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Cellular and Molecular Biology Letters

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Volume 13, Issue 4


In Vitro evaluation of the cytotoxic and anti-proliferative properties of resveratrol and several of its analogs

Blase Billack
  • Department of Pharmaceutical Sciences, College of Pharmacy and Allied Health Professions, St. John’s University, 8000 Utopia Parkway, Jamaica, NY, 11439, USA
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/ Vijayalaxmi Radkar
  • Department of Pharmaceutical Sciences, College of Pharmacy and Allied Health Professions, St. John’s University, 8000 Utopia Parkway, Jamaica, NY, 11439, USA
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/ Christelle Adiabouah
  • Department of Pharmaceutical Sciences, College of Pharmacy and Allied Health Professions, St. John’s University, 8000 Utopia Parkway, Jamaica, NY, 11439, USA
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Published Online: 2008-10-17 | DOI: https://doi.org/10.2478/s11658-008-0022-9


Resveratrol (RES), a component of red wine, possesses anti-inflammatory properties. The studies described in the present work were aimed at evaluating the potential for RES and related stilbene analogs (piceatannol, PIC; pterostilbene, TPS; trans-stilbene, TS; and trans-stilbene oxide, TSO) to exhibit toxicity towards RAW 264.7 mouse macrophages. The effect of TS, TSO, RES and TPS on RAW 264.7 macrophage viability was determined by two standard methods: (a) the MTT assay and (b) the trypan blue dye exclusion test. Whereas macrophages were more sensitive to PIC (LC50 trypan ∼ 1.3 μM) and to TPS (LC50 trypan ∼ 4.0 μM and LC50 MTT ∼ 8.3 μM) than to RES (LC50 trypan ∼ 8.9 μM and LC50 MTT ∼ 29.0 μM), they were relatively resistant to TSO (LC50 trypan ∼ 61.0 μM and LC50 MTT > 100 μM) and to TS (LC50 trypan ≥ 5.0 μM and LC50 MTT ≥ 5.0 μM). The ability of selected stilbenes (RES, TPS and PIC) to exhibit growth inhibitory effects was also examined. Although RES and TPS were observed to inhibit cell proliferation in macrophages (IC50 ≤ 25 μM), these cells were resistant to growth inhibition by PIC (IC50 ≥ 50 μM). The data obtained in the present analysis demonstrate that substituted stilbene compounds such as RES have the capacity to exhibit cytotoxic and anti-proliferative activities in macrophages.

Keywords: Resveratrol; Piceatannol; Pterostilbene; Stilbenes; Cell viability; Cell proliferation; Macrophages; TLR4 (−/−); Antioxidants

  • [1] Howard, A., Chopra, M., Thurnham, D., Strain, J., Fuhrman, B. and Aviram, M. Red wine consumption and inhibition of LDL oxidation: What are the important components? Med. Hypotheses 59 (2002) 101–104. http://dx.doi.org/10.1016/S0306-9877(02)00144-5CrossrefGoogle Scholar

  • [2] Ray, P.S., Maulik, G., Cordis, G.A., Bertelli, A.A., Bertelli, A. and Das, D.K. The red wine antioxidant resveratrol protects isolated rat hearts from ischemia reperfusion injury. Free. Radic. Biol. Med. 27 (1999) 160–169. http://dx.doi.org/10.1016/S0891-5849(99)00063-5CrossrefGoogle Scholar

  • [3] Hung, L.M., Chen, J.K., Huang, S.S., Lee, R.S. and Su, M.J. Cardioprotective effect of resveratrol, a natural antioxidant derived from grapes. Cardiovasc. Res. 47 (2000) 549–555. http://dx.doi.org/10.1016/S0008-6363(00)00102-4CrossrefGoogle Scholar

