003, 15, 721–730. [Google Scholar] [CrossRef] [Green Version]
- Gröne, A. Keratinocytes and cytokines. Vet. Immunol. Immunopathol. 2002, 88, 1–12. [Google Scholar] [CrossRef]
- Sauder, D.N.; Orr, F.W.; Matic, S.; Stetsko, D.; Parker, K.P.; Chizzonite, R.; Kilian, P.L. Human interleukin-1α is chemotactic for normal human keratinocytes. Immunol. Lett. 1989, 22, 123–127. [Google Scholar] [CrossRef]
- Komine, M.; Rao, L.S.; Freedberg, I.M.; Simon, M.; Milisavljevic, V.; Blumenberg, M. Interleukin-1 induces transcription of keratin K6 in human epidermal keratinocytes. J. Investig. Dermatol. 2001, 116, 330–338. [Google Scholar] [CrossRef] [Green Version]
- Darmstadt, G.L.; Fleckman, P.; Rubens, C.E. Tumor necrosis factor-α and interleukin-1α decrease the adherence of Streptococcus pyogenes to cultured keratinocytes. J. Infect. Dis. 1999, 180, 1718–1721. [Google Scholar] [CrossRef]
- Kothny-Wilkes, G.; Kulms, D.; Pöppelmann, B.; Luger, T.A.; Kubin, M.; Schwarz, T. Interleukin-1 protects transformed keratinocytes from tumor necrosis factor-related apoptosis-inducing ligand. J. Biol. Chem. 1998, 273, 29247–29253. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Feldmeyer, L.; Werner, S.; French, L.E.; Beer, H.D. Interleukin-1, inflammasomes and the skin. Eur. J. Cell Biol. 2010, 89, 638–644. [Google Scholar] [CrossRef]
- Yoshizaki, K.; Nishimoto, N.; Matsumoto, K.; Tagoh, H.; Taga, T.; Deguchi, Y.; Kuritani, T.; Hirano, T.; Hashimoto, K.; Okada, N.; et al. Interleukin 6 and expression of its receptor on epidermal keratinocytes. Cytokine 1990, 2, 381–387. [Google Scholar] [CrossRef]
- Sugawara, T.; Gallucci, R.M.; Simeonova, P.P.; Luster, M.I. Regulation and role of interleukin 6 in wounded human epithelial keratinocytes. Cytokine 2001, 15, 328–336. [Google Scholar] [CrossRef]
- Wang, X.P.; Schunck, M.; Kallen, K.J.; Neumann, C.; Trautwein, C.; Rose-John, S.; Proksch, E. The interleukin-6 cytokine system regulates epidermal permeability barrier homeostasis. J. Investig. Dermatol. 2004, 123, 124–131. [Google Scholar] [CrossRef] [Green Version]
- Kondo, S.; Kono, T.; Sauder, D.N.; McKenzie, R.C. IL-8 gene expression and production in human keratinocytes and their modulation by UVB. J. Investig. Dermatol. 1993, 101, 690–694. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Jiang, W.G.; Sanders, A.J.; Ruge, F.; Harding, K.G. Influence of interleukin-8 (IL-8) and IL-8 receptors on the migration of human keratinocytes, the role of plc-γ and potential clinical implications. Exp. Ther. Med. 2012, 3, 231–236. [Google Scholar] [CrossRef] [Green Version]
- Banno, T.; Gazel, A.; Blumenberg, M. Effects of tumor necrosis factor-α (TNFα) in epidermal keratinocytes revealed using global transcriptional profiling. J. Biol. Chem. 2004, 279, 32633–32642. [Google Scholar] [CrossRef] [Green Version]
- Kim, H.R.; Hwang, K.A.; Park, S.H.; Kang, I. IL-7 and IL-15: Biology and roles in T-cell immunity in health and disease. Crit. Rev. Immunol. 2008, 28, 325–339. [Google Scholar] [CrossRef]
- Williams, I.R.; Rawson, E.A.; Manning, L.; Karaoli, T.; Rich, B.E.; Kupper, T.S. IL-7 overexpression in transgenic mouse keratinocytes causes a lymphoproliferative skin disease dominated by intermediate TCR cells: Evidence for a hierarchy in IL-7 responsiveness among cutaneous T cells. J. Immunol. 1997, 159, 3044–30456. [Google Scholar]
- Takashima, A.; Matsue, H.; Bergstresser, P.R.; Ariizumi, K. Interleukin-7-dependent interaction of dendritic epidermal t cells with keratinocytes. J. Investig. Dematol. 1995, 105 (Suppl. 1), S50–S53. [Google Scholar] [CrossRef] [Green Version]
- Blauvelt, A.; Asada, H.; Klaus-Kovtun, V.; Altman, D.J.; Lucey, D.R.; Katz, S.I. Interleukin-15 mRNA is expressed by human keratinocytes, langerhans cells, and blood-derived dendritic cells and is downregulated by ultraviolet B radiation. J. Investig. Dermatol. 1996, 106, 1047–1052. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Moore, K.W.; De Waal Malefyt, R.; Coffman, R.L.; O’Garra, A. Interleukin-10 and the interleukin-10 receptor. Annu. Rev. Immunol. 2001, 19, 683–765. [Google Scholar] [CrossRef]
- Enk, C.D.; Sredni, D.; Blauvelt, A.; Katz, S.I. Induction of IL-10 gene expression in human keratinocytes by UVB exposure in vivo and in vitro. J. Immunol. 1995, 154, 4851–4856. [Google Scholar] [CrossRef]
- Hirohata, S. Human Th1 responses driven by IL-12 are associated with enhanced expression of CD40 ligand. Clin. Exp. Immunol. 1999, 115, 78–85. [Google Scholar] [CrossRef] [PubMed]
- Kulig, P.; Musiol, S.; Freiberger, S.N.; Schreiner, B.; Gyu’lveszi, G.; Russo, G.; Pantelyushin, S.; Kishihara, K.; Alessandrini, F.; Ku’ndig, T.; et al. IL-12 protects from psoriasiform skin inflammation. Nat. Commun. 2016, 7, 13466. [Google Scholar] [CrossRef] [PubMed]
- Werth, V.P.; Bashir, M.M.; Zhang, W. IL-12 completely blocks ultraviolet-induced secretion of tumor necrosis factor α from cultured skin fibroblasts and keratinocytes. J. Investig. Dermatol. 2003, 120, 116–122. [Google Scholar] [CrossRef] [Green Version]
- Nakanishi, K.; Yoshimoto, T.; Tsutsui, H.; Okamura, H. Interleukin-18 regulates both Th1 and Th2 responses. Annu. Rev. Immunol. 2001, 19, 423–474. [Google Scholar] [CrossRef]
- Rich, B.E.; Kupper, T.S. Cytokines: IL-20—A new effector in skin inflammation. Curr. Biol. 2001, 11, R531–R534. [Google Scholar] [CrossRef] [Green Version]
- Jiang, Y.; Tsoi, L.C.; Billi, A.C.; Ward, N.L.; Harms, P.W.; Zeng, C.; Maverakis, E.; Michelle Kahlenberg, J.; Gudjonsson, J.E. Cytokinocytes: The diverse contribution of keratinocytes to immune responses in skin. JCI Insight 2020, 5, e142067. [Google Scholar] [CrossRef] [PubMed]
- Alilou, M.; Marzocco, S.; Hofer, D.; Rapa, S.F.; Asadpour, R.; Schwaiger, S.; Troppmair, J.; Stuppner, H. Labdane-Type Diterpenes from the Aerial Parts of Rydingia persica: Their Absolute Configurations and Protective Effects on LPS-Induced Inflammation in Keratinocytes. J. Nat. Prod. 2020, 83, 2456–2468. [Google Scholar] [CrossRef]
- Pintatum, A.; Maneerat, W.; Logie, E.; Tuenter, E.; Sakavitsi, M.E.; Pieters, L.; Berghe, W.V.; Sripisut, T.; Deachathai, S.; Laphookhieo, S. In vitro anti-inflammatory, anti-oxidant, and cytotoxic activities of four curcuma species and the isolation of compounds from Curcuma aromatica rhizome. Biomolecules 2020, 10, 799. [Google Scholar] [CrossRef] [PubMed]
- Ahama-Esseh, K.; Bodet, C.; Quashie-Mensah-Attoh, A.; Garcia, M.; Théry-Koné, I.; Dorat, J.; De Souza, C.; Enguehard-Gueiffier, C.; Boudesocque-Delaye, L. Anti-inflammatory activity of Crateva adansonii DC on keratinocytes infected by Staphylococcus aureus: From traditional practice to scientific approach using HPTLC-densitometry. J. Ethnopharmacol. 2017, 204, 26–35. [Google Scholar] [CrossRef] [PubMed]
- Yang, J.H.; Yoo, J.M.; Lee, E.; Lee, B.H.; Cho, W.K.; Park, K.I.; Yeul Ma, J. Anti-inflammatory effects of Perillae herba ethanolic extract against TNF-α/IFN-γ-stimulated human keratinocyte HaCaT cells. J. Ethnopharmacol. 2018, 211, 217–223. [Google Scholar] [CrossRef]
- Khalilpour, S.; Sangiovanni, E.; Piazza, S.; Fumagalli, M.; Beretta, G.; Dell’Agli, M. In vitro evidences of the traditional use of Rhus coriaria L. fruits against skin inflammatory conditions. J. Ethnopharmacol. 2019, 238, 111829. [Google Scholar] [CrossRef]
- Choi, Y.A.; Yu, J.H.; Jung, H.D.; Lee, S.; Park, P.H.; Lee, H.S.; Kwon, T.K.; Shin, T.Y.; Lee, S.W.; Rho, M.C.; et al. Inhibitory effect of ethanol extract of Ampelopsis brevipedunculata rhizomes on atopic dermatitis-like skin inflammation. J. Ethnopharmacol. 2019, 238, 111850. [Google Scholar] [CrossRef]
- Yang, J.H.; Hwang, Y.H.; Gu, M.J.; Cho, W.K.; Ma, J.Y. Ethanol extracts of Sanguisorba officinalis L. suppress TNF-α/IFN-γ-induced pro-inflammatory chemokine production in HaCaT cells. Phytomedicine 2015, 22, 1262–1268. [Google Scholar] [CrossRef]
- Seo, C.S.; Lim, H.S.; Ha, H.; Jin, S.E.; Shin, H.K. Quantitative analysis and anti-inflammatory effects of Gleditsia sinensis thorns in RAW 264.7 macrophages and HaCaT keratinocytes. Mol. Med. Rep. 2015, 12, 4773–4781. [Google Scholar] [CrossRef]
- Hardianti, B.; Umeyama, L.; Li, F.; Yokoyama, S.; Hayakawa, Y. Anti-inflammatory compounds moracin O and P from Morus alba Linn. (Sohakuhi) target the NF-κB pathway. Mol. Med. Rep. 2020, 22, 5385–5391. [Google Scholar] [CrossRef]
- Jin, S.E.; Ha, H.; Shin, H.K.; Seo, C.S. Anti-allergic and anti-inflammatory effects of Kuwanon G and Morusin on MC/9 mast cells and HaCaT keratinocytes. Molecules 2019, 24, 265. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Marquardt, P.; Seide, R.; Vissiennon, C.; Schubert, A.; Birkemeyer, C.; Ahyi, V.; Fester, K. Phytochemical characterization and in vitro anti-inflammatory, antioxidant and antimicrobial activity of Combretum collinum Fresen leaves extracts from Benin. Molecules 2020, 25, 288. [Google Scholar] [CrossRef] [Green Version]
- Lim, H.S.; Jin, S.E.; Kim, O.S.; Shin, H.K.; Jeong, S.J. Alantolactone from Saussurea lappa Exerts Antiinflammatory Effects by Inhibiting Chemokine Production and STAT1 Phosphorylation in TNF-α and IFN-γ-induced in HaCaT cells. Phyther. Res. 2015, 29, 1088–1096. [Google Scholar] [CrossRef] [PubMed]
- Kim, M.; Yin, J.; Hwang, I.H.; Park, D.H.; Lee, E.K.; Kim, M.J.; Lee, M.W. Anti-Acne vulgaris effects of pedunculagin from the leaves of Quercus mongolica by anti-inflammatory activity and 5α-reductase inhibition. Molecules 2020, 25, 2154. [Google Scholar] [CrossRef]
