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Journal articles on the topic 'Heme-binding protein 2'

Author: Grafiati

Published: 11 March 2023

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1

Liu, Liu, Arti B. Dumbrepatil, Angela S. Fleischhacker, E. Neil G. Marsh, and Stephen W. Ragsdale. "Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site." Journal of Biological Chemistry 295, no. 50 (2020): 17227–40. http://dx.doi.org/10.1074/jbc.ra120.014919.

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Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for maintaining heme homeostasis. HO1 expression is transcriptionally regulated; however, HO2 expression is constitutive. How the cellular levels and activity of HO2 are regulated remains unclear. Here, we elucidate the mechanism of post-translational regulation of cellular HO2 levels by heme. We find that, under heme-deficient conditions, HO2 is destabili

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2

Nakamura, Nozomi, Yoichi Naoe, Akihiro Doi, Yoshitsugu Shiro, and Hiroshi Sugimoto. "Conformational change of periplasmic heme-binding protein in ABC transporter." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1496. http://dx.doi.org/10.1107/s2053273314085039.

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Iron is one of the essential elements for all living organisms. Pathogenic bacteria acquire heme from the host proteins as an iron source. Gram-negative opportunistic pathogen, Burkholderia cenocepacia have ATP-binding cassette (ABC) transporter BhuUV-T complex to permeate heme through inner membrane. BhuT, periplasmic binding protein (PBP), bind and deliver heme(s) to inner membrane transporter BhuUV complex. BhuUV is 2:2 complex of the transmembrane permease subunit and cytoplasmic ATP-binding subunit which couple ATP hydrolysis to solute translocation. The molecular level mechanism of heme

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3

Nath, Karl A., Joseph P. Grande, John D. Belcher, et al. "Antithrombotic effects of heme-degrading and heme-binding proteins." American Journal of Physiology-Heart and Circulatory Physiology 318, no. 3 (2020): H671—H681. http://dx.doi.org/10.1152/ajpheart.00280.2019.

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In the murine venous thrombosis model induced by ligation of the inferior vena cava (IVCL), genetic deficiency of heme oxygenase-1 (HO-1) increases clot size. This study examined whether induction of HO-1 or administration of its products reduces thrombosis. Venous HO-1 upregulation by gene delivery reduced clot size, as did products of HO activity, biliverdin, and carbon monoxide. Induction of HO-1 by hemin reduced clot formation, clot size, and upregulation of plasminogen activator inhibitor-1 (PAI-1) that occurs in the IVCL model, while leaving urokinase plasminogen activator (uPA) and tiss

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4

El-Mashtoly, Samir F., and Teizo Kitagawa. "Structural chemistry involved in information detection and transmission by gas sensor heme proteins: Resonance Raman investigation." Pure and Applied Chemistry 80, no. 12 (2008): 2667–78. http://dx.doi.org/10.1351/pac200880122667.

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A variety of heme-containing gas sensor proteins have been discovered by gene analysis from bacteria to mammals. In general, these proteins are composed of an N-terminal heme-containing sensor domain and a C-terminal catalytic domain. Binding of O2, CO, or NO to the heme causes a change in the structure of heme, which alters the protein conformation in the vicinity of the heme, and the conformational change is propagated to the catalytic domain, leading to regulation of the protein activity. This mini-review summarizes the recent resonance Raman studies obtained with both visible and UV excita

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5

Tiedemann, Michael T., Naomi Muryoi, David E. Heinrichs, and Martin J. Stillman. "Characterization of IsdH (NEAT domain 3) and IsdB (NEAT domain 2) in Staphylococcus aureus by magnetic circular dichroism spectroscopy and electrospray ionization mass spectrometry." Journal of Porphyrins and Phthalocyanines 13, no. 10 (2009): 1006–16. http://dx.doi.org/10.1142/s1088424609001352.

