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Journal articles on the topic 'Zinc protoporphyrin IX'

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Published: 4 June 2021

Last updated: 4 February 2022

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1

Nelson, Joanna C., Marie Westwood, K. R. Allen, K. E. Newton, and J. H. Barth. "The Ratio of Erythrocyte Zinc-Protoporphyrin to Protoporphyrin IX in Disease and its Significance in the Mechanism of Lead Toxicity on Haem Synthesis." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 35, no. 3 (1998): 422–26. http://dx.doi.org/10.1177/000456329803500313.

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Protoporphyrin and zinc-protoporphyrin were measured in the erythrocytes of normal subjects, workers exposed to lead and patients with iron deficiency and erythropoietic protoporphyria (EPP). Results showed significantly higher levels of zinc-protoporphyrin in the lead-exposed workers ( P < 0·0001), patients with iron deficiency ( P < 0·0001) and EPP patients ( P < 0·001) compared with normal subjects. The lead-exposed workers showed the highest levels of zinc-protoporphyrin, which were significantly greater than both the iron-deficient and EPP patients ( P < 0·0001). They also sho

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2

Wakamatsu, Jun-ichi, Nobutaka Hayashi, Takanori Nishimura, and Akihito Hattori. "Nitric oxide inhibits the formation of zinc protoporphyrin IX and protoporphyrin IX." Meat Science 84, no. 1 (2010): 125–28. http://dx.doi.org/10.1016/j.meatsci.2009.08.036.

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3

WAKAMATSU, Jun-ichi, Ayana KATO, Misako EZOE, and Takanori NISHIMURA. "Effect of zinc protoporphyrin IX on dietary zinc bioavailability." Nihon Chikusan Gakkaiho 86, no. 4 (2015): 481–89. http://dx.doi.org/10.2508/chikusan.86.481.

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4

ISHIKAWA, Hiroya, Taiki KAWABUCHI, Yuriko KAWAKAMI, Masahiko SATO, Masahiro NUMATA, and Kiyoshi MATSUMOTO. "Formation of Zinc Protoporphyrin IX and Protoporphyrin IX from Oxymyoglobin in Porcine Heart Mitochondria." Food Science and Technology Research 13, no. 1 (2007): 85–88. http://dx.doi.org/10.3136/fstr.13.85.

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5

Orfanos, Adam P., Robert Guthrie, David C. Jinks, and Daniel W. Vollmer. "Simultaneous assay of zinc protoporphyrin and protoporphyrin IX in dried blood." Clinica Chimica Acta 181, no. 2 (1989): 213–17. http://dx.doi.org/10.1016/0009-8981(89)90191-5.

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6

Bailey, G. G., and L. L. Needham. "Simultaneous quantification of erythrocyte zinc protoporphyrin and protoporphyrin IX by liquid chromatography." Clinical Chemistry 32, no. 12 (1986): 2137–42. http://dx.doi.org/10.1093/clinchem/32.12.2137.

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Abstract A simple, rapid, specific, and sensitive isocratic "high-performance" liquid-chromatographic procedure is described for measuring protoporphyrin (PPIX) and zinc protoporphyrin (ZPP) in erythrocytes. A 30-microL whole-blood sample is treated with a solution of formic acid, deproteinized with acetone, and centrifuged. A 20-microL aliquot of the supernate is injected into a system consisting of a stationary phase of mu-Bondapak C18 and a mobile phase of acetone, methanol, water, and formic acid. ZPP and PPIX are detected fluorometrically (lambda ex = 417 nm, lambda em = 635 nm) within 6

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7

Benedini, Riccardo, Valeria Raja, and Giovanni Parolari. "Zinc-protoporphyrin IX promoting activity in pork muscle." LWT - Food Science and Technology 41, no. 7 (2008): 1160–66. http://dx.doi.org/10.1016/j.lwt.2007.08.005.