- Albouchi, F.; Avola, R.; Dico, G.M.L.; Calabrese, V.; Graziano, A.C.E.; Abderrabba, M.; Cardile, V. Melaleuca styphelioides Sm. Polyphenols modulate interferon gamma/histamine-induced inflammation in human NCTC 2544 keratinocytes. Molecules 2018, 23, 2526. [Google Scholar] [CrossRef] [Green Version]
- Yin, J.; Hwang, I.H.; Lee, M.W. Anti-acne vulgaris effect including skin barrier improvement and 5α-reductase inhibition by tellimagrandin I from Carpinus tschonoskii. BMC Complement. Altern. Med. 2019, 19, 323. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ko, W.; Kim, N.; Lee, H.; Woo, E.R.; Kim, Y.C.; Oh, H.; Lee, D.S. Anti-inflammatory effects of compounds from Cudrania tricuspidata in hacat human keratinocytes. Int. J. Mol. Sci. 2021, 22, 7472. [Google Scholar] [CrossRef]
- Svensson, D.; Lozano, M.; Almanza, G.R.; Nilsson, B.O.; Sterner, O.; Villagomez, R. Sesquiterpene lactones from Ambrosia arborescens Mill. inhibit pro-inflammatory cytokine expression and modulate NF-κB signaling in human skin cells. Phytomedicine 2018, 50, 118–126. [Google Scholar] [CrossRef] [PubMed]
- Oh, C.T.; Jang, Y.J.; Kwon, T.R.; Im, S.; Kim, S.R.; Seok, J.; Kim, G.Y.; Kim, Y.H.; Mun, S.K.; Kim, B.J. Effect of isosecotanapartholide isolated from Artemisia princeps Pampanini on IL-33 production and STAT-1 activation in HaCaT keratinocytes. Mol. Med. Rep. 2017, 15, 2681–2688. [Google Scholar] [CrossRef] [PubMed]
- D’Orazio, J.; Jarrett, S.; Amaro-Ortiz, A.; Scott, T. UV radiation and the skin. Int. J. Mol. Sci. 2013, 14, 12222–12248. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Sun, X.; Kim, A.; Nakatani, M.; Shen, Y.; Liu, L. Distinctive molecular responses to ultraviolet radiation between keratinocytes and melanocytes. Exp. Dermatol. 2016, 25, 708–713. [Google Scholar] [CrossRef] [Green Version]
- Sesto, A.; Navarro, M.; Burslem, F.; Jorcano, J.L. Analysis of the ultraviolet B response in primary human keratinocytes using oligonucleotide microarrays. Proc. Natl. Acad. Sci. USA 2002, 99, 2965–2970. [Google Scholar] [CrossRef] [Green Version]
- El-Abaseri, T.B.; Putta, S.; Hansen, L.A. Ultraviolet irradiation induces keratinocyte proliferation and epidermal hyperplasia through the activation of the epidermal growth factor receptor. Carcinogenesis 2006, 27, 225–231. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Oda, K.; Matsuoka, Y.; Funahashi, A.; Kitano, H. A comprehensive pathway map of epidermal growth factor receptor signaling. Mol. Syst. Biol. 2005, 1, 2005.0010. [Google Scholar] [CrossRef] [Green Version]
- Calautti, E.; Li, J.; Saoncella, S.; Brissette, J.L.; Goetinck, P.F. Phosphoinositide 3-kinase signaling to Akt promotes keratinocyte differentiation versus death. J. Biol. Chem. 2005, 280, 32856–32865. [Google Scholar] [CrossRef] [Green Version]
- Takao, J.; Yudate, T.; Das, A.; Shikano, S.; Bonkobara, M.; Ariizumi, K.; Cruz, P.D. Expression of NF-κB in epidermis and the relationship between NF-κB activation and inhibition of keratinocyte growth. Br. J. Dermatol. 2003, 148, 680–688. [Google Scholar] [CrossRef]
- Barr, R.K.; Bogoyevitch, M.A. The c-Jun N-terminal protein kinase family of mitogen-activated protein kinases (JNK MAPKs). Int. J. Biochem. Cell Biol. 2001, 33, 1047–1063. [Google Scholar] [CrossRef]
- Syed, D.N.; Afaq, F.; Mukhtar, H. Differential activation of signaling pathways by UVA and UVB radiation in normal human epidermal keratinocytes. Photochem. Photobiol. 2012, 88, 1184–1190. [Google Scholar] [CrossRef] [PubMed]
- Adachi, M.; Gazel, A.; Pintucci, G.; Shuck, A.; Shifteh, S.; Ginsburg, D.; Rao, L.S.; Kaneko, T.; Freedberg, I.M.; Tamaki, K.; et al. Specificity in Stress Response: Epidermal Keratinocytes Exhibit Specialized UV-Responsive Signal Transduction Pathways. DNA Cell Biol. 2003, 22, 665–677. [Google Scholar] [CrossRef] [PubMed]
- Sano, S.; Chan, K.S.; Carbajal, S.; Clifford, J.; Peavey, M.; Kiguchi, K.; Itami, S.; Nickoloff, B.J.; DiGiovanni, J. Stat3 links activated keratinocytes and immunocytes required for development of psoriasis in a novel transgenic mouse model. Nat. Med. 2005, 11, 43–49. [Google Scholar] [CrossRef]
- Muthusamy, V.; Piva, T.J. A comparative study of UV-induced cell signalling pathways in human keratinocyte-derived cell lines. Arch. Dermatol. Res. 2013, 305, 817–833. [Google Scholar] [CrossRef]
- Marais, T.L.D.; Kluz, T.; Xu, D.; Zhang, X.; Gesumaria, L.; Matsui, M.S.; Costa, M.; Sun, H. Transcription factors and stress response gene alterations in human keratinocytes following Solar Simulated Ultra Violet Radiation. Sci. Rep. 2017, 7, 13622. [Google Scholar] [CrossRef]
- Assefa, Z.; Garmyn, M.; Bouillon, R.; Merlevede, W.; Vandenheede, J.R.; Agostinis, P. Differential stimulation of ERK and JNK activities by ultraviolet B irradiation and epidermal growth factor in human keratinocytes. J. Investig. Dermatol. 1997, 108, 886–891. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Quan, T.; Qin, Z.; Xia, W.; Shao, Y.; Voorhees, J.J.; Fisher, G.J. Matrix-degrading metalloproteinases in photoaging. J. Investig. Dermatol. Symp. Proc. 2009, 14, 20–24. [Google Scholar] [CrossRef] [Green Version]
- Young, M.L.; Yeon, K.K.; Kyu, H.K.; Su, J.P.; Sung, J.K.; Jin, H.C. A novel role for the TRPV1 channel in UV-induced matrix metalloproteinase (MMP)-1 expression in HaCaT cells. J. Cell. Physiol. 2009, 219, 766–775. [Google Scholar] [CrossRef]
- Kim, C.; Ryu, H.C.; Kim, J.H. Low-dose UVB irradiation stimulates matrix metalloproteinase-1 expression via a BLT2-linked pathway in HaCaT cells. Exp. Mol. Med. 2010, 42, 833–841. [Google Scholar] [CrossRef] [Green Version]
- Dong, K.K.; Damaghi, N.; Picart, S.D.; Markova, N.G.; Obayashi, K.; Okano, Y.; Masaki, H.; Grether-Beck, S.; Krutmann, J.; Smiles, K.A.; et al. UV-induced DNA damage initiates release of MMP-1 in human skin. Exp. Dermatol. 2008, 17, 1037–1044. [Google Scholar] [CrossRef]
- Onoue, S.; Kobayashi, T.; Takemoto, Y.; Sasaki, I.; Shinkai, H. Induction of matrix metalloproteinase-9 secretion from human keratinocytes in culture by ultraviolet B irradiation. J. Dermatol. Sci. 2003, 33, 105–111. [Google Scholar] [CrossRef]
- Lee, C.H.; Wu, S.B.; Hong, C.H.; Yu, H.S.; Wei, Y.H. Molecular mechanisms of UV-induced apoptosis and its effects on skin residential cells: The implication in UV-based phototherapy. Int. J. Mol. Sci. 2013, 14, 6414–6435. [Google Scholar] [CrossRef] [Green Version]
- Adewale, F.O.; Basiru, A.O.; Ayorinde, O.O.; Israel, O.I.; Oluwafemi, O.A. Regulation of Apoptotic and Necroptotic Cell Death in Skin Cancer. J. Cancer Biol. Res. 2017, 5, 1108. [Google Scholar]
- Chen, H.; Weng, Q.Y.; Fisher, D.E. UV signaling pathways within the skin. J. Investig. Dermatol. 2014, 134, 2080–2085. [Google Scholar] [CrossRef] [Green Version]
- Tron, V.A.; Trotter, M.J.; Tang, L.; Krajewska, M.; Reed, J.C.; Ho, V.C.; Li, G. p53-regulated apoptosis is differentiation dependent in ultraviolet B- irradiated mouse keratinocytes. Am. J. Pathol. 1998, 153, 579–585. [Google Scholar] [CrossRef] [Green Version]
- Qin, J.Z.; Chaturvedi, V.; Denning, M.F.; Bacon, P.; Panella, J.; Choubey, D.; Nickoloff, B.J. Regulation of apoptosis by p53 in UV-irradiated human epidermis, psoriatic plaques and senescent keratinocytes. Oncogene 2002, 21, 2991–3002. [Google Scholar] [CrossRef] [Green Version]
- Holley, A.K.; St Clair, D.K. Watching the watcher: Regulation of p53 by mitochondria. Futur. Oncol. 2009, 5, 117–130. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Calapre, L.; Gray, E.S.; Kurdykowski, S.; David, A.; Hart, P.; Descargues, P.; Ziman, M. Heat-mediated reduction of apoptosis in UVB-damaged keratinocytes in vitro and in human skin ex vivo. BMC Dermatol. 2016, 16, 6. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Aragane, Y.; Kulms, D.; Metze, D.; Wilkes, G.; Pöppelmann, B.; Luger, T.A.; Schwarz, T. Ultraviolet light induces apoptosis via direct activation of CD95 (Fas/APO-1) independently of its ligand CD95L. J. Cell Biol. 1998, 140, 171–182. [Google Scholar] [CrossRef] [Green Version]
- Lee, C.H.; Yu, C.L.; Liao, W.T.; Kao, Y.H.; Chai, C.Y.; Chen, G.S.; Yu, H.S. Effects and interactions of low doses of arsenic and UVB on keratinocyte apoptosis. Chem. Res. Toxicol. 2004, 17, 1199–1205. [Google Scholar] [CrossRef]
- Takasawa, R.; Nakamura, H.; Mori, T.; Tanuma, S. Differential apoptotic pathways in human keratinocyte HaCaT cells exposed to UVB and UVC. Apoptosis 2005, 10, 1121–1130. [Google Scholar] [CrossRef]
- Sitailo, L.A.; Tibudan, S.S.; Denning, M.F. Activation of caspase-9 is required for UV-induced apoptosis of human keratinocytes. J. Biol. Chem. 2002, 277, 19346–19352. [Google Scholar] [CrossRef] [Green Version]
- Assefa, Z.; Garmyn, M.; Vantieghem, A.; Declercq, W.; Vandenabeele, P.; Vandenheede, J.R.; Agostinis, P. Ultraviolet B radiation-induced apoptosis in human keratinocytes: Cytosolic activation of procaspase-8 and the role of Bcl-2. FEBS Lett. 2003, 540, 125–132. [Google Scholar] [CrossRef] [Green Version]
- Denning, M.F.; Wang, Y.; Tibudan, S.; Alkan, S.; Nickoloff, B.J.; Qin, J.Z. Caspase activation and disruption of mitochondrial membrane potential during UV radiation-induced apoptosis of human keratinocytes requires activation of protein kinase C. Cell Death Differ. 2002, 9, 40–52. [Google Scholar] [CrossRef]
- Daher, C.C.; Fontes, I.S.; De Oliveira Rodrigues, R.; Azevedo De Brito Damasceno, G.; Dos Santos Soares, D.; Flávio Soares Aragão, C.; Barreto Gomes, P.A.; Ferrari, M. Development of O/W emulsions containing euterpe oleracea extract and evaluation of photoprotective efficacy. Braz. J. Pharm. Sci. 2014, 50, 639–652. [Google Scholar] [CrossRef] [Green Version]
