Thymol, a bioactive component of ocimum gratissimum linn. leaf ameliorated diabetes-induced exocrine pancreas insufficiency in male wistar rats

Abstract

Background and aims: Exocrine pancreas insufficiency characterized by decreased pancreatic enzyme activity is one of the conditions associated with prolonged diabetes mellitus. Anti-diabetic activity of Ocimum gratissimum linn. leaf in experimental animals is well documented and using gas chromatography mass spectroscopy analysis, thymol has been identified as one of its bioactive components. This study investigated the effect of thymol on pancreatic alpha amylase activities and oxidative stress biomarkers in streptozotocin-induced diabetic rats. Methods: Twenty-four male Wistar rats grouped into four as Control, THY, DIA, and DIA+THY were used. Animals in DIA and DIA+THY were diabetic orally administered distilled water and thymol (20 mg/kg), respectively, while control and THY were normal rats treated similarly for 14 days. Fasting blood glucose (FBG), liver function, lipid profile, and oxidative stress biomarkers were determined in the blood while the pancreas was obtained for amylase activities. Results: Thymol treatment in the DIA+THY decreased FBG (119.75 ± 20.10 mg/dl), cholesterol (129.22 ± 8.34 mg/dl), triglycerides (116.41 ± 8.34 mg/dl), and low-density lipoprotein (101.89 ± 8.28 mg/dl) when compared with the DIA (209.25 ± 46.88 mg/dl, 156.31 ± 16.21 mg/dl, 143.13 ± 14.81 mg/dl, and 131.23 ± 13.38 mg/dl, respectively). Increased alanine transaminase and alkaline phosphatase observed in DIA were reversed in the Dia+THY. Pancreatic amylase activity was reduced in DIA (3.01 ± 0.50 Activity/mg.protein) compared with control (6.4 ± 0.42 Activity/mg.protein) and this was increased in DIA+THY (6.73 ± 0.39 Activity/mg.protein) relative to DIA. Increased plasma malondialdehyde and decreased catalase activity were observed in the DIA group and these were reversed in the DIA+THY group Conclusions: Thymol has hypoglycemic properties and stimulates pancreatic alpha-amylase activity through a mechanism that may be linked to its antioxidant properties.