Results 21 to 30 of about 118,565,731 (151)
Biliverdin reductase A is a major determinant of protective NRF2 signaling
Biliverdin reductase A (BVRA), the terminal enzyme in heme catabolism, generates the neuroprotective and lipophilic antioxidant bilirubin. Here, we identify a nonenzymatic role for BVRA in redox regulation. Through phylogenetic, genetic, biochemical, and enzymatic assays, we found that BVRA exerts critical nonenzymatic antioxidant activity ...
Chirag Vasavda +21 more
openaire +4 more sources
Cycling the Wagons for Biliverdin Reductase [PDF]
This letter was prompted by our reading of the article by Maghzal et al. (1). Bilirubin (BR) is a major physiologic antioxidant cytoprotectant. Tissue levels are only in nanomolar concentrations, because high levels are neurotoxic, yet BR protects against micromolar levels of oxidants because of a cycle wherein biliverdin (BV) generated by BR ...
Thomas W, Sedlak, Solomon H, Snyder
openaire +2 more sources
Biliverdin reductase: A major physiologic cytoprotectant [PDF]
Bilirubin, an abundant pigment that causes jaundice, has long lacked any clear physiologic role. It arises from enzymatic reduction by biliverdin reductase of biliverdin, a product of heme oxygenase activity. Bilirubin is a potent antioxidant that we show can protect cells from a 10,000-fold excess of H 2
David E, Baranano +3 more
openaire +2 more sources
Background Sickle cell disease, a genetic red cell disorder inherited in an autosomal recessive manner, occurs throughout the world. Hepatic dysfunction and liver damage may be present in sickle cell disease, but the pathogenesis of these conditions is ...
Angela Siciliano +10 more
doaj +1 more source
The Role of Bilirubin and the Other “Yellow Players” in Neurodegenerative Diseases
Bilirubin is a yellow endogenous derivate of the heme catabolism. Since the 1980s, it has been recognized as one of the most potent antioxidants in nature, able to counteract 10,000× higher intracellular concentrations of H2O2.
Sri Jayanti +3 more
doaj +1 more source
The Nuclear Translocation of Heme Oxygenase-1 in Human Diseases
Heme oxygenase-1 (HO-1) is a rate-limiting enzyme in the degradation of heme to generate carbon monoxide (CO), free iron and biliverdin, which could then be converted to bilirubin by biliverdin reductase.
Qing Yang, Wenqian Wang
doaj +1 more source
Heme oxygenase-1 deficiency presenting with interstitial lung disease and hemophagocytic flares
Background Heme oxygenase-1 (HMOX1) catalyzes the metabolism of heme into carbon monoxide, ferrous iron, and biliverdin. Through biliverdin reductase, biliverdin becomes bilirubin.
Alice S. Chau +8 more
doaj +1 more source
Biliverdin and bilirubin are breakdown products of normal heme catabolism, caused by the body's clearance of aged red blood cells which contain hemoglobin.
Sandra Barca +2 more
doaj +1 more source
Zika virus (ZIKV) has emerged as a global health issue, yet neither antiviral therapy nor a vaccine are available. ZIKV is an enveloped RNA virus, replicating in the cytoplasm in close association with ER membranes.
Solène Denolly +8 more
doaj +1 more source
The expanse of human biliverdin reductase (hBVR) functions in the cells is arguably umatched by any single protein. hBVR is a Ser/Thr/Tyr kinase, a scaffold protein, a transcription factor and an intracellular transporter of gene regulators.
Peter E.M. Gibbs +2 more
doaj +1 more source

