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Journal articles on the topic 'Biliverdin reductase'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Valasinas, Aldonia, and Benjamin Frydman. "Reduction of Biliverdins to Bilirubins: Its Metabolic Regulation Under Various Physiological Conditions." Current Medicinal Chemistry 3, no. 4 (1996): 291–302. http://dx.doi.org/10.2174/092986730304220302113254.

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Abstract: Heme and hemoproteins are degraded in mammals by oxidation to biliverdins. These linear tetrapyrroles are reduced to bilirubins by a cytosolic biliverdin reductase (BvR) at the rate of 250-400 mg per day. While the bulk of biliary biliverdin is biliverdin IX α , other isomers such as biliverdins IXβ and IXγ are formed under conditions of oxidative stress by the chemical degradation of hemoproteins, or from the degradation of abnormal hemoglobins. Rat liver BvR was found to. be a NADPH-dependent reductase with a broad substrate specificity, which efficiently reduces a large number of

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2

SHALLOE, Fiona, Gordon ELLIOTT, Orla ENNIS та Timothy J. MANTLE. "Evidence that biliverdin-IXβ reductase and flavin reductase are identical". Biochemical Journal 316, № 2 (1996): 385–87. http://dx.doi.org/10.1042/bj3160385.

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A search of the database shows that human biliverdin-IXβ reductase and flavin reductase are identical. We have isolated flavin reductase from bovine erythrocytes and show that the activity co-elutes with biliverdin-IXβ reductase. Preparations of the enzyme that are electrophoretically homogeneous exhibit both flavin reductase and biliverdin-IXβ reductase activities; however, they are not capable of catalysing the reduction of biliverdin-IXα. Although there is little obvious sequence identity between biliverdin-IXα reductase (BVR-A) and biliverdin-IXβ reductase (BVR-B), they do show weak immuno

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3

Yoshinaga, T., Y. Sudo та S. Sano. "Enzymic conversion of α-oxyprotohaem IX into biliverdin IXα by haem oxygenase". Biochemical Journal 270, № 3 (1990): 659–64. http://dx.doi.org/10.1042/bj2700659.

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Conversion of four isomers of meso-oxyprotohaem IX into the corresponding biliverdin IX was attempted with a reconstituted haem oxygenase system in the presence of NADPH-cytochrome c reductase and NADPH. Only the alpha-isomer of meso-oxyprotohaem IX was converted effectively into biliverdin IX alpha, which was further reduced to bilirubin IX alpha by biliverdin reductase. Only trace amounts of biliverdins IX beta, IX gamma and IX delta were respectively formed from the incubation mixture of the corresponding oxyprotohaemin IX isomers with the complete haem oxygenase system under the same condi

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4

Kikuchi, A., S.-Y. Park, H. Miyatake, et al. "Structure of Biliverdin Reductase." Seibutsu Butsuri 40, supplement (2000): S122. http://dx.doi.org/10.2142/biophys.40.s122_3.

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5

CUNNINGHAM, Orla, Michael G. GORE та Timothy J. MANTLE. "Initial-rate kinetics of the flavin reductase reaction catalysed by human biliverdin-IXβ reductase (BVR-B)". Biochemical Journal 345, № 2 (2000): 393–99. http://dx.doi.org/10.1042/bj3450393.

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The initial-rate kinetics of the flavin reductase reaction catalysed by biliverdin-IXβ reductase at pH 7.5 are consistent with a rapid-equilibrium ordered mechanism, with the pyridine nucleotide binding first. NADPH binding to the free enzyme was characterized using stopped-flow fluorescence quenching, and a Kd of 15.8 μM was calculated. Equilibrium fluorescence quenching experiments indicated a Kd of 0.55 μM, suggesting that an enzyme-NADPH encounter complex (Kd 15.8 μM) isomerizes to a more stable ‘nucleotide-induced’ conformation. The enzyme was shown to catalyse the reduction of FMN, FAD a

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6

Rigney, E. M., O. Phillips, and T. J. Mantle. "Some physical and immunological properties of ox kidney biliverdin reductase." Biochemical Journal 255, no. 2 (1988): 431–35. http://dx.doi.org/10.1042/bj2550431.