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8

Hirano, Chisato, and Toyoko Imae. "Electrochemical properties of protoporphyrin IX zinc(II) films." Journal of Colloid and Interface Science 280, no. 2 (2004): 478–83. http://dx.doi.org/10.1016/j.jcis.2004.08.027.

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9

De Maere, Hannelore, Marlena Jaros, Marta Dziewięcka, et al. "DETERMINATION OF HEMIN, PROTOPORPHYRIN IX, AND ZINC(II) PROTOPORPHYRIN IX IN PARMA HAM USING THIN LAYER CHROMATOGRAPHY." Journal of Liquid Chromatography & Related Technologies 37, no. 20 (2014): 2971–79. http://dx.doi.org/10.1080/10739149.2014.906995.

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10

Hennig, Georg, Christian Gruber, Michael Vogeser, et al. "Dual-wavelength excitation for fluorescence-based quantification of zinc protoporphyrin IX and protoporphyrin IX in whole blood." Journal of Biophotonics 7, no. 7 (2013): 514–24. http://dx.doi.org/10.1002/jbio.201200228.

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11

Harmatys, Kara M., Anthony J. Musso, Kasey J. Clear, and Bradley D. Smith. "Small molecule additive enhances cell uptake of 5-aminolevulinic acid and conversion to protoporphyrin IX." Photochemical & Photobiological Sciences 15, no. 11 (2016): 1408–16. http://dx.doi.org/10.1039/c6pp00151c.

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12

Sawicki, Artur, and Robert D. Willows. "S-Adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase from Rhodobacter capsulatus: mechanistic insights and stimulation with phospholipids." Biochemical Journal 406, no. 3 (2007): 469–78. http://dx.doi.org/10.1042/bj20070284.

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The enzyme BchM (S-adenosyl-L-methionine:magnesium-protoporphyrin IX O-methyltransferase) from Rhodobacter capsulatus catalyses an intermediate reaction in the bacteriochlorophyll biosynthetic pathway. Overexpression of His6-tagged protein in Escherichia coli resulted in the majority of polypeptide existing as inclusion bodies. Purification from inclusion bodies was performed using metal-affinity chromatography after an elaborate wash step involving surfactant polysorbate-20. Initial enzymatic assays involved an in situ generation of S-adenosyl-L-methionine substrate using a crude preparation

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13

SAKAI, Tadashi, Yukiko TAKEUCHI, Yumiko IKEYA, Takaharu ARAKI, and Koichi USHIO. "Automated HPLC method for determining zinc protoporphyrin ix and protoporphyrin ix in erythrocytes of workers exposed to lead." Sangyo Igaku 30, no. 6 (1988): 467–74. http://dx.doi.org/10.1539/joh1959.30.467.

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14

Zhou, Pei-Chen, Wei Huang, Rong-Bin Zhang, et al. "A Simple and Rapid Fluorimetric Method for Simultaneous Determination of Protoporphyrin IX and Zinc Protoporphyrin IX in Whole Blood." Applied Spectroscopy 62, no. 11 (2008): 1268–73. http://dx.doi.org/10.1366/000370208786401536.

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Derivative variable-angle synchronous fluorescence (DVASF) spectrometry improves the spectral resolution and selectivity of the fluorescence method. The feasibility of DVASF spectrometry for the simultaneous determination of protoporphyrin IX (PP) and zinc protoporphyrin IX (ZnPP) was investigated. PP and ZnPP were distinguished from each other simultaneously and rapidly by the DVASF method. The spectra were resolved well, and the two components were determined in a single scan, avoiding the spectral compensation factor for PP and chromatographic separation. The linear range of the calibration

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15

Rattan, Satish, Ya-Ping Fan, and Sushanta Chakder. "Mechanism of inhibition of VIP-induced LES relaxation by heme oxygenase inhibitor zinc protoporphyrin IX." American Journal of Physiology-Gastrointestinal and Liver Physiology 276, no. 1 (1999): G138—G145. http://dx.doi.org/10.1152/ajpgi.1999.276.1.g138.

