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Neuroprotective Roles of the Biliverdin Reductase-A/Bilirubin Axis in the Brain
BiomoleculesBiliverdin reductase-A (BVRA) is a multi-functional enzyme with a multitude of important roles in physiologic redox homeostasis. Classically, BVRA is well known for converting the heme metabolite biliverdin to bilirubin, which is a potent antioxidant in both the periphery and the brain.
Bindu D Paul, Andrew A Pieper
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Biliverdin reductase: a target for cancer therapy? [PDF]
Frontiers in Pharmacology, 2015 Biliverdin reductase (BVR) is a multifunctional protein that is the primary source of the potent antioxidant, bilirubin. BVR regulates activities/functions in the insulin/IGF-1/IRK/PI3K/MAPK pathways. Activation of certain kinases in these pathways is/are hallmark(s) of cancerous cells.
Gibbs, Peter E. M. +2 more
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Direct Antioxidant Properties of Bilirubin and Biliverdin. Is there a Role for Biliverdin Reductase? [PDF]
Frontiers in Pharmacology, 2012 Reactive oxygen species (ROS) and signaling events are involved in the pathogenesis of endothelial dysfunction and represent a major contribution to vascular regulation. Molecular signaling is highly dependent on ROS. But depending on the amount of ROS production it might have toxic or protective effects.
Jansen, Thomas, Daiber, Andreas
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Biliverdin reductase isozymes in metabolism [PDF]
Trends in Endocrinology and Metabolism, 2015 The biliverdin reductase (BVR) isozymes BVRA and BVRB are cell surface membrane receptors with pleiotropic functions. This review compares, for the first time, the structural and functional differences between the isozymes. They reduce biliverdin, a byproduct of heme catabolism, to bilirubin, display kinase activity, and BVRA, but not BVRB, can act as ...
Kezia John, David E Stec, Terry D Hinds
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Go Green: The Anti-Inflammatory Effects of Biliverdin Reductase [PDF]
Frontiers in Pharmacology, 2012 Biliverdin (BV) has emerged as a cytoprotective and important anti-inflammatory molecule. Conversion of BV to bilirubin (BR) is catalyzed by biliverdin reductase (BVR) and is required for the downstream signaling and nuclear localization of BVR.
Wegiel, Barbara, Otterbein, Leo E.
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The use of synthetic linear tetrapyrroles to probe the verdin sites of human biliverdin‐IXα reductase and human biliverdin‐IXβ reductase [PDF]
FEBS Journal, 2009 Many vertebrate species express two enzymes that are capable of catalysing the reduction of various isomers of biliverdin. Biliverdin‐IXα reductase (BVR‐A) is most active with its physiological substrate biliverdin‐IXα, but can also reduce the three other biliverdin isomers IXβ, IXδ and IXγ.
Katsuhiko Inomata +2 more
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EXCLI Journal : Experimental and Clinical Sciences, 2021 Biliverdin reductase, biliverdin and bilirubin are known as important components of cellular signaling pathways that play major roles in cell proliferation and apoptosis, although their physiological relevance is still under evaluation.
Seyedeh Zahra Shahrokhi +2 more
doaj +1 more source
Metabolic Functions of Biliverdin IXβ Reductase in Redox-Regulated Hematopoietic Cell Fate
Antioxidants, 2023 Cytoprotective heme oxygenases derivatize heme to generate carbon monoxide, ferrous iron, and isomeric biliverdins, followed by rapid NAD(P)H-dependent biliverdin reduction to the antioxidant bilirubin.
Wadie F. Bahou +2 more
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Microorganisms, 2023 Oxygenic photosynthesis requires metal-rich cofactors and electron-transfer components that can produce reactive oxygen species (ROS) that are highly toxic to cyanobacterial cells. Biliverdin reductase (BvdR) reduces biliverdin IXα to bilirubin, which is
Wendy M. Schluchter +6 more
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Cycling the Wagons for Biliverdin Reductase [PDF]
Journal of Biological Chemistry, 2009 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
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