- Jarzycka, A.; Lewińska, A.; Gancarz, R.; Wilk, K.A. Assessment of extracts of Helichrysum arenarium, Crataegus monogyna, Sambucus nigra in photoprotective UVA and UVB; Photostability in cosmetic emulsions. J. Photochem. Photobiol. B Biol. 2013, 128, 50–57. [Google Scholar] [CrossRef]
- Vijayakumar, R.; Abd Gani, S.S.; Zaidan, U.H.; Halmi, M.I.E.; Karunakaran, T.; Hamdan, M.R. Exploring the Potential Use of Hylocereus polyrhizus Peels as a Source of Cosmeceutical Sunscreen Agent for Its Antioxidant and Photoprotective Properties. Evid.-Based Complement. Altern. Med. 2020, 2020, 7520736. [Google Scholar] [CrossRef]
- Rocha de Carvalho, W.; Ceres Moreira, L.; Valadares, M.; Diniz, A.D.; Freitas Bara, M. Pterodon emarginatus hydroalcoholic extract: Antioxidant and photoprotective activities, noncytotoxic effect, and perspective of obtaining formulations with photochemoprotective activity. Pharmacogn. Mag. 2019, 15, 176–182. [Google Scholar] [CrossRef]
- Da Silva, A.C.P.; Paiva, J.P.; Diniz, R.R.; dos Anjos, V.M.; Silva, A.B.S.M.; Pinto, A.V.; dos Santos, E.P.; Leitão, A.C.; Cabral, L.M.; Rodrigues, C.R.; et al. Photoprotection assessment of olive (Olea europaea L.) leaves extract standardized to oleuropein: In vitro and in silico approach for improved sunscreens. J. Photochem. Photobiol. B Biol. 2019, 193, 162–171. [Google Scholar] [CrossRef]
- Era, B.; Floris, S.; Sogos, V.; Porcedda, C.; Piras, A.; Medda, R.; Fais, A.; Pintus, F. Anti-Aging Potential of Extracts from Washingtonia filifera Seeds. Plants 2021, 10, 151. [Google Scholar] [CrossRef]
- Surget, G.; Stiger-Pouvreau, V.; Le Lann, K.; Kervarec, N.; Couteau, C.; Coiffard, L.J.M.; Gaillard, F.; Cahier, K.; Guérard, F.; Poupart, N. Structural elucidation, in vitro antioxidant and photoprotective capacities of a purified polyphenolic-enriched fraction from a saltmarsh plant. J. Photochem. Photobiol. B Biol. 2015, 143, 52–60. [Google Scholar] [CrossRef]
- Cefali, L.C.; Ataide, J.A.; de Sousa, I.M.O.; Figueiredo, M.C.; Ruiz, A.L.T.G.; Foglio, M.A.; Mazzola, P.G. In vitro solar protection factor, antioxidant activity, and stability of a topical formulation containing Benitaka grape (Vitis vinifera L.) peel extract. Nat. Prod. Res. 2020, 34, 2677–2682. [Google Scholar] [CrossRef]
- Choquenet, B.; Couteau, C.; Paparis, E.; Coiffard, L.J.M. Quercetin and rutin as potential sunscreen agents: Determination of efficacy by an in vitro method. J. Nat. Prod. 2008, 71, 1117–1118. [Google Scholar] [CrossRef] [PubMed]
- Kazumy De Lima Yamaguchi, K.; Dos, L.; Santarém, S.; Lamarão, C.V.; Lima, E.S.; Florêncio Da Veiga-Junior, V. Avaliação in vitro da Atividade Fotoprotetora de Resíduos de Frutas Amazônicas. Sci. Amaz. 2016, 5, 109–116. [Google Scholar]
- Velasco, M.V.R.; Balogh, T.S.; Pedriali, C.A.; Sarruf, F.D.; Pinto, C.A.S.O.; Kaneko, T.M.; Baby, A.R. Rutin association with ethylhexyl methoxycinnamate and benzophenone-3: In vitro evaluation of the photoprotection effectiveness by reflectance spectrophotometry. Lat. Am. J. Pharm. 2008, 27, 23–27. [Google Scholar]
- Rajnochová Svobodová, A.; Gabrielová, E.; Michaelides, L.; Kosina, P.; Ryšavá, A.; Ulrichová, J.; Zálešák, B.; Vostálová, J. UVA-photoprotective potential of silymarin and silybin. Arch. Dermatol. Res. 2018, 310, 413–424. [Google Scholar] [CrossRef]
- Choquenet, B.; Couteau, C.; Paparis, E.; Coiffard, L.J.M. Flavonoids and polyphenols, molecular families with sunscreen potential: Determining effectiveness with an in vitro method. Nat. Prod. Commun. 2009, 4, 227–230. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Stevanato, R.; Bertelle, M.; Fabris, S. Photoprotective characteristics of natural antioxidant polyphenols. Regul. Toxicol. Pharmacol. 2014, 69, 71–77. [Google Scholar] [CrossRef] [PubMed]
- Kim, K.M.; Im, A.R.; Lee, S.; Chae, S. Dual protective effects of flavonoids from Petasites japonicus against UVB-induced apoptosis mediated via HSF-1 activated heat shock proteins and Nrf2-activated heme oxygenase-1 pathways. Biol. Pharm. Bull. 2017, 40, 765–773. [Google Scholar] [CrossRef] [Green Version]
- Wang, P.W.; Cheng, Y.C.; Hung, Y.C.; Lee, C.H.; Fang, J.Y.; Li, W.T.; Wu, Y.R.; Pan, T.L. Red raspberry extract protects the skin against UVB-induced damage with antioxidative and anti-inflammatory properties. Oxid. Med. Cell. Longev. 2019, 2019, 9529676. [Google Scholar] [CrossRef] [Green Version]
- Cerulli, A.; Masullo, M.; Mari, A.; Balato, A.; Filosa, R.; Lembo, S.; Napolitano, A.; Piacente, S. Phenolics from Castanea sativa leaves and their effects on UVB-induced damage. Nat. Prod. Res. 2018, 32, 1170–1175. [Google Scholar] [CrossRef]
- Xuan, S.H.; Hong, I.K.; Lee, Y.J.; Kim, J.W.; Park, S.N. Biological activities and chemical components of Potentilla kleiniana Wight & Arn. Nat. Prod. Res. 2020, 34, 3262–3266. [Google Scholar] [CrossRef] [PubMed]
- Kim, M.; Park, Y.G.; Lee, H.J.; Lim, S.J.; Nho, C.W. Youngiasides A and C Isolated from Youngia denticulatum Inhibit UVB-Induced MMP Expression and Promote Type I Procollagen Production via Repression of MAPK/AP-1/NF-κB and Activation of AMPK/Nrf2 in HaCaT Cells and Human Dermal Fibroblasts. J. Agric. Food Chem. 2015, 63, 5428–5438. [Google Scholar] [CrossRef]
- Sangiovanni, E.; Di Lorenzo, C.; Piazza, S.; Manzoni, Y.; Brunelli, C.; Fumagalli, M.; Magnavacca, A.; Martinelli, G.; Colombo, F.; Casiraghi, A.; et al. Vitis vinifera L. Leaf extract inhibits in vitro mediators of inflammation and oxidative stress involved in inflammatory-based skin diseases. Antioxidants 2019, 8, 134. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Ham, S.A.; Hwang, J.S.; Kang, E.S.; Yoo, T.; Lim, H.H.; Lee, W.J.; Paek, K.S.; Seo, H.G. Ethanol extract of Dalbergia odorifera protects skin keratinocytes against ultraviolet B-induced photoaging by suppressing production of reactive oxygen species. Biosci. Biotechnol. Biochem. 2015, 79, 760–766. [Google Scholar] [CrossRef]
- Petruk, G.; Di Lorenzo, F.; Imbimbo, P.; Silipo, A.; Bonina, A.; Rizza, L.; Piccoli, R.; Monti, D.M.; Lanzetta, R. Protective effect of Opuntia ficus-indica L. cladodes against UVA-induced oxidative stress in normal human keratinocytes. Bioorg. Med. Chem. Lett. 2017, 27, 5485–5489. [Google Scholar] [CrossRef] [Green Version]
- Pérez-Sánchez, A.; Barrajón-Catalán, E.; Herranz-López, M.; Castillo, J.; Micol, V. Lemon balm extract (Melissa officinalis, L.) promotes melanogenesis and prevents UVB-induced oxidative stress and DNA damage in a skin cell model. J. Dermatol. Sci. 2016, 84, 169–177. [Google Scholar] [CrossRef] [PubMed]
- Ha, S.J.; Lee, J.; Kim, H.; Song, K.M.; Lee, N.H.; Kim, Y.E.; Lee, H.; Kim, Y.H.; Jung, S.K. Preventive effect of Rhus javanica extract on UVB-induced skin inflammation and photoaging. J. Funct. Foods 2016, 27, 589–599. [Google Scholar] [CrossRef]
- Muzaffer, U.; Paul, V.I.; Prasad, N.R.; Karthikeyan, R.; Agilan, B. Protective effect of Juglans regia L. against ultraviolet B radiation induced inflammatory responses in human epidermal keratinocytes. Phytomedicine 2018, 42, 100–111. [Google Scholar] [CrossRef] [PubMed]
- Hwan, J.; Youngwan, O.; Kong, C.S. Anti-photoaging effects of solvent—Partitioned fractions from Portulaca oleracea L. on UVB -stressed human keratinocytes. J. Food Biochem. 2019, 43, e12814. [Google Scholar] [CrossRef]
- Kwak, C.S.; Yang, J.; Shin, C.Y.; Chung, J.H. Rosa multiflora Thunb Flower Extract Attenuates Ultraviolet-Induced Photoaging in Skin Cells and Hairless Mice. J. Med. Food 2020, 23, 988–997. [Google Scholar] [CrossRef]
- Shiratake, S.; Nakahara, T.; Iwahashi, H.; Onodera, T.; Mizushina, Y. Rose myrtle (Rhodomyrtus tomentosa) extract and its component, piceatannol, enhance the activity of DNA polymerase and suppress the inflammatory response elicited by UVB-induced DNA damage in skin cells. Mol. Med. Rep. 2015, 12, 5857–5864. [Google Scholar] [CrossRef]
- De Assis Dias Alves, G.; De Souza, R.O.; Rogez, H.L.G.; Masaki, H.; Fonseca, M.J.V. Cecropia obtusa extract and chlorogenic acid exhibit anti aging effect in human fibroblasts and keratinocytes cells exposed to UV radiation. PLoS ONE 2019, 14, e0216501. [Google Scholar] [CrossRef]
- Wang, Y.S.; Cho, J.G.; Hwang, E.S.; Yang, J.E.; Gao, W.; Fang, M.Z.; Zheng, S.; Yi, T.H. Enhancement of Protective Effects of Radix scutellariae on UVB-induced Photo Damage in Human HaCaT Keratinocytes. Appl. Biochem. Biotechnol. 2018, 184, 1073–1093. [Google Scholar] [CrossRef]
- Kwon, K.R.; Alam, M.B.; Park, J.H.; Kim, T.H.; Lee, S.H. Attenuation of UVB-induced photo-aging by polyphenolic-rich Spatholobus suberectus stem extract via modulation of MAPK/AP-1/MMPs signaling in human keratinocytes. Nutrients 2019, 11, 1341. [Google Scholar] [CrossRef] [Green Version]
- Ahn, H.S.; Kim, H.J.; Na, C.; Jang, D.S.; Shin, Y.K.; Lee, S.H. The protective effect of Adenocaulon himalaicum Edgew. And its bioactive compound neochlorogenic acid against uvb-induced skin damage in human dermal fibroblasts and epidermal keratinocytes. Plants 2021, 10, 1669. [Google Scholar] [CrossRef]
- Sun, Z.W.; Du, J.; Hwang, E.; Yi, T.H. Paeonol extracted from Paeonia suffruticosa Andr. ameliorated UVB-induced skin photoaging via DLD/Nrf2/ARE and MAPK/AP-1 pathway. Phyther. Res. 2018, 32, 1741–1749. [Google Scholar] [CrossRef] [PubMed]
- Wongwad, E.; Pingyod, C.; Saesong, T.; Waranuch, N.; Wisuitiprot, W.; Sritularak, B.; Temkitthawon, P.; Ingkaninan, K. Assessment of the bioactive components, antioxidant, antiglycation and anti-inflammatory properties of Aquilaria crassna Pierre ex Lecomte leaves. Ind. Crops Prod. 2019, 138, 111448. [Google Scholar] [CrossRef]