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The liver, kidney and spleen of the mouse and rat and the kidney and spleen of the ox express a monomeric form of biliverdin reductase (Mr 34,000), which in the case of the ox kidney enzyme exists in two forms (pI 5.4 and 5.2) that are probably charge isomers. The livers of the mouse and rats express, in addition, a protein (Mr 46,000) that cross-reacts with antibodies raised against the ox kidney enzyme and may be related to form 2 described by Frydman, Tomaro, Awruch & Frydman [(1983) Biochim. Biophys. Acta 759, 257-263]. Higher-Mr forms appear to exist in the guinea pig and hamster. The

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7

Briz, Oscar, Rocio I. R. Macias, Maria J. Perez, Maria A. Serrano, and Jose J. G. Marin. "Excretion of fetal biliverdin by the rat placenta-maternal liver tandem." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 290, no. 3 (2006): R749—R756. http://dx.doi.org/10.1152/ajpregu.00487.2005.

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Fetal liver immaturity is accompanied by active heme catabolism. Thus fetal biliary pigments must be excreted toward the mother by the placenta. To investigate biliverdin handling by the placenta-maternal liver tandem, biliverdin-IXα was administered to 21-day pregnant rats through the jugular vein or the umbilical artery of an in situ perfused placenta. Jugular administration resulted in the secretion into maternal bile of both bilirubin and biliverdin (3:1). However, when biliverdin was administered to the placenta, most of it was transformed into bilirubin before being transferred to the ma

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8

Smith, Liam J., Seamus Browne, Adrian J. Mulholland та Timothy J. Mantle. "Computational and experimental studies on the catalytic mechanism of biliverdin-IXβ reductase". Biochemical Journal 411, № 3 (2008): 475–84. http://dx.doi.org/10.1042/bj20071495.

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BVR-B (biliverdin-IXβ reductase) also known as FR (flavin reductase) is a promiscuous enzyme catalysing the pyridine-nucleotide-dependent reduction of a variety of flavins, biliverdins, PQQ (pyrroloquinoline quinone) and ferric ion. Mechanistically it is a good model for BVR-A (biliverdin-IXα reductase), a potential pharmacological target for neonatal jaundice and also a potential target for adjunct therapy to maintain protective levels of biliverdin-IXα during organ transplantation. In a commentary on the structure of BVR-B it was noted that one outstanding issue remained: whether the mechani

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9

Schluchter, Wendy M., and Alexander N. Glazer. "Characterization of Cyanobacterial Biliverdin Reductase." Journal of Biological Chemistry 272, no. 21 (1997): 13562–69. http://dx.doi.org/10.1074/jbc.272.21.13562.

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10

O’Brien, Luke, Peter A. Hosick, Kezia John, David E. Stec, and Terry D. Hinds. "Biliverdin reductase isozymes in metabolism." Trends in Endocrinology & Metabolism 26, no. 4 (2015): 212–20. http://dx.doi.org/10.1016/j.tem.2015.02.001.

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11

Huang, Tian-Jun. "Detection of Biliverdin Reductase Activity." Current Protocols in Toxicology 00, no. 1 (1999): 9.4.1–9.4.10. http://dx.doi.org/10.1002/0471140856.tx0904s00.

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12

Foresti, Roberta, Colin J. Green, and Roberto Motterlini. "Generation of bile pigments by haem oxygenase: a refined cellular strategy in response to stressful insults." Biochemical Society Symposia 71 (March 1, 2004): 177–92. http://dx.doi.org/10.1042/bss0710177.

