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Mendoza Meza, D. L. ., Sánchez Catalán, K. ., & Saavedra Ahumada, S. . (2016). Biochemical characterization of Ulomoides dermestoides (coleoptera, tenebrionidae) aqueous extracts: exploration of dual inhibition of lipoxygenase (15-lox) and cyclooxygenase (cox-1 and cox-2). Biosalud, 15(2), 37–54. https://doi.org/10.17151/biosa.2016.15.2.5
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Abstract
Ulomoides dermestoides is used in traditional oriental medicine to alleviate inflammatory diseases and as an aphrodisiac. In Colombia, rural communities consume it as treatment for asthma. The purpose of this study was to obtain aqueous extracts of whole body of U. dermestoides and explore their potential to inhibit enzymes involved in the biosynthesis of inflammation regulators, 15-lipoxygenase (15- LOX) and cyclooxygenases COX-1 and COX-2 (COXs). Extracts were obtained with phosphate buffered saline 0.01M (PBS) and ammonium bicarbonate 0.1M (NH4HCO3) in the presence of one detergent (Tween-20 or Sodium dodecyl sulfate, SDS). Then, total soluble protein, electrophoretic profile and enzymatic activities at 19 hydrolases were determined. Inhibition of 15-LOX and COXs were measured by colorimetric method and enzymatic immunoassay respectively. The highest protein yield was obtained with PBS/SDS buffer (1.603 %p/p). This extract showed 13 major electrophoretic bands with molecular weights between 8.8 and 151.2 kDa; also, enzymatic phosphohydrolase, peptidase, esterase, β-glucuronidase, α-glucosidase, N-acetyl-β-glucosaminidase and α-mannosidase activities were proven. All extracts showed dual inhibitory activity for 15-LOX and COXs. The higher inhibitions for 15-LOX and COX-1 were obtained with PBS/SDS extract (15-LOX: 62.8±2%; COX-1: 88.5±3.9%). Additionally, a simple linear regression analysis showed nonrelationship between the protein concentration and 15-LOX inhibition (p value = 0.493). This result suggests that anti-lipoxygenase activity could be due to non-protein compounds.
Keywords:
References
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2. Crusz SM, Balkwill FR. Inflammation and cancer: advances and new agents. Nat Rev ClinOncol. 2015; 12(10):584-96. doi:10.1038/nrclinonc.2015.105.
3. Medzhitov R1. Origin and physiological roles of inflammation. Nature. 2008; 454(7203):428-35. doi: 10.1038/nature07201.
4. Kotas ME, Medzhitov R. Homeostasis, inflammation, and disease susceptibility. Cell. 2015; 160(5):816- 27. doi: 10.1016/j.cell.2015.02.010.
5. Murakami M, Kudo I. Prostaglandin E synthase: a novel drug target for inflammation and cancer. Curr Pharm Des. 2006; 12(8):943-54.doi: 10.2174/138161206776055912.
6. Wisastra R, Dekker FJ. Inflammation, cancer and oxidative lipoxygenase activity are intimately linked. Cancers. 2014; 6:1500-21. doi: 10.3390/cancers6031500.
7. Shin K, Hwang JJ, Kwon BI, Kheradmand F, Corry DB, Lee SH. Leukotriene enhanced allergic lung inflammation through induction of chemokine production. ClinExp Med. 2015; 15(3):233-44. doi: 10.1007/s10238-014-0292-7.
8. Marnett LJ, Rowlinson SW, Goodwin DC, Kalgutkar AS, Lanzo CA. Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition. J Biol Chem. 1999; 274(33): 22903-6. doi: 10.1074/jbc.274.33.22903.
9. FAO Regional Office for Asia and the Pacific. Forest insects as food: humans bite back. Proceedings of a workshop on Asia-Pacific resources and their potential for development. Bangkok, Thailand. 2010; 151-60 pp. Disponible en: www.fao.org/docrep/012/i1380e/i1380e00.pdf.
10. Chu GS, Palmieri JR, Sullivan JT. Beetle-eating: a Malaysian folk medical practice and its public health implications. Trop Geogr Med. 1977; 29(4):422-427. PMID: 610028.
11. Sandroni P. Aphrodisiacs past and present: a historical review. ClinAuton Res. 2001; 11(5):303-7. doi: 10.1007/BF02332975.
12. Costa Neto E, Ramos-Elorduy J. Los insectos comestibles de Brasil: etnicidad, diversidad e importancia en la alimentación. Boletín Sociedad Entomológica Aragonesa. 2006; 38:423-42.
13. Crespo R, Villaverde ML, Girotti JR, Güerci A, Juárez MP, de Bravo MG. Cytotoxic and genotoxic effects of defence secretion of Ulomoides dermestoides on A549 cells. J Ethnopharmacol. 2011; 136(1):204- 9. doi: 10.1016/j.jep.2011.04.056.