- Razia, S.; Park, H.; Shin, E.; Shim, K.S.; Cho, E.; Kim, S.Y. Effects of Aloe vera flower extract and its active constituent isoorientin on skin moisturization via regulating involucrin expression: In vitro and molecular docking studies. Molecules 2021, 26, 2626. [Google Scholar] [CrossRef]
- Kim, Y.A.; Kim, D.H.; Park, C.B.; Park, T.S.; Park, B.J. Anti-inflammatory and skin-moisturizing effects of a flavonoid glycoside extracted from the aquatic plant Nymphoides indica in human keratinocytes. Molecules 2018, 23, 2342. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hwang, H.S.; Shim, J.H. Brazilin and Caesalpinia sappan L. extract protect epidermal keratinocytes from oxidative stress by inducing the expression of GPX7. Chin. J. Nat. Med. 2018, 16, 203–209. [Google Scholar] [CrossRef]
- Park, H.-A.; Kim, M.Y.; Lee, N.-Y.; Lim, J.; Park, K.-B.; Lee, C.-K.; Nguyen, V.D.; Kim, J.; Park, J.-T.; Park, J.-I. Variation of Triterpenic Acids in 12 Wild Syzygium formosum and Anti-Inflammation Activity on Human Keratinocyte HaCaT. Plants 2021, 10, 2428. [Google Scholar] [CrossRef]
- Kim, W.S.; Seo, J.H.; Lee, J.-I.; Ko, E.-S.; Cho, S.-M.; Kang, J.-R.; Jeong, J.-H.; Jeong, Y.J.; Kim, C.Y.; Cha, J.-D.; et al. The Metabolite Profile in Culture Supernatant of Aster yomena Callus and Its Anti-Photoaging Effect in Skin Cells Exposed to UVB. Plants 2021, 10, 659. [Google Scholar] [CrossRef]
- Oh, J.H.; Lee, J.I.; Karadeniz, F.; Park, S.Y.; Seo, Y.; Kong, C.S. Antiphotoaging Effects of 3,5-Dicaffeoyl-epi-quinic Acid via Inhibition of Matrix Metalloproteinases in UVB-Irradiated Human Keratinocytes. Evid.-Based Complement. Altern. Med. 2020, 2020, 8949272. [Google Scholar] [CrossRef]
- Kim, S.B.; Kim, J.E.; Kang, O.H.; Mun, S.H.; Seo, Y.S.; Kang, D.H.; Yang, D.W.; Ryu, S.Y.; Lee, Y.M.; Kwon, D.Y. Protective effect of ixerisoside A against UVB-induced pro-infammatory cytokine production in human keratinocytes. Int. J. Mol. Med. 2015, 35, 1411–1418. [Google Scholar] [CrossRef] [Green Version]
- Im, A.R.; Kim, Y.M.; Chin, Y.W.; Chae, S. Protective effects of compounds from Garcinia mangostana L. (mangosteen) against UVB damage in HaCaT cells and hairless mice. Int. J. Mol. Med. 2017, 40, 1941–1949. [Google Scholar] [CrossRef] [Green Version]
- Lin, K.W.; Wang, B.W.; Wu, C.M.; Yen, M.H.; Wei, B.L.; Hung, C.F.; Lin, C.N. Antioxidant prenylated phenols of Artocarpus plants attenuate ultraviolet radiation-induced damage on human keratinocytes and fibroblasts. Phytochem. Lett. 2015, 14, 190–197. [Google Scholar] [CrossRef]
- Landén, N.X.; Li, D.; Ståhle, M. Transition from inflammation to proliferation: A critical step during wound healing. Cell. Mol. Life Sci. 2016, 73, 3861–3885. [Google Scholar] [CrossRef] [Green Version]
- Barrientos, S.; Stojadinovic, O.; Golinko, M.S.; Brem, H.; Tomic-Canic, M. Growth factors and cytokines in wound healing. Wound Repair Regen. 2008, 16, 585–601. [Google Scholar] [CrossRef]
- Ridiandries, A.; Tan, J.T.M.; Bursill, C.A. The role of chemokines in wound healing. Int. J. Mol. Sci. 2018, 19, 3217. [Google Scholar] [CrossRef] [Green Version]
- Wojtowicz, A.M.; Oliveira, S.; Carlson, M.W.; Zawadzka, A.; Rousseau, C.F.; Baksh, D. The importance of both fibroblasts and keratinocytes in a bilayered living cellular construct used in wound healing. Wound Repair Regen. 2014, 22, 246–255. [Google Scholar] [CrossRef] [Green Version]
- Coulombe, P.A. Towards a molecular definition of keratinocyte activation after acute injury to stratified epithelia. Biochem. Biophys. Res. Commun. 1997, 236, 231–238. [Google Scholar] [CrossRef]
- Pora, A.; Yoon, S.; Dreissen, G.; Hoffmann, B.; Merkel, R.; Windoffer, R.; Leube, R.E. Regulation of keratin network dynamics by the mechanical properties of the environment in migrating cells. Sci. Rep. 2020, 10, 4574. [Google Scholar] [CrossRef] [Green Version]
- Wallis, S.; Lloyd, S.; Wise, I.; Ireland, G.; Fleming, T.P.; Garrod, D. The α isoform of protein kinase C is involved in signaling the response of desmosomes to wounding in cultured epithelial cells. Mol. Biol. Cell. 2000, 11, 1077–1092. [Google Scholar] [CrossRef]
- Savagner, P.; Kusewitt, D.F.; Carver, E.A.; Magnino, F.; Choi, C.; Gridley, T.; Hudson, L.G. Developmental transcription factor slug is required for effective re-epithelialization by adult keratinocytes. J. Cell. Physiol. 2005, 202, 858–866. [Google Scholar] [CrossRef] [Green Version]
- Choi, Y.J.; Laclef, C.; Yang, N.; Andreu-Cervera, A.; Lewis, J.; Mao, X.; Li, L.; Snedecor, E.R.; Takemaru, K.I.; Qin, C.; et al. RPGRIP1L is required for stabilizing epidermal keratinocyte adhesion through regulating desmoglein endocytosis. PLoS Genet. 2019, 15, e1007914. [Google Scholar] [CrossRef]
- Sumigray, K.; Zhou, K.; Lechler, T. Cell-cell adhesions and cell contractility are upregulated upon desmosome disruption. PLoS ONE 2014, 9, e101824. [Google Scholar] [CrossRef] [Green Version]
- Völlner, F.; Ali, J.; Kurrle, N.; Exner, Y.; Eming, R.; Hertl, M.; Banning, A.; Tikkanen, R. Loss of flotillin expression results in weakened desmosomal adhesion and Pemphigus vulgaris-like localisation of desmoglein-3 in human keratinocytes. Sci. Rep. 2016, 6, 28820. [Google Scholar] [CrossRef]
- Amagai, M.; Fujimori, T.; Masunaga, T.; Shimizu, H.; Nishikawa, T.; Shimizu, N.; Takeichi, M.; Hashimoto, T. Delayed assembly of desmosomes in keratinocytes with disrupted classic-cadherin-mediated cell adhesion by a dominant negative mutant. J. Investig. Dermatol. 1995, 104, 27–32. [Google Scholar] [CrossRef] [Green Version]
- Wanuske, M.T.; Brantschen, D.; Schinner, C.; Stüdle, C.; Walter, E.; Hiermaier, M.; Vielmuth, F.; Waschke, J.; Spindler, V. Clustering of desmosomal cadherins by desmoplakin is essential for cell-cell adhesion. Acta Physiol. 2021, 231, e13609. [Google Scholar] [CrossRef] [PubMed]
- Bodin, S.; Planchon, D.; Morris, E.R.; Comunale, F.; Gauthier-Rouviére, C. Flotillins in intercellular adhesion—From cellular physiology to human diseases. J. Cell Sci. 2014, 127, 5139–5147. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Litjens, S.H.M.; de Pereda, J.M.; Sonnenberg, A. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 2006, 16, 376–383. [Google Scholar] [CrossRef]
- Miranti, C.K.; Brugge, J.S. Sensing the environment: A historical perspective on integrin signal transduction. Nat. Cell Biol. 2002, 4, E83–E90. [Google Scholar] [CrossRef]
- Niculescu, C.; Ganguli-Indra, G.; Pfister, V.; Dupé, V.; Messaddeq, N.; De Arcangelis, A.; Georges-Labouesse, E. Conditional ablation of integrin alpha-6 in mouse epidermis leads to skin fragility and inflammation. Eur. J. Cell Biol. 2011, 90, 270–277. [Google Scholar] [CrossRef]
- Nguyen, B.P.; Ryan, M.C.; Gil, S.G.; Carter, W.G. Deposition of laminin 5 in epidermal wounds regulates integrin signaling and adhesion. Curr. Opin. Cell Biol. 2000, 12, 554–562. [Google Scholar] [CrossRef]
- Wilhelmsen, K.; Litjens, S.H.M.; Kuikman, I.; Margadant, C.; Van Rheenen, J.; Sonnenberg, A. Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor-induced hemidesmosome disruption. Mol. Biol. Cell. 2007, 18, 3512–3522. [Google Scholar] [CrossRef]
- Santoro, M.M.; Gaudino, G.; Marchisio, P.C. The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration. Dev. Cell. 2003, 5, 257–271. [Google Scholar] [CrossRef] [Green Version]
- Seeger, M.A.; Paller, A.S. The Roles of Growth Factors in Keratinocyte Migration. Adv. Wound Care 2015, 4, 213–224. [Google Scholar] [CrossRef] [Green Version]
- Sivamani, R.K.; Garcia, M.S.; Rivkah Isseroff, R. Wound re-epithelialization: Modulating keratinocyte migration in wound healing. Front. Biosci. 2007, 12, 2849–2868. [Google Scholar] [CrossRef] [Green Version]
- Gniadecki, R. Regulation of keratinocyte proliferation. Gen. Pharmacol. 1998, 30, 619–622. [Google Scholar] [CrossRef]
- Ando, Y.; Jensen, P.J. Epidermal growth factor and insulin-like growth factor I enhance keratinocyte migration. J. Investig. Dermatol. 1993, 100, 633–639. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Liu, Y.; Petreaca, M.; Yao, M.; Martins-Green, M. Cell and molecular mechanisms of keratinocyte function stimulated by insulin during wound healing. BMC Cell Biol. 2009, 10, 1. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Aijaz, A.; Faulknor, R.; Berthiaume, F.; Olabisi, R.M. Hydrogel Microencapsulated Insulin-Secreting Cells Increase Keratinocyte Migration, Epidermal Thickness, Collagen Fiber Density, and Wound Closure in a Diabetic Mouse Model of Wound Healing. Tissue Eng. Part A 2015, 21, 2723–2732. [Google Scholar] [CrossRef] [Green Version]
- Haase, I.; Evans, R.; Pofahl, R.; Watt, F.M. Regulation of keratinocyte shape, migration and wound epithelialization by IGF-1 and EGF-dependent signalling pathways. J. Cell Sci. 2003, 116, 3227–3238. [Google Scholar] [CrossRef] [Green Version]
- Marikovsky, M.; Vogt, P.; Eriksson, E.; Rubin, J.S.; Taylor, W.G.; Sasse, J.; Klagsbrun, M. Wound fluid-derived heparin-binding EGF-like growth factor (HB-EGF) is synergistic with insulin-like growth factor-I for Balb/MK keratinocyte proliferation. J. Investig. Dermatol. 1996, 106, 616–621. [Google Scholar] [CrossRef] [Green Version]
- Meyer, M.; Müller, A.K.; Yang, J.; Moik, D.; Ponzio, G.; Ornitz, D.M.; Grose, R.; Werner, S. FGF receptors 1 and 2 are key regulators of keratinocyte migration in vitro and in wounded skin. J. Cell Sci. 2012, 125, 5690–5701. [Google Scholar] [CrossRef] [Green Version]
- Peng, C.; Chen, B.; Kao, H.K.; Murphy, G.; Orgill, D.P.; Guo, L. Lack of FGF-7 further delays cutaneous wound healing in diabetic mice. Plast. Reconstr. Surg. 2011, 128, 673e–684e. [Google Scholar] [CrossRef]
