{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_SDA_Crosslinks.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_DSSO_Crosslinks.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_SDA.mzML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_DSSO.mzML"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_SDA.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/AIssaian_NorHyp_RBC_NO_xLinks_TMT16_DSSO.mzid"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/NorHyp_RBC_NO_xLinks_timsTOFwithFusion_Fasta_Gen4.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072059/Fusion_20250625_AIssaian_NorHyp_RBC_NO_xLinks_Frac17.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["angelo.dalessandro@cuanschutz.edu"],"submitter":["Shaun Bevers"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"disease":["Disease Free"],"software":[""],"submitter_keywords":["Red blood cells","Nitric oxide","Erythrocytes","Hyponia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072059"],"tissue":["Erythrocyte","Blood"],"sample_protocol":["RBCs were lysed in a hypotonic buffer for 1 hour on ice and diluted into crosslinking buffer (20 mM HEPES pH 7.5, 50 mM NaCl, 1X protease inhibitor cocktail) at a concentration of 2 mg/mL. Recombinant Band3 (1-56AA) was added to the prepared lysate at a concentration of 1 mg/mL. Completed lysate was transferred to an anaerobic chamber (5% H2, 20% CO2, and 75% N2) for 24-hour gas exchange. The following morning, an aliquot of lysate for normoxia was taken out of the anaerobic chamber and allowed exchange with oxygen for 30 minutes. Lysates in hypoxia and normoxia were split into five replicates and subsequently crosslinked with either 1 mM DSSO or 10 mM DMTMM for 1 hour. The reaction was quenched with the addition of 20 mM Tris. Samples were reduced and alkylated for 45 minutes with DTT (10 mM) and IAA (20 mM), respectively. Samples were precipitated by acetone overnight at -80 °C. Precipitated protein was centrifuged at 21,000 g and dried by speedvac. Samples were resuspended into digestion buffer (50 mM TEAB pH 8.0), and rAsp-N (Promega) and Chymotrypsin (Promega) were added at a ratio of 1:50 for overnight digestion at 37 °C. Digested peptides were labeled with TMT10plex reagent following the manufacturer’s protocol (ThermoFisher Scientific). Labeled peptides were dried down by speedvac and resuspended into high-pH reversed-phase buffer (10 mM NH4OH). Peptides were separated by high-pH reversed-phase chromatography and fractions were pooled dried down by speedvac. Fractions were desalted by C18 Spin Tips (Pierce) and analyzed by nanoLC-MS/MS on an Orbitrap Fusion Lumos (ThermoFisher Scientific) mass spectrometer."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Crosslinked peptides were identified using the XlinkX search node in Proteome Discoverer 2.5, and relative abundances were measured by TMT reporter ion intensities"],"omics_type":["Proteomics"],"labhead":["Angelo D'Alessandro"],"instrument_platform":[""],"labhead_affiliation":["University of Colorado - Anschutz Medical Campus Department of Biochemistry and Molecular Genetics"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"publication":["42224377 Issaian AV, Dzieciatkowska M, Bevers S, Safari Z, Hay AM, Cendali FI, Argabright A, Rogers SC, Saviola AJ, Redzic JS, Wartchow E, Reisz Haines J, Keele GR, Haiman ZB, Nemkov T, Stephenson D, Lisk C, Vallese F, Palsson BO, King SB, Page GP, Doctor A, Hudson KE, Hansen KC, Irwin DC, Mohandas N, Zimring JC, Eisenmesser EZ, D'Alessandro A. The red blood cell proteome and interactome identify a Band 3-BLVRB axis regulating hypoxic metabolic adaptation. Blood. 