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The family of haem oxygenase enzymes is unique in nature for its role in haem degradation. Haem is cleaved at the α-meso position by haem oxygenase with the support of electrons donated by cytochrome P450 reductase, the first products of this reaction being CO, iron and biliverdin. Biliverdin is then converted to bilirubin by biliverdin reductase. If haem is viewed as a substrate for an anabolic pathway, it becomes evident that haem oxygenases do not break down haem for elimination from the body, but rather use haem to generate crucial molecules that can modulate cellular functions. The facts

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13

Kobachi, Kenju, Sota Kuno, Shinya Sato, Kenta Sumiyama, Michiyuki Matsuda, and Kenta Terai. "Biliverdin Reductase-A Deficiency Brighten and Sensitize Biliverdin-binding Chromoproteins." Cell Structure and Function 45, no. 2 (2020): 131–41. http://dx.doi.org/10.1247/csf.20010.

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14

Yamaguchi, T., Y. Komoda, and H. Nakajima. "Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization." Journal of Biological Chemistry 269, no. 39 (1994): 24343–48. http://dx.doi.org/10.1016/s0021-9258(19)51088-2.

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15

Wegele, Rosalina, Ronja Tasler, Yuhong Zeng, Mario Rivera, and Nicole Frankenberg-Dinkel. "The Heme Oxygenase(s)-Phytochrome System ofPseudomonas aeruginosa." Journal of Biological Chemistry 279, no. 44 (2004): 45791–802. http://dx.doi.org/10.1074/jbc.m408303200.

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For many pathogenic bacteria likePseudomonas aeruginosaheme is an essential source of iron. After uptake, the heme molecule is degraded by heme oxygenases to yield iron, carbon monoxide, and biliverdin. The heme oxygenase PigA is only induced under iron-limiting conditions and produces the unusual biliverdin isomers IXβ and IXδ. The gene for a second putative heme oxygenase inP. aeruginosa,bphO, occurs in an operon with the genebphPencoding a bacterial phytochrome. Here we provide biochemical evidence thatbphOencodes for a second heme oxygenase inP. aeruginosa. HPLC,1H, and13C NMR studies indi

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16

KIKUCHI, Akihiro. "Structural Biological Study of Biliverdin Reductase." Nihon Kessho Gakkaishi 43, no. 5 (2001): 371–76. http://dx.doi.org/10.5940/jcrsj.43.371.

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17

Baranano, D. E., M. Rao, C. D. Ferris, and S. H. Snyder. "Biliverdin reductase: A major physiologic cytoprotectant." Proceedings of the National Academy of Sciences 99, no. 25 (2002): 16093–98. http://dx.doi.org/10.1073/pnas.252626999.

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18

Frydman, Rosalía B., María L. Tomaro, Jorge Rosenfeld, et al. "Biliverdin reductase: substrate specificity and kinetics." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 916, no. 3 (1987): 500–511. http://dx.doi.org/10.1016/0167-4838(87)90197-x.

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19

Sedlak, Thomas W., and Solomon H. Snyder. "Cycling the Wagons for Biliverdin Reductase." Journal of Biological Chemistry 284, no. 46 (2009): le11. http://dx.doi.org/10.1074/jbc.l109.037119.

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20

Maines, Mahin D. "New Insights into Biliverdin Reductase Functions: Linking Heme Metabolism to Cell Signaling." Physiology 20, no. 6 (2005): 382–89. http://dx.doi.org/10.1152/physiol.00029.2005.

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Biliverdin reductase (BVR) functions in cell signaling through three distinct tracks: a dual-specificity kinase that functions in the insulin receptor/MAPK pathways ( 25 , 29 , 51 ); a bzip-type transcription factor for ATF-2/CREB and HO-1 regulation ( 1 , 25 ); and a reductase that catalyzes the conversion of biliverdin to bilirubin ( 27 ). These, together with the protein’s primary and secondary features, intimately link BVR to the entire spectrum of cell-signaling cascades.

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21

Cunningham, Orla, Aisling Dunne, Portia Sabido, David Lightner та Timothy J. Mantle. "Studies on the Specificity of the Tetrapyrrole Substrate for Human Biliverdin-IXα Reductase and Biliverdin-IXβ Reductase". Journal of Biological Chemistry 275, № 25 (2000): 19009–17. http://dx.doi.org/10.1074/jbc.275.25.19009.