14. Deloya-Brito G, Deloya C. Sustancias producidas por el coleóptero Ulomoides dermestoides (Chevrolat, 1878) (Insecta: Coleoptera: Tenebrionidae): efecto anti-inflamatorio y citotóxico. Acta ZoolMex. 2014; 30(3): 665-61. Disponible en: http://www.scielo.org.mx/pdf/azm/v30n3/v30n3a14.pdf.
15. Amat G, Devia N. Estos escarabajos curan el asma. Publicación de la Unidad de Medios de Comunicación de la Universidad Nacional de Colombia (UNIMEDIOS). Bogotá, Colombia. Disponible en: http://historico.unperiodico.unal.edu.co/ediciones/103/17.html. Consultado Junio 2015.
16. Santos RC, Lunardelli A, Caberlon E, Bastos CM, Nunes FB, Pires MG, Biolchi V, Paul EL, Vieira FB, Resende do Carmo Aquino A, Corseuil E, de Oliveira JR. Anti-inflammatory and immunomodulatory effects of Ulomoides dermestoides on induced pleurisy in rats and lymphoproliferation in vitro. Inflammation. 2010; 33(3):173-9. doi: 10.1007/s10753-009-9171-x.
17. Tobón FA, Gutiérrez GP, Mejía ML. Evaluación del perfil neurofarmacológico del aceite de Ulomoides dermestoides (Coleoptera: Tenebrionidae). Revista Colombiana de Entomología. 2011; 37(2):251-5. Disponible en: http://www.scielo.org.co/pdf/rcen/v37n2/v37n2a16.pdf.
18. Yan S, Chu Z. Antioxidant effects of delipidized protein hydrolysate from Martianus dermestoides Chevrolat (Coleoptera, Tenebrionidae) beetles. Acta Entomológica Sinica. 2008; 51(8): 804-9. Disponible en: http://www.insect.org.cn/EN/abstract/abstract9541.shtml#.
19. ShanChun Y, Lei W, Qing L, Yong F. Anti-senile effects of water extraction of Martianus dermestoides (Coleoptera: Tenebrionidae) feeding different foods on aging mice. Acta Entomol Sin. 2009; 52(7): 820-4. Disponible en: http://www.insect.org.cn/EN/abstract/abstract9369.shtml#.
20. Mendoza DL, Maury C. Evaluación del contenido de fenoles totales y actividad captadora de radicales libres de extractos hidrometanólicos del escarabajo Ulomoides dermestoides (coleoptera: tenebrionidae). Rev. Asoc. Col. Cienc.(Col.). 2013; 25:135-41. Disponible en: http://www. asociacioncolombianadecienciasbiologicas.org/download/revistas/2013/art%2013.pdf.
21. Kim J, Jung BH. Contribution to the Tribes Diaperini Doyen in Korea (Coleoptera: Tenebrionidae: Diaperinae). Entomological Research. 2005; 35(2):95-100. doi: 10.1111/j.1748-5967.2005. tb00142.x.
22. Bradford M. A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein Dye Binding. Analytical Biochemistry 1972; 72:248-54. doi: 10.1016/0003-2697(76)90527-3.
23. Sambrook J, Russell D.W. SDS-Polyacrylamide Gel Electrophoresis of Proteins. CSH Protocols. 2006. doi: 10.1101/pdb.prot4540.
24. Yu WG, Zhang BB, Shen YJ, Li Y, Tian YB, Jiang MH. Purification and Characterization of Superoxide Dismutase from Martianus dermestoides Chevrolat. Adv Mat Res. 2013; 773:336-41. doi: 10.4028/www.scientific.net/AMR.773.336.
25. Long D, Defu C, Beibei Z, Xiaocan L, Jia Y. Optimization of extraction conditions for superoxide dismutase from Martianus dermestoides. Journal of Northeast Forestry University. 2009; 37(4): 69-
70.Disponible en: http://en.cnki.com.cn/Article_en/CJFDTOTAL-DBLY200904024.htm
26. Le Maire M, Champeil P, Møller JV. Interaction of membrane proteins and lipids with solubilizing detergents. BiochimicaetBiophysicaActa (BBA) – Biomembranes. 2000; 1508(1–2):86–111.doi:10.1016/S0304-4157(00)00010-1.
27. Zhao F1, Bi X, Hao Y, Liao X. Induction of viable but non culturable Escherichia coli O157: H7 by high pressure CO2 and its characteristics. PLoS One. 2013; 8(4):e62388. doi: 10.1371/journal.pone.0062388.
28. Budzyńska A, Sadowska B, Więckowska-Szakiel M, Różalska B. Enzymatic profile, adhesive and invasive properties of Candida albicans under the influence of selected plant essential oils. ActaBiochim Pol. 2014; 61(1):115-21. Disponible en: http://www.actabp.pl/pdf/1_2014/115.pdf.
29. Carnés J, Boquete M, Carballada FJ, Gallego MT, Fernández-Caldas E. Enzymatic activity in body and fecal extracts of the storage mite Chortoglyphus arcuatus. Int Arch Allergy Immunol. 2008; 145(3): 207-212.doi:10.1159/000109289.
