Characterization of the pro-inflammatory potencies of purified Jatropha phorbol esters by a gene expression-based in vitro bioassay

References

• Achten, W. M. J., L. Verchot, Y. J. Franken, E. Mathijs, V. P. Singh, R. Aerts, and B. Muys. 2008. “Jatropha Bio-Diesel Production and Use.” Biomass and Bioenergy 32 (12): 1063–1084.
   Web of Science ®Google Scholar
• Beutler, J., A. D. Alvarado, and T. G. McCloud. 1989. “Distribution of Phorbol Ester Bioactivity in the Euphorbiaceae.” Phytotherapy Research 3 (5): 188–192.
   Web of Science ®Google Scholar
• Blumberg, P. M. 1980. “In Vitro Studies on the Mode of Action of the Phorbol Esters, Potent Tumor Promoters: Part 1.” CRC Critical Reviews in Toxicology 8 (2): 153–197.
   Web of Science ®Google Scholar
• Borenfreund, E., and J. A. Puerner. 1985. “A Simple Quantitative Procedure Using Monolayer Cultures for Cytotoxicity Assays (HTD/NR-90).” Journal of Tissue Culture Methods 9 (1): 7–9.
   Google Scholar
• Brittaine, R., and N. Lutaladio. 2010. Jatropha: A Smallholder Bionergy Crop: The Potential for Pro-poor Development. Vol. 8 of Integrated Crop Management. Rome: FAO.
   Google Scholar
• Devappa, R. K., J. S. Roach, H. P. Makkar, and K. Becker. 2013. “Occular and Dermal Toxicity of Jatropha curcas Phorbol Esters.” Ecotoxicology and Environmental Safety 94: 172–178.
   PubMed Web of Science ®Google Scholar
• Devappa, R. K., J. P. Bingham, and S. K. Khanal. 2013. “High Performance Liquid Chromatography Method for Rapid Quantification of Phorbol Esters in Jatropha curcas Seed.” Industrial Crops and Products 49: 211–219.
   Web of Science ®Google Scholar
• Devappa, R. K., H. P. S. Makkar, and K. Becker. 2010. “Optimization of Conditions for the Extraction of Phorbol Esters From Jatropha Oil.” Biomass and Bioenergy 34 (8): 1125–1133.
   Web of Science ®Google Scholar
• EFSA CONTAM Panel (EFSA Panel on Contaminants in the Food Chain). 2015. “Scientific Opinion on Risks for Human and Animal Health Related to the Presence of Phorbol Esters in Jatropha Kernel Meal.” EFSA Journal 13 (12): 4321, 80 pp. doi:10.2903/j.efsa.2015.4321.
   Google Scholar
• Haas, W., and M. Mittelbach. 2000. “Detoxification Experiments with the Seed Oil From Jatropha Curcas L.” Industrial Crops and Products 12: 111–118.
   Web of Science ®Google Scholar
• Haas, W., H. Sterk, and M. Mittelbach. 2002. “Novel 12-Deoxy-16-Hydroxyphorbol Diesters Isolated From the Seed Oil of Jatropha curcas.” Journal of Natural Products 65 (10): 1434–1440.
   PubMed Web of Science ®Google Scholar
• Ichihashi, K., D. Yuki, H. Kurokawa, A. Igarashi, T. Yajima, M. Fujiwara, K. Maeno, S. Sekiguchi, M. Iwata, and H. Nishino. 2011. “Dynamic Analysis of Phorbol Esters in the Manufacturing Process of Fatty Acid Methyl Esters From Jatropha Curcas Seed Oil.” Journal of the American Oil Chemists' Society 88 (2): 851–861.
   Web of Science ®Google Scholar
• Li, C. Y., R. K Devappa, J. X. Liu, J. M. Lv, H. P. S. Makkar, and K. Becker. (2010). “Toxicity of Jatropha curcas Phorbol Esters in Mice.” Food and Chemical Toxicology 48 (2): 620–625.
   PubMed Web of Science ®Google Scholar
• Makkar, H. P. 2016. “State-of-the-Art on Detoxification of Jatropha Curcas Products Aimed for Use As Animal and Fish Feed: A Review.” Animal Feed Science and Technology 222: 87–99.
   Web of Science ®Google Scholar
• Makkar, H. P. S., V. Kumar, and K. Becker. 2012. “Use of detoxified jatropha kernel meal and protein isolate in diets of farm animals.” Chap 21 in Biofuel Co-Products as Livestock Feed - Opportunities and Challenges, edited by H.P.S. Makkar, 351–378. Rome: FAO.
   Google Scholar
• Makkar, H., J. Maes, W. De Greyt, and K. Becker. 2009. “Removal and Degradation of Phorbol Esters During Pre-Treatment and Transesterification of Jatropha Curcas Oil.” Journal of the American Oil Chemists' Society 86: 173–181.
