Partial Purification of a Serum Ferroportin and Evaluation of its Pharmacological Modulation: Implications for Hemodialysis Patients

Ferroportin (FPN1), encoded by the SLC40A1 gene, is the only known mammalian cellular iron exporter and plays a pivotal role in systemic iron regulation. In the present study, a protein suspected to be ferroportin (FPN1) was isolated and partially purified from healthy human serum using a sequential protocol involving ammonium sulfate precipitation (0–65%), dialysis, and gel filtration chromatography on Sephadex G-100. The purification process led to a substantial increase in specific activity, reaching 193.65 ng/mg protein after gel filtration, corresponding to a 21.3-fold purification relative to crude serum, with an overall recovery of 47.91%. The molecular weight of the isolated protein was estimated at approximately 64.6 ± 1 kDa, consistent with previously reported values for human ferroportin. The modulatory effects of selected medications on this suspected serum ferroportin were examined. The tested agents demonstrated divergent outcomes, ranging from strong activation to marked inhibition. Isosorbide dinitrate (+61.89%), darbepoetin alfa (+45.08%), and ascorbic acid (+35.71%) significantly increased protein activity, whereas doxycycline (–58.33%), heparin (–55.69%), and atorvastatin (–42.58%) strongly suppressed it. These findings suggest potential drug–protein interactions that may influence iron metabolism in clinical contexts. However, further confirmatory analyses, such as Western blotting or mass spectrometry, are required to definitively identify the isolated protein as FPN1. Such insights may inform future therapeutic strategies aimed at optimizing iron metabolism and alleviating anemia in patients with chronic kidney disease and those undergoing hemodialysis.