Hippophae rhamnoides/Cassia fistula Extracts
The work deals with the in vitro evaluations of the pod extracts of C. fistula which are shown to exert better antioxidant and enzymatic properties than those exhibited by the fruit extract of H. rhamnoides.
Antioxidants prevent oxidative damages (e.g., 8-hydroxyguanine, cell membrane lipid peroxidation) and subsequent diseases (e.g., inflammatory state-diseases such as cancers, Alzheimer's, diabetes, and strokes), by effectively quenching or inhibiting free radicals (e.g., hydroxyl and superoxide radicals). For a long time, synthetic antioxidants have been employed as food additives, but safety concerns have restricted their use, due to their possible involvement in chronic diseases. Therefore, much attention has been directed toward the isolation of natural antioxidants from botanical sources, especially edible plants . Furthermore, plant extracts that can inhibit specific enzymes (e.g., β-glucuronidase, α-glycosidase, and α-tyrosinase), particularly involved in the alteration of skin during aging, are appreciated for their potential use in original cosmetic formulations.
β-glucuronidase, an acid hydrolase, plays a crucial role in catalyzing the hydrolysis of glucuronide into glycones (i.e., alkyl, acyl, aryl groups) and free glucuronic acid . This catalysis releases the terminal glucuronide unit linked through the β-configuration by Carbon 1 (C1) . β-glucuronidase was first discovered in the rumen of sheep, although this enzyme has been recorded as present in all plants, animals, and bacteria so far studied . The research and development (R&D) of specific β-glucuronidase inhibitors (e.g., baicalin) is growing , most notably in the fields of drug detoxification  and cancer therapy , as well as in its ability to overcome glycosaminoglycan (GAG) impaired metabolism during skin aging , treat skin conditions such as psoriasis  and formulate cosmetics .
α-glycosidase comprises a family of hydrolases, which are enzymes located in the brush-border surface membrane of small intestinal cells . α-glycosidase is implicated in the hydrolysis of the 1,4 glycosidic linkage from the non-reducing end of the α-glucosides, α-linked oligosaccharide, and α-glucans substrates, producing α-d-glucose and other monosaccharides that are employed as carbon and energy sources . Therefore, α-glucosidase inhibitors are not only considered in the management of type-2 diabetes (T2D) , tumorigenesis , but also in the prevention of skin aging and skin damages .
α-tyrosinase is found in plant and animal tissues, and represents a rate-limiting and copper-containing oxidase, involved in controlling melanin synthesis through two distinct chemical reactions : (i) hydroxylation of a monophenol; and (ii) conversion of an o-diphenol into the corresponding o-quinone, which then undergoes several reactions, eventually forming melanin. In humans, the tyrosinase enzyme is encoded by the TYR gene expressed inside melanosomes . When a mutation in the TYR gene results in impaired tyrosinase production, it is usually associated with type I oculocutaneous albinism, or increased melanin synthesis in skin cancer (e.g., melanoma) . In addition to molecular strategies for controlling the tyrosinase activity , several polyphenols (e.g., flavonoids and stilbenoid substrate analogues), free radical scavengers and copper chelators, have been identified as potent tyrosinase inhibitors, capable of preventing skin hyperpigmentation and inducing skin whitening .
Hippophae rhamnoides L. (Elaeagnacea), commonly known as sea-buckthorn, is a flowering, spiny, deciduous shrub, native to fixed dunes and sea cliffs in Europe (e.g., Germany, France) and Asia (e.g., Nepal, India, China). It is both an agricultural and an ornamental plant. Although H. rhamnoides is a relatively expensive raw material, its fruits are quite beneficial due to their higher average content of ascorbic acid (aka vitamin C), in comparison to lemons and oranges . Consequently, the fruits of H. rhamnoides are used in traditional Austrian medicine to fight infections (e.g., flu), in the form of tea, juice, and syrup . H. rhamnoides exerts various pharmacological effects, including cytoprotection, protection against stress, immunomodulation, hepatoprotection, radioprotection, anti-atherogenicity, anti-tumorigenicity, anti-microbial activity, and tissue regeneration . We have recently shown the beneficial effects of H. rhamnoides extracts in the prevention of premature aging of human skin and melasma .
