Genetic Polymorphism of Glutathione-S-Transferase Gene (GSTP1) in Type 2 Diabetes Mellitus Patients in Basra Province/Iraq

Genetic Polymorphism of Glutathione-S-Transferase Gene (GSTP1) in Type 2 Diabetes Mellitus Patients in Basra Province/Iraq

Loading document ...
Page
of
Loading page ...

Author(s)

Author(s): Faizah AW Ahmed, Haneen S Al-bachary

Download Full PDF Read Complete Article

DOI: 10.18483/ijSci.1265 217 669 1-7 Volume 6 - May 2017

Abstract

Glutathione S-transferases (GSTs) are enzymes that included, in a wide range of detoxifying reactions by conjugation of glutathione, to electrophilic material. Polymorphisms in the genes that are responsible for GSTs affect, the function of the GSTs. GSTs play an active role in protection of cell against oxidative stress mechanism. Polymorphisms of GSTP1 at codon 105 amino acids forms GSTP1 important site for bind of hydrophobic electrophiles and the substitution of Ile/Val affect substrate specially catalytic activity of the enzyme and may correlate with reach to different diseases in human like diabetes mellitus type2 disease. Correlation between these polymorphisms and changes in the parameters file of diabetic patients has also been found, therefore, the results vary considerably among the studies. The polymerase chain reaction-restriction fragment length polymorphism was used to study GSTP1genetic polymorphism in 60 T2DM patients and 40 healthy individuals. Our results showed that presence of the GSTP1 heterozygous mutant allele Ile/Val was more common in subjects with T2DM than in the control group (35.00% and 17.50.00%, respectively. Among patients there is an association between GSTP1and the risk of T2MD, both genotypes Ile/Val and Val/Val were more prevalent which result in 2.90 and 2.58 respectively risk towards T2DM .According to Hardy–Weinberg principle there was no deviation appears in the distribution of GSTP1 Alleles. GSTP1 genotypes do not have an effect on blood lipids after infection with diabetes mellitus.