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The putative heme oxygenase inhibitor zinc protoporphyrin IX (ZnPP IX) is known to exert diverse actions, including inhibitory action on smooth muscle relaxation by vasoactive intestinal polypeptide (VIP). The studies were performed in the opossum lower esophageal sphincter (LES) smooth muscle to determine the site of the inhibitory action of ZnPP IX in the smooth muscle relaxation by VIP. We also examined the effect of a direct Gs protein activator, cholera toxin (CTX), known to stimulate adenylate cyclase (AC). CTX caused relaxation of the LES smooth muscle by its action directly at the smoo

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16

Orino, Koichi. "Binding of Immunoglobulin G to Protoporphyrin IX and Its Derivatives: Evidence the Fab Domain Recognizes the Protoporphyrin Ring." Antibodies 8, no. 1 (2019): 6. http://dx.doi.org/10.3390/antib8010006.

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Immunoglobulin G (IgG) is known to bind zinc via the Fc domain. In this study, biotinylated protoporphyrin IX (PPIX) was incubated with human IgG and then zinc-immobilized Sepharose beads (Zn-beads) were added to the mixture. After washing the beads, the binding of biotinylated PPIX with IgG trapped on Zn-beads was detected using alkaline phosphatase (ALP)-labeled avidin. Human IgG and its Fab domain coated on microtiter plate wells recognized biotin-labeled PPIX and its derivatives, Fe-PPIX and Zn-PPIX, whereas the Fc domain showed some extent of reaction only with Zn-PPIX. When rabbit anti-b

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17

Liu, Yi, Michael J. Trnka, Shenheng Guan та ін. "A Novel Mechanism for NF-κB-activation via IκB-aggregation: Implications for Hepatic Mallory-Denk-Body Induced Inflammation". Molecular & Cellular Proteomics 19, № 12 (2020): 1968–85. http://dx.doi.org/10.1074/mcp.ra120.002316.

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Mallory-Denk-bodies (MDBs) are hepatic protein aggregates associated with inflammation both clinically and in MDB-inducing models. Similar protein aggregation in neurodegenerative diseases also triggers inflammation and NF-κB activation. However, the precise mechanism that links protein aggregation to NF-κB-activation and inflammatory response remains unclear. Herein we find that treating primary hepatocytes with MDB-inducing agents (N-methylprotoporphyrin (NMPP), protoporphyrin IX (PPIX), or Zinc-protoporphyrin IX (ZnPP)) elicited an IκBα-loss with consequent NF-κB activation. Four known mech

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18

Kumar, A., and D. Goswami. "Effect of zinc substitution on molecular dynamics of protoporphyrin-IX." Indian Journal of Physics 89, no. 11 (2015): 1183–92. http://dx.doi.org/10.1007/s12648-015-0689-5.

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19

Liu, Yang-Sui. "Zinc protoporphyrin IX enhances chemotherapeutic response of hepatoma cells to cisplatin." World Journal of Gastroenterology 20, no. 26 (2014): 8572. http://dx.doi.org/10.3748/wjg.v20.i26.8572.

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20

ISHIKAWA, Hiroya, Miyuki YOSHIHARA, Ai BABA, et al. "Formation of Zinc Protoporphyrin IX from Myoglobin in Porcine Heart Extract." Food Science and Technology Research 12, no. 2 (2006): 125–30. http://dx.doi.org/10.3136/fstr.12.125.

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21

Grossi, Alberto B., Eduardo S. P. do Nascimento, Daniel R. Cardoso, and Leif H. Skibsted. "Proteolysis involvement in zinc–protoporphyrin IX formation during Parma ham maturation." Food Research International 56 (February 2014): 252–59. http://dx.doi.org/10.1016/j.foodres.2014.01.007.