Cassia fistula L. (Caesalpinaceae/Leguminosae), also known as the golden shower tree, is a famous yellow flowering plant from Asia (e.g., particularly found in the forests of India, Sri Lanka, Thailand and Pakistan), and displays numerous medicinal properties for protecting against skin conditions and inflammatory diseases . Thereby, we recently demonstrated that C. fistula's extracts are capable of preventing premature skin aging in healthy individuals , and melasma in a good number of patients when compared with treatment using a placebo (i.e., without the plant extract) . These beneficial effects are probably due to their relatively rich content of bioactive ingredients (i.e., phenolic compounds, fatty acids, flavonoids, tannins and glycosides) , and their ability to significantly decrease the tyrosine activity-mediated melanin level.
Extracts from C. fistula and H. rhamnoides are gaining much attention in medicine and esthetics, because of their relative high content of antioxidants (e.g., vitamin C, polyphenols such as flavonoids and saponins, unsaturated fatty acids (UFAs)), known to counteract naturally-occurring or induced molecular and cellular damage-mediated oxidation .
Recent investigations led by our research groups have proven that great skin benefits (e.g., slower skin aging; anti-melasma) can be produced when C. fistula and H. rhamnoides extracts are topically applied .
The phyto-antioxidant arsenal is composed of several chemicals (i.e., free radical scavenging) and enzymatic reactions. Therefore, the specificity and sensitivity of a single method is insufficient for providing an inclusive examination of all phenolic compounds in a given plant extract. A combination of reliable tests is necessary in order to evaluate a complete antioxidant and enzymatic activity profile (i.e., free radical scavenging and key enzymatic inhibition capacities).
Following this original approach, our data provided a better qualitative and quantitative understanding of the anti-oxidant and enzymatic inhibition abilities of C. fistula and H. rhamnoides, two traditional plant extracts, valuable in modern medicine.
3. Conclusions and Perspectives
Based on our various in vitro assays, which aimed to assess the antioxidant and key enzymatic activities of two major plant extracts used in traditional medicine, our results clearly confirmed that both H. rhamnoides and C. fistula extracts present potent antioxidant activities. More importantly, it was recorded that C. fistula's pod extracts exert the best antioxidant and enzymatic activities, when compared to those of H. rhamnoides' fruit extracts, which are known to contain a very high content of vitamin C (i.e., about 30 times more than orange fruit). Indeed, C. fistula's pods represent the richest polyphenolic part of the plant and exert valuable enzymatic activities for cosmetic use. Overall, our data strongly state that TPC in a given plant extract shall be attributed to particular free radical scavenging or enzymatic activities, exploitable for cosmetics, medical, or food applications. This implicates the use of multiple antioxidant and enzymatic assays in order to select the most valuable plant extract or phyto-ingredient. Ongoing studies from our lab aim to explore C. fistula's pod extracts in cells, animal models, and in humans of any age, including those suffering of chronic inflammatory-state diseases or premature skin aging. We also intend to characterize the safety and efficacy, both in vitro and in vivo, of nanoencapsulated C. fistula extracts.
The entry is from 10.3390/cosmetics4010003
- Menaa, F.; Badole, S.L.; Menaa, B.; Menaa, A. Promising plant extracts with in vivo anti-melanoma potential. In Bioactive Dietary Factors and Plant Extracts in Dermatology, 1st ed.; Watson, R.R., Preedy, V.R., Zibadi, S., Eds.; Humana Press Inc., Springer: New York, NY, USA, 2013; pp. 283–290.
- Menaa, F.; Menaa, A.; Tréton, J. Polyphenols against skin aging. In Polyphenols in Human Health and Disease, 1st ed.; Watson, R.R., Preedy, V.R., Zibadi, S., Eds.; Academic Press, Elsevier Publisher: Cambridge, MA, USA, 2013; pp. 819–829.
- Menaa, F.; Menaa, A. Skin photoprotection by polyphenols in animal models and humans. In Polyphenols in Human Health and Disease, 1st ed.; Watson, R.R., Preedy, V.R., Zibadi, S., Eds.; Academic Press, Elsevier Publisher: Cambridge, MA, USA, 2013; pp. 831–838.
- Zia-Ul-Haq, M.; Shakeel, A.; Mughal, Q.; Sezai, E. Compositional studies and anti-oxidant potential of Albizia lebbeck (L.) Benth. pods and seeds. Turk. J. Biol. 2013, 37, 25–32.
- Khan, B.A.; Akhtar, N.; Braga, V.A. Anti-Aging Effects of Hippophae rhamnoides Emulsion on Human Skin. Trop. J. Pharm. Res. 2012, 11, 955–962.
- Zenser, T.V.; Lakshmi, V.M.; Davis, B.B. Human and Escherichia Coli β-glucuronidase hydrolysis of glucuronide conjugates of benzidine and 4-aminobiphenyl, and their hydroxy metabolites. Drug Metab. Dispos. 1999, 27, 1064–1067.
