Alpha Tocopherol, Bilirubin and Some Liver Enzymes in Sickle Cell Subjects
- February 7, 2019
- Posted by: RSIS
- Category: Microbiology
International Journal of Research and Scientific Innovation (IJRSI) | Volume VI, Issue I, January 2019 | ISSN 2321–2705
Muhammad Y1,*, Maryam Z2, Ahmad MB3, Habeeb A4 and Zainab I.2
1 Department of Chemical Pathology, Rasheed Shekoni Teaching Hospital Dutse, Nigeria
2Department of Microbiology, Faculty of Sciences, Ahmadu Bello University Zaria, Nigeria
3Department of Chemical Pathology, School of Medical Laboratory Science, Bayero University Kano, Nigeria
4Department of Hematology and Blood Transfusion, Rasheed Shekoni Specialist Hospital, Dutse, Nigeria
Abstract: Derangement in liver enzymes and hyperbilirubinemia in Sickle cell disease (SCD) has long been documented, generation of free radicals via Fenton’s reaction results in oxidative stress. The serum levels of alphatocopherol, bilirubin and some liver enzymes were determined in forty-eight subjects (34 SCD and 14 apparently healthy age-sex matched controls). The serum levels of liver enzymes and bilirubin were significantly higher compared to the controls (p<0.005). Serum levels of Malondialdehyde (MDA) was significantly higher in sickle cell patients (p<0.005) than the controls. In conclusion, according to the findings of these results, SCD is associated with oxidative stress and deranged liver physiology. Supplementation and antioxidant and monitoring of liver physiology should be encouraged.
Key Words: Sickle cell disease, Free radicals, Oxidative stress, Bilirubin, Live enzymes
Sickle cell disease (SCD) is a genetic hereditary disorder found in tropical regions; particularly sub Saharan African, India and Middle East with three-quarter of the cases in Africa (Almeida and Roberts 2005). WHO reported an estimate of 2-3% newborns in Nigeria were affected by sickle cell anemia, accounting for 150,000 children every year (Elagouz et al., 2010). Sickle cell anemia is characterized by reduction in amount of erythrocytes and their function in the body (Platt et al., 1994), SCD is caused by point mutation at position six of β- chain of hemoglobin, this results when the hydrophilic glutamic acid is replaced with hydrophobic valine (Platt et al., 1994; Steingberg et al., 1994; Glover et al., 1999). Sickle cell individuals are those that inherited mutated hemoglobin gene from both parent (Azubuike and Nkanginieme, 2007). In a low oxygen tension environment, the replaced valine can bind to a complementary hydrophobic site on a β subunit of another hemoglobin tetramer in a non covalent polymerization process which leads to sickling and decreased elasticity of erythrocytes (Serjean, 1997).