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Journal articles on the topic 'BILIVERDINE'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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1

Wasbotten, Ingar, and Abhik Ghosh. "Biliverdine-Based Metalloradicals: Sterically Enhanced Noninnocence." Inorganic Chemistry 45, no. 13 (2006): 4914–21. http://dx.doi.org/10.1021/ic052037w.

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2

Steiner, Alexandre A., and Luiz G. S. Branco. "Carbon monoxide is the heme oxygenase product with a pyretic action: evidence for a cGMP signaling pathway." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 280, no. 2 (2001): R448—R457. http://dx.doi.org/10.1152/ajpregu.2001.280.2.r448.

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We have recently reported that the central heme oxygenase (HO) pathway has an important role in the genesis of lipopolysaccharide fever. However, the HO product involved, i.e., biliverdine, free iron, or carbon monoxide (CO), has not yet been identified with certainty. Therefore, in the present study, we tested the thermoregulatory effects of all HO products. Body core temperature (Tc) and gross activity of awake, freely moving rats was measured by biotelemetry. Intracerebroventricular administration of heme-lysinate (152 nmol), which induces the HO pathway, evoked a marked increase in Tc, a r

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3

Johnson, R. A., M. Lavesa, K. DeSeyn, M. J. Scholer, and A. Nasjletti. "Heme oxygenase substrates acutely lower blood pressure in hypertensive rats." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 3 (1996): H1132—H1138. http://dx.doi.org/10.1152/ajpheart.1996.271.3.h1132.

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Heme oxygenase catalyzes the metabolism of heme to biliverdine, free iron, and carbon monoxide. The current study was designed to determine if treatment with the heme oxygenase substrates heme-L-arginate or heme-L-lysinate, to stimulate formation of heme oxygenase products, can lower blood pressure in the rat. Heme-L-arginate (45 mumol/kg ip) and heme-L-lysinate (45 mumol/kg ip) acutely lowered blood pressure in awake spontaneously hypertensive rats (SHR) by approximately 35 mmHg. For both heme oxygenase substrates, this effect was blunted by pretreatment with an inhibitor of heme oxygenase, z

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4

Niemevz, Fernando, and Graciela Y. Buldain. "Phenyl biliverdin isomers obtained by chemical oxidation of iron(III) complex of 5-phenyl protoporphyrin IX." Journal of Porphyrins and Phthalocyanines 08, no. 07 (2004): 989–95. http://dx.doi.org/10.1142/s1088424604000350.

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Oxidative cleavage of synthetic 5-phenyl protohemin IX in pyridine solution in the presence of ascorbic acid (coupled oxidation), followed by esterification of the products with boron trifluoride-methanol rendered mainly three isomeric biliverdins. These were identified by MS and 1D and 2D 1 H NMR as 15-phenyl biliverdin IXβ (1), 10-phenyl biliverdin IXγ (2) and 5-phenyl biliverdin IXδ (3) dimethyl esters. The fact that biliverdin IXα dimethyl ester derivative is not obtained indicates that oxidation fails to occur in the α-meso-carbon bearing the phenyl group.

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5

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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6

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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7

McDonagh, Antony F., David A. Lightner, Ari K. Kar, and Wilma S. Norona. "Hepatobiliary excretion of biliverdin isomers and C10-substituted biliverdins in Mrp2-deficient (TR−) rats." Biochemical and Biophysical Research Communications 293, no. 3 (2002): 1077–83. http://dx.doi.org/10.1016/s0006-291x(02)00325-x.

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8

Andresen, Jon J., Nadeem I. Shafi, William Durante, and Robert M. Bryan. "Effects of carbon monoxide and heme oxygenase inhibitors in cerebral vessels of rats and mice." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 1 (2006): H223—H230. http://dx.doi.org/10.1152/ajpheart.00058.2006.