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22

BERI, RIPLA, and RAMESH CHANDRA. "Biliverdin reductase activity in relation to bilirubin." Biochemical Society Transactions 20, no. 4 (1992): 353S. http://dx.doi.org/10.1042/bst020353s.

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23

RIGNEY, E. M., and T. J. MANTLE. "Nucleotide binding to ox kidney biliverdin reductase." Biochemical Society Transactions 13, no. 2 (1985): 502. http://dx.doi.org/10.1042/bst0130502.

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24

Kikuchi, A., S. Y. Park, D. Sun, M. Sato, T. Yoshida та Y. Shiro. "Crystal structure of rat biliverdin-IXα reductase". Acta Crystallographica Section A Foundations of Crystallography 58, s1 (2002): c118. http://dx.doi.org/10.1107/s0108767302089754.

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25

Weaver, Lauren, Abdul-rizaq Hamoud, David E. Stec, and Terry D. Hinds. "Biliverdin reductase and bilirubin in hepatic disease." American Journal of Physiology-Gastrointestinal and Liver Physiology 314, no. 6 (2018): G668—G676. http://dx.doi.org/10.1152/ajpgi.00026.2018.

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The buildup of fat in the liver (hepatic steatosis) is the first step in a series of incidents that may drive hepatic disease. Obesity is the leading cause of nonalcoholic fatty liver disease (NAFLD), in which hepatic steatosis progresses to liver disease. Chronic alcohol exposure also induces fat accumulation in the liver and shares numerous similarities to obesity-induced NAFLD. Regardless of whether hepatic steatosis is due to obesity or long-term alcohol use, it still may lead to hepatic fibrosis, cirrhosis, or possibly hepatocellular carcinoma. The antioxidant bilirubin and the enzyme tha

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26

Bell, J. Ellis, and Mahin D. Maines. "Kinetic properties and regulation of biliverdin reductase." Archives of Biochemistry and Biophysics 263, no. 1 (1988): 1–9. http://dx.doi.org/10.1016/0003-9861(88)90607-8.

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27

Maines, M. D., and G. M. Trakshel. "Purification and Characterization of Human Biliverdin Reductase." Archives of Biochemistry and Biophysics 300, no. 1 (1993): 320–26. http://dx.doi.org/10.1006/abbi.1993.1044.

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28

Gibbs, Peter E. M., та Mahin D. Maines. "Biliverdin inhibits activation of NF-κB: Reversal of inhibition by human biliverdin reductase". International Journal of Cancer 121, № 11 (2007): 2567–74. http://dx.doi.org/10.1002/ijc.22978.

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29

Iwamori, Saki, Emiko Sato, Daisuke Saigusa, et al. "A novel and sensitive assay for heme oxygenase activity." American Journal of Physiology-Renal Physiology 309, no. 7 (2015): F667—F671. http://dx.doi.org/10.1152/ajprenal.00210.2015.

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Heme oxygenase (HO) is a renoprotective protein in the microsome that degrades heme and produces biliverdin. Biliverdin is then reduced to a potent antioxidant bilirubin by biliverdin reductase in the cytosol. Because HO activity does not necessarily correlate with HO mRNA or protein levels, a reliable assay is needed to determine HO activity. Spectrophotometric measurement is tedious and requires a relatively large amount of kidney samples. Moreover, bilirubin is unstable and spontaneously oxidized to biliverdin in vitro. We developed a novel and sensitive liquid chromatography-tandem mass sp

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30

Miralem, Tihomir, Nicole Lerner-Marmarosh, Peter E. M. Gibbs, Cicerone Tudor, Fred K. Hagen та Mahin D. Maines. "The Human Biliverdin Reductase-based Peptide Fragments and Biliverdin Regulate Protein Kinase Cδ Activity". Journal of Biological Chemistry 287, № 29 (2012): 24698–712. http://dx.doi.org/10.1074/jbc.m111.326504.

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31

Ding, Zhaokun, and Youqing Xu. "Purification and Properties of Cow Splenic Biliverdin Reductase." Preparative Biochemistry 24, no. 3-4 (1994): 193–201. http://dx.doi.org/10.1080/10826069408010093.

