Analysis of Glycosylation Profiles of Serum Glycoprotein from Iron Overload Thalassemia.

BACKGROUND

The aim of this study was to use a lectin microarray to detect differential glycan profiling of serous glycoprotein in iron overload thalassemia patients.

METHODS

This study enrolled iron overload α/β-thalassemia patients and no iron overload α/β-thalassemia patients. Lectin microarray was used to detect the alteration of protein glycosylation. The reliability of the lectin microarray results was verified by the lectin blotting technique. Expression level of hepcidin, erythropoietin, ferritin, and transferrin were measured by western blotting. Data were analyzed using the SPSS 16.0 software.

RESULTS

In this study, 19 differentiating lectins were screened from the iron overload α-thalassemia group, and 15 were screened from the iron overload β-thalassemia group. The agglutinin blotting technique demonstrated that the results of the Aleuria aurantia lectin (AAL), Lens culinaris agglutinin (LCA), and Wheat germ agglutinin (WGA) agglutinin affinity for serum glycoproteins were consistent with the results of the lectin microarray. In iron overload thalassemia groups, expression levels of erythropoietin and ferritin were increased, but hepcidin and transferrin were significantly reduced.

CONCLUSIONS

The differentially expressed glycoprotein database of iron overload thalassemia was successfully created, and the specific glycan patterns of serous glycoprotein might be efficient biomarkers for diagnosis or progression of iron overload thalassemia.