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Current Trends in Biotechnology and PharmacyVol. 5 (1) 1073-1082 January 2011. ISSN 0973-8916 (Print), 2230-7303 (Online)1079peroxidase and glutathionetransferase, is readilyavailable to neutralize the free radicals generatedby t-BHP.SOD catalyses the depletion of thesuperoxide radical and protects oxygenmetabolizingcells against harmful effects ofsuperoxide free radicals. Some types of SODlike MnSOD which contains a manganeseprosthetic group, resides in the mitochondria,perhaps because of the need to protectmitochondrial proteins, membranes, and DNAfrom . O 2generated as a result of the respiratorychain. Figure 5 showing total SOD levels in humanerythrocytes with reference to sub fraction F2-3.SOD levels in 12.5 µg/ml treated group at thetime intervals of 0, 30, 60, 90 min, t-BHP-controland control were 1.2, 1.9, 3, 3.23, 1.85 and 11.02IU/g Hb protein at the concentration of 25 µg/mlMDA, SOD levels were 1.22, 2.5, 5.2 and 5.2and at the concentration of 50 µg/ml SOD levelswere 1.1, 5.3, 9.4 and 9.7 IU/g Hb, respectively(Fig.5).CAT, a soluble protein in erythrocytes, playsa role in the decomposition of hydrogen peroxideto give H 2O. In humans, the highest levels ofFig. 5. Effect of fraction F2-3 on t-BHP induced oxidativestress in erythrocytes was monitored by measuringthe superoxide dismutase activity. Results are mean ±SD.catalase are found in liver, kidney and erythrocytes,where it is believed to account for the majority ofhydrogen peroxide decomposition. Figure 6showing catalase activity in human erythrocyteswith reference to FME sub fraction F2-3. CATlevels in 12.5 µg/ml treated group at the timeintervals of 0, 30, 60, 90 min, t-BHP-control andcontrol were 50.1, 55.4, 61.8, 62.4, 53.9 and 99.78µmol H 2O 2/g Hb/min. at the concentration of 25µg/ml MDA levels were 52.8, 60.9, 72.3 and 76.6and at the concentration of 50 µg/ml MDA levelswere 51.1, 62.5, 98.3 and 100.7 µmol H 2O 2/g Hb/min., respectively (Fig.6). Since both the enzymesSOD and CAT are directly involved in theneutralization of free radicals, these enzymes playa pivotal role in the oxidative stress. Theseenzyme levels were significantly reduced in t-BHPtreated groups indicating that antioxidant abilityof the erythrocytes are reduced in t-BHP treatedgroup. Since these enzymes are replenished inresponse to F2-3 fraction of the fruit, erythrocytesagain gained the antioxidant potentials to combatagainst the free radicals generated in the variousmetabolic reactions.The present findings show that L.acutangula fruit aqueous fraction F2-3pretreatment attenuated t-BHP induced lipidperoxidation in human erythrocyes. Specifically,fraction F2-3 prevented t-BHP induced increasesin MDA levels, and concomitantly restored GSHcontent, SOD and CAT activity in erythrocytes,though to a different degrees. These effects mayreflect the ability of fraction F2-3 to enhance thescavenging and inactivation of H 2O 2and hydroxylradicals. In addition, fraction F2-3 may serve asa chealator and directly bind to Fe 2+ , whichcatalyzes formation of free radicals via the Fentonreactions (28, 29). Fraction F2-3 may alsoterminate lipid peroxidation by induction ofenzymatic and non-enzymatic antioxidants, suchas GSH, SOD and CAT (30). Accordingly, theRole of Luffa acutangula in Oxidative damage
Current Trends in Biotechnology and PharmacyVol. 5 (1) 1073-1082 January 2011. ISSN 0973-8916 (Print), 2230-7303 (Online)1080protection afforded by fraction F2-3 against t-BHP induced ROS generation is likely attributableto its antioxidant effects.In conclusion, L. acutangula methanolicextract fraction F2-3 showed significantantioxidant activity in human erythrocytes andfurther studies are required to elucidate thefraction components and their molecularmechanism. Systemically, superoxides could beproduced in huge amounts by various metabolicand physiological processes (31, 32, 33). Theformation of superoxide radical leads to a cascadeformation of other ROS in the cell, whenever theantioxidant system fails to combat with ROS thatcan cause to lethal damage to the system (34).Hence, our data for the first time reports theoxidative stress inhibitory property of the L.autangula fruit. So that it may help to preventdiseases caused by the ROS. However, one thingwe should consider that antioxidant activity maydiffer from organism to organism because of thegenetic configurations to respective antioxidantmechanism (16). So we can expect less or moreactivity from different organism.Fig. 6. Eeffect of fraction F2-3 on t-BHP inducedoxidative stress in erythrocytes was monitored bymeasuring the activity levels of catalase. Results areMean ± SD.AcknowledgementsThis study was supported by Financial support(Senior Research Fellowship) from CSIR, NewDelhi, India.Reference1. Herbette Stephane, Roeckel-DrevetPatricia and Drevet, Joel R. (2007). Selenoindependentglutathione peroxidases: Morethan simple antioxidant scavengers. FEBSJ., 274: 2163-2180.2. Mc Cord, J.M. and Fridovich, I. (1969).Superoxide dismutase an enzymic functionfor erythrocuprein (hemocuprein). J BiolChem., 244: 6049-55.3. Marian, V. (2007). Free radicals andantioxidants in normal physiologicalfunctions and human disease. Int JBiochem, Cell Biol., 39: 44–84.4. Aygul, R., Demircan B. Erdem .F, Ulvi, H.,Yildirim, A. and Demirbas, F. (2005).Plasma Values of Oxidants andAntioxidants in Acute Brain Hemorrhage:Role of Free Radicals in the Developmentof Brain Injury. Biol Trace Elem Res.,108(1-3): 43-52.5. Ji, L. (2007). Antioxidant signaling in skeletalmuscle: A brief review. Exp Gerontol., 420:582–593.6. Bravo, L. (1998). Polyphenols: Chemistry,dietary sources, metabolism, and nutritionalsignificance. Nutr Rev, 56: 317-333.7. Chung, K.T., Wong, T.Y., Wei, CI., Huang,Y.W. and Lin, Y. (1998). Tannins and humanhealth: a review. Crit Rev Food Sci Nutr,38: 421-464.8. Crozier, A., Burns, J., Aziz, A.A., Stewart,A.J., Rabiasz, H.S., Jenkins, G.I., Edwards,C.A. and Lean Mej. (2000). AntioxidantPurushotham Reddy et al.
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