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Carbon monoxide (CO) has been postulated to be a signaling molecule in many tissues, including the vasculature. We examined vasomotor responses of adult rat and mouse cerebral arteries to both exogenously applied and endogenously produced CO. The diameter of isolated, pressurized, and perfused rat middle cerebral arteries (MCAs) was not altered by authentic CO (10−6 to 10−4 M). Mouse MCAs, however, dilated by 21 ± 10% at 10−4 M CO. Authentic nitric oxide (NO·, 10−10 to 10−7 M) dilated both rat and mouse MCAs. At 10−8 M NO·, rat vessels dilated by 84 ± 4%, and at 10−7 M NO·, mouse vessels dilat

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9

Itano, H. A., and T. Hirota. "A two-molecule mechanism of haem degradation." Biochemical Journal 226, no. 3 (1985): 767–71. http://dx.doi.org/10.1042/bj2260767.

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Coupled oxidation of octaethylhaemin and phenylhydrazine hydrochloride with 16,16O2 and 18,18O2 produced octaethyl[16O]verdohaemochrome and octaethyl[18O]-verdohaemochrome respectively. Reactions of these products with 16,16O2 in the presence of phenylhydrazine hydrochloride yielded octaethyl[16O, 16O]biliverdin and octaethyl[18O, 16O]biliverdin. The same reactions with 18,18O2 yielded octaethyl[16O, 18O]biliverdin and octaethyl[18O, 18O]biliverdin. Accordingly, the two oxygen atoms of biliverdin are incorporated from different O2 molecules in separate reactions, namely the formation of verdoh

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10

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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11

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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12

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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13

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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14

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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15

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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16

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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17

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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18

Wu, Tai-Wing, Doug Carey, Jun Wu, and Hiroshi Sugiyama. "The cytoprotective effects of bilirubin and biliverdin on rat hepatocytes and human erythrocytes and the impact of albumin." Biochemistry and Cell Biology 69, no. 12 (1991): 828–34. http://dx.doi.org/10.1139/o91-123.

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The hypothesis that unconjugated bilirubin and biliverdin are cytoprotective antioxidants has been examined for the first time in systems containing cells. In primary rat hepatocytes exposed to xanthine oxidase and hypoxanthine, bilirubin (0–60 μM) failed to prolong cell survival. In contrast, biliverdin (20–100 μM) markedly delayed hepatocyte necrosis in a concentration-dependent manner. When 0.3 mM of albumin was present, bilirubin (0–50 μM) became protective of hepatocytes, while biliverdin was less dramatically enhanced in its cytoprotective effect. In human erythrocytes exposed to peroxyl

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19

Overhaus, Marcus, Beverley A. Moore, Joel E. Barbato, Florian F. Behrendt, Julia G. Doering, and Anthony J. Bauer. "Biliverdin protects against polymicrobial sepsis by modulating inflammatory mediators." American Journal of Physiology-Gastrointestinal and Liver Physiology 290, no. 4 (2006): G695—G703. http://dx.doi.org/10.1152/ajpgi.00152.2005.

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Highly inducible heme oxygenase (HO)-1 is protective against acute and chronic inflammation. HO-1 generates carbon monoxide (CO), ferrous iron, and biliverdin. The aim of this study was to investigate the protective effects of biliverdin against sepsis-induced inflammation and intestinal dysmotility. Cecal ligation and puncture (CLP) was performed on Sprague-Dawley rats under isoflurane anesthesia with and without intraperitoneal biliverdin injections, which were done before, at the time of CLP, and after CLP. In vivo gastrointestinal transit was carried out with fluorescein-labeled dextran. J

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20

Hirota, K., S. Yamamoto, and H. A. Itano. "Urinary excretion of isomers of biliverdin after destruction in vivo of haemoproteins and haemin." Biochemical Journal 229, no. 2 (1985): 477–83. http://dx.doi.org/10.1042/bj2290477.

