Natural products-characterized moringa oleifera leaves methanolic extract and anti-diabetic properties mechanisms of its fractions in streptozotocin-induced diabetic rats
Keywords:
AMP-Kinase, Diabetes, α-amylase, Moringa oleifera,, Mechanism of actionAbstract
Background: The study characterized natural products and investigated the mechanisms of antidiabetic properties in Moringa oleifera leaves methanolic extract in Streptozotocin-induced diabetic male rats.
Methods: the natural bioactive compounds in difffferent fractions were obtained by column chromatography on 60-120 silica gel mesh and assayed using gas chromatography-mass spectrometric (GC-MS) technique. Also, possible anti-diabetic properties mechanisms of the fractions of extracts investigated using standard methods.
Results: Lethality study indicated safety of the extract at 5000mg/kgbwt. The GC- MS analysis of the methanolic extract revealed seven out of eleven common bioactive constituents with reported antidiabetic activity. Results of possible anti-diabetic properties mechanisms based on studied glucose homeostasis-related bio-indicators showed signifificant (P<0.05) increase in serum lipoprotein lipase, whole blood GLUT 1, liver homogenate G-6-P-DH, Intestine homogenate Na+ /K+ -ATPase, Muscle homogenate GLUT 4 and liver homogenate AMP-Kinase activities in rats administered with the drug (glibenclamide) and fractions 3,4,5 compared with the diabetic group. A signifificant (P<0.05) inhibition of serum α-amylase activity in rat administered drug and fractions 3,4,5 was observed when compared with diabetic control and fractions 1 and 2 . Histological outcomes of rats' pancreas corroborated these fifindings.
Conclusion: Thus, characterized natural bioactive constituents of M. oleifera fractions exerted concerted potent anti-diabetic activity in streptozotocin-induced diabetic rats by probable mechanisms involving concerted α-amylase inhibition, AMP-kinase and Lipo-protein lipase activation and glucose transport Proteins (GLUT-1 and GLUT-4) and liver homogenate Glucose-6-phosphate dehydrogenase up-regulation.
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