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22

Ishikawa, Hiroya, Miyuki Yoshihara, Ai Baba, et al. "Formation of Zinc Protoporphyrin IX form Myoglobin with Pork Loin Extract." Journal of the Faculty of Agriculture, Kyushu University 51, no. 1 (2006): 93–97. http://dx.doi.org/10.5109/4716.

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23

Chen, Qiuying, and Rhoda Elison Hirsch. "A direct and simultaneous detection of zinc protoporphyrin IX, free protoporphyrin IX, and fluorescent heme degradation product in red blood cell hemolysates." Free Radical Research 40, no. 3 (2006): 285–94. http://dx.doi.org/10.1080/10715760500522630.

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24

Becker, Eleonora Miquel, Signe Westermann, Mats Hansson, and Leif H. Skibsted. "Parallel enzymatic and non-enzymatic formation of zinc protoporphyrin IX in pork." Food Chemistry 130, no. 4 (2012): 832–40. http://dx.doi.org/10.1016/j.foodchem.2011.07.090.

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25

Zaitoun, Mohammed A. "Spectroscopic study of protoporphyrin IX zinc(II) encapsulated in sol–gel glass." Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 61, no. 8 (2005): 1715–19. http://dx.doi.org/10.1016/j.saa.2004.07.001.

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26

Murakami, Hiroto, Genki Nakamura, Takuro Nomura, Takeshi Miyamoto, and Naotoshi Nakashima. "Noncovalent porphyrin-functionalized single-walled carbon nanotubes: solubilization and spectral behaviors." Journal of Porphyrins and Phthalocyanines 11, no. 06 (2007): 418–27. http://dx.doi.org/10.1142/s1088424607000473.

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We describe the solubilization/dispersion of as-produced and purified single-walled carbon nanotubes (raw-SWNTs and p-SWNTs) with protoporphyrin IX derivatives and tetraphenylporphyrin iron(III) chloride, the spectral behavior of the octaalkylporphyrins-solubilized shortened-SWNTs (s-SWNTs), and the electrochemistry of a p-SWNTs/FePP cast film on a glassy carbon electrode. Transmission electron and atomic force microscopies, as well as UV-visible-near IR spectroscopy, revealed that the protoporphyrin IX derivatives individually dissolved the p-SWNTs in polar solvents under mild conditions of s

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27

Cooperman, Sharon S., Esther G. Meyron-Holtz, Hayden Olivierre-Wilson, Manik C. Ghosh, Joseph P. McConnell, and Tracey A. Rouault. "Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2." Blood 106, no. 3 (2005): 1084–91. http://dx.doi.org/10.1182/blood-2004-12-4703.

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Abstract Iron-regulatory proteins (IRPs) 1 and 2 posttranscriptionally regulate expression of transferrin receptor (TfR), ferritin, and other iron metabolism proteins. Mice with targeted deletion of IRP2 overexpress ferritin and express abnormally low TfR levels in multiple tissues. Despite this misregulation, there are no apparent pathologic consequences in tissues such as the liver and kidney. However, in the central nervous system, evidence of abnormal iron metabolism in IRP2-/- mice precedes the development of adult-onset progressive neurodegeneration, characterized by widespread axonal de

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28

Nasrulhaq-Boyce, A., W. T. Griffiths, and O. T. G. Jones. "The use of continuous assays to characterize the oxidative cyclase that synthesizes the chlorophyll isocyclic ring." Biochemical Journal 243, no. 1 (1987): 23–29. http://dx.doi.org/10.1042/bj2430023.

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A continuous spectroscopic assay has been developed for magnesium protoporphyrin monomethyl ester oxidative cyclase, which records either the dark formation of both free and protein-bound magnesium phaeoporphyrin or, following flash illumination, its corresponding chlorin. The properties of the enzyme were studied in wheat etioplasts. When plastids were pre-illuminated in the presence of NADPH all endogenous protochlorophyllide was converted into chlorophyllide and the product of dark incubation with magnesium protoporphyrin monomethyl ester was protein-bound magnesium 2-vinyl phaeoporphyrin a

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29

Linden, D. J., K. Narasimhan, and D. Gurfel. "Protoporphyrins modulate voltage-gated Ca current in AtT-20 pituitary cells." Journal of Neurophysiology 70, no. 6 (1993): 2673–77. http://dx.doi.org/10.1152/jn.1993.70.6.2673.