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The amount and isomeric composition of urinary biliverdin in rabbits were analysed by h.p.l.c. Physiological values were maintained after the injection of haemin. On the other hand, when haemoglobins from several mammalian species were injected into rabbits, the excretion of biliverdin-IX alpha and biliverdin-IX beta were increased 6-18-fold and 32-66-fold respectively over physiological excretion. Injection of myoglobin resulted in a 44-fold increase in excretion of the IX alpha-isomer. Coupled oxidation with ascorbate of haemoglobin and myoglobin by oxygen produced mainly the IX alpha- and I

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21

Wang, Hong, Jeffrey L. Garvin, Martin A. D'Ambrosio, et al. "Heme oxygenase metabolites inhibit tubuloglomerular feedback in vivo." American Journal of Physiology-Heart and Circulatory Physiology 300, no. 4 (2011): H1320—H1326. http://dx.doi.org/10.1152/ajpheart.01118.2010.

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Tubuloglomerular feedback (TGF) is a renal autoregulatory mechanism that constricts the afferent arteriole in response to increases in distal NaCl. Heme oxygenases (HO-1 and HO-2) release carbon monoxide (CO) and biliverdin, which may help control renal function. We showed in vitro that HO products inhibit TGF; however, we do not know whether this also occurs in vivo or the mechanism(s) involved. We hypothesized that in vivo HO-1 and HO-2 in the nephron inhibit TGF via release of CO and biliverdin. We first performed laser capture microdissection followed by real-time PCR and found that both H

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22

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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23

Montecinos-Franjola, Felipe, John Y. Lin, and Erik A. Rodriguez. "Fluorescent proteins for in vivo imaging, where's the biliverdin?" Biochemical Society Transactions 48, no. 6 (2020): 2657–67. http://dx.doi.org/10.1042/bst20200444.

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Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light &gt;600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate

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24

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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25

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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26

McPHEE, Fiona, Patricia S. CALDERA, Guy W. BEMIS, Antony F. McDONAGH, Irwin D. KUNTZ, and Charles S. CRAIK. "Bile pigments as HIV-1 protease inhibitors and their effects on HIV-1 viral maturation and infectivity in vitro." Biochemical Journal 320, no. 2 (1996): 681–86. http://dx.doi.org/10.1042/bj3200681.

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Using recently developed molecular-shape description algorithms, we searched the Available Chemical Directory for known compounds similar in shape to the potent HIV-1 protease inhibitor Merck L-700,417; 15 compounds most similar in shape to the inhibitor were selected for testing in vitro. Four of these inhibited the protease at 100 µM or less and the most active of the four were the naturally occurring pigments biliverdin and bilirubin. Biliverdin and bilirubin inhibited recombinant HIV-1 protease in vitro at pH 7.8 with Ki values of approx. 1 µM, and also inhibited HIV-2 and simian immunodef

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27

Taboada, Carlos, Andrés E. Brunetti, Mariana L. Lyra, et al. "Multiple origins of green coloration in frogs mediated by a novel biliverdin-binding serpin." Proceedings of the National Academy of Sciences 117, no. 31 (2020): 18574–81. http://dx.doi.org/10.1073/pnas.2006771117.

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Many vertebrates have distinctive blue-green bones and other tissues due to unusually high biliverdin concentrations—a phenomenon called chlorosis. Despite its prevalence, the biochemical basis, biology, and evolution of chlorosis are poorly understood. In this study, we show that the occurrence of high biliverdin in anurans (frogs and toads) has evolved multiple times during their evolutionary history, and relies on the same mechanism—the presence of a class of serpin family proteins that bind biliverdin. Using a diverse combination of techniques, we purified these serpins from several specie

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28

Sato, Hideaki, Masakazu Sugishima, Hiroshi Sakamoto, et al. "Crystal structure of rat haem oxygenase-1 in complex with ferrous verdohaem: presence of a hydrogen-bond network on the distal side." Biochemical Journal 419, no. 2 (2009): 339–45. http://dx.doi.org/10.1042/bj20082279.