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Absorption and magnetic circular dichroism (MCD) spectra, together with electrospray ionization mass spectral (ESI-MS) data are reported for the first two proteins in the Isd sequence of proteins in Staphylococcus aureus. IsdH-NEAT domain 3 (IsdH-N3) and IsdB-NEAT domain 2 (IsdB-N2) are considered to be involved in heme transport following heme scavenging from the hemoglobin of the host. The ESI-MS data show that a single heme binds to each of these NEAT domains. The charge states of the native proteins indicate that there is minimal change in conformation when heme binds to the heme-free nati

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6

Freeman, Samuel L., Hanna Kwon, Nicola Portolano, et al. "Heme binding to human CLOCK affects interactions with the E-box." Proceedings of the National Academy of Sciences 116, no. 40 (2019): 19911–16. http://dx.doi.org/10.1073/pnas.1905216116.

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The circadian clock is an endogenous time-keeping system that is ubiquitous in animals and plants as well as some bacteria. In mammals, the clock regulates the sleep–wake cycle via 2 basic helix–loop–helix PER-ARNT-SIM (bHLH-PAS) domain proteins—CLOCK and BMAL1. There is emerging evidence to suggest that heme affects circadian control, through binding of heme to various circadian proteins, but the mechanisms of regulation are largely unknown. In this work we examine the interaction of heme with human CLOCK (hCLOCK). We present a crystal structure for the PAS-A domain of hCLOCK, and we examine

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7

Fleischhacker, Angela S., Amanda L. Gunawan, Brent A. Kochert, et al. "The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation." Journal of Biological Chemistry 295, no. 16 (2020): 5177–91. http://dx.doi.org/10.1074/jbc.ra120.012803.

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Heme-regulatory motifs (HRMs) are present in many proteins that are involved in diverse biological functions. The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme. Heme binding to the HRMs occurs independently of the HO2 catalytic active site in the core of the protein, where heme binds with high affinity and is degraded to biliverdin. Here, we describe the reversible, protein-mediated transfer of heme between the HRMs and the HO2 core. Using hydrogen-deuterium e

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8

Lechuga, Guilherme C., Franklin Souza-Silva, Carolina Q. Sacramento, et al. "SARS-CoV-2 Proteins Bind to Hemoglobin and Its Metabolites." International Journal of Molecular Sciences 22, no. 16 (2021): 9035. http://dx.doi.org/10.3390/ijms22169035.

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(1) Background: coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has been linked to hematological dysfunctions, but there are little experimental data that explain this. Spike (S) and Nucleoprotein (N) proteins have been putatively associated with these dysfunctions. In this work, we analyzed the recruitment of hemoglobin (Hb) and other metabolites (hemin and protoporphyrin IX-PpIX) by SARS-Cov2 proteins using different approaches. (2) Methods: shotgun proteomics (LC–MS/MS) after affinity column adsorption identified hemin-binding SAR

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9

Jeong, Jinsook, Tracey A. Rouault, and Rodney L. Levine. "Identification of a Heme-sensing Domain in Iron Regulatory Protein 2." Journal of Biological Chemistry 279, no. 44 (2004): 45450–54. http://dx.doi.org/10.1074/jbc.m407562200.

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Iron regulatory protein 2 coordinates the cellular regulation of iron metabolism by binding to iron-responsive elements in mRNA. The protein is synthesized constitutively but is rapidly degraded when iron stores are replete. The mechanisms that prevent degradation during iron deficiency or promote degradation during iron sufficiency are not delineated. Iron regulatory protein 2 contains a domain not present in the closely related iron regulatory protein 1, and we found that this domain binds heme with high affinity. A cysteine within the domain is axially liganded to the heme, as occurs in cyt

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10

Yang, Jianhua, Kevin D. Kim, Andrew Lucas, et al. "A Novel Heme-Regulatory Motif Mediates Heme-Dependent Degradation of the Circadian Factor Period 2." Molecular and Cellular Biology 28, no. 15 (2008): 4697–711. http://dx.doi.org/10.1128/mcb.00236-08.