  • [4] Mokni, M., Limam, F., Elkahoui, S., Amri, M. and Aouani, E. Strong cardioprotective effect of resveratrol, a red wine polyphenol, on isolated rat hearts after ischemia/reperfusion injury. Arch. Biochem. Biophys. 457 (2007) 1–6. http://dx.doi.org/10.1016/j.abb.2006.10.015CrossrefGoogle Scholar

  • [5] Constant, J. Alcohol, ischemic heart disease, and the French paradox. Coron. Artery Dis. 8 (1997) 645–649. http://dx.doi.org/10.1097/00019501-199710000-00007CrossrefGoogle Scholar

  • [6] Jang, D.S., Kang, B.S., Ryu, S.Y., Chang, I.M., Min, K.R. and Kim, Y. Inhibitory effects of resveratrol analogs on unopsonized zymosan-induced oxygen radical production. Biochem. Pharmacol. 57 (1999) 705–712. http://dx.doi.org/10.1016/S0006-2952(98)00350-5CrossrefGoogle Scholar

  • [7] Cao, Z. and Li, Y. Potent induction of cellular antioxidants and phase 2 enzymes by resveratrol in cardiomyocytes: protection against oxidative and electrophilic injury. Eur. J. Pharmacol. 489 (2004) 39–48. http://dx.doi.org/10.1016/j.ejphar.2004.02.031CrossrefGoogle Scholar

  • [8] Murias, M., Handler, N., Erker, T., Pleban, K., Ecker, G., Saiko, P., Szekeres, T. and Jager, W. Resveratrol analogues as selective cyclooxygenase-2 inhibitors: synthesis and structure-activity relationship. Bioorg. Med. Chem. 12 (2004) 5571–5578. http://dx.doi.org/10.1016/j.bmc.2004.08.008CrossrefGoogle Scholar

  • [9] Pervaiz, S. Resveratrol: from grapevines to mammalian biology. FASEB J. 17 (2003) 1975–1985. http://dx.doi.org/10.1096/fj.03-0168revCrossrefGoogle Scholar

  • [10] Jeandet, P., Douillet-Breuil, A.C., Bessis, R., Debord, S., Sbaghi, M. and Adrian, M. Phytoalexins from the vitaceae: biosynthesis, phytoalexin gene expression in transgenic plants, antifungal activity, and metabolism. J. Agric. Food Chem. 50 (2002) 2731–2741. http://dx.doi.org/10.1021/jf011429sCrossrefGoogle Scholar

  • [11] Murias, M., Jager, W., Handler, N., Erker, T., Horvath, Z., Szekeres, T., Nohl, H. and Gille, L. Antioxidant, prooxidant and cytotoxic activity of hydroxylated resveratrol analogues: structure-activity relationship. Biochem. Pharmacol. 69 (2005) 903–912. http://dx.doi.org/10.1016/j.bcp.2004.12.001CrossrefGoogle Scholar

  • [12] Kageura, T., Matsuda, H., Morikawa, T., Toguchida, I., Harima, S., Oda, M. and Yoshikawa, M. Inhibitors from rhubarb on lipopolysaccharide-induced nitric oxide production in macrophages: structural requirements of stilbenes for the activity. Bioorg. Med. Chem. 9 (2001) 1887–1893. http://dx.doi.org/10.1016/S0968-0896(01)00093-1CrossrefGoogle Scholar

  • [13] Rimando, A.M., Cuendet, M., Desmarchelier, C., Mehta, R.G., Pezzuto, J.M. and Duke, S.O. Cancer chemopreventive and antioxidant activities of pterostilbene, a naturally occurring analogue of resveratrol. J. Agric. Food Chem. 50 (2002) 3453–3457. http://dx.doi.org/10.1021/jf0116855CrossrefGoogle Scholar

