Emerging perspectives on cytoglobin, beyond NO dioxygenase and peroxidase.
Cancer
Cardiovascular disease
Cytoglobin
Fibrosis
Hemoglobin
Hydrogen peroxide
Hypoxia
Myoglobin
Nitric oxide
Oxidative stress
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
15
01
2020
revised:
05
02
2020
accepted:
13
02
2020
pubmed:
23
2
2020
medline:
22
6
2021
entrez:
23
2
2020
Statut:
ppublish
Résumé
Cytoglobin is an evolutionary ancient hemoglobin with poor functional annotation. Rather than constrained to penta coordination, cytoglobin's heme iron may exist either as a penta or hexacoordinated arrangement when exposed to different intracellular environments. Two cysteine residues at the surface of the protein form an intramolecular disulfide bond that regulates iron coordination, ligand binding, and peroxidase activity. Overall, biochemical results do not support a role for cytoglobin as a direct antioxidant enzyme that scavenges hydrogen peroxide because the rate of the reaction of cytoglobin with hydrogen peroxide is several orders of magnitude slower than metal and thiol-based peroxidases. Thus, alternative substrates such as fatty acids have been suggested and regulation of nitric oxide bioavailability through nitric oxide dioxygenase and nitrite reductase activities has received experimental support. Cytoglobin is broadly expressed in connective, muscle, and nervous tissues. Rational for differential cellular distribution is poorly understood but inducibility in response to hypoxia is one of the most established features of cytoglobin expression with regulation through the transcription factor hypoxia-inducible factor (HIF). Phenotypic characterization of cytoglobin deletion in the mouse have indicated broad changes that include a heightened inflammatory response and fibrosis, increase tumor burden, cardiovascular dysfunction, and hallmarks of senescence. Some of these changes might be reversed upon inhibition of nitric oxide synthase. However, subcellular and molecular interactions have been seldom characterized. In addition, specific molecular mechanisms of action are still lacking. We speculate that cytoglobin functionality will extend beyond nitric oxide handling and will have to encompass indirect regulatory antioxidant and redox sensing functions.
Identifiants
pubmed: 32087552
pii: S2213-2317(20)30086-0
doi: 10.1016/j.redox.2020.101468
pmc: PMC7033357
pii:
doi:
Substances chimiques
Cytoglobin
0
Globins
9004-22-2
Peroxidases
EC 1.11.1.-
Peroxidase
EC 1.11.1.7
Oxygenases
EC 1.13.-
nitric oxide dioxygenase
EC 1.14.13.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
101468Subventions
Organisme : NHLBI NIH HHS
ID : R01 HL142807
Pays : United States
Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest None.
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