Molecular and Cellular Biochemistry

, Volume 284, Issue 1–2, pp 95–101 | Cite as

Oxalate mediated nephronal impairment and its inhibition by c-phycocyanin: A study on urolithic rats

  • Shukkur Muhammed Farooq
  • Abdul Shukkur Ebrahim
  • Karthik Harve Subramhanya
  • Ramasamy Sakthivel
  • Nachiappa Ganesh Rajesh
  • Palaninathan VaralakshmiEmail author


The assumption of oxidative stress as a mechanism in oxalate induced renal damage suggests that antioxidants might play a beneficial role against oxalate toxicity. An in vivo model was used to investigate the effect of C-phycocyanin (from aquatic micro algae; Spirulina spp.), a known antioxidant, against calcium oxalate urolithiasis. Hyperoxaluria was induced in two of the 4 groups of Wistar albino rats (n = 6 in each) by intraperitoneally injecting sodium oxalate (70,mg/kg body weight). A pretreatment of phycocyanin (100,mg/kg body weight) as a single oral dosage was given, one hour prior to oxalate challenge. An untreated control and drug control (phycocyanin alone) were employed. Phycocyanin administration resulted in a significant improvement (p < 0.001) in the thiol content of renal tissue and RBC lysate via increasing glutathione and reducing malondialdehyde levels in the plasma of oxalate induced rats (p < 0.001), indicating phycocyanin’s antioxidant effect on oxalate mediated oxidative stress. Administering phycocyanin after oxalate treatment significantly increased catalase and glucose-6-phosphate dehydrogenase activity (p < 0.001) in RBC lysate suggesting phycocyanin as a free radical quencher. Assessing calcium oxalate crystal retention in renal tissue using polarization microscopy and renal ultrastructure by electron microscopy reveals normal features in phycocyanin – pretreated groups. Thus the study presents positive pharmacological implications of phycocyanin against oxalate mediated nephronal impairment and warrants further work to tap this potential aquatic resource for its medicinal application. (Mol Cell Biochem xxx: 1–7, 2004)