  • [14] Tolomeo, M., Grimaudo, S., Di Cristina, A., Roberti, M., Pizzirani, D., Meli, M., Dusonchet, L., Gebbia, N., Abbadessa, V., Crosta, L., Barucchello, R., Grisolia, G., Invidiata, F. and Simoni, D. Pterostilbene and 3′-hydroxypterostilbene are effective apoptosis-inducing agents in MDR and BCR-ABL-expressing leukemia cells. Int. J. Biochem. Cell Biol. 37 (2005) 1709–1726. http://dx.doi.org/10.1016/j.biocel.2005.03.004CrossrefGoogle Scholar

  • [15] Wolter, F., Clausnitzer, A., Akoglu, B. and Stein, J. Piceatannol, a natural analog of resveratrol, inhibits progression through the S phase of the cell cycle in colorectal cancer cell lines. J. Nutr. 132 (2002) 298–302. Google Scholar

  • [16] Larrosa, M., Tomas-Barberan, F.A. and Espin, JC. Grape polyphenol resveratrol and the related molecule 4-hydroxystilbene induce growth inhibition, apoptosis, S-phase arrest, and upregulation of cyclins A, E, and B1 in human SK-Mel-28 melanoma cells. J. Agric. Food Chem. 51 (2003) 4576–4584. http://dx.doi.org/10.1021/jf030073cCrossrefGoogle Scholar

  • [17] Wieder, T., Prokop, A., Bagci, B., Essmann, F., Bernicke, D., Schulze-Osthoff, K., Dorken, B., Schmalz, H. G., Daniel, P. T. and Henze, G. Piceatannol, a hydroxylated analog of the chemopreventive agent resveratrol, is a potent inducer of apoptosis in the lymphoma cell line BJAB and in primary, leukemic lymphoblasts. Leukemia 15 (2001) 1735–1742. CrossrefGoogle Scholar

  • [18] Radkar, V., Hardej, D., Lau-Cam, C. and Billack, B. Evaluation of resveratrol and piceatannol cytotoxicity in macrophages, T cells, and skin cells. Arh. Hig. Rada. Toksikol. 58 (2007) 293–304. Google Scholar

  • [19] Crowell, J.A., Korytko, P.J., Morrissey, R.L., Booth, T.D. and Levine, B.S. Resveratrol-associated renal toxicity. Toxicol. Sci. 82 (2004) 614–619. http://dx.doi.org/10.1093/toxsci/kfh263CrossrefGoogle Scholar

  • [20] Ferry-Dumazet, H., Garnier, O., Mamani-Matsuda, M., Vercauteren, J., Belloc, F., Billiard, C., Dupouy, M., Thiolat, D., Kolb, J. P., Marit, G., Reiffers, J. and Mossalayi, M. D. Resveratrol inhibits the growth and induces the apoptosis of both normal and leukemic hematopoietic cells. Carcinogenesis 23 (2002) 1327–1333. http://dx.doi.org/10.1093/carcin/23.8.1327CrossrefGoogle Scholar

  • [21] Azmi, A.S., Bhat, S.H., Hanif, S. and Hadi, S.M. Plant polyphenols mobilize endogenous copper in human peripheral lymphocytes leading to oxidative DNA breakage: a putative mechanism for anticancer properties. FEBS Lett. 580 (2006) 533–538. http://dx.doi.org/10.1016/j.febslet.2005.12.059CrossrefGoogle Scholar

  • [22] Hebbar, V., Shen, G., Hu, R., Kim, B.R., Chen, C., Korytko, P.J., Crowell, J.A., Levine, B.S. and Kong, A.N. Toxicogenomics of resveratrol in rat liver. Life Sci. 76 (2005) 2299–2314. http://dx.doi.org/10.1016/j.lfs.2004.10.039CrossrefGoogle Scholar

  • [23] Schmitt, E., Lehmann, L., Metzler, M. and Stopper, H. Hormonal and genotoxic activity of resveratrol. Toxicol. Lett. 136 (2002) 133–142. http://dx.doi.org/10.1016/S0378-4274(02)00290-4CrossrefGoogle Scholar