- Radek, K.A.; Taylor, K.R.; Gallo, R.L. FGF-10 and specific structural elements of dermatan sulfate size and sulfation promote maximal keratinocyte migration and cellular proliferation. Wound Repair Regen. 2009, 17, 118–126. [Google Scholar] [CrossRef] [Green Version]
- Viac, J.; Palacio, S.; Schmitt, D.; Claudy, A. Expression of vascular endothelial growth factor in normal epidermis, epithelial tumors and cultured keratinocytes. Arch. Dermatol. Res. 1997, 289, 158–163. [Google Scholar] [CrossRef]
- Mann, A.; Breuhahn, K.; Schirmacher, P.; Blessing, M. Keratinocyte-derived granulocyte-macrophage colony stimulating factor accelerates wound healing: Stimulation of keratinocyte proliferation, granulation tissue formation, and vascularization. J. Investig. Dermatol. 2001, 117, 1382–1390. [Google Scholar] [CrossRef] [Green Version]
- Oike, Y.; Yasunaga, K.; Ito, Y.; Matsumoto, S.; Maekawa, H.; Morisada, T.; Arai, F.; Nakagata, N.; Takeya, M.; Masuho, Y.; et al. Angiopoietin-related growth factor (AGF) promotes epidermal proliferation, remodeling, and regeneration. Proc. Natl. Acad. Sci. USA 2003, 100, 9494–9499. [Google Scholar] [CrossRef] [Green Version]
- Ranzato, E.; Patrone, M.; Pedrazzi, M.; Burlando, B. HMGb1 promotes scratch wound closure of HaCaT keratinocytes via ERK1/2 activation. Mol. Cell. Biochem. 2009, 332, 199–205. [Google Scholar] [CrossRef]
- Straino, S.; Di Carlo, A.; Mangoni, A.; De Mori, R.; Guerra, L.; Maurelli, R.; Panacchia, L.; Di Giacomo, F.; Palumbo, R.; Di Campli, C.; et al. High-mobility group box 1 protein in human and murine skin: Involvement in wound healing. J. Investig. Dermatol. 2008, 128, 1545–1553. [Google Scholar] [CrossRef] [PubMed]
- Woodley, D.T.; Wysong, A.; DeClerck, B.; Chen, M.; Li, W. Keratinocyte Migration and a Hypothetical New Role for Extracellular Heat Shock Protein 90 Alpha in Orchestrating Skin Wound Healing. Adv. Wound Care 2015, 4, 203–212. [Google Scholar] [CrossRef] [Green Version]
- Guo, J.; Chang, C.; Li, W. The role of secreted heat shock protein-90 (Hsp90) in wound healing—How could it shape future therapeutics? Expert Rev. Proteom. 2017, 14, 665–675. [Google Scholar] [CrossRef]
- Cheng, C.-F.; Fan, J.; Fedesco, M.; Guan, S.; Li, Y.; Bandyopadhyay, B.; Bright, A.M.; Yerushalmi, D.; Liang, M.; Chen, M.; et al. Transforming Growth Factor α (TGFα)-Stimulated Secretion of HSP90α: Using the Receptor LRP-1/CD91 To Promote Human Skin Cell Migration against a TGFβ-Rich Environment during Wound Healing. Mol. Cell. Biol. 2008, 28, 3344–3358. [Google Scholar] [CrossRef] [Green Version]
- Zhang, Y.; Bai, X.; Wang, Y.; Li, N.; Li, X.; Han, F.; Su, L.; Hu, D. Role for heat shock protein 90α in the proliferation and migration of HaCaT cells and in the deep second-degree burn wound healing in mice. PLoS ONE 2014, 9, e103723. [Google Scholar] [CrossRef] [PubMed]
- Tang, A.; Gilchrest, B.A. Regulation of keratinocyte growth factor gene expression in human skin fibroblasts. J. Dermatol. Sci. 1996, 11, 41–50. [Google Scholar] [CrossRef]
- Gallucci, R.M.; Sloan, D.K.; Heck, J.M.; Murray, A.R.; O’Dell, S.J. Interleukin 6 indirectly induces keratinocyte migration. J. Investig. Dermatol. 2004, 122, 764–772. [Google Scholar] [CrossRef] [Green Version]
- Devalaraja, R.M.; Nanney, L.B.; Qian, Q.; Du, J.; Yu, Y.; Devalaraja, M.N.; Richmond, A. Delayed wound healing in CXCR 2 knockout mice. J. Investig. Dermatol. 2000, 115, 234–244. [Google Scholar] [CrossRef] [Green Version]
- Yates, C.C.; Whaley, D.; Hooda, S.; Hebda, P.A.; Bodnar, R.J.; Wells, A. Delayed reepithelialization and basement membrane regeneration after wounding in mice lacking CXCR3. Wound Repair Regen. 2009, 17, 34–41. [Google Scholar] [CrossRef] [Green Version]
- Tortelli, F.; Pisano, M.; Briquez, P.S.; Martino, M.M.; Hubbell, J.A. Fibronectin Binding Modulates CXCL11 Activity and Facilitates Wound Healing. PLoS ONE 2013, 8, e79610. [Google Scholar] [CrossRef] [Green Version]
- Iocono, J.A.; Colleran, K.R.; Remick, D.G.; Gillespie, B.W.; Ehrlich, H.P.; Garner, W.L. Interleukin-8 levels and activity in delayed-healing human thermal wounds. Wound Repair Regen. 2000, 8, 216–225. [Google Scholar] [CrossRef]
- Da Silva, L.; Carvalho, E.; Cruz, M.T. Role of neuropeptides in skin inflammation and its involvement in diabetic wound healing. Expert Opin. Biol. Ther. 2010, 10, 1427–1439. [Google Scholar] [CrossRef]
- Roggenkamp, D.; Köpnick, S.; Stäb, F.; Wenck, H.; Schmelz, M.; Neufang, G. Epidermal nerve fibers modulate keratinocyte growth via neuropeptide signaling in an innervated skin model. J. Investig. Dermatol. 2013, 133, 1620–1628. [Google Scholar] [CrossRef] [Green Version]
- Wollina, U.; Huschenbeck, J.; Knöll, B.; Sternberg, B.; Hipler, U.C. Vasoactive intestinal peptide supports induced migration of human keratinocytes and their colonization of an artificial polyurethane matrix. Regul. Pept. 1997, 70, 29–36. [Google Scholar] [CrossRef]
- Sung, K.J.; Chang, S.E.; Paik, E.M.; Lee, M.W.; Choi, J.H. Vasoactive intestinal polypeptide stimulates the proliferation of HaCat cell via TGF-α. Neuropeptides 1999, 33, 435–446. [Google Scholar] [CrossRef]
- Kakurai, M.; Demitsu, T.; Umemoto, N.; Kobayashi, Y.; Inoue-Narita, T.; Fujita, N.; Ohtsuki, M.; Furukawa, Y. Vasoactive intestinal peptide and inflammatory cytokines enhance vascular endothelial growth factor production from epidermal keratinocytes. Br. J. Dermatol. 2009, 161, 1232–1238. [Google Scholar] [CrossRef]
- Altun, V.; Hakvoort, T.E.; van Zuijlen, P.P.M.; van der Kwast, T.H.; Prens, E.P. Nerve outgrowth and neuropeptide expression during the remodeling of human burn wound scars. Burns 2001, 27, 717–722. [Google Scholar] [CrossRef]
- Delgado, A.V.; McManus, A.T.; Chambers, J.P. Exogenous administration of substance P enhances wound healing in a novel skin-injury model. Exp. Biol. Med. 2005, 230, 271–280. [Google Scholar] [CrossRef]
- Gibran, N.S.; Tamura, R.; Tsou, R.; Isik, F.F. Human dermal microvascular endothelial cells produce nerve growth factor: Implications for wound repair. Shock 2003, 19, 127–130. [Google Scholar] [CrossRef] [Green Version]
- McGovern, U.B.; Jones, K.T.; Sharpe, G.R. Intracellular calcium as a second messenger following growth stimulation of human keratinocytes. Br. J. Dermatol. 1995, 132, 892–896. [Google Scholar] [CrossRef]
- Tanaka, T.; Danno, K.; Ikai, K.; Imamura, S. Effects of substance P and substance K on the growth of cultured keratinocytes. J. Investig. Dermatol. 1988, 90, 399–401. [Google Scholar] [CrossRef] [Green Version]
- Shi, X.; Wang, L.; Clark, J.D.; Kingery, W.S. Keratinocytes express cytokines and nerve growth factor in response to neuropeptide activation of the ERK1/2 and JNK MAPK transcription pathways. Regul. Pept. 2013, 186, 92–103. [Google Scholar] [CrossRef] [Green Version]
- Kumar, S.; Tan, Y.; Berthiaume, F. Neuropeptide substance p enhances skin wound healing in vitro and in vivo under hypoxia. Biomedicines 2021, 9, 222. [Google Scholar] [CrossRef]
- Gibran, N.S.; Jang, Y.C.; Isik, F.F.; Greenhalgh, D.G.; Muffley, L.A.; Underwood, R.A.; Usui, M.L.; Larsen, J.; Smith, D.G.; Bunnett, N.; et al. Diminished neuropeptide levels contribute to the impaired cutaneous healing response associated with diabetes mellitus. J. Surg. Res. 2002, 108, 122–128. [Google Scholar] [CrossRef]
- Spenny, M.L.; Muangman, P.; Sullivan, S.R.; Bunnett, N.W.; Ansel, J.C.; Olerud, J.E.; Gibran, N.S. Neutral endopeptidase inhibition in diabetic wound repair. Wound Repair Regen. 2002, 10, 295–301. [Google Scholar] [CrossRef]
- Moura, L.I.; Cruz, M.T.; Carvalho, E. The effect of neurotensin in human keratinocytes—Implication on impaired wound healing in diabetes. Exp. Biol. Med. 2014, 239, 6–12. [Google Scholar] [CrossRef]
- Dallos, A.; Kiss, M.; Polyánka, H.; Dobozy, A.; Kemény, L.; Husz, S. Effects of the neuropeptides substance P, calcitonin gene-related peptide, vasoactive intestinal polypeptide and galanin on the production of nerve growth factor and inflammatory cytokines in cultured human keratinocytes. Neuropeptides 2006, 40, 251–263. [Google Scholar] [CrossRef]
- Dallos, A.; Kiss, M.; Polyánka, H.; Dobozy, A.; Kemény, L.; Husz, S. Galanin receptor expression in cultured human keratinocytes and in normal human skin. J. Peripher. Nerv. Syst. 2006, 11, 156–164. [Google Scholar] [CrossRef]
- Bigliardi, P.L.; Büchner, S.; Rufli, T.; Bigliardi-Qi, M. Specific stimulation of migration of human keratinocytes by μ-opiate receptor agonists. J. Recept. Signal Transduct. Res. 2002, 22, 191–199. [Google Scholar] [CrossRef]
- Chernyavsky, A.I.; Arrendondo, J.; Marubio, L.M.; Grando, S.A. Differential regulation of keratinocyte chemokinesis and chemotaxis through distinct nicotinic receptor subtypes. J. Cell Sci. 2004, 117, 5665–5679. [Google Scholar] [CrossRef] [Green Version]
- Chernyavsky, A.I.; Arredondo, J.; Vetter, D.E.; Grando, S.A. Central role of α9 acetylcholine receptor in coordinating keratinocyte adhesion and motility at the initiation of epithelialization. Exp. Cell Res. 2007, 313, 3542–3555. [Google Scholar] [CrossRef] [Green Version]
- Chernyavsky, A.I.; Arredondo, J.; Wess, J.; Karlsson, E.; Grando, S.A. Novel signaling pathways mediating reciprocal control of keratinocyte migration and wound epithelialization through M3 and M4 muscarinic receptors. J. Cell Biol. 2004, 166, 261–272. [Google Scholar] [CrossRef] [Green Version]