2026:blood.2025032915 10.1182/blood.2025032915"],"submitter_mail":["shaun.bevers@cuanschutz.edu"],"submitter_affiliation":["University of Colorado - Anschutz Medical Campus"],"submitter_country":["United States"],"doi":["10.6019/PXD072059"],"pubmed_abstract":["Red blood cells (RBCs) are transcriptionally silent yet dynamically remodel metabolism in response to oxygen tension. Using ultra-pure human RBCs, we generated the deepest contamination-free proteome to date (3,775 proteins) and mapped the oxygen-dependent interactome. These datasets reveal an oxygen-responsive metabolon centered on the Band 3 (SLC4A1) N-terminus. We identify biliverdin reductase B (BLVRB) as a previously unrecognized Band 3 interactor that dissociates under hypoxia, coincident with increased Band 3-deoxyhemoglobin contacts. This reversible assembly functions as an oxygen-sensitive switch coordinating redox and glycolytic remodeling. Humanized mice lacking Band 3 N-terminal segments exhibit impaired oxygen-dependent regulation of BLVRB binding to band 3, impaired hypoxic activation of glycolysis, reduced 2,3-bisphosphoglycerate synthesis, and diminished exercise tolerance, demonstrating physiological relevance. Population-scale cis-pQTLs for SLC4A1 and BLVRB suggest functions beyond canonical heme catabolism. Mechanistically, biochemical analyses in vitro suggest that hemoglobin β (HBB), Band 3, and BLVRB can undergo S-nitrosation and may participate in trans-nitrosation reactions with the glycolytic enzyme GAPDH, whose modification at C152 inhibits enzymatic activity in vitro. Collectively, these findings define a Band 3-BLVRB axis that integrates oxygen-dependent protein interactions with thiol-based redox chemistry, providing a framework for understanding how an anucleate cell achieves metabolic adaptability through reversible protein-protein interactions and post-translational modification. These findings suggest that perturbation of the Band 3-BLVRB axis may influence oxygen delivery and metabolic flexibility during hypoxic stress, with potential relevance to high-altitude adaptation, exercise physiology, and cardiopulmonary disease."],"pubmed_title":["The red blood cell proteome and interactome identify a Band 3-BLVRB axis regulating hypoxic metabolic adaptation."],"pubmed_authors":["Issaian Aaron Vahe AV, Dzieciatkowska Monika M, Bevers Shaun S, Safari Zohreh Z, Hay Ariel M AM, Cendali Francesca I FI, Argabright Amy A, Rogers Stephen C SC, Saviola Anthony J AJ, Redzic Jasmina S JS, Wartchow Eric E, Reisz Haines Julie J, Keele Gregory R GR, Haiman Zachary B ZB, Nemkov Travis T, Stephenson Daniel D, Lisk Christina C, Vallese Francesca F, Palsson Bernhard O BO, King S Bruce SB, Page Grier P GP, Doctor Allan A, Hudson Krystalyn E KE, Hansen Kirk C KC, Irwin David C DC, Mohandas Narla N, Zimring James C JC, Eisenmesser Elan Z EZ, D'Alessandro Angelo A"],"additional_accession":[]},"is_claimable":false,"name":"Deep Red Blood Cell Proteome Defines the Band 3 N-Terminus Interactome as a Regulator of Hypoxic Adaptation via BLVRB-Dependent S-Nitroso Transfer","description":"Red blood cells (RBCs) are transcriptionally silent yet dynamically remodel metabolism in response to oxygen tension. Using ultra-pure human RBCs, we generated the deepest contamination-free proteome to date (3,775 proteins) and mapped the oxygen-dependent interactome. These datasets reveal an oxygen-responsive metabolon centered on the Band 3 (SLC4A1) N-terminus. We identify biliverdin reductase B (BLVRB) as a previously unrecognized Band 3 interactor that dissociates under hypoxia, coincident with increased Band 3–deoxyhemoglobin contacts. This reversible assembly functions as an oxygen-sensitive switch coordinating redox and glycolytic remodeling. Humanized mice lacking Band 3 N-terminal segments exhibit impaired glycolytic activation, reduced 2,3-bisphosphoglycerate synthesis, and diminished exercise tolerance, demonstrating physiological relevance. Population-scale cis-pQTLs for SLC4A1 and BLVRB suggest functions beyond canonical heme catabolism. Mechanistically, BLVRB serves as a nitric-oxide relay that trans-nitrosates the glycolytic enzyme GAPDH at C152, transiently inhibiting glycolysis. Together, these findings define a Band 3–BLVRB–hemoglobin axis integrating oxygen sensing and metabolic 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