  • [24] Djoko, B., Chiou, R.Y., Shee, J.J. and Liu, Y.W. Characterization of immunological activities of peanut stilbenoids, arachidin-1, piceatannol, and resveratrol on lipopolysaccharide-induced inflammation of RAW 264.7 macrophages. J. Agric. Food Chem. 55 (2007) 2376–2383. http://dx.doi.org/10.1021/jf062741aCrossrefGoogle Scholar

  • [25] Sanoh, S., Kitamura, S., Sugihara, K. and Ohta, S. Cytochrome P450 1A1/2 mediated metabolism of trans-stilbene in rats and humans. Biol. Pharm. Bull. 25 (2002) 397–400. http://dx.doi.org/10.1248/bpb.25.397CrossrefGoogle Scholar

  • [26] Sanoh, S., Kitamura, S., Sugihara, K., Kohta, R., Ohta, S. and Watanabe, H. Effects of stilbene and related compounds on reproductive organs in B6C3F1/Crj mouse. J. Health Sci. 52 (2006) 613–622. http://dx.doi.org/10.1248/jhs.52.613CrossrefGoogle Scholar

  • [27] Grohs, B.M. and Kunz, B. Fungitoxicity of chemical analogs with heartwood toxins. Curr. Microbiol. 37 (1998) 67–69. http://dx.doi.org/10.1007/s002849900340CrossrefGoogle Scholar

  • [28] Meijer, J., DePierre, J.W., Wang, P.P. and Guengerich, F.P. Purification and characterization of the major microsomal cytochrome P-450 form induced by trans-stilbene oxide in rat liver. Biochim. Biophys. Acta. 789 (1984) 1–9. Google Scholar

  • [29] Bucker, M., Golan, M., Schmassmann, H.U., Glatt, H.R., Stasiecki, P. and Oesch, F. The epoxide hydratase inducer trans-stilbene oxide shifts the metabolic epoxidation of benzo(a)pyrene from the bay-to the K-region and reduces its mutagenicity. Mol. Pharmacol. 16 (1979) 656–666. Google Scholar

  • [30] Williams, J.B., Wang, R., Lu, A.Y. and Pickett, C.B. Rat liver DT-diaphorase: Regulation of functional mRNA levels by 3-methylcholanthrene, trans-stilbene oxide, and phenobarbital. Arch. Biochem. Biophys. 232 (1984) 408–413. http://dx.doi.org/10.1016/0003-9861(84)90556-3CrossrefGoogle Scholar

  • [31] Raschke, W.C., Baird, S., Ralph, P. and Nakoinz, I. Functional macrophage cell lines transformed by abelson leukemia virus. Cell 15 (1978) 261–267. http://dx.doi.org/10.1016/0092-8674(78)90101-0CrossrefGoogle Scholar

  • [32] Giard, D.J., Aaronson, S.A., Todaro, G.J., Arnstein, P., Kersey, J.H., Dosik, H. and Parks, W.P. In vitro cultivation of human tumors: Establishment of cell lines derived from a series of solid tumors. J. Natl. Cancer Inst. 51 (1973) 1417–1423. Google Scholar

  • [33] Lorenz, E., Patel, D.D., Hartung, T. and Schwartz, D.A. Toll-like receptor 4 (TLR4)-deficient murine macrophage cell line as an in vitro assay system to show TLR4-independent signaling of bacteroides fragilis lipopolysaccharide. Infect. Immun. 70 (2002) 4892–4896. http://dx.doi.org/10.1128/IAI.70.9.4892-4896.2002CrossrefGoogle Scholar

  • [34] Foley, G.E., Lazarus, H., Farber, S., Uzman, B.G., Boone, B.A and McCarthy, RE. Continuous culture of human lymphoblasts from peripheral blood of a child with acute leukemia. Cancer 18 (1965) 522–529. http://dx.doi.org/10.1002/1097-0142(196504)18:4<522::AID-CNCR2820180418>3.0.CO;2-JCrossrefGoogle Scholar

