Okra Modulates Regulatory Enzymes and Metabolites of Glucose-Utilizing Pathways in Diabetic Rats

Abstract

Objective

Using a rat diabetes model, the authors examined how substrates and products of glycolysis and key regulatory enzymes for glycolysis, gluconeogenesis, Kreb’s cycle, and glycogen metabolism react to treatment with okra diet therapy, relative to glibenclamide treatment.

Method

The animal grouping involved normoglycemic rats, untreated diabetic rats, and diabetic rats treated with glibenclamide, 50% w/w okra sauce, exclusive okra sauce diet, or sauce without okra. Alloxan monohydrate was the diabetogenic agent. Insulin and adiponectin were assayed with enzyme-linked immunosorbent assay (ELISA) while the metabolites and enzymes were assed using standard spectrophotometric methods.

Results

The exclusive diet therapy significantly (p < 0.05) improved insulin activities after 60 days and reversed the altered adiponectin activities. Glucose-6-phosphate, fructose-6-phosphate, and fructose-1,6-bisphosphate levels were depleted during diabetes, but phosphoenolpyruvate and pyruvate accumulated during the first short phase of diabetes. Rats in the glibenclamide and 100% okra diet groups showed comparable hexokinase, phosphofructokinase, and pyruvate kinase activities relative to the normoglycemic rats, while the gluconeogenic enzymes, glucose-6-phosphatase, and fructose-1,6-bisphosphatase remained altered. The authors observed that extended treatment with glibenclamide restored the activities of all the Kreb’s cycle enzymes, while succinate dehydrogenase and α-ketoglutarate dehydrogenase were nonresponsive to the okra diet therapy relative to their control levels. The glycogen stores were normalized by the exclusive diet therapy, but glycogen synthase and phosphorylase activities were unresponsive.

Conclusions

Okra diet has shown insulin-sensitizing potentials with prolonged intake during diabetes as well as the potential to reverse alterations in the major carbohydrate-metabolizing enzyme.

Keywords:

• Okra
• diabetes
• insulin
• regulatory enzymes

Acknowledgements

We appreciate the financial support provided to us by Associate Professor E.N. Agomuo of the Department of Biochemistry, Imo State University, Owerri, Imo State, Nigeria.

Disclosure statement

No potential conflict of interest was reported by the authors.