30. Morales M, Iraola V, Leonor J, Carnés J. Enzymatic Activity of Allergenic House Dust and Storage Mite Extracts. J Med Entomol. 2013. 50(1): 147-54. doi: http://dx.doi.org/10.1603/ME12154.
31. Kramer Kj, Aoki H. Chitinolytic enzymes from pupae of the red flour beetle, Tribolium castaneum. Comp BiochemPhysiol B Biochem Mol Biol. 1987; 86(3):613-21. http://dx.doi.org/10.1016/0305-0491(87)90457-3.
32. Merzendorfer H, Zimoch L. Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J Exp Biol. 2003; 206: 4393-441. doi: 10.1242/jeb.00709.
33. Chun Geun Lee. Chitin, Chitinases and Chitinase-like Proteins in Allergic Inflammation and Tissue Remodeling. Yonsei Med J. 2009; 50(1):22–30. doi: 10.3349/ymj.2009.50.1.22.
34. O’Neil S, Heinrich T, Hales B, Hazell L, Holt D, Fischer K et al. The chitinase allergens Der p15 and Der p18 from Dermatophagoide spteronyssinus. ClinExp Allergy 2006; 36(6):831-9. doi:10.1111/j.1365-2222.2006.02497.x.
35. Schultze-Werninghaus G, Zachgo W, Rotermund H, Wiewrodt R, Merget R, Wahl R, Burow G, zurStrassen R. Tribolium confusum (confused flour beetle, rice flour beetle) an occupational allergen in bakers: demonstration of IgE antibodies. Int Arch Allergy ApplImmunol. 1991; 94(1-4):371-2.doi:10.1159/000235407.
36. Alanko K, Tuomi T, Vanhanen M, Pajari-Backas M, Kanerva L, Havu K, Saarinen K, Bruynzeel DP. Occupational IgE-mediated allergy to Tribolium confusum (confused flour beetle). Allergy. 2000;55(9):879-82. doi: 10.1034/j.1398-9995.2000.00572.x.
37. Wahrendorf M, Wink M. Pharmacologically active natural products in the defence secretion of Palembus ocularis (Tenebrionidae, Coleoptera). J Ethnopharmacol. 2006; 106(1): 51-6. doi: 10.1016/j.jep.2005.12.007.
38. Skrzypczak-Jankun E, Chorostowska-Wynimko J, Selman SH, Jankun J. Lipoxygenases- A challenging problem in enzyme inhibition and drug development. CurrEnzymInhib. 2007; 3(2):119-132. doi:http://dx.doi.org/10.2174/157340807780598350.
39. Chedea VS, Jisaka M. Inhibition of Soybean Lipoxygenases-Structural and Activity Models for the LipoxygenaseIsoenzymes Family. INTECH Open Access Publisher. 2011. Disponible en: http://cdn.intechweb.org/pdfs/22600.pdf.
40. Kohyama N, Nagata T, Fujimoto S, Sekiya K.Inhibition of arachidonatelipoxygenase activities by 2-(3, 4-dihydroxyphenyl) ethanol, a phenolic compound from olives. BiosciBiotechnolBiochem. 1997; 61(2):347-50. doi: 10.1271/bbb.61.347.
41. Landa P, Kutil Z, Malik J, Kokoska L, Widowitz U, Marsik P, Bauer R, Vanek T. In vitro inhibition of 5-lipoxygenase by natural quinone compounds. Planta Med 2011; 77-102. doi: 10.1055/s-0031-1282860.
42. Deszcz L, Kozubek A. Inhibition of soybean lipoxygenases by resorcinolic lipids from cereal bran. Cell MolBiolLett. 1997; 2:213-22. Disponible en: http://www.ibmb.uni.wroc.pl/publak/soybean.pdf.
43. Kotsyfakis M, Sá-Nunes A, Francischetti IM, Mather TN, Andersen JF, Ribeiro JM. Antiinflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodesscapularis. J Biol Chem. 2006; 281(36):26298-307. doi: 10.1074/jbc.M513010200.
44. Jurenka RA, Howard RW, Blomquist GJ. Prostaglandin synthetase inhibitors in insect defensive secretions. Naturwissenschaften. 1986; 73(12):735-7. doi: 10.1007/BF00399245.
45. Howard R, Jurenka R, Blomquist G. Prostaglandin synthetase inhibitors in the defensive secretion of the red flour beetle Tribolium castaneum (Herbst) (Coleoptera: Tenebrionidae). Insect biochemistry.1986; 16(5):757-60. doi: 10.1016/0020-1790(86)90111-3.
46. Andersen S. Cuticular sclerotization in the beetles Pachynodae epphipiata and Tenebrio molitor. J Insect Physiol. 1975; 21(6): 1225-32. doi: 10.1016/0022-1910(75)90091-8.
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