Keywords

GSTP1, Polymorphism, T2DM, Type2 Diabetes Mellitus

References

  1. American Diabetes Association( 2012). Diagnosis and classification of diabetes mellitus, Diabetes Care. 3(7): 64–71.
  2. Amer, M. A., Ghattas, M. H., Abo-Elmatty, D. M., Abou-el-Ela, S.H. (2011). Influence of glutathione S-transferase polymorphisms on type-2 diabetes mellitus risk, Genet Mol. Res. 10(9) : 3722–30
  3. Bid, H. K., Konwar, R. and Saxena, M.( 2010). Association of glutathione S-transferase (GSTM1, T1 and P1) gene polymorphisms with type 2 diabetes mellitus in north Indian population, J. Postgrad Med. 56 (3): 176–181
  4. Board ,P.G.,Webb,G.C., and Coggan,M.(1989).isolation of ACdn Clon and localization of the human glutathion -S transferase 3 genes to chromosome Bands 11q13 and 12q13-14," Ann Hum Genet;53 (3):205-213.
  5. Cowell ,I.G.;Dixon, K.H.; Pemble ,S.E.; Ketter, B.andTaylor, J.B.(1988). The structure of the human glutathione Stransferase pi gene. Biochem J;255:79–83.
  6. Delles, C., Padmanabhan S., Lee, W. K., Miller, W. H.( 2008). Glutathione S-transferase variants and hypertension, J. Hypertens. 26(1): 1343-1352
  7. Hayes, J. D., Flanagan, J. U., Jowsey, I.R. (2005). Glutathione transferases, Annu Rev harmacol Toxicol . 45(5): 51–88.
  8. Harries, L.W.,Stubbins ,M.J.,Forman, D., Howard, G.C.and Wolf C.R.(1997). Identification of genetic polymorphisms at the glutathione S-transferase Pi locus and association with susceptibility to bladder, testicular and prostate cancer. Carcinogenesis.;18(4):641-4
  9. Hengstler, J.G., Arand, M., Herrero, M.E.and Oesch, F.( 1998). Polymorphisms of N-acetyltransferases, glutathione S-transferases, microsomal epoxide hydrolase and sulfotransferases: influence on cancer susceptibility. Eur. PubMed Central 154, 47–85.
  10. Kano, T., Sakai, M.and Muramatsu, M.( 1987). Structure and expression of a human class pi glutathione S-transferase messenger RNA. Cancer Res. 47, 5626–5630.
  11. Oniki, K., Umemoto, Y. and Nagata, R.( 2008). Glutathione S-transferase A1 polymorphism as a risk factor for smoking related type 2 diabetes among Japanese, Toxicol Lett . 178(3): 143-5
  12. Pereira, E. C. S., Ferderbar, M. C., Bertolami, A. A., Faludi, O., Monte, H. T., Xavier, T. V., Pereira, D. S. and Abdalla.( 2008). Biomarkers of oxidative stress and endothelial dysfunction in glucose intolerance and diabetes mellitus, Clin Biochem .41(2): 1454-1460.
  13. Pereira, E. C. S., Ferderbar, M. C., Bertolami, A. A., Faludi, O., Monte, H. T., Xavier, T. V., Pereira, D. S. and Abdalla.( 2008). Biomarkers of oxidative stress and endothelial dysfunction in glucose intolerance and diabetes mellitus, Clin Biochem .41(2): 1454-1460.
  14. Pitocco, D. F., Zaccardi, E., DIistasio, F., Romitelli, S. A., Santini, C., zuppi, G. and Ghirlanda. (2010). Oxidative stress, nitric oxide, and diabetes, Rev Diabet Stud. 7(5): 15-25.
  15. Ramprasath, T., Senthil- Murugan, P., Prabakaran, A. D.,Gomathi, P. and Rathinavel, A. (2011). Potential risk modifications of GSTT1, GSTM1 and GSTP1 (glutathione-S transferase) variants and their association to CAD in patients with type2 diabetes, Biochem. Biophys. Res. Commun.407 (3): 49–53
  16. Turner, R. C., Millns, H. and Neil, H. A. (1998) . Risk factors for coronary artery disease in Non-insulin dependent diabetes mellitus, United kingdom prospective diabetes study. 316(5):82
  17. Watson, M. A., Stewart, R. K., Smith, G. B.,Massey, T. E. and Bell, D. A. (1998).Human glutathione S-transferase P1 polymorphisms: relationship to lung tissue enzyme activity and population frequency distribution. Carcinogenesis (Lond.), 19: 275–280
  18. West, J. C. (2000). Radicals and oxidative stress in diabetes. Diabet. Med. 17(2): 171-180
  19. Yalin, S., Hatungil, R., Tamer, L., Ates, N. A., Dogruer, N., Yildirim ,H., Karakas ,S.and Atik, U . (2007). Glutathione S-transferase gene polymorphisms in Turkish patients with diabetes mellitus, Cell Biochem Funct . 25(2): 509–513
  20. Zimniak, P., Nanduri, B., and Pikula, S. (1994). Naturally occurring human glutathione S-transferase GSTP1-1 isoforms with isoleucine and valine in position 104 differ in enzymic properties, Eur J Biochem . 224 (3): 893–899

Cite this Article:

  • BibTex
  • RIS
  • APA
  • Harvard
  • IEEE
  • MLA
  • Vancouver
  • Chicago

International Journal of Sciences is Open Access Journal.
This article is licensed under a Creative Commons Attribution 4.0 International (CC BY 4.0) License.
Author(s) retain the copyrights of this article, though, publication rights are with Alkhaer Publications.

Search Articles

Issue October 2019

Volume 8, October 2019


Table of Contents


Order Print Copy

World-wide Delivery is FREE

Share this Issue with Friends:


Submit your Paper