Heat shock proteins in iron deficiency anemia and β thalassemia minor

Heat shock proteins, found in all eukaryotic and prokaryotic cells, are a group of proteins, has molecular chaperone function. Hypoxia, DNA damage, cytotoxic drugs, cell death signals, toxicity, oxidative stress and absence of growth factors may lead to increased expression of Hsp. In the present study, it was aimed to investigate the levels of Hsp theoretically related with EPO expression and/or secretion and the relationship between hepcidin levels and EPO in the patients with IDA and β-thalassemia minor which both are hypochromic microcytic anemia and healthy group. 84 children with IDA, 20 children with β-thalassemia minor and 45 healthy children matched in terms of age and sex were included to the present study. The levels of Hsp60, Hsp70, Hsp90, EPO and hepcidin were measured by ELISA method. Significant difference was not recorded among three groups in terms of age and gender (p> 0.051). Hsp60 was higher in the IDA group compared to the β-thalassemia minor and control groups. Hsp90 was significantly higher in IDA compared to the control group. EPO was higher in IDA and β-thalassemia minor groups compared to the control group. Hsp70 and hepcidin levels did not differ between patients and control group. It is thought that regulation of Hsp70 and Hsp90 aren't associated with the degree of hypoxia and anemia, they are associated with iron deficiency because Hsp60 and Hsp70 levels are higher independently EPO levels in IDA. Apoptotic properties of Hsp60 can be an effective factor for RBC count difference between two groups of anemia.