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ABSTRACT Although efforts have been made to identify circadian-controlled genes regulating cell cycle progression and cell death, little is known about the metabolic signals modulating circadian regulation of gene expression. We identify heme, an iron-containing prosthetic group, as a regulatory ligand controlling human Period-2 (hPer2) stability. Furthermore, we define a novel heme-regulatory motif within the C terminus of hPer2 (SC841PA) as necessary for heme binding and protein destabilization. Spectroscopy reveals that whereas the PAS domain binds to both the ferric and ferrous forms of he

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11

Franceschi, Lucia De, Mariarita Bertoldi, Maria Domenica Cappellini та ін. "OXIDATIVE STRESS MODULATES HEME LEVELS and INDUCES PEROXIREDOXIN-2 IN β THALASSEMIC ERYTHROPOIESIS as NOVEL CYTOPROTECTIVE RESPONSE". Blood 116, № 21 (2010): 4266. http://dx.doi.org/10.1182/blood.v116.21.4266.4266.

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Abstract Abstract 4266 Beta thalassemia (β-thal) syndromes are worldwide distributed congenital red cell disorders. Increased levels of reactive-oxygen-species (ROS) have been reported to contribute to anemia in β-thal but the mechanism(s) involved in cell protection against ROS damage has only partially investigated. Here, we studied in vitro normal and β-thal erythropoiesis in erythroid cell cultures from CD34+ cells isolated from peripheral blood from adult normal volunteers and from homozygous (bcod39) b-thalassemia patients. We showed increased ROS production in β-thal erythropoiesis and

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12

Choi, Clara Y. H., Jose F. Cerda, Hsiu-An Chu, Gerald T. Babcock, and Michael A. Marletta. "Spectroscopic Characterization of the Heme-Binding Sites inPlasmodium falciparumHistidine-Rich Protein 2†." Biochemistry 38, no. 51 (1999): 16916–24. http://dx.doi.org/10.1021/bi991665k.

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13

Airola, Michael V., Jing Du, John H. Dawson, and Brian R. Crane. "Heme Binding to the Mammalian Circadian Clock Protein Period 2 Is Nonspecific." Biochemistry 49, no. 20 (2010): 4327–38. http://dx.doi.org/10.1021/bi901945w.

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14

Uchida, Takeshi, Julie M. Stevens, Oliver Daltrop, et al. "The Interaction of Covalently Bound Heme with the CytochromecMaturation Protein CcmE." Journal of Biological Chemistry 279, no. 50 (2004): 51981–88. http://dx.doi.org/10.1074/jbc.m408963200.

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The heme chaperone CcmE is a novel protein that binds heme covalently via a histidine residue as part of its essential function in the process of cytochromecbiogenesis in many bacteria as well as plant mitochondria. In the continued absence of a structure of the holoform of CcmE, identification of the heme ligands is an important step in understanding the molecular function of this protein and the role of covalent heme binding to CcmE during the maturation ofc-type cytochromes. In this work, we present spectroscopic data that provide insight into the ligation of the heme iron in the soluble do

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15

Zenke-Kawasaki, Yukari, Yoshihiro Dohi, Yasutake Katoh, et al. "Heme Induces Ubiquitination and Degradation of the Transcription Factor Bach1." Molecular and Cellular Biology 27, no. 19 (2007): 6962–71. http://dx.doi.org/10.1128/mcb.02415-06.

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ABSTRACT The transcription repressor Bach1 is a sensor and effector of heme that regulates the expression of heme oxygenase 1 and globin genes. Heme binds to Bach1, inhibiting its DNA binding activity and inducing its nuclear export. We found that hemin further induced the degradation of endogenous Bach1 in NIH 3T3 cells, murine embryonic fibroblasts, and murine erythroleukemia cells. In contrast, succinylacetone, an inhibitor of heme synthesis, caused accumulation of Bach1 in murine embryonic fibroblasts, indicating that physiological levels of heme regulated the Bach1 turnover. Polyubiquitin

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16

Hopp, Marie-Thérèse, Daniel Domingo-Fernández, Yojana Gadiya, et al. "Linking COVID-19 and Heme-Driven Pathophysiologies: A Combined Computational–Experimental Approach." Biomolecules 11, no. 5 (2021): 644. http://dx.doi.org/10.3390/biom11050644.

