Fowler, J. F., Woolery-Lloyd, H., Waldorf, H. & Saini, R. Innovations in natural ingredients and their use in skin care. J. Drugs Dermatol. 9, S72–S81 (2010) (quiz s82–3).
He, C.-N. et al. Phytochemical and biological studies of Paeoniaceae. Chem. Biodivers. 7, 805–838 (2010).
Dienaitė, L. et al. Isolation of strong antioxidants from paeonia officinalis roots and leaves and evaluation of their bioactivities. Antioxidants 8, 249 (2019).
Xu, S.-P. Antiproliferation and apoptosis induction of paeonol in HepG 2 cells. World J. Gastroenterol. 13, 250 (2007).
Guo, J.-P. In vitro screening of traditionally used medicinal plants in China against Enteroviruses. World J. Gastroenterol. 12, 4078 (2006).
Zheng, Y.-Q., Wei, W., Zhu, L. & Liu, J.-X. Effects and mechanisms of Paeoniflorin, a bioactive glucoside from paeony root, on adjuvant arthritis in rats. Inflamm. Res. 56, 182–188 (2007).
Yang, H. O., Ko, W. K., Kim, J. Y. & Ro, H. S. Paeoniflorin: An antihyperlipidemic agent from Paeonia lactiflora. Fitoterapia 75, 45–49 (2004).
Ning, C., Jiang, Y., Meng, J., Zhou, C. & Tao, J. Herbaceous peony seed oil: A rich source of unsaturated fatty acids and γ-tocopherol. Eur. J. Lipid Sci. Technol. 117, 532–542 (2015).
Papandreou, V. et al. Volatiles with antimicrobial activity from the roots of Greek Paeonia taxa. J. Ethnopharmacol. 81, 101–104 (2002).
Chaita, E. et al. Anti-melanogenic properties of Greek plants. A novel depigmenting agent from Morus alba wood. Molecules 22, 514 (2017).
Ali, A. M. A., El-Nour, M. E. M. & Yagi, S. M. Total phenolic and flavonoid contents and antioxidant activity of ginger (Zingiber officinale Rosc.) rhizome, callus and callus treated with some elicitors. J. Genet. Eng. Biotechnol. 16, 677–682 (2018).
Esmaeili, A. K., Taha, R. M., Mohajer, S. & Banisalam, B. Antioxidant activity and total phenolic and flavonoid content of various solvent extracts from in vivo and in vitro grown Trifolium pratense L. (red clover). Biomed. Res. Int. 2015, 1–11 (2014).
Dilkalal, A. & Umesh, T. G. Evaluation of antioxidant potential and reducing power of callus induced from leaves of a Systasia Gangetica (L.) T. Anderson. Int. J. Pharm. Pharm. Sci. 6, 532–538 (2014).
Crouch, S. P. M., Kozlowski, R., Slater, K. J. & Fletcher, J. The use of ATP bioluminescence as a measure of cell proliferation and cytotoxicity. J. Immunol. Methods 160, 81–88 (1993).
Deters, A. M., Schröder, K. R. & Hensel, A. Kiwi fruit (Actinidia chinensis L.) polysaccharides exert stimulating effects on cell proliferation via enhanced growth factor receptors, energy production, and collagen synthesis of human keratinocytes, fibroblasts, and skin equivalents. J. Cell. Physiol. 202, 717–722 (2005).
Tsai, H.-Z., Lin, R.-K. & Hsieh, T.-S. Drosophila mitochondrial topoisomerase III alpha affects the aging process via maintenance of mitochondrial function and genome integrity. J. Biomed. Sci. 23, 38 (2016).
Giampieri, F. et al. Polyphenol-rich strawberry extract protects human dermal fibroblasts against hydrogen peroxide oxidative damage and improves mitochondrial functionality. Molecules 19, 7798–7816 (2014).
Sulyok, S., Wankell, M., Alzheimer, C. & Werner, S. Activin: An important regulator of wound repair, fibrosis, and neuroprotection. Mol. Cell. Endocrinol. 225, 127–132 (2004).
Jones, K. L., de Kretser, D. M., Patella, S. & Phillips, D. J. Activin A and follistatin in systemic inflammation. Mol. Cell. Endocrinol. 225, 119–125 (2004).
Eisinger, M., Sadan, S., Silver, I. A. & Flick, R. B. Growth regulation of skin cells by epidermal cell-derived factors: Implications for wound healing. Proc. Natl. Acad. Sci. 85, 1937–1941 (1988).
Mantovani, A. et al. The chemokine system in diverse forms of macrophage activation and polarization. Trends Immunol. 25, 677–686 (2004).
Koch, A. et al. Interleukin-8 as a macrophage-derived mediator of angiogenesis. Science (80-). 258, 1798–1801 (1992).