- Ho, K.J.; Ho, L.H. Determination of urinary beta-glucuronidase activity. Single-point versus enzyme kinetic measuring system. Enzyme 1980, 25, 361–370.
- Sanjeev, J.; William, B.D.; Zhi-wel, C.F.; Sly, W.S.; Jeffery, H.G. Structure of human β-glucuronidase reveals candidate lysosomal targeting and active site motifs. Nat. Struct. Biol. 1996, 3, 375–381.
- Marsh, C.A. A glucuronide-decomposing enzyme from rumen micro-organisms. 2. Purification and kinetics. Biochem. J. 1954, 58, 609–617.
- Takasuna, K.; Kasai, Y.; Kitano, Y.; Mori, K.; Kobayashi, R.; Hagiwara, T.; Kakihata, K.; Hirohashi, M.; Nomura, M.; Nagai, E. Protective effects of kampo medicines and baicalin against intestinal toxicity of a new anticancer camptothecin derivative, irinotecan hydrochloride (CPT-11), in rats. Jpn. J. Cancer Res. 1995, 86, 978–984.
- Sperker, B.; Backman, J.T.; Kroemer, H.K. The role of beta-glucuronidase in drug disposition and drug targeting in humans. Clin. Pharmacokinet. 1997, 33, 18–31.
- Takasuna, K.; Hagiwara, T.; Hirohashi, M.; Kato, M.; Nomura, M.; Nagai, E.; Yokoi, T.; Kamataki, T. Inhibition of intestinal microflora beta-glucuronidase modifies the distribution of the active metabolite of the antitumor agent, irinotecan hydrochloride (CPT-11) in rats. Cancer Chemother. Pharmacol. 1998, 42, 280–286.
- Schmiegelow, P.; Nüssgen, A.; Grasedyck, K.; Lindner, J. Skin changes in advanced age Biochemical findings corresponding to morphology? Z. Gerontol. 1986, 19, 179–189.
- Koehler, V. Topical Compositions e.g., Ointment Contg. Beta-Glucuronidase—For Treatment of Non-Infectious Skin Disorders e.g., Psoriasis. German Patent DE 2819129 A1, 15 November 1979.
- Holtzinger, G. Cosmetic Composition and Method for Suppressing Human Body Malodor Arise from Sweat. European Patent EP0714655 A1, 5 June 1996.
- Lembcke, B.; Löser, C.; Fölsch, U.R.; Wöhler, J.; Creutzfeldt, W. Adaptive responses to pharmacological inhibition of small intestinal alpha-glucosidases in the rat. Gut 1987, 28, 181–187.
- Chiba, S. Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem. 1997, 61, 1233–1239.
- Lebovitz, H.E. Alpha glucosidase inhibitors. Endocrinol. Metab. Clin. N. Am. 1997, 26, 539–551.
- Hirsh, A.J.; Yao, S.Y.; Young, J.D.; Cheeseman, C.I. Inhibition of glucose absorption in the rat jejunum: A novel action of alpha-d-glucosidase inhibitors. Gastroenterology 1997, 113, 205–211.
- Walaszek, Z.M.; Hanausek, W. Inhibition of 7,12 dimethylbenzanthracene-induced rat mammary tumorigenesis by 2,5-di-o-acetyl-d-glucaro-1,4:6,3-dilactone, an in vivo ß-glucuronidase inhibitor. Carcinogenesis 1984, 5, 767–772.
- Declercq, L.; Maes, D.H.; Corstjens, H.A. Cosmetic Compositions Containing Alpha Glucosidase Inhibitors and Methods of Use. U.S. Patent 9072717 B2, 7 July 2007.
- Declercq, L.; Maes, D.H.; Corstjens, H.A. Cosmetic Compositions Containing Alpha Glucosidase Inhibitors and Methods of Use. U.S. Patent 20090074822 A1, 19 March 2009.
- Menaa, F.; Menaa, A. Progressive genetic architecture of human skin pigmentation. J. Primatol. 2013, 3, 116.
- Kumar, C.M.; Sathisha, U.V.; Dharmesh, S.; Rao, A.G.; Singh, S.A. Interaction of sesamol (3,4-methylenedioxyphenol) with tyrosinase and its effect on melanin synthesis. Biochimie 2011, 93, 562–569.
- Barton, D.E.; Kwon, B.S.; Francke, U. Human tyrosinase gene, mapped to chromosome 11 (q14 → q21), defines second region of homology with mouse chromosome 7. Genomics 1988, 3, 17–24.