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The SARS-CoV-2 outbreak was declared a worldwide pandemic in 2020. Infection triggers the respiratory tract disease COVID-19, which is accompanied by serious changes in clinical biomarkers such as hemoglobin and interleukins. The same parameters are altered during hemolysis, which is characterized by an increase in labile heme. We present two computational–experimental approaches aimed at analyzing a potential link between heme-related and COVID-19 pathophysiologies. Herein, we performed a detailed analysis of the common pathways induced by heme and SARS-CoV-2 by superimposition of knowledge g

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17

Chen, Jane-Jane. "Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias". Blood 109, № 7 (2006): 2693–99. http://dx.doi.org/10.1182/blood-2006-08-041830.

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Abstract During erythroid differentiation and maturation, it is critical that the 3 components of hemoglobin, α-globin, β-globin, and heme, are made in proper stoichiometry to form stable hemoglobin. Heme-regulated translation mediated by the heme-regulated inhibitor kinase (HRI) provides one major mechanism that ensures balanced synthesis of globins and heme. HRI phosphorylates the α-subunit of eukaryotic translational initiation factor 2 (eIF2α) in heme deficiency, thereby inhibiting protein synthesis globally. In this manner, HRI serves as a feedback inhibitor of globin synthesis by sensing

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18

Shibata, Tomokazu, Eisuke Furuichi, Kiyohiro Imai, Akihiro Suzuki, and Yasuhiko Yamamoto. "Effects of heme modification on oxygen affinity and cooperativity of human adult hemoglobin." Journal of Porphyrins and Phthalocyanines 19, no. 01-03 (2015): 301–7. http://dx.doi.org/10.1142/s1088424615500200.

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We substituted strongly electron-withdrawing trifluoromethyl ( CF 3) group(s) as heme side chain(s) of human adult hemoglobin (Hb) to achieve large alterations of the heme electronic structure, in order to elucidate the relationship between the oxygen ( O 2) binding properties of Hb and the electronic properties of heme peripheral side chains. The obtained results were compared with those of similar studies performed on myoglobin (Mb), e.g. (Nishimura R, Matsumoto D, Shibata T, Yanagisawa S, Ogura T, Tai H, Matsuo T, Hirota S, Neya S, Suzuki A, and Yamamoto Y. Inorg. Chem. 2014; 53: 9156–9165)

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19

Crosby, John S., Peter J. Chefalo, Irene Yeh та ін. "Regulation of hemoglobin synthesis and proliferation of differentiating erythroid cells by heme-regulated eIF-2α kinase". Blood 96, № 9 (2000): 3241–48. http://dx.doi.org/10.1182/blood.v96.9.3241.

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Abstract Protein synthesis in reticulocytes depends on the availability of heme. In heme deficiency, inhibition of protein synthesis correlates with the activation of heme-regulated eIF-2α kinase (HRI), which blocks the initiation of protein synthesis by phosphorylating eIF-2α. HRI is a hemoprotein with 2 distinct heme-binding domains. Heme negatively regulates HRI activity by binding directly to HRI. To further study the physiological function of HRI, the wild-type (Wt) HRI and dominant-negative inactive mutants of HRI were expressed by retrovirus-mediated transfer in both non-erythroid NIH 3

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20

Crosby, John S., Peter J. Chefalo, Irene Yeh та ін. "Regulation of hemoglobin synthesis and proliferation of differentiating erythroid cells by heme-regulated eIF-2α kinase". Blood 96, № 9 (2000): 3241–48. http://dx.doi.org/10.1182/blood.v96.9.3241.h8003241_3241_3248.

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Protein synthesis in reticulocytes depends on the availability of heme. In heme deficiency, inhibition of protein synthesis correlates with the activation of heme-regulated eIF-2α kinase (HRI), which blocks the initiation of protein synthesis by phosphorylating eIF-2α. HRI is a hemoprotein with 2 distinct heme-binding domains. Heme negatively regulates HRI activity by binding directly to HRI. To further study the physiological function of HRI, the wild-type (Wt) HRI and dominant-negative inactive mutants of HRI were expressed by retrovirus-mediated transfer in both non-erythroid NIH 3T3 and mo

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21

Varfaj, Fatbardha, Jed N. Lampe, and Paul R. Ortiz de Montellano. "Role of Cysteine Residues in Heme Binding to Human Heme Oxygenase-2 Elucidated by Two-dimensional NMR Spectroscopy." Journal of Biological Chemistry 287, no. 42 (2012): 35181–91. http://dx.doi.org/10.1074/jbc.m112.378042.

