This research provides novel insights into the underlying mechanism whereby the cyto- and neuro-protective heme binding protein hemopexin can be inactivated by reactive nitrogen species generated during the heme- and cytokine- driven inflammation that accompanies hemolysis. Nitration of amino acids is generally considered a selective and specific effect reflecting biological events. As we describe in a summary in the next paragraph, three tyrosine resides are preferentially targeted that reside in the heme binding site of apo-hemopexin. Hemopexin deficiency states develop in clinical sepsis and such modifications of hemopexin that we have identified and describe could also provide evidence-based guidance to physicians when heme toxicity is driving pathology to assess the timing and extent of hemopexin replenishment therapies and the patient responses to such treatment.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: hemopexin ; tyrosine nitration ; mass spectrometry ; proteomics ; reactive oxygen species ; covalent modification ; reactive nitrogen species
Principal Investigators: (in alphabetical order) |
Dr. Ann Smith |
Submitting User: | smithan |
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Owner | Reanalyses | |
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