Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease

Reeder, Brandon J.

doi:10.1089/ars.2016.6803

Cited by 30 publications

(21 citation statements)

References 132 publications

(125 reference statements)

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“…Here, we extend this concept by showing that eNOS can reduce globin proteins, including α-globin (bound to AHSP), Cygb, and neuroglobin (data not shown). This finding may have broad implications, considering that the related proteins inducible NOS (iNOS) and neuronal NOS (nNOS) could also modulate the redox states of Cygb and neuroglobin to regulate their functions in various tissues (47).…”

Section: Table 1 Pe Dose Responses For Vasoconstriction Of Isolated mentioning

confidence: 99%

Endothelial cell α-globin and its molecular chaperone α-hemoglobin–stabilizing protein regulate arteriolar contractility

Lechauve

Butcher

Freiwan

et al. 2018

Journal of Clinical Investigation

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Section: Table 1 Pe Dose Responses For Vasoconstriction Of Isolated mentioning

confidence: 99%

Endothelial cell α-globin and its molecular chaperone α-hemoglobin–stabilizing protein regulate arteriolar contractility

Lechauve

Butcher

Freiwan

et al. 2018

Journal of Clinical Investigation

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“…Pseudo-peroxidases are different in terms of their heme and activity characteristics, but all of them have one common feature: exposure to H 2 O 2 causes immediate oxidation of protein amino acids that are close to the active center (most commonly tyrosine, tryptophan, or histidine) [ 62 , 63 ]. Compound I was not detected for pseudo-peroxidases.…”

Section: Diversity Of Human Hemoproteins With Peroxidase Activitymentioning

confidence: 99%

“…Under some pathological conditions, particularly as a result of microangiopathic hemolytic anemia, concentrations of Hb in plasma can reach micromolar levels [ 149 ]. Under uncontrolled pathological conditions accompanied by inflammation and oxidative stress, depletion of antioxidants and generation of superoxide radicals by activated neutrophils induce the redox activity of the hemoproteins, resulting in damage to plasma proteins and lipids [ 62 ]. The globin-based free radicals of ferryl hemoglobin were detected in normal human blood upon H 2 O 2 treatment [ 150 ].…”

Section: Hemoglobin and Myoglobinmentioning

confidence: 99%

Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control

Vlasova

2018

Molecules

110

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The heme in the active center of peroxidases reacts with hydrogen peroxide to form highly reactive intermediates, which then oxidize simple substances called peroxidase substrates. Human peroxidases can be divided into two groups: (1) True peroxidases are enzymes whose main function is to generate free radicals in the peroxidase cycle and (pseudo)hypohalous acids in the halogenation cycle. The major true peroxidases are myeloperoxidase, eosinophil peroxidase and lactoperoxidase. (2) Pseudo-peroxidases perform various important functions in the body, but under the influence of external conditions they can display peroxidase-like activity. As oxidative intermediates, these peroxidases produce not only active heme compounds, but also protein-based tyrosyl radicals. Hemoglobin, myoglobin, cytochrome c/cardiolipin complexes and cytoglobin are considered as pseudo-peroxidases. Рeroxidases play an important role in innate immunity and in a number of physiologically important processes like apoptosis and cell signaling. Unfavorable excessive peroxidase activity is implicated in oxidative damage of cells and tissues, thereby initiating the variety of human diseases. Hence, regulation of peroxidase activity is of considerable importance. Since peroxidases differ in structure, properties and location, the mechanisms controlling peroxidase activity and the biological effects of peroxidase products are specific for each hemoprotein. This review summarizes the knowledge about the properties, activities, regulations and biological effects of true and pseudo-peroxidases in order to better understand the mechanisms underlying beneficial and adverse effects of this class of enzymes.

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“…It is a dynamic mediator in the maintenance of redox homeostasis and performs the activities of peroxidase and nitric oxide dioxygenase (NOD), which catalyzes nitric oxide (NO) or nitrite to nitrate in rat hepatocytes. [11][12][13][14] Emerging evidences indicated that Cygb is negatively associated with liver fibrosis and HCC tumorigenesis via regulating oxidative stress pathways. [15][16][17][18][19] Cygb absence accounts for a high incidence of multiple malignancies including liver, lung and colon cancer and lymphoma in aged Cygb −/− mice, compared with wide-type mice.…”

Section: The Interaction Of Ons Withmentioning

confidence: 99%

“…Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin. It is a dynamic mediator in the maintenance of redox homeostasis and performs the activities of peroxidase and nitric oxide dioxygenase (NOD), which catalyzes nitric oxide (NO) or nitrite to nitrate in rat hepatocytes . Emerging evidences indicated that Cygb is negatively associated with liver fibrosis and HCC tumorigenesis via regulating oxidative stress pathways .…”

Section: Introductionmentioning

confidence: 99%

Cytoglobin ameliorates the stemness of hepatocellular carcinoma via coupling oxidative‐nitrosative stress signals

Zhang

Pei

Yang

et al. 2018

Molecular Carcinogenesis

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Cancer stem cells (CSCs) account for tumor self‐renewal and heterogeneity. Oxidative‐nitrosative stress (ONS) is an independent etiologic factor throughout tumorigenesis. Emerging evidences indicated that the interaction of ONS with CSCs contributes to tumor progression and resistance to chemoradiotherapy. Cytoglobin (Cygb) is a member of human hexacoordinate hemoglobin family and acts as a dynamic mediator of redox homeostasis. We observed that Cygb is significantly deregulated in human hepatocellular carcinoma (HCC) tissue and its decrease aggravates the growth of liver cancer stem cells (LCSCs) and increases the subpopulation of CD133(+) LCSCs. Cygb restoration inhibits HCC proliferation and LCSC growth, and decreases the subpopulation of CD133 (+) LCSCs in vitro. We found that Cygb absence promotes LCSC phenotypes and PI3 K/AKT activation, whereas Cygb restoration inhibits LCSC phenotypes and PI3 K/AKT activation. Furthermore, exogenous antioxidants can eliminate the inhibitory effect of Cygb to LCSC growth and phenotypes, as well as PI3 K/AKT activation. Collectively, this study demonstrated that cytoglobin functions as a tumor suppressor and targets CSCs at an ONS‐dependent manner. Thus, Cygb restoration could be a novel and promising therapeutic strategy against HCC with aberrant ROS/RNS accumulation.

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Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease

Abstract: Significance: Erythrocyte hemoglobin and myocyte myoglobin, although primarily oxygen carrying proteins, have the capacity to do redox chemistry.

Cited by 30 publications

References 132 publications

Endothelial cell α-globin and its molecular chaperone α-hemoglobin–stabilizing protein regulate arteriolar contractility

Endothelial cell α-globin and its molecular chaperone α-hemoglobin–stabilizing protein regulate arteriolar contractility

Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control

Cytoglobin ameliorates the stemness of hepatocellular carcinoma via coupling oxidative‐nitrosative stress signals

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