- Sudbeck, B.D.; Pilcher, B.K.; Welgus, H.G.; Parks, W.C. Induction and repression of collagenase-1 by keratinocytes is controlled by distinct components of different extracellular matrix compartments. J. Biol. Chem. 1997, 272, 22103–22110. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Varani, J.; Perone, P.; Deming, M.O.B.; Warner, R.L.; Aslam, M.N.; Bhagavathula, N.; Dame, M.K.; Voorhees, J.J. Impaired keratinocyte function on matrix metalloproteinase-1 (MMP-1) damaged collagen. Arch. Dermatol. Res. 2009, 301, 497–506. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Imai, K.; Hiramatsu, A.; Fukushima, D.; Pierschbacher, M.D.; Okada, Y. Degradation of decorin by matrix metalloproteinases: Identification of the cleavage sites, kinetic analyses and transforming growth factor-β1 release. Biochem. J. 1997, 322, 809–814. [Google Scholar] [CrossRef]
- Ruttanapattanakul, J.; Wikan, N.; Okonogi, S.; Na Takuathung, M.; Buacheen, P.; Pitchakarn, P.; Potikanond, S.; Nimlamool, W. Boesenbergia rotunda extract accelerates human keratinocyte proliferation through activating ERK1/2 and PI3K/Akt kinases. Biomed. Pharmacother. 2021, 133, 111002. [Google Scholar] [CrossRef]
- Ziemlewska, A.; Zagórska-Dziok, M.; Nizioł-Łukaszewska, Z. Assessment of cytotoxicity and antioxidant properties of berry leaves as by-products with potential application in cosmetic and pharmaceutical products. Sci. Rep. 2021, 11, 3240. [Google Scholar] [CrossRef]
- Muniandy, K.; Gothai, S.; Tan, W.S.; Kumar, S.S.; Mohd Esa, N.; Chandramohan, G.; Al-Numair, K.S.; Arulselvan, P. In Vitro Wound Healing Potential of Stem Extract of Alternanthera sessilis. Evid.-Based Complement. Altern. Med. 2018, 2018, 142073. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Di Martino, O.; Tito, A.; De Lucia, A.; Cimmino, A.; Cicotti, F.; Apone, F.; Colucci, G.; Calabrò, V. Hibiscus syriacus Extract from an Established Cell Culture Stimulates Skin Wound Healing. Biomed. Res. Int. 2017, 2017, 7932019. [Google Scholar] [CrossRef] [Green Version]
- Park, S.M.; Won, K.J.; Hwang, D.I.; Kim, D.Y.; Kim, H.B.; Li, Y.; Lee, H.M. Potential Beneficial Effects of Digitaria ciliaris Flower Absolute on the Wound Healing-Linked Activities of Fibroblasts and Keratinocytes. Planta Med. 2020, 86, 348–355. [Google Scholar] [CrossRef] [PubMed]
- Csepregi, R.; Temesfői, V.; Das, S.; Alberti, Á.; Tóth, C.A.; Herczeg, R.; Papp, N.; Kőszegi, T. Cytotoxic, antimicrobial, antioxidant properties and effects on cell migration of phenolic compounds of selected transylvanian medicinal plants. Antioxidants 2020, 9, 166. [Google Scholar] [CrossRef] [Green Version]
- Paudel, S.B.; Park, J.; Kim, N.H.; Choi, H.; Seo, E.K.; Woo, H.A.; Nam, J.W. Constituents of the leaves and twigs of Elaeagnus umbellata and their proliferative effects on human keratinocyte HaCaT cells. Fitoterapia 2019, 139, 104374. [Google Scholar] [CrossRef]
- Prado, L.G.; Arruda, H.S.; Peixoto Araujo, N.M.; de Oliveira Braga, L.E.; Banzato, T.P.; Pereira, G.A.; Figueiredo, M.C.; Ruiz, A.L.T.G.; Eberlin, M.N.; de Carvalho, J.E.; et al. Antioxidant, antiproliferative and healing properties of araticum (Annona crassiflora Mart.) peel and seed. Food Res. Int. 2020, 133, 109168. [Google Scholar] [CrossRef]
- Kisseih, E.; Lechtenberg, M.; Petereit, F.; Sendker, J.; Zacharski, D.; Brandt, S.; Agyare, C.; Hensel, A. Phytochemical characterization and in vitro wound healing activity of leaf extracts from Combretum mucronatum Schum. & Thonn.: Oligomeric procyanidins as strong inductors of cellular differentiation. J. Ethnopharmacol. 2015, 174, 628–636. [Google Scholar] [CrossRef] [PubMed]
- Dorjsembe, B.; Lee, H.J.; Kim, M.; Dulamjav, B.; Jigjid, T.; Nho, C.W. Achillea asiatica extract and its active compounds induce cutaneous wound healing. J. Ethnopharmacol. 2017, 206, 306–314. [Google Scholar] [CrossRef]
- Chin, C.Y.; Jalil, J.; Ng, P.Y.; Ng, S.F. Development and formulation of Moringa oleifera standardised leaf extract film dressing for wound healing application. J. Ethnopharmacol. 2018, 212, 188–199. [Google Scholar] [CrossRef] [PubMed]
- De Moura Sperotto, N.D.; Steffens, L.; Veríssimo, R.M.; Henn, J.G.; Péres, V.F.; Vianna, P.; Chies, J.A.B.; Roehe, A.; Saffi, J.; Moura, D.J. Wound healing and anti-inflammatory activities induced by a Plantago australis hydroethanolic extract standardized in verbascoside. J. Ethnopharmacol. 2018, 225, 178–188. [Google Scholar] [CrossRef]
- Azmi, L.; Shukla, I.; Goutam, A.; Rao, C.V.; Jawaid, T.; Kamal, M.; Awaad, A.S.; Alqasoumi, S.I.; AlKhamees, O.A. In vitro wound healing activity of 1-hydroxy-5,7-dimethoxy-2-naphthalene-carboxaldehyde (HDNC)and other isolates of Aegle marmelos L.: Enhances keratinocytes motility via Wnt/β-catenin and RAS-ERK pathways. Saudi Pharm. J. 2019, 27, 532–539. [Google Scholar] [CrossRef]
- Juneja, K.; Mishra, R.; Chauhan, S.; Gupta, S.; Roy, P.; Sircar, D. Metabolite profiling and wound-healing activity of Boerhavia diffusa leaf extracts using in vitro and in vivo models. J. Tradit. Complement. Med. 2020, 10, 52–59. [Google Scholar] [CrossRef]
- Mazumdar, S.; Ghosh, A.K.; Dinda, M.; Das, A.K.; Das, S.; Jana, K.; Karmakar, P. Evaluation of wound healing activity of ethanol extract of Annona reticulata L. leaf both in vitro and in diabetic mice model. J. Tradit. Complement. Med. 2021, 11, 27–37. [Google Scholar] [CrossRef] [PubMed]
- Azis, H.A.; Taher, M.; Ahmed, A.S.; Sulaiman, W.M.A.W.; Susanti, D.; Chowdhury, S.R.; Zakaria, Z.A. In vitro and In vivo wound healing studies of methanolic fraction of Centella asiatica extract. S. Afr. J. Bot. 2017, 108, 163–174. [Google Scholar] [CrossRef]
- Petpiroon, N.; Suktap, C.; Pongsamart, S.; Chanvorachote, P.; Sukrong, S. Kaempferol-3-O-rutinoside from Afgekia mahidoliae promotes keratinocyte migration through FAK and Rac1 activation. J. Nat. Med. 2015, 69, 340–348. [Google Scholar] [CrossRef]
- Moriyama, M.; Moriyama, H.; Uda, J.; Kubo, H.; Nakajima, Y.; Goto, A.; Akaki, J.; Yoshida, I.; Matsuoka, N.; Hayakawa, T. Beneficial effects of the genus Aloe on wound healing, cell proliferation, and differentiation of epidermal keratinocytes. PLoS ONE 2016, 11, e0164799. [Google Scholar] [CrossRef] [PubMed]
- Girija, D.M.; Kalachaveedu, M.; Subbarayan, R.; Jenifer, P.; Rao, S.R. Aristolochia bracteolata enhances wound healing in vitro through anti-inflammatory and proliferative effect on human dermal fibroblasts and keratinocytes. Pharmacogn. J. 2017, 9, s129–s136. [Google Scholar] [CrossRef] [Green Version]
- Kim, M.; Lee, H.J.; Randy, A.; Yun, J.H.; Oh, S.R.; Nho, C.W. Stellera chamaejasme and its constituents induce cutaneous wound healing and anti-inflammatory activities. Sci. Rep. 2017, 7, 42490. [Google Scholar] [CrossRef] [Green Version]
- Seo, S.H.; Lee, S.H.; Cha, P.H.; Kim, M.Y.; Min, D.S.; Choi, K.Y. Polygonum aviculare L. And its active compounds, quercitrin hydrate, caffeic acid, and rutin, activate the Wnt/β-catenin pathway and induce cutaneous wound healing. Phyther. Res. 2016, 30, 848–854. [Google Scholar] [CrossRef] [PubMed]
- Bridi, H.; Beckenkamp, A.; Ccana-Ccapatinta, G.V.; de Loreto Bordignon, S.A.; Buffon, A.; von Poser, G.L. Characterization of Phloroglucinol-enriched Fractions of Brazilian Hypericum Species and Evaluation of Their Effect on Human Keratinocytes Proliferation. Phyther. Res. 2017, 31, 62–68. [Google Scholar] [CrossRef] [Green Version]
- Évora, A.; De Freitas, V.; Mateus, N.; Fernandes, I. The effect of anthocyanins from red wine and blackberry on the integrity of a keratinocyte model using ECIS. Food Funct. 2017, 8, 3989–3998. [Google Scholar] [CrossRef]
- Moghadam, S.E.; Ebrahimi, S.N.; Salehi, P.; Farimani, M.M.; Hamburger, M.; Jabbarzadeh, E. Wound healing potential of chlorogenic acid and myricetin-3-o-β-rhamnoside isolated from Parrotia persica. Molecules 2017, 22, 1501. [Google Scholar] [CrossRef] [PubMed] [Green Version]
Name of the Species/Family | Part of the Plant | Type of Extract | Cell Line | Identified Compounds | Mechanism of Action | Effects | Ref. |
---|---|---|---|---|---|---|---|
Andrographis paniculata (Burm.f.) Nees (Acanthaceae) | leaves | methanolic | HaCaT stimulated by hydrogen peroxide | andrographolide | Inhibition: ROS production | antioxidant | [37] |
Acer rubrum L. (Sapindaceae) | leaves | MaplifaTM | HaCaT stimulated by hydrogen peroxide and methylglyoxal | ginnalin A | Induction: cell viability Inhibition: ROS production, caspases-3/7 and -8 release | antioxidant cytoprotective anti-apoptotic | [38] |
Moringa oleifera Lam. (Moringaceae) | stem | ethanolic | HaCaT stimulated by hydrogen peroxide | luteolin, rutin, quercetin | Induction: SOD and CAT, activation of PPARα Inhibition: ROS production | antioxidant | [39] |
Lagerstroemia speciosa (L.) Pers. and Lagerstroemia floribunda Jack (Lythraceae) | flowers | ethanolic | HaCaT stimulated by hydrogen peroxide | ellagic acid, epicatechin gallate, and quercetin | Inhibition: hydrogen peroxide-induced cell death | antioxidant anti-apoptotic | [40] |
Punica granatum L. (Lythraceae) | fruits | Pomella® | HaCaT stimulated by hydrogen peroxide | punicalagins, ellagic acid and urolithin A | Inhibition: ROS production, apoptotic cells formation, caspase 3 production | anti-oxidant anti-apoptotic | [41] |
Castanea sativa Mill. (Fagaceae) | chestnut shells, and inner chestnut shells | aqueous | HaCaT stimulated by hydrogen peroxide | gallic acid | Inhibition: oxidized lipids, NO and iNOS production, collagen degradation | cytoprotective antioxidant | [42] |
Oenothera biennis L. (Onagraceae) | aerial parts | ethanolic | HaCaT stimulated by hydrogen peroxide | 3-caeoylquinic acid, ellagic acid, and quercetin 3-O-glucuronide, quercetin | Induction: cell viability, heme oxygenase-1 (HO-1) Inhibition: DNA damages, caspase-3, PARP | cytoprotective antioxidant anti-apoptotic | [43] |