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Human heme oxygenases 1 and 2 (HO-1 and HO-2) degrade heme in the presence of oxygen and NADPH-cytochrome P450 reductase, producing ferrous iron, CO, and biliverdin. HO-1 is an inducible enzyme, but HO-2 is constitutively expressed in selected tissues and is involved in signaling and regulatory processes. HO-2 has three cysteine residues that have been proposed to modulate the affinity for heme, whereas HO-1 has none. Here we use site-specific mutagenesis and two-dimensional NMR of l-[3-13C]cysteine-labeled proteins to determine the redox state of the individual cysteines in HO-2 and assess th

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22

Choi, Clara Y. H., Eric L. Schneider, Jin M. Kim, et al. "Interference with Heme Binding to Histidine-Rich Protein-2 as an Antimalarial Strategy." Chemistry & Biology 9, no. 8 (2002): 881–89. http://dx.doi.org/10.1016/s1074-5521(02)00183-7.

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23

Kranz, Robert G., Cynthia Richard-Fogal, John-Stephen Taylor, and Elaine R. Frawley. "Cytochrome c Biogenesis: Mechanisms for Covalent Modifications and Trafficking of Heme and for Heme-Iron Redox Control." Microbiology and Molecular Biology Reviews 73, no. 3 (2009): 510–28. http://dx.doi.org/10.1128/mmbr.00001-09.

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SUMMARY Heme is the prosthetic group for cytochromes, which are directly involved in oxidation/reduction reactions inside and outside the cell. Many cytochromes contain heme with covalent additions at one or both vinyl groups. These include farnesylation at one vinyl in hemes o and a and thioether linkages to each vinyl in cytochrome c (at CXXCH of the protein). Here we review the mechanisms for these covalent attachments, with emphasis on the three unique cytochrome c assembly pathways called systems I, II, and III. All proteins in system I (called Ccm proteins) and system II (Ccs proteins) a

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24

Alvarado, Gerardo, Attila Tóth, Éva Csősz, et al. "Heme-Induced Oxidation of Cysteine Groups of Myofilament Proteins Leads to Contractile Dysfunction of Permeabilized Human Skeletal Muscle Fibres." International Journal of Molecular Sciences 21, no. 21 (2020): 8172. http://dx.doi.org/10.3390/ijms21218172.

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Heme released from red blood cells targets a number of cell components including the cytoskeleton. The purpose of the present study was to determine the impact of free heme (20–300 µM) on human skeletal muscle fibres made available during orthopedic surgery. Isometric force production and oxidative protein modifications were monitored in permeabilized skeletal muscle fibre segments. A single heme exposure (20 µM) to muscle fibres decreased Ca2+-activated maximal (active) force (Fo) by about 50% and evoked an approximately 3-fold increase in Ca2+-independent (passive) force (Fpassive). Oxidatio

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25

Detzel, Milena Sophie, Benjamin Franz Schmalohr, Francèl Steinbock, et al. "Revisiting the interaction of heme with hemopexin." Biological Chemistry 402, no. 6 (2021): 675–91. http://dx.doi.org/10.1515/hsz-2020-0347.

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Abstract In hemolytic disorders, erythrocyte lysis results in massive release of hemoglobin and, subsequently, toxic heme. Hemopexin is the major protective factor against heme toxicity in human blood and currently considered for therapeutic use. It has been widely accepted that hemopexin binds heme with extraordinarily high affinity of <1 pM in a 1:1 ratio. However, several lines of evidence point to a higher stoichiometry and lower affinity than determined 50 years ago. Here, we re-analyzed these data. SPR and UV/Vis spectroscopy were used to monitor the interaction of heme with the human

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26

Lemli, Beáta, Zuzana Lomozová, Tamás Huber, András Lukács, and Miklós Poór. "Effects of Heme Site (FA1) Ligands Bilirubin, Biliverdin, Hemin, and Methyl Orange on the Albumin Binding of Site I Marker Warfarin: Complex Allosteric Interactions." International Journal of Molecular Sciences 23, no. 22 (2022): 14007. http://dx.doi.org/10.3390/ijms232214007.

