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Cell Biology and Toxicology

, Volume 25, Issue 4, pp 415–424 | Cite as

Effect of oral administration of diphenyl diselenide on antioxidant status, and activity of delta aminolevulinic acid dehydratase and isoforms of lactate dehydrogenase, in streptozotocin-induced diabetic rats

  • I. J. Kade
  • V. C. Borges
  • L. Savegnago
  • E. O. Ibukun
  • G. Zeni
  • C. W. Nogueira
  • J. B. T. Rocha
Article

Abstract

Male albino rats with diabetes induced by the administration of streptozotocin (STZ) (45 mg/kg, i.v.) were treated with oral administration of diphenyl diselenide (DPDS) pre-dissolved in soya bean oil. A significant reduction in blood glucose levels was observed in STZ-induced diabetic rats treated with DPDS compared with an untreated STZ diabetic group. The pharmacological effect of DPDS was accompanied by a marked reduction in the level of glycated proteins, and restoration of the observed decreased levels of vitamin C and reduced glutathione (GSH; in liver and kidney tissues) of STZ-treated rats. DPDS also caused a marked reduction in the high levels of thiobarbituric acid reactive substances (TBARS) observed in STZ-induced diabetic group. Finally, the inhibition of catalase, delta aminolevulinic acid dehydratase (ð-ALA-D) and isoforms of lactate dehydrogenase (LDH) accompanied by hyperglycemia were prevented by DPDS in all tissues examined. Hence, in comparison with our earlier report, the present findings suggests that, irrespective of the route of administration and the delivery vehicle, DPDS can be considered as an anti-diabetic agent due to its anti-hyperglycemic and antioxidant properties.

Keywords

Delta aminolevulinic acid dehydratase Diabetes Diphenyl diselenide Lactate dehydrogenase Streptozotocin 

Abbreviations

STZ

Streptozotocin

DPDS

Diphenyl diselenide

LDH

Lactate dehydrogenase

ð-ALA-D

Delta aminolevulinic acid dehydratase

TBARS

Thiobarbituric acid reactive substance

GSH

Reduced glutathione

DTNB

5,5′-Dithio-bis-(2-nitrobenzoic acid)

AST

Aspartate aminotransferase

ALT

Alanine aminotransferase

MDA

Malondialdhyde

Notes

Acknowledgments

I.J.K. is specifically grateful for the financial support of TWAS and CNPq. I.J.K. is a beneficiary of the TWAS-CNPq postgraduate (doctoral) fellowship program. J.B.T. gratefully acknowledges the financial support of CNPq, FAPERGS, CAPES, CAPES/SAUX and VITAE.

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Copyright information

© Springer Science+Business Media B.V. 2008

Authors and Affiliations

  • I. J. Kade
    • 1
    • 2
  • V. C. Borges
    • 1
  • L. Savegnago
    • 1
  • E. O. Ibukun
    • 2
  • G. Zeni
    • 1
  • C. W. Nogueira
    • 1
  • J. B. T. Rocha
    • 1
  1. 1.Postgraduate Programme in Biochemical Toxicology, Centre for Natural and Exact SciencesFederal University of Santa MariaCamobiBrazil
  2. 2.Department of BiochemistryFederal University of TechnologyAkureNigeria

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