Esposito, E. & Cuzzocrea, S. TNF-alpha as a therapeutic target in inflammatory diseases, ischemia-reperfusion injury and trauma. Curr. Med. Chem. 16, 3152–3167 (2009).
Danti, S. et al. Chitin nanofibrils and nanolignin as functional agents in skin regeneration. Int. J. Mol. Sci. 20, 2669 (2019).
Coltelli, M.-B. et al. Properties and skin compatibility of films based on poly(lactic acid) (PLA) bionanocomposites incorporating chitin nanofibrils (CN). J. Funct. Biomater. 11, 21 (2020).
Azimi, B. et al. Electrosprayed chitin nanofibril/electrospun polyhydroxyalkanoate fiber mesh as functional nonwoven for skin application. J. Funct. Biomater. 11, 62 (2020).
Donnarumma, G. et al. β-defensins: Work in progress. in 59–76 (2015). https://doi.org/10.1007/5584_2015_5016.
Fusco, A. et al. Beta-defensin-2 and beta-defensin-3 reduce intestinal damage caused by salmonella typhimurium modulating the expression of cytokines and enhancing the probiotic activity of Enterococcus faecium. J. Immunol. Res. 2017, 1–9 (2017).
Johansen, C., Bertelsen, T., Ljungberg, C., Mose, M. & Iversen, L. Characterization of TNF-α- and IL-17A-mediated synergistic induction of defb4 gene expression in human keratinocytes through IκBζ. J. Invest. Dermatol. 136, 1608–1616 (2016).
Adorno-Cruz, V. & Liu, H. Regulation and functions of integrin α2 in cell adhesion and disease. Genes Dis. 6, 16–24 (2019).
Cheli, Y. et al. Transcriptional and epigenetic regulation of the integrin collagen receptor locus ITGA1-PELO-ITGA2. Biochim. Biophys. Acta Gene Struct. Expr. 1769, 546–558 (2007).
Li, D. & Mrsny, R. J. Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin. J. Cell Biol. 148, 791–800 (2000).
Miyagawa, M. et al. Glycosylceramides purified from the japanese traditional non-pathogenic fungus aspergillus and koji increase the expression of genes involved in tight junctions and ceramide delivery in normal human epidermal keratinocytes. Fermentation 5, 43 (2019).
Pummi, K. et al. Epidermal tight junctions: ZO-1 and occludin are expressed in mature, developing, and affected skin and in vitro differentiating keratinocytes. J. Invest. Dermatol. 117, 1050–1058 (2001).
Jia, Z. et al. Calycosin alleviates allergic contact dermatitis by repairing epithelial tight junctions via down-regulating HIF-1α. J. Cell. Mol. Med. 22, 4507–4521 (2018).
Chen, D. et al. Abnormal expression of paxillin correlates with tumor progression and poor survival in patients with gastric cancer. J. Transl. Med. 11, 277 (2013).
Turner, C. E. Paxillin and focal adhesion signalling. Nat. Cell Biol. 2, E231–E236 (2000).
Sando, G. N. et al. Caveolin expression and localization in human keratinocytes suggest a role in lamellar granule biogenesis. J. Invest. Dermatol. 120, 531–541 (2003).
Blouin, C. M. et al. Lipid droplet analysis in caveolin-deficient adipocytes: alterations in surface phospholipid composition and maturation defects. J. Lipid Res. 51, 945–956 (2010).
Ovaere, P., Lippens, S., Vandenabeele, P. & Declercq, W. The emerging roles of serine protease cascades in the epidermis. Trends Biochem. Sci. 34, 453–463 (2009).
De Benedetto, A., Kubo, A. & Beck, L. A. Skin Barrier Disruption: A Requirement for Allergen Sensitization?. J. Invest. Dermatol. 132, 949–963 (2012).
Kishibe, M. Physiological and pathological roles of kallikrein-related peptidases in the epidermis. J. Dermatol. Sci. 95, 50–55 (2019).
de Koning, H. D. et al. Expression profile of cornified envelope structural proteins and keratinocyte differentiation-regulating proteins during skin barrier repair. Br. J. Dermatol. 166, 1245–1254 (2012).
Anderson, C. M. & Stahl, A. SLC27 fatty acid transport proteins. Mol. Aspects Med. 34, 516–528 (2013).
Khnykin, D., Miner, J. H. & Jahnsen, F. Role of fatty acid transporters in epidermis. Dermatoendocrinology 3, 53–61 (2011).
Lehner, R. & Quiroga, A. D. Fatty acid handling in mammalian cells. in Biochemistry of Lipids, Lipoproteins and Membranes 149–184 (Elsevier, 2016). https://doi.org/10.1016/B978-0-444-63438-2.00005-5.