  • [35] Mosmann, T. Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55–63. http://dx.doi.org/10.1016/0022-1759(83)90303-4CrossrefGoogle Scholar

  • [36] Shah, Y.M., Al-Dhaheri, M., Dong, Y., Ip, C., Jones, F.E. and Rowan, B.G. Selenium disrupts estrogen receptor (alpha) signaling and potentiates tamoxifen antagonism in endometrial cancer cells and tamoxifen-resistant breast cancer cells. Mol. Cancer Ther. 4 (2005) 1239–1249. http://dx.doi.org/10.1158/1535-7163.MCT-05-0046CrossrefGoogle Scholar

  • [37] Bruggisser, R., von Daeniken, K., Jundt, G., Schaffner, W. and Tullberg-Reinert, H. Interference of plant extracts, phytoestrogens and antioxidants with the MTT tetrazolium assay. Planta Med. 68 (2002) 445–448. http://dx.doi.org/10.1055/s-2002-32073CrossrefGoogle Scholar

  • [38] Ovesna, Z., Kozics, K., Bader, Y., Saiko, P., Handler, N., Erker, T. and Szekeres, T. Antioxidant activity of resveratrol, piceatannol and 3,3′,4,4′,5,5′-hexahydroxy-trans-stilbene in three leukemia cell lines. Oncol. Rep. 16 (2006) 617–624. Google Scholar

  • [39] Potter, G.A., Patterson, L.H., Wanogho, E., Perry, P.J., Butler, P.C., Ijaz, T., Ruparelia, K.C., Lamb, J.H., Farmer, P.B., Stanley, L.A. and Burke, M.D. The cancer preventative agent resveratrol is converted to the anticancer agent piceatannol by the cytochrome P450 enzyme CYP1B1. Br. J. Cancer 86 (2002) 774–778. http://dx.doi.org/10.1038/sj.bjc.6600197CrossrefGoogle Scholar

  • [40] Piver, B., Fer, M., Vitrac, X., Merillon, J.M., Dreano, Y., Berthou, F. and Lucas, D. Involvement of cytochrome P450 1A2 in the biotransformation of trans-resveratrol in human liver microsomes. Biochem. Pharmacol. 68 (2004) 773–782. http://dx.doi.org/10.1016/j.bcp.2004.05.008CrossrefGoogle Scholar

  • [41] Zheng, L.F., Wei, Q.Y., Cai, Y.J., Fang, J.G., Zhou, B., Yang, L. and Liu, Z.L. DNA damage induced by resveratrol and its synthetic analogues in the presence of cu (II) ions: mechanism and structure-activity relationship. Free Radic. Biol. Med. 41 (2006) 1807–1816. http://dx.doi.org/10.1016/j.freeradbiomed.2006.09.007CrossrefGoogle Scholar

  • [42] Huang, X.F., Ruan, B.F., Wang, X.T., Xu, C., Ge, H.M., Zhu, H.L. and Tan, R.X. Synthesis and cytotoxic evaluation of a series of resveratrol derivatives modified in C2 position. Eur. J. Med. Chem. 42 (2007) 263–267. http://dx.doi.org/10.1016/j.ejmech.2006.08.006CrossrefGoogle Scholar

  • [43] Roberti, M., Pizzirani, D., Simoni, D., Rondanin, R., Baruchello, R., Bonora, C., Buscemi, F., Grimaudo, S. and Tolomeo, M. Synthesis and biological evaluation of resveratrol and analogues as apoptosis-inducing agents. J. Med. Chem. 46 (2003) 3546–3554. http://dx.doi.org/10.1021/jm030785uCrossrefGoogle Scholar

  • [44] Matsuoka, A., Takeshita, K., Furuta, A., Ozaki, M., Fukuhara, K. and Miyata, N. The 4′-hydroxy group is responsible for the in vitro cytogenetic activity of resveratrol. Mutat. Res. 521(2002) 29–35. Google Scholar