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32

Elliott, Gordon, and Timothy J. Mantle. "PURIFICATION AND PROPERTIES OF SALMON LIVER BILIVERDIN REDUCTASE." Biochemical Society Transactions 23, no. 2 (1995): 389S. http://dx.doi.org/10.1042/bst023389s.

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33

Rigney, Elizabeth, and Timothy J. Mantle. "The reaction mechanism of bovine kidney biliverdin reductase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 957, no. 2 (1988): 237–42. http://dx.doi.org/10.1016/0167-4838(88)90278-6.

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34

Florczyk, Urszula, Slawomir Golda, Agata Zieba, Jaroslaw Cisowski, Alicja Jozkowicz, and Jozef Dulak. "Overexpression of biliverdin reductase enhances resistance to chemotherapeutics." Cancer Letters 300, no. 1 (2011): 40–47. http://dx.doi.org/10.1016/j.canlet.2010.09.003.

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35

Wu, Song, Zongdong Li, Dmitri V. Gnatenko, et al. "BLVRB redox mutation defines heme degradation in a metabolic pathway of enhanced thrombopoiesis in humans." Blood 128, no. 5 (2016): 699–709. http://dx.doi.org/10.1182/blood-2016-02-696997.

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Key PointsA biliverdin IXβ reductase redox coupling mutation with associated ROS dysregulation has been identified in thrombocytosis cohorts. Defective BLVRB enzymatic activity involving heme degradation pathway alters metabolic consequences of hematopoietic lineage fate.

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36

Shum, Michael, Chitra A. Shintre, Thorsten Althoff, et al. "ABCB10 exports mitochondrial biliverdin, driving metabolic maladaptation in obesity." Science Translational Medicine 13, no. 594 (2021): eabd1869. http://dx.doi.org/10.1126/scitranslmed.abd1869.

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Although the role of hydrophilic antioxidants in the development of hepatic insulin resistance and nonalcoholic fatty liver disease has been well studied, the role of lipophilic antioxidants remains poorly characterized. A known lipophilic hydrogen peroxide scavenger is bilirubin, which can be oxidized to biliverdin and then reduced back to bilirubin by cytosolic biliverdin reductase. Oxidation of bilirubin to biliverdin inside mitochondria must be followed by the export of biliverdin to the cytosol, where biliverdin is reduced back to bilirubin. Thus, the putative mitochondrial exporter of bi

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37

Franklin, Edward M., Seamus Browne, Anne M. Horan та ін. "The use of synthetic linear tetrapyrroles to probe the verdin sites of human biliverdin-IXα reductase and human biliverdin-IXβ reductase". FEBS Journal 276, № 16 (2009): 4405–13. http://dx.doi.org/10.1111/j.1742-4658.2009.07148.x.

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38

Sugishima, Masakazu, Kei Wada, Keiichi Fukuyama та Ken Yamamoto. "Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome". Journal of Biological Chemistry 295, № 3 (2019): 771–82. http://dx.doi.org/10.1074/jbc.ra119.011431.

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Phytochromobilin (PΦB) is a red/far-red light sensory pigment in plant phytochrome. PΦB synthase is a ferredoxin-dependent bilin reductase (FDBR) that catalyzes the site-specific reduction of bilins, which are sensory and photosynthesis pigments, and produces PΦB from biliverdin, a heme-derived linear tetrapyrrole pigment. Here, we determined the crystal structure of tomato PΦB synthase in complex with biliverdin at 1.95 Å resolution. The overall structure of tomato PΦB synthase was similar to those of other FDBRs, except for the addition of a long C-terminal loop and short helices. The struct

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39

Montgomery, Beronda L., Keara A. Franklin, Matthew J. Terry, et al. "Biliverdin Reductase-Induced Phytochrome Chromophore Deficiency in Transgenic Tobacco." Plant Physiology 125, no. 1 (2001): 266–77. http://dx.doi.org/10.1104/pp.125.1.266.