Amen, N. et al. Differentiation of epidermal keratinocytes is dependent on glucosylceramide:ceramide processing. Hum. Mol. Genet. 22, 4164–4179 (2013).
Kolter, T. & Sandhoff, K. Sphingolipids—Their metabolic pathways and the pathobiochemistry of neurodegenerative diseases. Angew. Chemie Int. Ed. 38, 1532–1568 (1999).
Furuse, M. et al. Claudin-based tight junctions are crucial for the mammalian epidermal barrier. J. Cell Biol. 156, 1099–1111 (2002).
Radner, F. P. W. et al. Growth retardation, impaired triacylglycerol catabolism, hepatic steatosis, and lethal skin barrier defect in mice lacking comparative gene identification-58 (CGI-58). J. Biol. Chem. 285, 7300–7311 (2010).
Scharschmidt, T. C. et al. Filaggrin deficiency confers a paracellular barrier abnormality that reduces inflammatory thresholds to irritants and haptens. J. Allergy Clin. Immunol. 124, 496-506.e6 (2009).
Macheleidt, O., Sandhoff, K. & Kaiser, H. W. Deficiency of epidermal protein-bound ω-hydroxyceramides in atopic dermatitis. J. Invest. Dermatol. 119, 166–173 (2002).
Li, Y. et al. Golmaenone, a new diketopiperazine alkaloid from the marine-derived fungus Aspergillus sp.. Chem. Pharm. Bull. (Tokyo). https://doi.org/10.1248/cpb.52.375 (2004).
Hong, K.-K., Cho, H.-R., Ju, W.-C., Cho, Y. & Kim, N.-I. A study on altered expression of serine palmitoyltransferase and ceramidase in psoriatic skin lesion. J. Korean Med. Sci. 22, 862 (2007).
Hannun, Y. A. & Obeid, L. M. Sphingolipids and their metabolism in physiology and disease. Nat. Rev. Mol. Cell Biol. 19, 175–191 (2018).
Holleran, W. M., Takagi, Y. & Uchida, Y. Epidermal sphingolipids: Metabolism, function, and roles in skin disorders. FEBS Lett. 580, 5456–5466 (2006).
Wennekes, T. et al. Glycosphingolipids-nature, function, and pharmacological modulation. Angew. Chemie Int. Ed. 48, 8848–8869 (2009).
van Smeden, J., Janssens, M., Gooris, G. S. & Bouwstra, J. A. The important role of stratum corneum lipids for the cutaneous barrier function. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1841, 295–313 (2014).
Ishikawa, J. et al. Changes in the ceramide profile of atopic dermatitis patients. J. Invest. Dermatol. 130, 2511–2514 (2010).
Faller, C., Bracher, M., Dami, N. & Roguet, R. Predictive ability of reconstructed human epidermis equivalents for the assessment of skin irritation of cosmetics. Toxicol. Vitr. 16, 557–572 (2002).
Cannon, C. L., Neal, P. J., Southee, J. A., Kubilus, J. & Klausner, M. New epidermal model for dermal irritancy testing. Toxicol. Vitr. 8, 889–891 (1994).
Murashige, Skoog. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15, 473–492 (1962).
Chakraborthy, G. S. & Ghorpade, P. M. Free radical scavenging activity of Abutilon indicum (Linn) sweet stem extracts. Int. J. ChemTech Res. 2, 526–531 (2010).
Brand-Williams, W., Cuvelier, M. E. & Berset, C. Use of a free radical method to evaluate antioxidant activity. Leb. Technol. 30, 25–30 (1995).
Molyneux. The use of the stable free radical diphenylpicrylhydrazyl (DPPH) for estimating antioxidant activity. Songklanakarin J. Sci Technol. 26, 211–219 (2003).
Letsiou, S. et al. In vitro protective effects of marine-derived Aspergillus puulaauensis TM124-S4 extract on H2O2-stressed primary human fibroblasts. Toxicol. Vitr. 66, 104869 (2020).
Letsiou, S., Kapazoglou, A. & Tsaftaris, A. Transcriptional and epigenetic effects of Vitis vinifera L. leaf extract on UV-stressed human dermal fibroblasts. Mol. Biol. Rep. 47, 5763–5772 (2020).
Letsiou, S. et al. Skin protective effects of Nannochloropsis gaditana extract on H2O2-stressed human dermal fibroblasts. Front. Mar. Sci. 4, (2017).
Ramakers, C., Ruijter, J. M., Deprez, R. H. L. & Moorman, A. F. Assumption-free analysis of quantitative real-time polymerase chain reaction (PCR) data. Neurosci. Lett. 339, 62–66 (2003).
Löwenau, L. J. et al. Increased permeability of reconstructed human epidermis from UVB-irradiated keratinocytes. Eur. J. Pharm. Biopharm. 116, 149–154 (2017).