Himantoglossum robertianum (Loisel.) P.Delforge (Orchidaceae) | flowers | ethanolic | HaCaT stimulated by hydrogen peroxide | flavones and flavan-3-ols, scopoletin, and phenolic acids | Induction: cell viability and motility Inhibition: elastase and collagenase | cytoprotective antioxidant stimulate migration | [44] |
Myrciaria dubia (Kunth) McVaugh (Myrtaceae) | fruit | ethanolic | HaCaT stimulated by high glucose | ellagic acid and quercetin | Induction: Nrf2 Inhibition: MAPK/AP-1, NF-κB | antioxidant anti-inflammatory | [45] |
Clitoria ternatea L. (Fabaceae) | flowers | aqueous | HaCaT stimulated by hydrogen peroxide | anthocyanins derived from delphinidin, including polyacylated ternatins, and flavonol glycosides derived from quercetin and kaempferol | Inhibition: cytotoxicity effects of H2O2 | antioxidant | [46] |
Name of the Species/Family | Part of the Plant | Type of Extract | Cell Line | Identified Compounds | Mechanism of Action | Effects | Ref. |
---|---|---|---|---|---|---|---|
Rydingia persica (Burm.f.) Scheen & V.A.Albert (Lamiaceae) | aerial parts | methanolic | HaCaT stimulated by LPS | labdane-type diterpenoids | Inhibition: IL-6 and TNF-α release | anti-inflammatory | [78] |
Andrographis paniculata (Burm.f.) Nees (Acanthaceae) | leaves | methanolic | HaCaT stimulated by LPS/TNF-α | andrographolide | Induction: IL-8 secretion Inhibition: TNF-α expression | anti-inflammatory | [37] |
Curcuma aromatica Salisb. (Zingiberaceae) | rhizome | ethanolic | HaCaT stimulated by TNF-α | germacrone, curdione, dehydrocurdione, zederone, curcumenol, curcumin | Inhibition: NF-κB activation | anti-inflammatory | [79] |
Crateva adansonii DC. (Capparaceae) | leaves | aqueous | HPEKs infected by Staphylococcus aureus | quercitrin, isoquercitrin, quercetin-3-O-(b-d-xylopyranosyl-a-l-rhamnopyranoside) | Inhibition: IL-6, IL-8 and TNFα expression | anti-inflammatory | [80] |
Perilla frutescens var. crispa (Thunb.) H.Deane (Lamiaceae) | leaves | ethanolic | HaCaT stimulated by TNF-α/IFN-γ | caffeic acid, rosmarinic acid, luteolin | Inhibition: p38, ERK, and JNK expression; STAT-1 and NK-κB activation | anti-inflammatory | [81] |
Rhus coriaria L. (Anacardiaceae) | fruits | ethanolic | HaCaT stimulated by TNF-α | rutin, quercetin derivative, gallotannins | Inhibition: NF-κB activation; ICAM-1, and MMP-9 secretion | anti-inflammatory | [82] |
Ampelopsis glandulosa (Wall.) Momiy. (Vitaceae) | rhizome | ethanolic | HaCaT stimulated by TNF-α/IFN-γ | betulin, betulinic acid, β-sitosterol, β-5 sitosterol glucoside, dihydrokaempferol, dihydrokaempferol 3-O-glycoside, catechin, gallic acid, vanillic acid, ethyl gallate, ethyl gallate 4-O-β-D7glucopyranoside, syringic acid, benzyl 6ʹ-O-galloyl-β-d-glucopyranoside, ellagic acid, 3ʹ-O-methylellagic acid 4-O-α-l-rhamnopyranoside, 3,3′4′-O-tri-methylellagic acid 4-O-β-d-glucopyranoside, and resveratrol | Inhibition: TNF-α, IL-6, IL-1β, and CCL17 expression; STAT-1, NK-κB, ERK and p38 activation | anti-inflammatory | [83] |
Sanguisorba officinalis L. (Rosaceae) | roots | ethanolic | HaCaT stimulated by TNF-α/IFN-γ | (+)-catechin, (–)-epicatechin, ziyuglycoside | Inhibition: macrophage-derived chemokine (MDC), normal T-cell expressed and secreted (RANTES), IL-8 and thymus and activation regulated chemokine (TARC) production; STAT-1, ERK and NF-κB activation | anti-inflammatory | [84] |
Gleditsia sinensis Lam. (Fabaceae) | thorns | ethanolic | HaCaT stimulated by TNF-α/IFN-γ | (+)catechin, epicatechin, eriodictyol and quercetin, caffeic acid and ethyl gallate | Inhibition: MDC and TARC production | anti-inflammatory | [85] |
Morus alba L. (Moraceae) | barks | aqueous | HaCaT stimulated by TRAIL | moracin O and P | Induction: antiapoptotic proteins Bcl-xL and Bcl-2 Inhibition: NFκB activation | anti-inflammatory anti-apoptotic | [86] |
Morus alba L. (Moraceae) | root bark | ethanolic | HaCaT stimulated by TNF- α/IFN-γ | kuwanon G and morusin | Inhibition: RANTES/CCL5, TARC/CCL17, and MDC/CCL22 secretion; STAT 1 and NF-κB activation | anti-inflammatory | [87] |
Combretum collinum Fresen. (Combretaceae) | leaves | aqueous | HaCaT stimulated by TNF-α | myricetin-3-O-rhamnoside and myricetin-3-O-glucoside | Inhibition: IL-8 secretion | anti-inflammatory | [88] |
Aucklandia lappa DC. (Asteraceae) | whole extract | methanolic | HaCaT stimulated by TNF-α/IFN-γ | alantolactone, caryophyllene, costic acid, costunolide, and dehydrocostuslactone | Inhibition: TARC, RANTES, MDC and IL-8 production; STAT1 activation | anti-inflammatory | [89] |
Quercus mongolica Fisch. ex Ledeb. (Fagaceae) | leaves | acetone | HaCaT stimulated by LPS | pedunculagin | Inhibition: IL-6 and IL-8 production | anti-inflammatory | [90] |
Melaleuca styphelioides Sm. (Myrtaceae) | leaves | methanolic | NCTC 2544 keratinocytes stimulated by IFN-γ/histamine | quercetin, gallic acid, ellagic acid | Inhibition: ICAM-1, iNOS, COX-2, NF-κB | anti-inflammatory antioxidant | [91] |
Carpinus tschonoskii Maxim. (Betulaceae) | leaves | ethanolic | HaCaT cells stimulated by LPS | tellimagrandin I | Inhibition: IL-6 production | anti-inflammatory | [92] |
Name of the Species/Family | Part of the Plant | Type of Extract | Cell Line | Identified Compounds | Mechanism of Action | Effects | Ref. |
---|---|---|---|---|---|---|---|
Petasites japonicus (Siebold & Zucc.) Maxim. (Asteraceae) | leaves | methanolic | NHEKs exposed to UVB irradiation | kaempferol-3-O-(6″-acetyl)-β-d-glucoside, quercetin-3-O-(6″-acetyl)-β-d-glucoside, kaempferol-3-O-β-d-glucoside, and quercetin-3-O-β-d-glucoside | Induction: Nrf2 and heat-shock response transcription elements (HSE) that resulted in the induction of heme oxygenase-1 (HO-1) and HSP70, respectively | Protection against UV-induced cell damages, anti-apoptotic | [142] |
Rubus idaeus L. (Rosaceae) | fruits | ethanolic | HaCaT exposed to UVB radiation | cyanidin, ellagic acid, pelagonidin-3-sophoroside, methylquercetin-pentose conjugate, and cyanidin-3-rutinoside | Induction: SOD, Nrf2, and HO-1. Inhibition: caspase-3, c-jun modulation; NF-κB and COX-2 activation | antioxidant, anti-apoptototic anti-inflammatory | [143] |
Castanea sativa Mill. (Fagaceae) | leaves | methanolic | HaCaT exposed to UVB radiation | crenatin, chestanin, gallic acid, cretanin, 5-O-p-coumaroylquinic acid, p-methylgallic acid and quercetin-3-O-glucoside | Inhibition: p53 expression | protection against UVB-induced cell damages, antioxidant | [144] |
Potentilla kleiniana Wight et Arn (Rosaceae) | whole plant | ethanolic | HaCaT exposed to UVB radiation | diosmetin-7-O-neohesperidoside, dimethylellagic acid hexose, zizybeoside I, 4-O-[b-d-xylopyranosyl]-3,30-di-O-methylellagic acid, and buddlenol A | Inhibition: caspase-3 | cytoprotective effect | [145] |
Crepidiastrum denticulatum (Houtt.) Pak & Kawano (Asteraceae) | whole plant | ethanolic | HaCaT exposed to UVB radiation | chicoric acid, 3,5dicaffeoylquinic acid, chlorogenic acid, luteolin 7-O-glucuronide, youngiaside A, youngiaside B, youngiaside C | Induction: antioxidant enzymes expression Inhibition: ROS release, MAPKs, AP-1 and NF-κB activation | antioxidant, anti-inflammatory | [146] |
Vitis vinifera L. (Vitaceae) | leaves | aqueous | HaCaT exposed to UVB radiation | caftaric acid, rutin, hyperoside, quercetin 3-O-glucoside, quercetin 3-O-glucuronide, kaempferol 3-O-glucoside, delphinidin 3-O-glucoside, cyanidin 3-O-glucoside, petunidin 3-O-glucoside, peonidin 3-O-glucoside, malvidin 3-O-glucoside | Inhibition: IL-8 secretion | anti-inflammatory | [147] |
Dalbergia odorifera T.C.Chen (Fabaceae) | heartwood | ethanolic | HPEKs exposed to UVB radiation | sativanone | Inhibition: ROS release, p53 and p21 protein production | antioxidant, anti-senescence | [148] |
Opuntia ficus-indica (L.) Mill. (Cactaceae) | stems | aqueous | HaCaT exposed to UVA radiation | eucomic and piscidic acids | Inhibition: ROS production, lipid peroxidation and GSH depletion | antioxidant | [149] |
Melissa officinalis L. (Lamiaceae) | leaves | ethanolic | HaCaT exposed to UVB radiation | rosmarinic acid, salvianolic acid derivatives, caffeic acid and luteolin glucuronide | Inhibition: ROS production, DNA damage and DNA damage response | cytoprotective antioxidant | [150] |
Rhus javanica L. (Anacardiaceae) | whole plant | ethanolic | HaCaT exposed to UVB radiation | gallic acid, 5-O-galloyl-β-d-glucose, Methyl gallate, Syringic acid, Protocatechuic acid | Inhibition: COX-1, MMP-1 exprwssion; MAPK, AKT, EGFR activity | antioxidant, anti-inflammatory | [151] |
Juglans regia L. (Juglandaceae) | flowers | methanolic | HaCaT exposed to UVB radiation | 3,7-dimethyl-1,6-octadiene, pentadecanoic acid, 14-methyl, methyl ester, 2-(2,6-dimethoxy-benzoylamino)-propionic acid, ethyl ester, hexadecanoic acid, ethyl ester (palmitic acid), 10-octadecenoic acid, methyl ester, erucic acid; 1,2,3-benzothiadiazole; estra-1,3,5(10),6-tetraene-3,17-diol, (17β)-; 17-acetate, 2,2,4-trimethyl-3- (3,8,12,16-tetramethyl-heptadeca-3,7,11,15-tetraenyl)-cyclohexanol and oleic acid, trimethylsilyl ester | Inhibition: ROS production, lipid peroxidation, TNF-α, IL-1, IL-6, NF-κB, COX-2 activation | antioxidant, anti-inflammatory | [152] |
Portulaca oleracea L. (Portulacaceae) | whole plant | methanolic | HaCaT exposed to UVB radiation | portulacanone A and portulacanon D | Induction: SOD expression, and HO-1 via Nrf2 pathway Inhibition: ROS production | antioxidant | [153] |
Rosa multiflora Thunb. (Rosaceae) | flowers | ethanolic | HaCaT exposed to UVB radiation | quercitrin, hyperin, and isoquercetin | Inhibition: ROS production, IL-6, IL-8 MMP1; NF-κB activation | anti-oxidant anti-inflammatory | [154] |
