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Anti-Hyperglycemic Property Of Medicinal Plants
Published in Amit Baran Sharangi, K. V. Peter, Medicinal Plants, 2023
Karanpreet Singh Bhatia, Arpita Roy, Navneeta Bhardavaj
Capparis deciduas with a vernacular name karira, is a fellow of Capparaceae family and found in deserted regions in Southern Asia, Africa, and Middle East. To investigate upon antihyperglycemic potential of aqueous and ethanolic extract of C. deciduas, an investigation was conducted on albino rats. Extracts (at a dosage of 0.25 and 0.5 g/kg b.w.) were fed orally to diabetic rats for 21 days and after 21 days a quite noticeable decrease in FBG levels was observed (58.5, 83.6% for aqueous extract and 60.2, 98.5% for ethanolic extract) (Rathee et al., 2010). In another study, alkaloid rich fraction of karira was given to STZ-induced hyperglycemic rats for 28 days. It was found that alkaloid rich fraction prevented acute increase in sugar levels during OGT test and also lowered triglyceride and total cholesterol. There was impairment in glucose-6-phosphatase activity by 44%, and also glycogen content in muscle and liver were significantly improved. Gene expression of phosphoenolpyruvate carboxykinase (PEPCK), G6Pase, tumor necrosis factor-alpha (TNF-alpha) and aldose reductase were significantly decreased on other hand expression of GLUT-4, PPAR-gamma, and GK improved significantly (Sharma et al., 2009).
Inborn Errors of Metabolism
Published in Praveen S. Goday, Cassandra L. S. Walia, Pediatric Nutrition for Dietitians, 2022
Surekha Pendyal, Areeg Hassan El-Gharbawy
Glucose 6-phosphatase (G6Pase) is required for the final step of glycogenolysis and gluconeogenesis to cleave glucose from glucose 6-phosphate (Figure 23.5). Glucose 6-phosphate is formed from the breakdown of glycogen and from fructose and galactose. In the absence of G6Pase, hypoglycemia is the primary consequence of GSD I with secondary consequences of lactic acidosis, hyperlipidemia, and hyperuricemia. GSD I has two sub-types: GSD Ia results from deficiency of G6Pase and GSD Ib results from deficiency of the enzyme translocase that transports G6Pase across the endoplasmic reticulum.
Glycogenosis type I – von Gierke disease
Published in William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop, Atlas of Inherited Metabolic Diseases, 2020
William L. Nyhan, Georg F. Hoffmann, Aida I. Al-Aqeel, Bruce A. Barshop
The glucose-6-phosphatase system also depends on the transport of glucose. A number of glucose transport proteins has been identified and they have been designated GLUT 1–6. Deficiency of GLUT 2 causes the syndrome of hepatic glycogenosis in the Fanconi-Bickel syndrome [81].
Justicia carnea extracts ameliorated hepatocellular damage in streptozotocin-induced type 1 diabetic male rats via decrease in oxidative stress, inflammation and increasing other risk markers
Published in Biomarkers, 2023
John Adeolu Falode, Oluwaseun Igbekele Ajayi, Tolulope Victoria Isinkaye, Akinwunmi Oluwaseun Adeoye, Basiru Olaitan Ajiboye, Bartholomew I. C. Brai
The two most significant gluconeogenic organs, the liver and kidney cortex, express the most glucose-6-phosphatase (G-6-pase) (Hers and de Duve 1950). In addition, pancreatic islet-cells express it (Khan et al.1995). In addition, in the intestinal mucosa of humans, mice (Ockerman, 1965) and rats (Chatelain et al.1998), particularly in states of starvation and diabetes (Rajas et al.1999). The liver’s G6Pase activity increases by 2–3 folds in response to starvation and diabetes (Segal and Washko 1959; Ashmore and Weber 1959; Arion and Nordlie 1965). These results are likely the result of the reciprocal variations in glucagon and insulinaemia. When diabetes mellitus is not treated or is poorly controlled, there is abnormally high liver glucose-6-phosphatase. G-6-Pase activity does, however, significantly decrease when J. carnea extracts are administered.
The protective effect of green tea on diabetes-induced hepato-renal pathological changes: a histological and biochemical study
Published in Archives of Physiology and Biochemistry, 2023
Tarek Atia, Hader I. Sakr, Ahmed A. Damanhory, Karim Moawad, Moustfa Alsawy
Hepatocyte damage causes the release of aminotransferases (ALT and AST) enzymes into circulation. Increased levels of ALT and AST, and decreased serum albumin may be attributable to the hepato-renal cellular damage induced by STZ injection and by oxidative stress of hyperglycaemia (Yazdi et al.2019). In the current study, liver function (ALT and AST) and plasma albumin were improved significantly by using GLB and GrT therapy (p < .05) compared to the diabetic control group. Chronic hyperglycaemic and hyperlipidemic conditions have been reported to damage the membrane architecture resulting in increased alkaline and acid phosphatases (ALP and ACP) activities. The role of glucose-6-phosphatase (G-6-Pase) in the release of glucose molecules to the blood is also to be noted (Rajendran et al.2007). GLB treatment results in a significant decline in the activities of ALP, ACP, and G-6-Pase (Vasant et al.2010).
Research progress of nanocarriers for gene therapy targeting abnormal glucose and lipid metabolism in tumors
Published in Drug Delivery, 2021
Xianhu Zeng, Zhipeng Li, Chunrong Zhu, Lisa Xu, Yong Sun, Shangcong Han
Gluconeogenesis can generate free glucose from non-carbohydrate carbon substrates (such as glycerol, lactic acid, pyruvate, and glycogenic amino acids). Although it is less studied than catabolic glycolysis or oxidative phosphorylation (OXPHOS), this anabolic pathway plays the same role in controlling the aerobic glycolysis of cancer cells (Seenappa et al. 2016). The complete pathway consists of 11 enzyme-catalyzed reactions, of which there are 7 reactions that are the opposite steps of glycolysis, and 3 reactions that are not involved in gluconeogenesis: (i) the conversion of pyruvate to phosphoenolpyruvate, which is determined by the reaction that catalyzes pyruvate carboxylase (PC) and phosphoenolpyruvate carboxykinase (PEPCK); (ii) the catalyzation of the conversion of fructose-1,6-diphosphate to fructose-6-phosphate by fructose-1,6-bisphosphatase (FBPase); (iii) the catalyzation of the conversion of glucose-6-phosphate to glucose by glucose-6-phosphatase (G6Pase) (Icard et al. 2019). PEPCK, FBPase, and G6Pase are the key enzymes that control the gluconeogenesis flux, thereby affecting glycolysis, the TCA cycle, the PPP and other branched metabolic pathways (serine biosynthesis, glycogen health, gluconeogenesis, and glutamine decomposition) (Kang et al. 2016; Icard et al. 2019).