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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Biliverdin reductase A

biliverdin reductase
catalyzes the conversion of biliverdin to bilirubin in heme degradation [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, ACID, HO-2, fibrillin-1, V1a
Papers on biliverdin reductase
Translational Significance of Heme Oxygenase in Obesity and Metabolic Syndrome.
Drummond et al., Valhalla, United States. In Trends Pharmacol Sci, Jan 2016
This review reflects the dramatic increase in research on the role of increased expression of heme oxygenase (HO)-1/HO-2, biliverdin reductase, and HO activity on vascular disease.
An Integrated Clinico-transcriptomic Approach Identifies a Central Role of the Heme Degradation Pathway for Septic Complications after Trauma.
Wanner et al., Jena, Germany. In Ann Surg, Jan 2016
Using quantitative RT-PCR analyses (validation set), the key components haptoglobin (HP), cluster of differentiation (CD) 163, heme oxygenase-1 (HMOX1), and biliverdin reductase A (BLVRA) showed robust changes following trauma.
MiR-127-5p targets the biliverdin reductase B/NF-κB pathway to suppress cell growth in hepatocellular carcinoma cells.
He et al., Shanghai, China. In Cancer Sci, Jan 2016
miR-127-5p inhibited the growth and colony formation of hepatocellular carcinoma (HCC) cells and decreased biliverdin reductase B (BLVRB) expression by directly binding to its 3'-UTR.
Impairment of biliverdin reductase-A promotes brain insulin resistance in Alzheimer disease: A new paradigm.
Perluigi et al., Roma, Italy. In Free Radic Biol Med, Jan 2016
Biliverdin reductase-A (BVR-A) emerged as a unique Ser/Thr/Tyr kinase directly involved in the insulin signaling and represents an up-stream regulator of the insulin signaling cascade.
Extract of Ziziphus jujuba Fruit (Jujube) Stimulates Expression of Enzymes Responsible for Heme Recycle via Anti-oxidant Response Element in Cultured Murine Macrophages.
Tsim et al., Shenzhen, China. In Phytother Res, Jan 2016
To study the beneficial role of jujube in heme iron recycling during erythrophagocytosis, the expression of heme oxygenase-1 (HO-1), biliverdin reductase A and B, and ferroportin were determined in jujube-treated cultured RAW 264.7 macrophages.
Evidences of Biological Functions of Biliverdin Reductase A in the Bovine Epididymis.
Sullivan et al., Québec, Canada. In J Cell Physiol, Oct 2015
We identified biliverdin reductase A (BLVRA) as a partner of ELSPBP1 by immunoprecipitation followed by tandem mass spectrometry.
The acute impact of polyphenols from Hibiscus sabdariffa in metabolic homeostasis: an approach combining metabolomics and gene-expression analyses.
Joven et al., Reus, Spain. In Food Funct, Sep 2015
Among other effects, the activation of the heme oxygenase-biliverdin reductase axis, the systemic inhibition of the renin-angiotensin system, the inhibition of the angiotensin-converting enzyme, and several actions mirroring those of the peroxisome proliferator-activated receptor agonists further support this notion.
Biliverdin reductase isozymes in metabolism.
Hinds et al., Toledo, United States. In Trends Endocrinol Metab, Apr 2015
The biliverdin reductase (BVR) isozymes BVRA and BVRB are cell surface membrane receptors with pleiotropic functions.
Biliverdin Reductase A (BVRA) Mediates Macrophage Expression of Interleukin-10 in Injured Kidney.
Xu et al., Wuhan, China. In Int J Mol Sci, 2014
Biliverdin reductase A is an enzyme, with serine/threonine/tyrosine kinase activation, converting biliverdin (BV) to bilirubin (BR) in heme degradation pathway.
Ferulic Acid Regulates the Nrf2/Heme Oxygenase-1 System and Counteracts Trimethyltin-Induced Neuronal Damage in the Human Neuroblastoma Cell Line SH-SY5Y.
Mancuso et al., Roma, Italy. In Front Pharmacol, 2014
Over the past years, several lines of evidence have pointed out the efficacy of ferulic acid (FA) in counteracting oxidative stress elicited by β-amyloid or free radical initiators, based on the ability of this natural antioxidant to up-regulate the heme oxygenase-1 (HO-1) and biliverdin reductase (BVR) system.
Statins more than cholesterol lowering agents in Alzheimer disease: their pleiotropic functions as potential therapeutic targets.
Butterfield et al., Lexington, United States. In Biochem Pharmacol, 2014
The aim of this review is to provide an overview on the new discoveries about the effects of statin therapy on the oxidative and nitrosative stress levels as well as on the modulation of the heme oxygenase/biliverdin reductase (HO/BVR) system in the brain.
The Janus face of the heme oxygenase/biliverdin reductase system in Alzheimer disease: it's time for reconciliation.
Butterfield et al., Lexington, United States. In Neurobiol Dis, 2014
The up-regulation of the heme oxygenase-1/biliverdin reductase-A (HO-1/BVR-A) system is one of the earlier events in the adaptive response to stress.
Heme oxygenase-1: an emerging therapeutic target to curb cardiac pathology.
Motterlini et al., Paris, France. In Basic Res Cardiol, 2013
These diversified effects are achieved through the degradation of heme to carbon monoxide (CO), biliverdin (which is rapidly converted to bilirubin by biliverdin reductase) and ferric iron.
The coordinated increased expression of biliverdin reductase and heme oxygenase-2 promotes cardiomyocyte survival: a reductase-based peptide counters β-adrenergic receptor ligand-mediated cardiac dysfunction.
Maines et al., Rochester, United States. In Faseb J, 2011
Data show that siRNA blockage of BVR protein expression in cardiomyocytes inhibits HO-2 protein induction but not vice versa.
Pharmacological and clinical aspects of heme oxygenase.
Kappas et al., Valhalla, United States. In Pharmacol Rev, 2008
The HO system includes the heme catabolic pathway, comprising HO and biliverdin reductase, and the products of heme degradation, carbon monoxide (CO), iron, and biliverdin/bilirubin.
Activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions.
Mantle et al., Dublin, Ireland. In Biochem J, 2007
Results describe the activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions.
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
Maines et al., Salt Lake City, United States. In J Mol Biol, 2002
X-ray crystal structures of apo rat BVR and its complex with NADH at 1.2 A and 1.5 A resolution, respectively
Heme oxygenase: a novel target for the modulation of the inflammatory response.
Willoughby et al., London, United Kingdom. In Nat Med, 1996
Heme oxygenase ((HO); EC is the rate-limiting enzyme in the catabolism of heme to biliverdin (which is converted to bilirubin by biliverdin reductase), free iron and carbon monoxide (CO).
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