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1. Zinc-protoporphyrin-IX (ZnPP-IX) is an inhibitor of the enzyme heme-oxygenase-2 (HO-2) and consequently has been used to examine the role of carbon monoxide production in neural tissues. We have measured voltage-gated Ca current in AtT-20 pituitary cells using the whole-cell patch-clamp technique and have assessed the effects of extracellularly applied ZnPP-IX and related compounds. 2. Ca currents evoked by depolarizing steps from a holding potential of -90 mV were of the high-threshold, slowly inactivating type. Fifty-six percent of this current was blocked by 10 microM nifedipine and 16%

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30

Kumari, Rina, Sumit Singh, Mohan Monisha, et al. "Hierarchical coassembly of DNA–triptycene hybrid molecular building blocks and zinc protoporphyrin IX." Beilstein Journal of Nanotechnology 7 (May 12, 2016): 697–707. http://dx.doi.org/10.3762/bjnano.7.62.

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Herein, we describe the successful construction of composite DNA nanostructures by the self-assembly of complementary symmetrical 2,6,14-triptycenetripropiolic acid (TPA)–DNA building blocks and zinc protoporphyrin IX (Zn PpIX). DNA–organic molecule scaffolds for the composite DNA nanostructure were constructed through covalent conjugation of TPA with 5′-C12-amine-terminated modified single strand DNA (ssDNA) and its complementary strand. The repeated covalent conjugation of TPA with DNA was confirmed by using denaturing polyacrylamide gel electrophoresis (PAGE), reverse-phase high-performance

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31

WAKAMATSU, Jun-ichi, Juichi UEMURA, Hiroko ODAGIRI, et al. "Formation of zinc protoporphyrin IX in Parma-like ham without nitrate or nitrite." Animal Science Journal 80, no. 2 (2009): 198–205. http://dx.doi.org/10.1111/j.1740-0929.2008.00619.x.

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32

Bellingham, R. M. A., A. H. Gibbs, F. de Matteis, L. Y. Lian, and G. C. K. Roberts. "Determination of the structure of an N-substituted protoporphyrin isolated from the livers of griseofulvin-fed mice." Biochemical Journal 307, no. 2 (1995): 505–12. http://dx.doi.org/10.1042/bj3070505.

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Feeding mice with griseofulvin, a widely used anti-fungal agent which induces protoporphyria as a side-effect, leads to the formation in the liver of two green pigments which have been shown to be porphyrin adducts. In this work, the major porphyrin adduct isolated from the livers of griseofulvin-fed mice has been characterized structurally using one- and two-dimensional NMR spectroscopy. The adduct was shown to be an N-alkylated protoporphyrin IX in which the whole of griseofulvin (less a hydrogen atom) is attached to a pyrrole ring nitrogen of the porphyrin. It was shown that the drug-to-por

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33

Palma, JF, X. Gao, CH Lin, S. Wu, and WB Solomon. "Iron protoporphyrin IX (hemin) but not tin or zinc protoporphyrin IX can stimulate gene expression in K562 cells from enhancer elements containing binding sites for NF-E2." Blood 84, no. 4 (1994): 1288–97. http://dx.doi.org/10.1182/blood.v84.4.1288.1288.