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Human serum albumin (HSA) is the most abundant plasma protein in circulation. The three most important drug-binding sites on HSA are Sudlow’s Site I (subdomain IIA), Sudlow’s Site II (subdomain IIIA), and Heme site (subdomain IB). Heme site and Site I are allosterically coupled; therefore, their ligands may be able to allosterically modulate the binding affinity of each other. In this study, the effects of four Heme site ligands (bilirubin, biliverdin, hemin, and methyl orange) on the interaction of the Site I ligand warfarin with HSA were tested, employing fluorescence spectroscopic, ultrafil

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27

Matsuura, Kenji, Mieko Otani, Masaoki Takano, Keiichi Kadoyama, and Shogo Matsuyama. "Proteomic Analysis of Hippocampus and Cortex in Streptozotocin-Induced Diabetic Model Mice Showing Dementia." Journal of Diabetes Research 2018 (2018): 1–11. http://dx.doi.org/10.1155/2018/8953015.

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Aim. Diabetes with its associated hyperglycemia induces various type of peripheral damage and also impairs the central nervous system (CNS). This study is aimed at clarifying the precise mechanism of diabetes-induced dementia as an impairment of CNS. Methods. The proteomic analysis of the hippocampus and cortex in streptozotocin- (STZ-) treated mouse diabetic model showing dementia was performed using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (n=3/group). Results. Significant changes in the expression of 32 proteins and 7 phosphoproteins were observed in the hipp

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28

De Simone, Giovanna, Paolo Ascenzi, Alessandra di Masi, and Fabio Polticelli. "Nitrophorins and nitrobindins: structure and function." Biomolecular Concepts 8, no. 2 (2017): 105–18. http://dx.doi.org/10.1515/bmc-2017-0013.

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AbstractClassical all α-helical globins are present in all living organisms and are ordered in three lineages: (i) flavohemoglobins and single domain globins, (ii) protoglobins and globin coupled sensors and (iii) truncated hemoglobins, displaying the 3/3 or the 2/2 all α-helical fold. However, over the last two decades, all β-barrel and mixed α-helical-β-barrel heme-proteins displaying heme-based functional properties (e.g. ligand binding, transport and sensing) closely similar to those of all α-helical globins have been reported. Monomeric nitrophorins (NPs) and α1-microglobulin (α1-m), belo

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29

Nath, Karl A. "Heme, Iron, and the Kidney." Blood 116, no. 21 (2010): SCI—26—SCI—26. http://dx.doi.org/10.1182/blood.v116.21.sci-26.sci-26.

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Abstract Abstract SCI-26 The kidney is often the target of injury by heme proteins and states of iron overload. Exogenous heme proteins, such as hemoglobin delivered to the kidney in hemolytic states, or myoglobin imposed upon the kidney following rhabdomyolysis, can injure the kidney via pathways that include vasoconstriction, direct cytotoxicity, and tubular cast formation. The former two pathways critically involve the heme prosthetic group: heme can bind vasodilator gases such as nitric oxide and carbon monoxide, while free heme can be cytotoxic because it is lipophilic, lipid membrane-tra

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30

Szigeti, Andras, Szabolcs Bellyei, Balazs Gasz, et al. "Induction of necrotic cell death and mitochondrial permeabilization by heme binding protein 2/SOUL." FEBS Letters 580, no. 27 (2006): 6447–54. http://dx.doi.org/10.1016/j.febslet.2006.10.067.

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Machado, Ednildo A., Pedro L. Oliveira, Monica F. Moreira, Wanderley de Souza, and Hatisaburo Masuda. "Uptake ofRhodnius heme-binding protein (RHBP) by the ovary ofRhodnius prolixus." Archives of Insect Biochemistry and Physiology 39, no. 4 (1998): 133–43. http://dx.doi.org/10.1002/(sici)1520-6327(1998)39:4<133::aid-arch1>3.0.co;2-d.

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Zhang, Ping, John D. Belcher, Julia Nguyen, Fuad Abdulla, and Gregory M. Vercellotti. "Increased Release of Soluble MD-2 in Sickle Cell Disease and Its Role in Pro-Inflammatory Signaling in Endothelial Cells." Blood 134, Supplement_1 (2019): 208. http://dx.doi.org/10.1182/blood-2019-122912.