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HO (haem oxygenase) catalyses the degradation of haem to biliverdin, CO and ferrous iron via three successive oxygenation reactions, i.e. haem to α-hydroxyhaem, α-hydroxyhaem to α-verdohaem and α-verdohaem to ferric biliverdin–iron chelate. In the present study, we determined the crystal structure of ferrous α-verdohaem–rat HO-1 complex at 2.2 Å (1 Å=0.1 nm) resolution. The overall structure of the verdohaem complex was similar to that of the haem complex. Water or OH− was co-ordinated to the verdohaem iron as a distal ligand. A hydrogen-bond network consisting of water molecules and several a

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29

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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30

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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31

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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32

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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33

Ditto, Manfred, Harald Brunner, and Max E. Lippitsch. "Picosecond spectroscopy of dihydro biliverdin." Chemical Physics Letters 185, no. 1-2 (1991): 61–64. http://dx.doi.org/10.1016/0009-2614(91)80140-s.

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34

Ren, YiLin, Martin A. D'Ambrosio, Hong Wang, Ruisheng Liu, Jeffrey L. Garvin, and Oscar A. Carretero. "Heme oxygenase metabolites inhibit tubuloglomerular feedback (TGF)." American Journal of Physiology-Renal Physiology 295, no. 4 (2008): F1207—F1212. http://dx.doi.org/10.1152/ajprenal.90243.2008.

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Tubuloglomerular feedback (TGF) is the mechanism by which the macula densa (MD) senses increases in luminal NaCl concentration and sends a signal to constrict the afferent arteriole (Af-Art). The kidney expresses constitutively heme oxygenase-2 (HO-2) and low levels of HO-1. HOs release carbon monoxide (CO), biliverdin, and free iron. We hypothesized that renal HOs inhibit TGF via release of CO and biliverdin. Rabbit Af-Arts and attached MD were simultaneously microperfused in vitro. The TGF response was determined by measuring Af-Art diameter before and after increasing NaCl in the MD perfusa

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35

Zahedi, Mansour, Homayoon Bahrami, Shant Shahbazian, Nasser Safari, and Seik Weng Ng. "An ab initio/hybrid (ONIOM) investigation of biliverdin isomers and metal–biliverdin analogue complexes." Journal of Molecular Structure: THEOCHEM 633, no. 1 (2003): 21–33. http://dx.doi.org/10.1016/s0166-1280(03)00271-9.

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36

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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37

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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38

Eng, F., and J. H. Youson. "Biliverdin in the serum of ammocoetes of Lampetra lamottenii (Le Sueur)." Canadian Journal of Zoology 69, no. 4 (1991): 1126–29. http://dx.doi.org/10.1139/z91-159.

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Green sera collected from larval lampreys of Lampetra lamottenii were assayed and were shown to contain biliverdin at a concentration ranging from 141.5 to 305.0 μmol/L (mean 231.0 ± 27.4). These levels of serum biliverdin are compared with those of other lower vertebrates and with those observed during several human pathological conditions and are discussed with regard to the location of larval nematodes of Truttaedacnitis stelmioides within the bile ducts of these lampreys.

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39

Brown, S. B., J. A. Holroyd, D. I. Vernon, Y. K. Shim, and K. M. Smith. "The biosynthesis of the chromophore of phycocyanin. Pathway of reduction of biliverdin to phycocyanobilin." Biochemical Journal 261, no. 1 (1989): 259–63. http://dx.doi.org/10.1042/bj2610259.

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The later stages in the pathway of biosynthesis of phycocyanobilin, the chromophore of phycocyanin, were studied by using radiolabelled intermediates. Three possible pathways from biliverdin IX-alpha to phycocyanobilin were considered. 14C-labelled samples of key intermediates in two of the pathways, 3-vinyl-18-ethyl biliverdin IX-alpha and 3-ethyl-18-vinyl biliverdin IX-alpha, were synthesized chemically and were administered to cultures of Cyanidium caldarium that were actively synthesizing photosynthetic pigments in the light. Neither of these two compounds was apparently incorporated into

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Laude, Jean-Pierre, and Giulio Fanti. "Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud." Applied Spectroscopy 71, no. 10 (2017): 2313–24. http://dx.doi.org/10.1177/0003702817715291.

