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The results obtained in this study (1) show that plasma-produced reactive oxygen and nitrogen species can extensively oxidize proteins and (2) that the oxidation status of two redox-active cysteines lead to different conformations of CYGB.
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Endothelial cells facilitate the ability of smooth muscle cells to metabolize nitric oxide through upregulation of cytoglobin.
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FGF2 initiates CYGB transcription via the JNK pathway.
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the study reveals a novel mechanism for the regulated expression of Cygb and also assigns a new role to Cygb in cell cycle control.
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Data suggest that cytochrome b5 (CYB5) and cytochrome b5 reductase 3 (CYB5R3) can reduce human cytoglobin (CYGB) and zebrafish cytoglobins at rates up to 250-fold higher than those reported for the known physiological substrates, hemoglobin and myoglobin; the three proteins (CYB5+CYB5R3+CYGB) appear to constitute a metabolon involved in generation of nitric oxide.
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DeltaNp63-CYGB axis is also present in lung and breast cancer cell lines, indicating that CYGB-mediated ROS-scavenging activity may also have a role in epithelial tumours
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Propose a bipartite lipid binding model that rationalizes the modes of interactions of cytoglobin with phospholipids, the effects on structural re-arrangements and the peroxidase activity of the hemoprotein.
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This review provides an overview of the proposed role of cytoglobin and explores its potential functional role as a biomarker for cancer and other diseases
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Cygb, expressed in hepatic stellate cells during liver fibrosis, plays role in cancer development with nonalcoholic steatohepatitis.
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Cygb stabilizes p53 by inhibiting its ubiquitination and elicit cell cycle arrest in DNA damaged cells.
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The cysteine redox state of the monomer controls histidine dissociation rate constants and hence extrinsic ligand binding in human cytoglobin.
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The monomeric cytoglobin protein with an internal disulfide bond between the two cysteine residues Cys38 and Cys83, interacts with lipids to induce a change in haem co-ordination.
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Protein multimerization may be a mechanism that triggers physiological functions of human cytoglobin.
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Our data provides evidence that cytoglobin regulates the ovarian cancer cell proliferation and invasion.
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This review outlines the current understanding of Cygb's involvement in tumor hypoxia and discusses its role in tumorigenesis.
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Molecular dynamics studies of four cytoglobinCO models indicated that the distal E7 residue was a crucial influence on the dynamics of cytoglobinCO in terms of loop fluctuations, cavity rearrangement, and slight heme motion.
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Reduction of the internal disulfide bond between Cys 38 and 83 switches the ligand migration pathway in cytoglobin.
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Cytoglobin is expressed in hepatic stellate cells, but not in myofibroblasts, in normal and fibrotic human liver, so it thus a useful marker to distinguish these cells.
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Results show that CYGB revealed Tumor Suppressor Gene properties in normoxia but promoted tumourigenic potential of the cells exposed to stress, suggesting a bimodal function in lung tumourigenesis.
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Ngb and Cygb are expressed in the solitary tract nucleus and in the carotid body, and may have roles in the processing of cardiovascular and respiratory reflex inputs
