Ask about this productRelated genes to: BLVRB Blocking Peptide
- Gene:
- BLVRB NIH gene
- Name:
- biliverdin reductase B
- Previous symbol:
- FLR
- Synonyms:
- SDR43U1
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-04-13
- Date modifiied:
- 2016-10-05
Related products to: BLVRB Blocking Peptide
Related articles to: BLVRB Blocking Peptide
- 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. - Source: PubMed
Publication date: 2026/06/01
Issaian Aaron VaheDzieciatkowska MonikaBevers ShaunSafari ZohrehHay Ariel MCendali Francesca IArgabright AmyRogers Stephen CSaviola Anthony JRedzic Jasmina SWartchow EricReisz Haines JulieKeele Gregory RHaiman Zachary BNemkov TravisStephenson DanielLisk ChristinaVallese FrancescaPalsson Bernhard OKing S BrucePage Grier PDoctor AllanHudson Krystalyn EHansen Kirk CIrwin David CMohandas NarlaZimring James CEisenmesser Elan ZD'Alessandro Angelo - This study aimed to characterize systemic molecular signatures in the serum of patients with age-related cataracts and explore specific variations through integrated proteomic and metabolomic profiling. - Source: PubMed
Publication date: 2026/01/12
Chen SilongGuo JiaruiRong JieFu QiuliYao KeZhou ZheminYu Yibo - Flavin reductase (FR), also known as Biliverdin IXβ Reductase (BLVRB), is a monomeric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) protein family, characterized by its NADPH-dependent catalytic conversion of biliverdin to bilirubin, a key antioxidant in fetal heme catabolism and cellular defense. Structurally, BLVRB features a Rossmann-fold domain with dynamic loop regions (Loop80 and Loop120) and coenzyme clamps (Arg14, Arg78) critical for substrate and cofactor binding. Under hyperglycemic conditions, BLVRB undergoes glycation by methylglyoxal (MG), further enhancing the diabetic complications due to advanced glycation end-products (AGEs) production. Here, molecular dynamics simulations were employed to examine glycation-induced structural changes. Results reveal a transition from open to closed loop conformations, tighter Thr12-Arg78 clamp association, narrowed NADPH binding pocket, reduced solvent accessibility, and altered interhelical orientations. Principal Component Analysis (PCA) and Free Energy Landscape (FEL) analyses confirmed significant shifts in conformational space and stability. These findings suggest glycation disrupts BLVRB dynamics, potentially impairing activity and its antioxidant function. - Source: PubMed
Publication date: 2026/05/03
Jeevanandam JayanthEsackimuthu PBhuvana KRuupha Shree A SHarshini V RRaghavendran SrikanthSaraswathi N T - Type 2 diabetes mellitus (T2DM) is a prevalent metabolic disorder, and identifying robust biomarkers is crucial for improving diagnosis and understanding its pathogenesis. - Source: PubMed
Publication date: 2026/03/10
Cui FangqinLi LiHu MingjiLi BaoDu BangFang QingqingHuang DakeZhang Xiaonan - BACKGROUND: Understanding the pathophysiology of unstable atherosclerosis is imperative to prevent myocardial infarction and stroke. Here, we used multi-omics integration to identify key molecular targets with diagnostic and therapeutic potential. METHODS: Biobank of Karolinska Endarterectomies encompassing patients with symptomatic (S) and asymptomatic (AS) carotid atherosclerosis was the main resource. Plaques, peripheral blood monocytes and plasma sampled locally from around plaque or periphery of n > 700 individuals, were profiled by transcriptomics, proteomics and metabolomics. A supervised machine learning method DIABLO was used for patient data integration. Multi-omics layers were integrated separately across local and peripheral disease sites, and their intersection, with stratification for symptomatology. Identified analytes were investigated using scRNAseq, clinical and outcome data. RESULTS: In peripheral circulation, FABP4, IL6, Bilirubin and Sphingomyelin were the most prominent analytes. F11, ANGPTL3, ICOSLG, ITGB1 and Sphingomyelin were enriched in the local disease site, while FABP4, C1R, IL6, Bilirubin and Sphingomyelin appeared at the intersection. Coagulation, necroptosis, inflammation and cholesterol metabolism were confirmed as key pathways determining symptomatology. Clinical analyses showed an impact of lipid-lowering therapy on ICOSLG expression, anti-hypertensives on plasma FABP4 and BLVRB levels, anti-diabetics on plasma Sphingomyelins, while no medications affected ANGPTL3. Association with future adverse events was shown for plasma Bilirubin, Sphingomyelin, ANGPTL3 and ICOSLG plaque levels. Open-source target analyses suggested genetic involvement of F11, C1S, EGFR, IL6, ANGPTL3 in the disease. CONCLUSIONS: Using an innovative, multi-modal data integration machine learning framework, this study provides confirmatory and novel information on mechanisms behind atherosclerotic instability. The findings raise possibilities for translational prioritizations to aid personalized medicine. - Source: PubMed
Publication date: 2026/02/06
Das VivekNarayanan SampathZhang XiangBergman OttoDjordjevic DjordjeKronqvist MalinChemaly MelodyKaradimou GlykeriaSundman SofijaPrasad InikaBuckler Andrew JKnape Karin CondeMichaelsen Natasha BarascukHedin UlfMatic Ljubica