Biocatalysis and agricultural biotechnology | 2019

Bacoside-A diminishes liver functional enzymes and improves carbohydrate metabolic key enzymes in streptozotocin a rat model of T2DM

 
 
 

Abstract


Abstract Type 2 diabetes mellitus (T2DM) is a global alarming predominant metabolic disease than other diabetes and incurs substantial burden to public and healthcare systems. Our study is designed to endeavor the valuable effect of bacoside-A on hepatic key enzymes of carbohydrate metabolism in streptozotocin (STZ) induced diabetic rats. A single intraperitoneal (i.p) injection of STZ (40\u202fmg/kg body weight [BW]) is administered to adult male Wistar rats for the attainment of diabetes. Diabetic rats were orally treated with bacoside-A of various doses (5, 10 and 20\u202fmg/kg BW) for 45 days. Bacoside-A (10\u202fmg/kg BW) showed more pronounced effect than the other doses and thus resulted in a significant reduction in the level of plasma glucose, glycosylated hemoglobin (HbA1c) and an rise in insulin and hemoglobin levels. Administration of bacoside-A showed significant elevated in the activity of glycolytic enzyme (hexokinase) and hepatic shunt enzyme (glucose-6-phophate dehydrogenase) whereas significant decline in the activity of gluconeogenic enzymes (glucose-6-phosphatase and fructose-1,6-bisphosphatase) in diabetic rats. Further, bacoside-A administration to diabetic rats enhanced body weight, liver glycogen content and modulating its metabolizing enzymes (glycogen synthase and glycogen phosphorylase) demonstrated the antihyperglycemic potential of bacoside-A in diabetic rats. Furthermore, hepatic marker enzymes such as aspartate transaminases (AST) and alanine transaminases (ALT) activities significantly decreased in diabetic rats and tend to normalcy in bacoside-A treated diabetic rats. Glibenclamide, a reference drug. In conclusion, our data explicated the bacoside-A, a promising antidiabetic agent which infers in modulating hepatic key enzymes by preventing defect in carbohydrate metabolism against T2DM.

Volume 21
Pages 101331
DOI 10.1016/j.bcab.2019.101331
Language English
Journal Biocatalysis and agricultural biotechnology

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