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Sickle cell disease (SCD) is the most common hemoglobinopathy worldwide, resulting from a mutation in the beta globin gene. SCD has significant pathophysiological consequences -- hemolysis, inflammation, oxidative stress, hypercoagulability, endothelial dysfunction and painful vaso-occlusive crises. The latter can be precipitated by infection or other metabolic stressors. Hemolysis chronically exposes endothelial cells, leukocytes, and platelets to hemoglobin and heme that promote pro-inflammatory and prothrombotic phenotypes. We previously demonstrated that toll-like receptor 4 (TLR4) signali

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Hayashi, Takashi, Hideaki Sato, Takashi Matsuo, Takaaki Matsuda, Yutaka Hitomi, and Yoshio Hisaeda. "Enhancement of enzymatic activity for myoglobins by modification of heme-propionate side chains." Journal of Porphyrins and Phthalocyanines 08, no. 03 (2004): 255–64. http://dx.doi.org/10.1142/s1088424604000246.

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The modification of myoglobin is an attractive process not only for understanding its molecular mechanism but also for engineering the protein function. The strategy of myoglobin functionalization can be divided into at least two approaches: site-directed mutagenesis and reconstitution with a non-natural prosthetic group. The former method enables us to mainly modulate the physiological function, while the latter has the advantage of introducing a new function on the protein. Particularly, replacement of the native hemin with an artificially created hemin having hydrophobic moieties at the ter

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Zhou, Huchen, and John T. Groves. "Host-guest interactions of cyclodextrins and metalloporphyrins: supramolecular building blocks toward artificial heme proteins." Journal of Porphyrins and Phthalocyanines 08, no. 02 (2004): 125–40. http://dx.doi.org/10.1142/s108842460400012x.

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Cyclodextrins are versatile building blocks for a variety of macromolecules due to the inclusion complexes that are formed with hydrophobic organic molecules. Cyclodextrin-porphyrin interactions are of particular interest since cyclodextrins can serve as a non-covalent binding pocket while metalloporphyrins could serve as the heme analogs in the construction of heme protein model compounds. Various approaches to the design and assembly of biomimetic porphyrin constructs are compared and contrasted in this minireview with a particular emphasis on self-assembled and porphyrin-cyclodextrin system

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Nakagawa, Toshiyuki, and Kazunori Ohta. "Quercetin Regulates the Integrated Stress Response to Improve Memory." International Journal of Molecular Sciences 20, no. 11 (2019): 2761. http://dx.doi.org/10.3390/ijms20112761.

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The initiation of protein synthesis is suppressed under several stress conditions, inducing phosphorylation of the α-subunit of the eukaryotic initiation factor 2 (eIF2α), thereby inactivating the GTP-GDP recycling protein eIF2B. By contrast, the mammalian activating transcription factor 4 (ATF4, also known as cAMP response element binding protein 2 (CREB2)) is still translated under stress conditions. Four protein kinases (general control nonderepressible-2 (GCN2) kinase, double-stranded RNA-activated protein kinase (PKR), PKR-endoplasmic reticulum (ER)-related kinase (PERK), and heme-regulat

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Endo, R., H. Ishikawa, K. Iwai, I. Morishima, and K. Ishimori. "2P063 Spectroscopic Characterization of Heme Binding and Coordination Structure in Iron Regulatory Protein 2(IRP2)." Seibutsu Butsuri 44, supplement (2004): S125. http://dx.doi.org/10.2142/biophys.44.s125_3.

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Lok, Chun-Nam, and Prem Ponka. "Stimulation of Transferrin Receptor Expression by Enhanced Heme Biosynthesis in Murine Erythroleukemia Cells." Blood 104, no. 11 (2004): 3200. http://dx.doi.org/10.1182/blood.v104.11.3200.3200.