Rhodomyrtus tomentosa (Aiton) Hassk. (Myrtaceae) | fruits | ethanolic | NHEKs exposed to UVB radiation | piceatannol | Inhibition: cyclobutane pyrimidine dimers formation, prostaglandin E2 secretion Induction: enzyme activity of the DNA polymerases | cytoprotective anti-inflammatory | [155] |
Cecropia obtusa Trécul (Urticaceae) | leaves | methanol | HaCaT exposed to UVB radiation | chlorogenic acid, luteolin-C-hexoside, luteolin-Chexose-O-deoxy-hexose, and apigenin-C-hexose-O-deoxy-hexose | Inhibition: MMP-1, IL-1β and IL-6 | anti-inflammatory | [156] |
Scutellaria baicalensis Georgi (Lamiaceae) | roots | ethanolic | HaCaT exposed to UVB radiation | baicalin, wogonoside, baicalein and wogonin | Induction: HO-1; Nrf2 activation Inhibition: MMP-1, IL-6; MAPK, AP-1 and NF-κB activation | cytoprotective anti-inflammatory antioxidant | [157] |
Spatholobus suberectus Dunn (Fabaceae) | stem | aqueous and ethanolic | HaCaT exposed to UVB radiation | gallic acid, catechin, vanillic acid, syringic acid and epicatechin | Inhibition: ROS production; MAPKs, NF-κB, c-Jun activation | anti-inflammatory antioxidant | [158] |
Adenocaulon himalaicum Edgew. (Asteraceae) | leaves | ethanol | HaCaT exposed to UVB radiation | neochlorogenic acid | Induction: filaggrin, involucrin, loricrin expression Inhibition: MMP-1; MAPK, AP-1 activation | hydration anti-inflammatory antioxidant | [159] |
Paeonia × suffruticosa Andrews (Paeoniaceae) | roots | ethanol | HaCaT exposed to UVB radiation | paeonol | Induction HO-1; Nrf2 activation Inhibition: MAPK | cytoprotective, antioxidant | [160] |
Aquilaria crassna Pierre ex Lecomte (Thymelaeaceae) | leaves | aqueous/ethanolic | NHEKs exposed to UVB radiation | iriflophenone 3,5-C-β-d-diglucoside, iriflophenone 3-C-β-d-glucoside, mangiferin and genkwanin 5-O-β-primevoside | Inhibition: IL-1α, IL-8 and prostaglandin E2 (PGE2) | anti-inflammatory | [161] |
Aloe vera (L.) Burm.f. (Asphlodelaceae) | flowers | aqueous | HaCaT exposed to UVB radiation | isoorientin | Induction: involucrin expression | hydration | [162] |
Nymphoides indica (L.) Kuntze (Menyanthaceae) | whole plant | methanolic | HaCaT exposed to UVB radiation | quercetin 3,7-dimethyl ether 4′-glucoside | Induction: filaggrin, involucrin, loricrin expression Inhibition: MAPK, NF-κB activation | hydration cytoprotective antioxidant | [163] |
Biancaea sappan (L.) Tod. (Fabaceae) | whole plant | methanolic | NHDKs exposed to UVBA radiation | brazilin | Induction: glutathione peroxidase 7 | antioxidant | [164] |
Clitoria ternatea L. (Fabaceae) | flowers | aqueous | HaCaT exposed to UVB radiation | delphinidin, including polyacylated ternatins, and flavonol glycosides derived from quercetin and kaempferol | Inhibition: mtDNA damage | cytoprotective | [46] |
Syzygium formosum (Wall.) Masam (Myrtaceae) | leaves | ethanolic | HaCaT exposed to UVB radiation | triterpenic acids | Inhibition: IL-1β, IL-6, IL-8 and COX-2 expression | anti-inflammatory | [165] |
Aster yomena (Kitam.) Honda. (Astereae) | callus | aqueous | HaCaT exposed to UVB radiation | robustic acid, 3,5-Di-O-methyl-8-prenylafzelechin-4beta-ol, acetylpterosin C and pterosin N, L-thyronine, 3,4-dicaffeoyl-1,5-quinolactone, dehydrophytosphingosine and phytosphingosine, α-linolenic acid, palmitic amide, olemaide, and 13Z-docosenamide, and glycerophospholipids | Inducttion: type I procollagen synthesis, TGF-β expression Inhibition: ROS production, elastase production, MMP-1, MMP-3, MMP-9, TNF-α, IL-1β, IL-8 expression | cytoprotective antioxidant anti-inflammatory | [166] |
Name of the Species/Family | Part of the Plant | Type of Extract | Cell Line | Identified Compounds | Mechanism of Action | Effects | Ref. |
---|---|---|---|---|---|---|---|
Boesenbergia rotunda (L.) Mansf. (Zingiberaceae) | rhizomes | ethanolic | HaCaT | kaempferol | Induction: ERK 1/2, Akt Activation: MAPK and PI3K/Akt pathways | stimulate proliferation | [241] |
Rubus fruticosus L. (Rosaceae) | leaves | aqueous | HaCaT | phenolic compounds | - | stimulate migration | [242] |
Alternanthera sessilis (L.) R.Br. ex DC. (Amaranthaceae) | stems | ethanolic | HaCaT | 2,4-dihydroxy-2,5-dimethyl-3(2H)-furan-3-one, hexadecanoic acid <n->, 2-1,2,4-trioxolane,3-phenyl-, palmitate <ethyl- and L-glutamic acid | - | stimulate migration and proliferation | [243] |
Hibiscus syriacus L. (Malvaceae) | leaves | ethanolic | HaCaT | flavonoids, coumarins | - | stimulate migration | [244] |
Digitaria sanguinalis (L.) Scop. (Poaceae) | flowers | ethanolic | HaCaT | xycaine, hexadecanoic acid, linolenic acid, octadecanoic acid, phenol, 2,2′-methylenebis [6-(1,1-dimethylethyl)-4-methyl-, pentacosane, heptacosane, squalene, 1-docosene, cyclooctacosane, campesterol, stigmasterol, lanosterol, multiflora-7,9(11)-dien-3β-ol, sitostenone | - | stimulate proliferation | [245] |
Fuchsia magellanica Lam. (Onagraceae) | leaves | aqueous, ethanolic | HaCaT | gallic acid derivatives, hydroxycinnamic acid derivatives and flavonoid glycosides, anthocyanins | - | stimulate migration | [246] |
Elaeagnus umbellata Thunb. (Elaeagnaceae) | leaves and twigs | acetone | HaCaT | N-[2-(5-hydroxyl-1H- indol-3-yl)ethyl]-butanamide, kaempferol-3-O-β-d-xylopyranosyl(1→2)-β-d-galactopyranoside-7-O-α-l-rhamnopyranoside, kaempferol-3-O-β-d-galactopyranoside-7-O-α-Lrhamnopyranoside, kaempferol-3-O-α-l-rhamnopyranosyl(1→6)-β-d-galactopyranoside-7-O-α-l-rhamnopyranoside, kaempferol-3-O-β-d-xylopyranosyl(1→2)-β-d-galactopyranoside | - | stimulate proliferation | [247] |
Annona crassiflora Mart. (Annonaceae) | seeds | aqueous | HaCaT | catechin, epicatechin, rutin, quercetin, naringenin, protocatechuic acid, 4-hydroxybenzoic acid, vanillic acid, chlorogenic acid, caffeic acid, p-coumaric acid, ferulic acid | - | stimulate migration | [248] |
Combretum mucronatum Schumach. & Thonn. (Combretaceae) | leaf | aqueous | NHEKs | epicatechin, procyanidinB2, vitexin and isovitexin | - | stimulate migration and differentiation | [249] |
Achillea asiatica Serg. (Asteraceae) | aerial part | ethanolic | HaCaT | chlorogenic acid, schaftoside, quercetin-3-O arabinosyl(1→6)glucoside, apigenin-7-O-glucoside, luteolin, and apigenin | Induction: β-catenin, Akt | stimulate migration | [250] |
Moringa oleifera Lam. (Moringaceae) | leaves | aqueous | NHEKs | vicenin-2, chlorogenic acid, gallic acid, quercetin, kaempferol, rosmarinic acid and rutin | - | stimulate migration and proliferation | [251] |
Plantago australis Lam. (Plantaginaceae) | leaves | ethanolic | HaCaT | verbascoside | - | stimulate migration | [252] |
Aegle marmelos (L.) Corrêa (Rutaceae) | flower | ethanolic | HaCaT | cineol, aegelin, cuminaldehyde, luvangetin, 1-hydroxy-5,7-dimethoxy-2-naphthalene-carboxaldehyde, eugenol | - | stimulate migration | [253] |
Boerhavia diffusa L. (Nyctaginaceae) | leaves | methanolic | HaCaT | caffeic acid, ferulic acid and D-pinitol | - | stimulate migration | [254] |
Annona reticulata L. (Annonaceae) | leaves | ethanolic | HaCaT | quercetin and β-sitosterol | Increased: VEGF and Akt | stimulate migration and proliferation | [255] |
Centella asiatica (L.) Urb. (Apiaceae) | whole plant | methanolic | HaCaT | asiaticoside | - | stimulate migration | [256] |
Afgekia mahidoliae B. L. Burtt & Chermsir. (Fabaceae) | leaves | chloroform/methanol | HaCaT | kaempferol-3-O-arabinoside, kaempferol-3-O-glucoside, and kaempferol-3-O-rutinoside, | Induction: filopodia and lamellipodia formation, Akt | stimulate migration | [257] |
Aloe vera (L.) Burm.f. (Asphodelaceae) | leaves | aqueous | HPEKs | anthraquinones | Induction: β1-, α6-, β4-integrin, and E-cadherin expression | stimulate migration | [258] |
Aristolochia bracteolata Lam. (Aristolochiaceae) | leaves | methanolic | HaCaT | quercetin | - | stimulate migration | [259] |
Stellera chamaejasme L. (Thymelaeaceae) | aerial parts | ethanolic | HaCaT | daphnin, daphnetin-8-O-glucoside, daphnetin, rutarensin, isoquercitrin, chamechromone and daphnoretin | Induction: β-catenin, ERK and Akt | stimulate migration | [260] |
Polygonum aviculare L (Polygonaceae) | whole plant | ethanolic | HaCaT | quercitrin hydrate, caffeic acid, and rutin | Induction: Wnt/β-catenin signaling | stimulate migration | [261] |
Hypericum carinatum Griseb. (Hypericaceae) | aerial parts | n-hexane | HaCat cells | uliginosin A, japonicin A, uliginosin B, hyperbrasilol B, and the three benzopyrans, that is, 6-isobutyryl-5,7-dimethoxy-2,2-dimethyl-benzopyran, 7-hydroxy-6-isobutyryl-5-methoxy-2,2-dimethyl-benzopyran, and 5-hydroxy-6-isobutyryl-7-methoxy-2,2-dimethyl-benzopyran | - | stimulate migration | [262] |
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
Merecz-Sadowska, A.; Sitarek, P.; Zajdel, K.; Kucharska, E.; Kowalczyk, T.; Zajdel, R. The Modulatory Influence of Plant-Derived Compounds on Human Keratinocyte Function. Int. J. Mol. Sci. 2021, 22, 12488. https://doi.org/10.3390/ijms222212488
Merecz-Sadowska A, Sitarek P, Zajdel K, Kucharska E, Kowalczyk T, Zajdel R. The Modulatory Influence of Plant-Derived Compounds on Human Keratinocyte Function. International Journal of Molecular Sciences. 2021; 22(22):12488. https://doi.org/10.3390/ijms222212488
Chicago/Turabian StyleMerecz-Sadowska, Anna, Przemysław Sitarek, Karolina Zajdel, Ewa Kucharska, Tomasz Kowalczyk, and Radosław Zajdel. 2021. "The Modulatory Influence of Plant-Derived Compounds on Human Keratinocyte Function" International Journal of Molecular Sciences 22, no. 22: 12488. https://doi.org/10.3390/ijms222212488