- Theos, A.C.; Tenza, D.; Martina, J.A.; Hurbain, I.; Peden, A.A.; Sviderskaya, E.V.; Stewart, A.; Robinson, M.S.; Bennett, D.C.; Cutler, D.F.; et al. Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes. Mol. Biol. Cell. 2005, 16, 5356–5372.
- Witkop, C.J. Albinism: Hematologic-storage disease, susceptibility to skin cancer, and optic neuronal defects shared in all types of oculocutaneous and ocular albinism. Ala. J. Med. Sci. 1979, 16, 327–330.
- Menaa, F. Latest Approved Therapies for Metastatic Melanoma: What Comes Next? J. Skin Cancer 2013, 2013, 735282.
- Ubeid, A.A. Short-sequence oligopeptides with inhibitory activity against mushroom and human tyrosinase. J. Investig. Dermatol. 2009, 129, 2242–2249.
- Fais, A. Tyrosinase inhibitor activity of coumarin-resveratrol hybrids. Molecules 2009, 14, 2514–2520.
- Chang, T.S. An Updated Review of Tyrosinase Inhibitor. Int. J. Mol. Sci. 2009, 10, 2440–2475.
- Choi, S. Aloesin inhibits the hyperpigmentation induced by UV radiation. Clin. Exp. Dermatol. 2002, 27, 513–515.
- Chen, W.C.; Tseng, T.S.; Hsiao, N.W.; Lin, Y.L.; Wen, Z.H.; Tsai, C.C.; Lee, Y.C.; Lin, H.H.; Tsai, K.C. Discovery of Highly Potent Tyrosinase Inhibitor, T1, with Significant Anti-Melanogenesis Ability by zebrafish in vivo Assay and Computational Molecular Modeling. Sci. Rep. 2015, 5, 7995.
- Hussain, I.; Khan, L.; Marwat, G.A.; Ahmed, N.; Saleem, M. Comparative study of Vitamin C contents in fruits and medicinal plants. J. Chem. Soc. Pak. 2008, 30, 406–409.
- Vogl, S.; Picker, P.; Mihaly-Bison, J.; Fakhrudin, N.; Atanasov, A.G.; Heiss, E.H.; Wawrosch, C.; Reznicek, G.; Dirsch, V.M.; Saukel, J.; et al. Ethnopharmacological in vitro studies on Austria’s folk medicine—An unexplored lore in vitro anti-inflammatory activities of 71 Austrian traditional herbal drugs. J. Ethnopharmacol. 2013, 49, 750–771.
- Suryakumar, G.; Gupta, A. Medicinal and therapeutic potential of Sea buckthorn (Hippophae rhamnoides L.). J. Ethnopharmacol. 2011, 138, 268–278.
- Khan, B.A.; Akhtar, N.; Hussain, I.; Abbas, K.A.; Rasul, A. Whitening efficacy of plant extracts including Hippophae rhamnoides and Cassia fistula extracts on the skin of Asian patients with melasma. Postep. Dermatol. Alergol. 2013, 30, 226–232.
- Bahorun, T.; Neergheen, V.S.; Aruoma, O.I. Phytochemical constituents of Cassia fistula. Afr. J. Biotechnol. 2005, 4, 1530–1540.
- Khan, B.A.; Akhtar, N.; Menaa, A.; Menaa, F. A Novel Cassia fistula (L)-Based Emulsion Elicits Skin Anti-Aging Benefits in Humans. Cosmetics 2015, 2, 368–383.
- Bhalodia, N.R.; Nariya, P.B.; Acharya, R.N.; Shukla, V.J. In vitro anti-oxidant activity of hydro alcoholic extract from the fruit pulp of Cassia fistula Linn. Ayu 2013, 34, 209–214.
- Manonmani, G.; Bhavapriya, V.; Kalpana, S.; Govindasamy, S.; Apparanantham, T. Anti-oxidant activity of Cassia fistula (Linn.) flowers in alloxan induced diabetic rats. J. Ethnopharmacol. 2005, 97, 39–42.
- Khan, B.A.; Akhtar, N. Phytochemical analysis and acute toxicity tests of two medicinal plant extracts. J. Med. Plant Res. 2012, 6, 3545–3548.
- Korekar, G.; Stobdan, T.S.; Chaurasia, O.P.; Singh, S.B. Phenolic content and anti-oxidant capacity of various solvent extracts from Seabuckthorn (Hippophae rhamnoides L.) fruit pulp, seeds, leaves and stem bark. Acta Aliment. 2011, 40, 449–458.