Resumen

MENDOZA MEZA, Dary Luz; SANCHEZ CATALAN, Karen  y  SAAVEDRA AHUMADA, Stephanie. 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 [online]. 2016, vol.15, n.2, pp.37-54. ISSN 1657-9550.  https://doi.org/10.17151/biosa.2016.15.2.5.

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, B-glucuronidase, a-glucosidase, N-acetyl-B-glucosaminidase and a-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 non-relationship 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.

Palabras clave : Ulomoides dermestoides; inflammation; 15-lipoxygenase; cyclooxygenase.

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