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Abstract Many genes whose transcription is erythroid-specific contain enhancer or promoter elements that bind the transcription factor NF-E2. Hemin induction increases the expression of globin genes in the human erythroleukemia cell line K562, and increases the expression of reporters gene regulated by an enhancer elements containing binding sites for NF-E2. The failure of metalloporphyrins other than hemin to stimulate the transient expression of a CAT reporter gene linked to an enhancer element containing a binding site for NF-E2 was correlated with their failure to induce benzidine-positive

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34

Palma, JF, X. Gao, CH Lin, S. Wu, and WB Solomon. "Iron protoporphyrin IX (hemin) but not tin or zinc protoporphyrin IX can stimulate gene expression in K562 cells from enhancer elements containing binding sites for NF-E2." Blood 84, no. 4 (1994): 1288–97. http://dx.doi.org/10.1182/blood.v84.4.1288.bloodjournal8441288.

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Many genes whose transcription is erythroid-specific contain enhancer or promoter elements that bind the transcription factor NF-E2. Hemin induction increases the expression of globin genes in the human erythroleukemia cell line K562, and increases the expression of reporters gene regulated by an enhancer elements containing binding sites for NF-E2. The failure of metalloporphyrins other than hemin to stimulate the transient expression of a CAT reporter gene linked to an enhancer element containing a binding site for NF-E2 was correlated with their failure to induce benzidine-positive K562 cel

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35

Naik, Jay S., and Benjimen R. Walker. "Heme oxygenase-mediated vasodilation involves vascular smooth muscle cell hyperpolarization." American Journal of Physiology-Heart and Circulatory Physiology 285, no. 1 (2003): H220—H228. http://dx.doi.org/10.1152/ajpheart.01131.2002.

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Chronic hypoxia is associated with both blunted agonist-induced and myogenic vascular reactivity and is possibly due to an enhanced production of heme oxygenase (HO)-derived carbon monoxide (CO). However, the mechanism of endogenous CO-meditated vasodilation remains unclear. Isolated pressurized mesenteric arterioles from chronically hypoxic rats were administered the HO substrate heme-l-lysinate (HLL) in the presence or absence of iberiotoxin, 1 H-[1,2,4]oxadiazolo[4,3- a]quinoxalin-1-one (ODQ), ryanodine, or free radical spin traps ( N- tert-butyl-α-phenylnitrone and 4,5-dihydroxy-1,3-benzen

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36

Takizawa, Shunya, Hitoshi Fujita, Saori Ogawa, and Yukito Shinohara. "Carbon Monoxide, a Novel Neural Messenger, Does Not Modulate Extracellular Glutamate Concentration in Forebrain Ischemia." Journal of Cerebral Blood Flow & Metabolism 16, no. 5 (1996): 1075–78. http://dx.doi.org/10.1097/00004647-199609000-00033.

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We investigated the role of carbon monoxide as a neural modulator of extracellular glutamate concentration in rat hippocampus CA1 in transient forebrain ischemia by using metalloporphyrins, which block the production of carbon monoxide through the inhibition of heme oxygenase (HO) activity. Infusion of 10 and 100 μ M zinc protoporphyrin IX, which inhibits nitric oxide synthase activity as well as HO activity, significantly increased glutamate concentration compared with that on the vehicle-treated side. However, infusion of 100 μ M tin mesoporphyrin IX, which inhibits only HO activity, did not

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Metz, Richard, James B. DuHadaway, Sonja Rust, et al. "Zinc Protoporphyrin IX Stimulates Tumor Immunity by Disrupting the Immunosuppressive Enzyme Indoleamine 2,3-Dioxygenase." Molecular Cancer Therapeutics 9, no. 6 (2010): 1864–71. http://dx.doi.org/10.1158/1535-7163.mct-10-0185.

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Akter, Mofassara, Akiko Shiraishi, Haruto Kumura, Toru Hayakawa, and Jun‐ichi Wakamatsu. "Investigation of contributors to zinc protoporphyrin IX formation at optimum pH 5.5 in pork." Animal Science Journal 90, no. 6 (2019): 774–80. http://dx.doi.org/10.1111/asj.13201.