  • [45] Fukuhara, K., Nagakawa, M., Nakanishi, I., Ohkubo, K., Imai, K., Urano, S., Fukuzumi, S., Ozawa, T., Ikota, N., Mochizuki, M., Miyata, N. and Okuda, H. Structural basis for DNA-cleaving activity of resveratrol in the presence of cu(II). Bioorg. Med. Chem. 14 (2006) 1437–1443. http://dx.doi.org/10.1016/j.bmc.2005.09.070CrossrefGoogle Scholar

  • [46] Cadenas, E. Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism. Biochem. Pharmacol. 49 (1995) 127–140. http://dx.doi.org/10.1016/S0006-2952(94)00333-5CrossrefGoogle Scholar

  • [47] Galati, G. and O’Brien, P.J. Potential toxicity of flavonoids and other dietary phenolics: significance for their chemopreventive and anticancer properties. Free Rad. Biol. Med. 37 (2004) 287–303. http://dx.doi.org/10.1016/j.freeradbiomed.2004.04.034CrossrefGoogle Scholar

  • [48] Bernhard, D., Tinhofer, I., Tonko, M., Hubl, H., Ausserlechner, M.J., Greil, R., Kofler, R. and Csordas, A. Resveratrol causes arrest in the S-phase prior to fas-independent apoptosis in CEM-C7H2 acute leukemia cells. Cell Death Differ. 7 (2000) 834–842. http://dx.doi.org/10.1038/sj.cdd.4400719CrossrefGoogle Scholar

  • [49] Tsan, M.F., White, J.E., Maheshwari, J.G. and Chikkappa, G. Anti-leukemia effect of resveratrol. Leuk. Lymphoma 43 (2002) 983–987. CrossrefGoogle Scholar

  • [50] Zunino, S.J. and Storms, D. H. Resveratrol-induced apoptosis is enhanced in acute lymphoblastic leukemia cells by modulation of the mitochondrial permeability transition pore. Cancer Lett. 240 (2006) 123–134. http://dx.doi.org/10.1016/j.canlet.2005.09.001CrossrefGoogle Scholar

  • [51] Wu, S.L., Yu, L., Pan, C.E., Jiao, X.Y., Lv, Y., Fu, J. and Meng, K.W. Apoptosis of lymphocytes in allograft in a rat liver transplantation model induced by resveratrol. Pharmacol. Res. 54 (2006) 19–23. http://dx.doi.org/10.1016/j.phrs.2006.01.011CrossrefGoogle Scholar

  • [52] Mizutani, K., Ikeda, K., Kawai, Y. and Yamori, Y. Resveratrol stimulates the proliferation and differentiation of osteoblastic MC3T3-E1 cells. Biochem. Biophys. Res. Commun. 253 (1998) 859–863. http://dx.doi.org/10.1006/bbrc.1998.9870CrossrefGoogle Scholar

  • [53] Dai, Z., Li, Y., Quarles, L.D., Song, T., Pan, W., Zhou, H. and Xiao, Z. Resveratrol enhances proliferation and osteoblastic differentiation in human mesenchymal stem cells via ER-dependent ERK1/2 activation. Phytomed. 14 (2007) 806–814. http://dx.doi.org/10.1016/j.phymed.2007.04.003CrossrefGoogle Scholar

  • [54] Inoue, K. and Creveling, C.R. Immunocytochemical localization of catechol-O-methyltransferase in the oviduct and in macrophages in corpora lutea of rat. Cell Tissue Res. 245 (1986) 623–628. http://dx.doi.org/10.1007/BF00218564CrossrefGoogle Scholar

About the article

Published Online: 2008-10-17

Published in Print: 2008-12-01

Citation Information: Cellular and Molecular Biology Letters, Volume 13, Issue 4, Pages 553–569, ISSN (Online) 1689-1392, DOI: https://doi.org/10.2478/s11658-008-0022-9.

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