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40

Paukovich, Natasia, Mengjun Xue, James R. Elder, et al. "Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding." Journal of Molecular Biology 430, no. 18 (2018): 3234–50. http://dx.doi.org/10.1016/j.jmb.2018.06.015.

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41

PETERS, J. "Localization of Blvr, biliverdin reductase, on mouse chromosome 2." Genomics 5, no. 2 (1989): 270–74. http://dx.doi.org/10.1016/0888-7543(89)90057-8.

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42

George, Jeanne W., Kathryn Nulk, Andrew Weiss, Michael L. Bruss, and Charles E. Cornelius. "Biliverdin reductase activity in cattle, sheep, rabbits and rats." International Journal of Biochemistry 21, no. 5 (1989): 477–81. http://dx.doi.org/10.1016/0020-711x(89)90127-4.

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43

Wegiel, Barbara, Catherine J. Baty, David Gallo, et al. "Cell Surface Biliverdin Reductase Mediates Biliverdin-induced Anti-inflammatory Effects via Phosphatidylinositol 3-Kinase and Akt." Journal of Biological Chemistry 284, no. 32 (2009): 21369–78. http://dx.doi.org/10.1074/jbc.m109.027433.

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44

Gonzalez-Sanchez, E., M. J. Perez, N. S. Nytofte, et al. "344 PROTECTIVE EFFECT OF BILIVERDIN AND BILIVERDIN REDUCTASE AGAINST BILE ACID-INDUCED TOXICITY IN LIVER CELLS." Journal of Hepatology 56 (April 2012): S140. http://dx.doi.org/10.1016/s0168-8278(12)60357-2.

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45

Duff, Michael R., Jasmina S. Redzic, Lucas P. Ryan, et al. "Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family." Journal of Biochemistry 168, no. 2 (2020): 191–202. http://dx.doi.org/10.1093/jb/mvaa039.

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Abstract Biliverdin reductase B (BLVRB) family members are general flavin reductases critical in maintaining cellular redox with recent findings revealing that BLVRB alone can dictate cellular fate. However, as opposed to most enzymes, the BLVRB family remains enigmatic with an evolutionarily changing active site and unknown structural and functional consequences. Here, we applied a multi-faceted approach that combines X-ray crystallography, NMR and kinetics methods to elucidate the structural and functional basis of the evolutionarily changing BLVRB active site. Using a panel of three BLVRB i

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46

Maghzal, Ghassan J., Meng-Choo Leck, Emma Collinson, Cheng Li, and Roland Stocker. "Limited Role for the Bilirubin-Biliverdin Redox Amplification Cycle in the Cellular Antioxidant Protection by Biliverdin Reductase." Journal of Biological Chemistry 284, no. 43 (2009): 29251–59. http://dx.doi.org/10.1074/jbc.m109.037119.

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47

Wegiel, B., D. Gallo, E. Csizmadia, et al. "Biliverdin inhibits Toll-like receptor-4 (TLR4) expression through nitric oxide-dependent nuclear translocation of biliverdin reductase." Proceedings of the National Academy of Sciences 108, no. 46 (2011): 18849–54. http://dx.doi.org/10.1073/pnas.1108571108.

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48

Sedlak, T. W., and S. H. Snyder. "Bilirubin Benefits: Cellular Protection by a Biliverdin Reductase Antioxidant Cycle." PEDIATRICS 113, no. 6 (2004): 1776–82. http://dx.doi.org/10.1542/peds.113.6.1776.

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49

KOMURO, Akihiko, Takashi TOBE, Ken HASHIMOTO, et al. "Molecular Cloning and Expression of Human Liver Biliverdin-IX.BETA. Reductase." Biological & Pharmaceutical Bulletin 19, no. 6 (1996): 796–804. http://dx.doi.org/10.1248/bpb.19.796.

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50

CUNNINGHAM, ORLA, та TIMOTHY J. MANTLE. "78 Cloning, Overexpression and Purification of Biliverdin IX-β Reductase". Biochemical Society Transactions 25, № 4 (1997): S613. http://dx.doi.org/10.1042/bst025s613.

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