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Zigrino, Addolorata, Valentina Leo, Giuseppe Renna, Monica Montagnani, and Maria Antonietta De Salvia. "Hemin and Zinc Protoporphyrin IX Affect Granisetron Constipating Effects In Vitro and In Vivo." ISRN Gastroenterology 2013 (June 20, 2013): 1–9. http://dx.doi.org/10.1155/2013/612037.

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Granisetron is a 5-HT3 receptors antagonist used in the management of emesis associated with anticancer chemotherapy. It affects intestinal motility with constipating effect. Since the pathway heme oxygenase/carbon monoxide (HO/CO) is involved in gastrointestinal motility, we evaluated the possible interplay between granisetron and agents affecting HO/CO pathways such as zinc protoporphyrin IX (ZnPPIX), an HO inhibitor, or hemin, an HO-1 inducer. ZnPPIX (10 µM) or hemin (10 µM), but not granisetron (0.1, 0.3, 1 µM), affected spontaneous basal activity recorded in rat duodenal strips, in noncho

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40

Liu, Jung-Tung, Huey-Yi Chen, Wen-Chi Chen, Kee-Ming Man, and Yung-Hsiang Chen. "Red Yeast Rice Protects Circulating Bone Marrow-Derived Proangiogenic Cells against High-Glucose-Induced Senescence and Oxidative Stress: The Role of Heme Oxygenase-1." Oxidative Medicine and Cellular Longevity 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/3831750.

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The inflammation and oxidative stress of bone marrow-derived proangiogenic cells (PACs), also named endothelial progenitor cells, triggered by hyperglycemia contributes significantly to vascular dysfunction. There is supporting evidence that the consumption of red yeast rice (RYR; Monascus purpureus-fermented rice) reduces the vascular complications of diabetes; however, the underlying mechanism remains unclear. This study aimed to elucidate the effects of RYR extract in PACs, focusing particularly on the role of a potent antioxidative enzyme, heme oxygenase-1 (HO-1). We found that treatment w

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41

Asojo, Oluwatoyin A., and Christopher Ceccarelli. "Structure of glutathioneS-transferase 1 from the major human hookworm parasiteNecator americanus(Na-GST-1) in complex with glutathione." Acta Crystallographica Section F Structural Biology Communications 70, no. 9 (2014): 1162–66. http://dx.doi.org/10.1107/s2053230x1401646x.

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GlutathioneS-transferase 1 fromNecator americanus(Na-GST-1) is a vaccine candidate for hookworm infection that has a high affinity for heme and metal porphyrins. As part of attempts to clarify the mechanism of heme detoxification by hookworm GSTs, co-crystallization and soaking studies ofNa-GST-1 with the heme-like molecules protoporphyrin IX disodium salt, hematin and zinc protoporphyrin were undertaken. While these studies did not yield the structure of the complex ofNa-GST-1 with any of these molecules, co-crystallization experiments resulted in the first structures of the complex ofNa-GST-

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42

Yu, Jianbo, Jia Shi, Dan Wang, et al. "Heme Oxygenase-1/Carbon Monoxide-regulated Mitochondrial Dynamic Equilibrium Contributes to the Attenuation of Endotoxin-induced Acute Lung Injury in Rats and in Lipopolysaccharide-activated Macrophages." Anesthesiology 125, no. 6 (2016): 1190–201. http://dx.doi.org/10.1097/aln.0000000000001333.

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Abstract Background Sepsis-associated acute lung injury remains the major cause of mortality in critically ill patients and is characterized by marked oxidative stress and mitochondrial dysfunction. Mitochondrial dynamics are indispensable for functional integrity. Additionally, heme oxygenase (HO)-1/carbon monoxide conferred cytoprotection against end-organ damage during endotoxic shock. Herein, we tested the hypothesis that HO-1/carbon monoxide played a critical role in maintaining the dynamic process of mitochondrial fusion/fission to mitigate lung injury in Sprague-Dawley rats or RAW 264.7

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43

Biswas, Sudipta, Debdyuti Mukherjee, Swati De, and Arunkumar Kathiravan. "Probing the Highly Efficient Electron Transfer Dynamics between Zinc Protoporphyrin IX and Sodium Titanate Nanosheets." Journal of Physical Chemistry A 120, no. 36 (2016): 7121–29. http://dx.doi.org/10.1021/acs.jpca.6b06363.