   Web of Science ®Google Scholar
• Molina-Holgado, E., S. Ortiz, F. Molina-Holgado, and C. Guaza. 2000. “Induction of COX-2 and PGE2 Biosynthesis by IL6 Is Mediated by PKC and Mitogen-activated Protein Kinases in Murine Astrocytes.” British Journal of Pharmacology 131 (1): 152–159.
   PubMed Web of Science ®Google Scholar
• Ohuchi, K., and L. Levine. 1978. “Stimulation of Prostaglandin Synthesis by Tumor-Promoting Phorbol-12, 13-Diesters in Canine Kidney (MDCK) Cells. Cycloheximide Inhibits the Stimulated Prostaglandin Synthesis, Deacylation of Lipids, and Morphological Changes.” Journal of Biological Chemistry 253 (13): 4783–4790.
   PubMed Web of Science ®Google Scholar
• Ono, Y., T. O. M. O. FuJII, K. Igarashi, T. Kuno, C. Tanaka, U. Kikkawa, and Y. Nishizuka. 1989. “Phorbol Ester Binding to Protein Kinase C Requires a Cysteine-Rich Zinc-Finger-Like Sequence.” Proceedings of the National Academy of Sciences 86 (13): 4868–4871.
   PubMed Web of Science ®Google Scholar
• Oskoueian, E., N. Abdullah, and S. Ahmad. 2012. “Phorbol Esters Isolated From Jatropha Meal Induced Apoptosis-Mediated Inhibition in Proliferation of Chang and Vero Cell Lines.” International Journal of Molecular Sciences 13 (11): 13816–13829.
   PubMed Web of Science ®Google Scholar
• Pelletier, G., B. K. Padhi, J. Hawari, G. I. Sunahara, and R. Poon. 2015. “Development of a Sensitive in Vitro Assay to Quantify the Biological Activity of Pro-Inflammatory Phorbol Esters in Jatropha Oil.” In Vitro Cellular & Developmental Biology - Animal 51 (6): 644–650.
   PubMed Web of Science ®Google Scholar
• Poon, R., V. E. Valli, W. M. Ratnayake, M. Rigden, and G. Pelletier. 2013. “Effects of Jatropha Oil on Rats Following 28-Day Oral Treatment.” Journal of Applied Toxicology 33 (7): 618–625.
   PubMed Web of Science ®Google Scholar
• Roach, J. S., R. K. Devappa, H. P. S. Makkar, and K. Becker. 2012. “Isolation, Stability and Bioactivity of Jatropha curcas Phorbol Esters.” Fitoterapia 83 (3): 586–592.
   PubMed Web of Science ®Google Scholar
• Safe, S. 1997. “Limitations of the Toxic Equivalency Factor Approach for Risk Assessment of TCDD and Related Compounds.” Teratogenesis, Carcinogenesis, and Mutagenesis 17 (4–5): 285–304.
   PubMedGoogle Scholar
• Safe, S. H. 1998. “Development Validation and Problems With the Toxic Equivalency Factor Approach for Risk Assessment of Dioxins and Related Compounds.” Journal of Animal Science 76 (1): 134–141.
   PubMed Web of Science ®Google Scholar
• Singh, R. K., D. Singh, and A. G. Mahendrakar. 2010. “Jatropha Poisoning in Children.” Medical Journal Armed Forces India 66 (1): 80–81.
   PubMedGoogle Scholar
• Ueda, Y., S. i. Hirai, S. i. Osada, A. Suzuki, K. Mizuno, and S. Ohno. 1996. “Protein Kinase C Activates the MEK-ERK Pathway in a Manner Independent of Ras and Dependent on Raf.” Journal of Biological Chemistry 271 (38): 23512–23519.
   PubMed Web of Science ®Google Scholar
• Van den Berg, M., L. S. Birnbaum, M. Denison, V. M. De, W. Farland, M. Feeley, H. Fiedler et al. 2006. “The 2005 World Health Organization Reevaluation of Human and Mammalian Toxic Equivalency Factors for Dioxins and Dioxin-Like Compounds.” Toxicological Sciences 93 (2): 223–241.
   PubMed Web of Science ®Google Scholar
• Vogg, G., S. Achatz, A. Kettrup, and H. Sandermann, Jr. 1999. “Fast, Sensitive and Selective Liquid Chromatographic-Tandem Mass Spectrometric Determination of Tumor-Promoting Diterpene Esters.” Journal of Chromatography A 855 (2): 563–573.
   PubMed Web of Science ®Google Scholar
• Windal, I., M. S. Denison, L. S. Birnbaum, W. N. Van, W. Baeyens, and L. Goeyens. 2005. “Chemically Activated Luciferase Gene Expression (CALUX) Cell Bioassay Analysis for the Estimation of Dioxin-Like Activity: Critical Parameters of the CALUX Procedure That Impact Assay Results.” Environmental Science & Technology 39 (19): 7357–7364.
   PubMed Web of Science ®Google Scholar
• Yang, C., and M. G. Kazanietz. 2003. “Divergence and Complexities in DAG Signaling: Looking Beyond PKC.” Trends in Pharmacological Sciences 24 (11): 602–608.
   PubMed Web of Science ®Google Scholar