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The Raman spectrum of a microsubstance, smeared on a fiber coming from the Shroud of Turin, was compared with numerous spectra published for old or modern pigment dyes, whole bloods, dried bloods, red blood cells, albumin, very ancient blood stains, and various “degradation” products of heme. Within the wavenumber measure accuracy, it is shown that all Raman lines detected above background could correspond to vibration frequencies found in biliverdin-derived compounds except a weak line that we tentatively attributed to amide I. Biliverdin is known as an oxidative ring cleavage product of the

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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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Fernández, Marcelo, Rosalia B. Frydman, Sara Bari, and Benjamin Frydman. "Reconstitution of apomyoglobin with extended biliverdins." Biochemical and Biophysical Research Communications 183, no. 3 (1992): 1209–15. http://dx.doi.org/10.1016/s0006-291x(05)80319-5.

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43

Vachharajani, Tushar J., Jack Work, Andrew C. Issekutz, and D. Neil Granger. "Heme oxygenase modulates selectin expression in different regional vascular beds." American Journal of Physiology-Heart and Circulatory Physiology 278, no. 5 (2000): H1613—H1617. http://dx.doi.org/10.1152/ajpheart.2000.278.5.h1613.

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Heme oxygenase (HO) catalyzes the degradation of heme to biliverdin, iron, and CO. The inducible isoform (HO-1) has been implicated as a modulator of the inflammatory response. HO-1 activity can be induced by hemin and inhibited with zinc protoporphyrin IX (ZnPP). Using these reagents, we assessed the possibility that HO-1 modulates the inflammatory response by altering the expression of endothelial cell adhesion molecules. Endotoxin (lipopolysaccharide, LPS)-induced expression of P- and E-selectin expression was quantified in different vascular beds of the rat using the dual radiolabeled mono

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Zheng, Jing, Toyoshi Inoguchi, Shuji Sasaki, et al. "Phycocyanin and phycocyanobilin fromSpirulina platensisprotect against diabetic nephropathy by inhibiting oxidative stress." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 304, no. 2 (2013): R110—R120. http://dx.doi.org/10.1152/ajpregu.00648.2011.

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We and other investigators have reported that bilirubin and its precursor biliverdin may have beneficial effects on diabetic vascular complications, including nephropathy, via its antioxidant effects. Here, we investigated whether phycocyanin derived from Spirulina platensis, a blue-green algae, and its chromophore phycocyanobilin, which has a chemical structure similar to that of biliverdin, protect against oxidative stress and renal dysfunction in db/db mice, a rodent model for Type 2 diabetes. Oral administration of phycocyanin (300 mg/kg) for 10 wk protected against albuminuria and renal m

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Coleman, William F. "Photochemical Oxidation of Bilirubin to Biliverdin." Journal of Chemical Education 83, no. 9 (2006): 1329. http://dx.doi.org/10.1021/ed083p1329.

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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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Smit, Kurt, Joerg Matysik, Peter Hildebrandt, and Franz Mark. "Vibrational analysis of biliverdin dimethyl ester." Journal of Physical Chemistry 97, no. 46 (1993): 11887–900. http://dx.doi.org/10.1021/j100148a009.

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Montorzi, Marcelo, T. Scott Dziedzic, and Kenneth H. Falchuk. "Biliverdin duringXenopus laevisOogenesis and Early Embryogenesis†." Biochemistry 41, no. 31 (2002): 10115–22. http://dx.doi.org/10.1021/bi020204n.

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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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Sturrock, Edward D., James R. Bull, Ralph E. Kirsch, Ravindra K. Pandey, Mathias O. Senge, and Kevin M. Smith. "A novel 2,18-bridged biliverdin derivative." Journal of the Chemical Society, Chemical Communications, no. 10 (1993): 872. http://dx.doi.org/10.1039/c39930000872.

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