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Komatsu, Teruyuki, Rong-Min Wang, Patricia A. Zunszain, Stephen Curry, and Eishun Tsuchida. "Photosensitized Reduction of Water to Hydrogen Using Human Serum Albumin Complexed with Zinc−Protoporphyrin IX." Journal of the American Chemical Society 128, no. 50 (2006): 16297–301. http://dx.doi.org/10.1021/ja0656806.

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Stefan‐van Staden, Raluca‐Ioana, and Mariana Mincu. "Nanocarbon Materials Modified with the Zinc Complex of Protoporphyrin IX, Recognized Antibiotics in Water Samples." Electroanalysis 32, no. 5 (2020): 1060–64. http://dx.doi.org/10.1002/elan.201900688.

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Sharp, R. Eryl, James R. Diers, David F. Bocian, and P. Leslie Dutton. "Differential Binding of Iron(III) and Zinc(II) Protoporphyrin IX to Synthetic Four-Helix Bundles." Journal of the American Chemical Society 120, no. 28 (1998): 7103–4. http://dx.doi.org/10.1021/ja980432y.

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Li, Chun, and Toyoko Imae. "Protoporphyrin IX Zinc(II) Organization at the Air/Water Interface and Its Langmuir−Blodgett Films." Langmuir 19, no. 3 (2003): 779–84. http://dx.doi.org/10.1021/la026524p.

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Iyer, Jayasree K., Lirong Shi, Anuraj H. Shankar, and David J. Sullivan. "Zinc Protoporphyrin IX Binds Heme Crystals to Inhibit the Process of Crystallization in Plasmodium falciparum." Molecular Medicine 9, no. 5-8 (2003): 175–82. http://dx.doi.org/10.1007/bf03402182.

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Abo El Gheit, R., and MN Emam. "Targeting heme oxygenase-1 in early diabetic nephropathy in streptozotocin-induced diabetic rats." Physiology International 103, no. 4 (2016): 413–27. http://dx.doi.org/10.1556/2060.103.2016.4.001.

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Abstract:

Diabetic nephropathy (DN) is one of the most common microvascular diabetic complications. This study was designed to evaluate the possible protective effect and underlying mechanisms of HO-1 induction in streptozotocin (STZ)-induced early DN in rats. The diabetic rats were divided into three groups: STZ-diabetic, cobalt protoporphyrin (CoPP)-treated diabetic, and zinc protoporphyrin IX (ZnPP)-treated diabetic groups. Compared to the STZ-diabetic group, CoPP-induced HO-1 upregulation improved the diabetic state and renal functional parameters, suppressed the renal proinflammatory marker, NF-κB,

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Grover, Theresa R., Robyn L. Rairigh, Jeanne P. Zenge, Steven H. Abman, and John P. Kinsella. "Inhaled carbon monoxide does not cause pulmonary vasodilation in the late-gestation fetal lamb." American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 4 (2000): L779—L784. http://dx.doi.org/10.1152/ajplung.2000.278.4.l779.

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Abstract:

As observed with nitric oxide (NO), carbon monoxide (CO) binds and may activate soluble guanylate cyclase and increase cGMP levels in smooth muscle cells in vitro. Because inhaled NO (INO) causes potent and sustained pulmonary vasodilation, we hypothesized that inhaled CO (ICO) may have similar effects on the perinatal lung. To determine whether ICOcan lower pulmonary vascular resistance (PVR) during the perinatal period, we studied the effects of ICOon late-gestation fetal lambs. Catheters were placed in the main pulmonary artery, left pulmonary artery (LPA), aorta, and left atrium to measure

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