Modification of renal oxidative stress and lipid peroxidation in streptozotocin-induced diabetic rats treated with extracts from Gongronema latifolium leaves. 2003

Ngozi H Ugochukwu, and Makini K Cobourne
Department of Chemistry, Florida Agricultural and Mechanical University, Tallahassee, FL 32307, USA. ngozi.ugochukwu@famu.edu

BACKGROUND Gongronema latifolium is a tropical plant traditionally used in controlling weight gain in lactating women, as well as diabetic and overall health management. In this experiment, the aqueous and ethanolic extracts were tested to evaluate their effect on renal oxidative stress and lipid peroxidation in non-diabetic and streptozotocin-induced diabetic rats. METHODS Diabetes was induced in male Wistar rats by intraperitoneal (i.p.) injection of streptozotocin (STZ) (65 mg/kg). The rats were divided into non-diabetic (18) and STZ-induced diabetic (18) rats, and both groups subdivided according to their treatments: aqueous extract (100 mg/kg), ethanolic extract (100 mg/kg) and control (saline solution). Aqueous and ethanolic extracts were administered by gavage in 12-h cycles over a 14-day period. RESULTS The results indicated that the ethanolic extract significantly normalized catalase (CAT) activity (p<0.01), increased glutathione peroxidase (GPx) activity (p<0.05), and reduced reactive oxygen species (ROS) concentrations (p<0.001). It also nonsignificantly normalized superoxide dismutase (SOD) activity, increased GSH/GSSG ratio and reduced malondialdehyde (MDA) concentrations in the diabetic kidney. The aqueous extract had no effect on the superoxide dismutase activity in the diabetic animals and caused a nonsignificant increase in catalase activity. CONCLUSIONS The ethanolic extract appeared to be more effective in reducing oxidative stress, lipid peroxidation, and increasing the GSH/GSSG ratio, thus confirming the ethnopharmacological use of G. latifolium in ameliorating the oxidative stress found in diabetics and indicating promise of possible use in lessening morbidity in affected individuals.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008297 Male Males
D008315 Malondialdehyde The dialdehyde of malonic acid. Malonaldehyde,Propanedial,Malonylaldehyde,Malonyldialdehyde,Sodium Malondialdehyde,Malondialdehyde, Sodium
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010936 Plant Extracts Concentrated pharmaceutical preparations of plants obtained by removing active constituents with a suitable solvent, which is evaporated away, and adjusting the residue to a prescribed standard. Herbal Medicines,Plant Extract,Extract, Plant,Extracts, Plant,Medicines, Herbal
D002374 Catalase An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA. Catalase A,Catalase T,Manganese Catalase,Mn Catalase
D003921 Diabetes Mellitus, Experimental Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY. Alloxan Diabetes,Streptozocin Diabetes,Streptozotocin Diabetes,Experimental Diabetes Mellitus,Diabete, Streptozocin,Diabetes, Alloxan,Diabetes, Streptozocin,Diabetes, Streptozotocin,Streptozocin Diabete
D005978 Glutathione A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. Reduced Glutathione,gamma-L-Glu-L-Cys-Gly,gamma-L-Glutamyl-L-Cysteinylglycine,Glutathione, Reduced,gamma L Glu L Cys Gly,gamma L Glutamyl L Cysteinylglycine
D005979 Glutathione Peroxidase An enzyme catalyzing the oxidation of 2 moles of GLUTATHIONE in the presence of HYDROGEN PEROXIDE to yield oxidized glutathione and water. Cytosolic Glutathione Peroxidase,Glutathione Lipoperoxidase,Selenoglutathione Peroxidase,Glutathione Peroxidase, Cytosolic,Lipoperoxidase, Glutathione,Peroxidase, Glutathione,Peroxidase, Selenoglutathione
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

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