antioxidant hyperoxaluria oxidative stress phycocyanin 


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  1. 1.
    Hirata T, Tanaka M, Ooike M, Tsunomura T, Sakaguchi M: Antioxidant activities of phycocyanobilin prepared from Spirulina platensis. J Appl Phycol 12: 435–439, 2000CrossRefGoogle Scholar
  2. 2.
    Neuzil J, Stocker R: Free and albumin-bound bilirubins are efficient co-antioxidants for alpha-tocopherol, inhibiting plasma and low-density lipoprotein lipid peroxidation. J Biol Chem 17: 16712–16719, 1999Google Scholar
  3. 3.
    Lissi EA, Pizarro M, Aspee A, Romay C: Kinetic of phycocyanin bilin groups destruction by peroxyl radicals. Free Radical Biol Med 28: 1051–1055, 2000CrossRefGoogle Scholar
  4. 4.
    Rimbau V, Caminis A, Romay C, Gonzalez R, Pallas M: Protective effects of C-phycocyanin against kainic acid-induced neuronal damage in rat hippocampus. Neuroscience Letters 276: 75–78, 1999PubMedCrossRefGoogle Scholar
  5. 5.
    Selvam R: Calcium oxalate stone disease: role of lipid peroxidation and antioxidants. Urol Res 30: 35–47, 2002PubMedCrossRefGoogle Scholar
  6. 6.
    Byers T, Perry G: Carotenes, vitamin C, and vitamin E as protective antioxidants in human cancer. Annu Rev Nutr 12: 139–159, 1992PubMedCrossRefGoogle Scholar
  7. 7.
    Retsky KL, Chen K, Zeind J, Frei B: Inhibition of copper-induced LDL oxidation of vitamin C is associated with decreased copper-binding to LDL, and 2-oxo-histiding formation. Free Radical Biol Med 26: 90–98, 1999CrossRefGoogle Scholar
  8. 8.
    Zhang YM, Chen F: A simple method for efficient separation and purification of c-phycocyanin and allophycocyanin from Spirulina platensis. Biotech Tech 13: 601–603, 1999CrossRefGoogle Scholar
  9. 9.
    Largilliere C, Melancon SB: Free malondialdehyde determination in human plasma by high-performance liquid chromatography. Anal Biochem 126: 123–126, 1988CrossRefGoogle Scholar
  10. 10.
    Orozco TJ, Wang JF, Keen CL: Chronic consumption of a flavanol- and procyanindin-rich diet is associated with reduced levels of 8-hydroxy-2prime-deoxyguanosine in rat testes. J Nutr Biochem 14: 104–110, 2003PubMedCrossRefGoogle Scholar
  11. 11.
    Hunt JV, Dean RT, Wolff SP: Hydroxyl radical production and autooxidative glycosylation. Glucose oxidation as the cause of protein damage in the experimental glycation model of diabetic mellitus and aging. Biochem J 256: 205–212, 1988PubMedGoogle Scholar
  12. 12.
    Shinha AK: Colorimetric assay of catalase. Anal Biochem 47: 389–395, 1972CrossRefGoogle Scholar
  13. 13.
    Beulter E: Active transport of glutathione disulfide from erythrocytes. In: A. Larson, S. Orrenius, A. Holmgren, B. Manerwik (eds). Functions of glutathione: Biochemical, physiological, Toxicological and Clinical Aspects, Raven press, New York, 1983, pp. 65–71Google Scholar
  14. 14.
    Hammes MS, Lieske JJC, Spargo BH, Toback FG: Calcium oxalate monohydrate crystals stimulate gene expression in renal epithelial cells. Kid Int 48: 501–509, 1995CrossRefGoogle Scholar
  15. 15.
    Loidl-Stahlbofen A, Spiteller G: Alpha-Hydroxyaldehydes, products of lipid peroxidation. Biochim Biophys Acta 1211: 156–160, 1994Google Scholar
  16. 16.
    Luo X, Evrovsky Y, Cole D, Trines J, Benson LN, Lehotay DC: Doxorubicin-induced acute changes in cytotoxic aldehydes, antioxidant status and cardiac function in the rat. Biochim Biophy Acta 1360: 45–52, 1997Google Scholar
  17. 17.
    May JM, Qu ZC, Whitesell RR, Cobb CE: Ascorbate recycling in human erythrocytes: role of GSH in reducing dehydroascorbate. Free Radical Biol Med 20: 543–551, 1996CrossRefGoogle Scholar
  18. 18.
    Shang F, Lu M, Duder E, Reddan J. Taylor A: Vitamin C and vitamin E restore the resistance of GSH- depleted lens cells to hydrogen peroxide. Free Radical Biol Med 34: 521–530, 2003CrossRefGoogle Scholar
  19. 19.
    Jain A, Martensson J, Stole E, Auld PA, Meister A: Glutathione deficiency leads to mitochondrial damage in brain. Proc Natl Acad Sci USA 88: 1913–1917, 1991PubMedCrossRefGoogle Scholar
  20. 20.
    Droge W, Breitkreutz R: Glutathione and immune function. Proc Nutr Soc 59: 595–600, 2000PubMedGoogle Scholar
  21. 21.
    Stokes AH, Lewis DY, Lash LH, Jerome WG, Grant KW, Aschner M, Vrana KE: Dopamine toxicity in neuroblastoma cells: role of glutathione depletion by L-BSO and apoptosis. Brain Res 858: 1–8, 2000PubMedCrossRefGoogle Scholar
  22. 22.
    Brigelius R: Regulation of glucose-6-phosphate dehydrogenase under oxidative stress. In: G. Rotho (eds). Superoxide and superoxide dismutase in chemistry, biology and medicine, Elsevier Science Publishers, BV, 1986, pp. 401–403Google Scholar

Copyright information

© Springer Science + Business Media, Inc. 2006

Authors and Affiliations

  • Shukkur Muhammed Farooq
    • 1
  • Abdul Shukkur Ebrahim
    • 2
  • Karthik Harve Subramhanya
    • 3
  • Ramasamy Sakthivel
    • 1
  • Nachiappa Ganesh Rajesh
    • 4
  • Palaninathan Varalakshmi
    • 1
    Email author
  1. 1.Department of Medical Biochemistry, Dr. A.L.M. Postgraduate Institute of Basic Medical, SciencesUniversity of MadrasChennaiIndia
  2. 2.Lab for Neurogenetics, BSI, RIKENSaitamaJapan
  3. 3.Division of BioengineeringNUSKent RidgeSingapore
  4. 4.Department of Pathology, Dr. A.L.M. Postgraduate Institute of Basic Medical SciencesUniversity of MadrasChennaiIndia

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