ArticleRedox biology2013
Protein disulfide isomerase may facilitate the efflux of nitrite derived S-nitrosothiols from red blood cells.
Article in Redox biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- Protein disulfide isomerase integrates toll-like receptor 4 and P2X7 receptor signaling pathways during lipopolysaccharide-induced neuroinflammation.Scientific reports · 2025Article
- Determination of Nitric Oxide and Its Metabolites in Biological Tissues Using Ozone-Based Chemiluminescence Detection: A State-of-the-Art Review.Antioxidants (Basel, Switzerland) · 2024Review
- PDI augments kainic acid-induced seizure activity and neuronal death by inhibiting PP2A-GluA2-PICK1-mediated AMPA receptor internalization in the mouse hippocampus.Scientific reports · 2023Article
- CDDO-Me Abrogates Aberrant Mitochondrial Elongation in Clasmatodendritic Degeneration by Regulating NF-κB-PDI-Mediated S-Nitrosylation of DRP1.International journal of molecular sciences · 2023Article
- Role of Erythrocytes in Nitric Oxide Metabolism and Paracrine Regulation of Endothelial Function.Antioxidants (Basel, Switzerland) · 2022Review
- The enzymatic function of the honorary enzyme: S-nitrosylation of hemoglobin in physiology and medicine.Molecular aspects of medicine · 2022Review
- Protein Transnitrosylation Signaling Networks Contribute to Inflammaging and Neurodegenerative Disorders.Antioxidants & redox signaling · 2021Review
- Native structure of the RhopH complex, a key determinant of malaria parasite nutrient acquisition.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bacitracin and Rutin Regulate Tissue Factor Production in Inflammatory Monocytes and Acute Myeloid Leukemia Blasts.Cancers · 2021Article
- Red Blood Cell-Mediated S-Nitrosohemoglobin-Dependent Vasodilation: Lessons Learned from a β-Globin Cys93 Knock-In Mouse.Antioxidants & redox signaling · 2021Review
- Essential Role of Hemoglobin βCys93 in Cardiovascular Physiology.Physiology (Bethesda, Md.) · 2020Review
- Protein disulfide isomerase in cardiovascular disease.Experimental & molecular medicine · 2020Review
- Role of Nitric Oxide Carried by Hemoglobin in Cardiovascular Physiology: Developments on a Three-Gas Respiratory Cycle.Circulation research · 2020Review
- Microcirculation dysfunction in endotoxic shock rabbits is associated with impaired S-nitrosohemoglobin-mediated nitric oxide release from red blood cells: a preliminary study.Intensive care medicine experimental · 2019Article
- PDI-mediated S-nitrosylation of DRP1 facilitates DRP1-S616 phosphorylation and mitochondrial fission in CA1 neurons.Cell death & disease · 2018Article
- Conserved Residues LysFrontiers in molecular biosciences · 2018Article
- PDI Knockdown Inhibits Seizure Activity in Acute Seizure and Chronic Epilepsy Rat Models viaFrontiers in cellular neuroscience · 2018Article
- Antagonists of the system L neutral amino acid transporter (LAT) promote endothelial adhesivity of human red blood cells.Thrombosis and haemostasis · 2017Article
- Recent insights into nitrite signaling processes in blood.Biological chemistry · 2017Article
- Pathological Impact of the Interaction of NO and CO with Mitochondria in Critical Care Diseases.Frontiers in medicine · 2017Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerase (PDI) is an abundant protein primarily found in the endoplasmic reticulum and also secreted into the blood by a variety of vascular cells. The evidence obtained here, suggests that PDI could directly participate in the efflux of NO(+) from red blood cells (RBC). PDI was detected both in RBC membranes and in the cytosol. PDI was S-nitrosylated when RBCs were exposed to nitrite under ∼50% oxygen saturation but not under ∼100% oxygen saturation. Furthermore, it was observed that hemoglobin (Hb) could promote PDI S-nitrosylation in the presence of ∼600 nM nitrite. In addition, three lines of evidence were obtained for PDI-Hb interactions: (1) Hb co-immunoprecipitated with PDI; (2) Hb quenched the intrinsic PDI fluorescence in a saturable manner; and (3) Hb-Fe(II)-NO absorption spectrum decreased in a [PDI]-dependent manner. Finally, PDI was detected on the surface RBC under ∼100% oxygen saturation and released as soluble under ∼50% oxygen saturation. The soluble PDI detected under ∼50% oxygen saturation was S-nitrosylated. Based on these data it is proposed that PDI is taken up by RBC and forms a complex with Hb. Hb-Fe(II)-NO that is formed from nitrite reduction under ∼50% O2, then transfers NO(+) to either Hb-Cys β93 or directly to PDI resulting in S-nitroso-PDI which transverses the RBC membrane and attaches to the RBC surface. When RBCs enter tissues the S-nitroso-PDI is released from the RBC-surface into the blood where its NO(+) is transferred into the endothelium thereby inducing vasodilation, suggesting local oxygen-dependent dynamic interplays between nitrite, NO and S-nitrosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.