Heme- and Hemoglobin Stress in Human Diseases

Dear Colleagues,

The aim of this Special Issue is to promote research concerning the involvement of heme and heme proteins in the pathogenesis of various diseases as well as preventive and therapeutic strategies to minimize damage through associated pathways.

Heme is the principal iron complex in the human body with vital physiological functions and strictly regulated metabolism, responsible for oxygen and electron transport among many other roles. This diverse capability is achieved through the numerous combinations that result from associations of heme with various protein chains.

Under pathological conditions, heme can escape from its safe and functional sanctuaries and interact with cellular domains and tissue constituents, allowing pathophysiologic remodeling. Given the hydrophobic nature of heme, it is no surprise that it easily crosses cell membranes and can synergistically enhance cellular oxidant damage. In addition, through binding, it alters the functions of proteins, lipids, and nucleic acids, affecting signaling pathways, cell differentiation, cell–cell interactions, contractility, etc.

Heme moieties of some heme proteins may react with peroxides, leading to the formation of protein radicals and thereby altering their structures, actions, and functions. Hydrogen sulfide, nitrogen monoxide, and carbon monoxide were shown to have impact on such physiology and pathophysiology.

Of all the sites in the body, the vasculature may be at the greatest risk of harm exhibited by heme and heme proteins, including hemoglobin. Substantial evidence is accumulating regarding the existence of heme and hemoglobin stress as well as adaptation against its damaging effects.

Prof. Dr. József Balla
Guest Editor

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