MassIVE MSV000080394

Partial Public PXD005560

Identification of oxidative modifications of hemopexin and their physiological relevance

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Description

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

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Principal Investigators:
(in alphabetical order) 		Dr. Ann Smith
Submitting User: smithan
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