Publications by authors named "F Jourd'Heuil"
Transient early endosome (EE)-mitochondria interactions can mediate mitochondrial iron translocation, but the associated mechanisms are still elusive. We showed that Divalent Metal Transporter 1 (DMT1) sustains mitochondrial iron translocation via EE-mitochondria interactions in triple-negative MDA-MB-231, but not in luminal A T47D breast cancer cells. DMT1 silencing increases labile iron pool (LIP) levels and activates PINK1/Parkin-dependent mitophagy in MDA-MB-231 cells.
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- Identifying new regulators of vascular smooth muscle cell function is key to understanding cardiovascular diseases; the study focuses on cytoglobin, a hemoglobin-like protein with unique roles in blood vessel health.
- Research found that when cytoglobin was deleted in mice, there was a quicker loss of contractile genes and increased DNA damage in injured carotid arteries.
- The study revealed that cytoglobin moves into the nucleus of vascular smooth muscle cells, where it interacts with a chromatin protein called HMGB2, potentially regulating gene expression and protecting against DNA damage.
Article Synopsis
- Identifying new regulators of vascular smooth muscle cell function is crucial for understanding cardiovascular diseases, and cytoglobin has been found to play important roles in this area.
- Studies show that when cytoglobin is deleted, it leads to quicker loss of contractile genes and increased DNA damage in injured carotid arteries.
- The research reveals that cytoglobin moves into the nucleus of vascular smooth muscle cells, interacting with the protein HMGB2 to help prevent DNA damage and regulate gene activity in the vascular system.
The oxidant hydrogen peroxide serves as a signaling molecule that alters many aspects of cardiovascular functions. Recent studies suggest that cytoglobin - a hemoglobin expressed in the vasculature - may promote electron transfer reactions with proposed functions in hydrogen peroxide decomposition. Here, we determined the extent to which cytoglobin regulates intracellular hydrogen peroxide and established mechanisms.
View Article and Find Full Text PDFCytoglobin 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.
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