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Abstract In erythroid cells iron uptake from transferrin (Tf) is utilized largely for heme synthesis. Here we provide evidence that Tf receptor (TfR) expression and cellular uptake of iron from Tf is stimulated by enhanced heme synthesis. Incubation of murine erythroleukemia (MEL) cells with 5-aminolevulinic acid (ALA) resulted in an increase in TfR expression accompanied by enhanced uptake of iron from Tf and incorporation of iron into heme. ALA-mediated enhancement of TfR mRNA expression was completely prevented by succinylacetone, an inhibitor of ALA dehydratase, and N-methylprotoporphyrin,

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Ma, Jing, Xianfeng Zhang, Yanbin Feng, et al. "Structural and Functional Study of Apoptosis-linked Gene-2·Heme-binding Protein 2 Interactions in HIV-1 Production." Journal of Biological Chemistry 291, no. 52 (2016): 26670–85. http://dx.doi.org/10.1074/jbc.m116.752444.

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Zager, Richard A., Ali C. M. Johnson та Kirsten Frostad. "An evaluation of the antioxidant protein α1-microglobulin as a renal tubular cytoprotectant". American Journal of Physiology-Renal Physiology 311, № 3 (2016): F640—F651. http://dx.doi.org/10.1152/ajprenal.00264.2016.

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α1-Microglobulin (A1M) is a low-molecular-weight heme-binding antioxidant protein that is readily filtered by the glomerulus and reabsorbed by proximal tubules. Given these properties, recombinant A1M (rA1M) has been proposed as a renal antioxidant and therapeutic agent. However, little direct evidence to support this hypothesis exists. Hence, we have sought “proof of concept” in this regard. Cultured proximal tubule (HK-2) cells or isolated mouse proximal tubule segments were challenged with a variety of prooxidant insults: 1) hemin, 2) myoglobin; 3) “catalytic” iron, 4) H2O2/Fenton reagents,

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Muñoz-Sánchez, Jorge, and María Elena Chánez-Cárdenas. "A Review on Hemeoxygenase-2: Focus on Cellular Protection and Oxygen Response." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–16. http://dx.doi.org/10.1155/2014/604981.

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Hemeoxygenase (HO) system is responsible for cellular heme degradation to biliverdin, iron, and carbon monoxide. Two isoforms have been reported to date. Homologous HO-1 and HO-2 are microsomal proteins with more than 45% residue identity, share a similar fold and catalyze the same reaction. However, important differences between isoforms also exist. HO-1 isoform has been extensively studied mainly by its ability to respond to cellular stresses such as hemin, nitric oxide donors, oxidative damage, hypoxia, hyperthermia, and heavy metals, between others. On the contrary, due to its apparently c

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Sanchez, Mayka, Bruno Galy, Bjoern Schwanhaeusser, et al. "Iron regulatory protein-1 and -2: transcriptome-wide definition of binding mRNAs and shaping of the cellular proteome by iron regulatory proteins." Blood 118, no. 22 (2011): e168-e179. http://dx.doi.org/10.1182/blood-2011-04-343541.

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Abstract Iron regulatory proteins (IRPs) 1 and 2 are RNA-binding proteins that control cellular iron metabolism by binding to conserved RNA motifs called iron-responsive elements (IREs). The currently known IRP-binding mRNAs encode proteins involved in iron uptake, storage, and release as well as heme synthesis. To systematically define the IRE/IRP regulatory network on a transcriptome-wide scale, IRP1/IRE and IRP2/IRE messenger ribonucleoprotein complexes were immunoselected, and the mRNA composition was determined using microarrays. We identify 35 novel mRNAs that bind both IRP1 and IRP2, an

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Noh, Seung-Jae, Y. Terry Lee, Colleen Byrnes, Antoinette Rabel, and Jeffery L. Miller. "Trafficking Kinesin Binding Protein Is Essential for Human Erythropoiesis." Blood 118, no. 21 (2011): 683. http://dx.doi.org/10.1182/blood.v118.21.683.683.

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Abstract Abstract 683 Mitochondrial specialization in erythroblasts is important for efficient heme synthesis, with defects or reduced expression of several mitochondrial proteins causing anemia. Trafficking kinesin binding 2 (TRAK2) is known to participate in mitochondrial movement along microtubule by interacting with kinesin motor protein and making a complex with Miro that is localized on the mitochondrial outer membrane. Transcriptome data suggest that TRAK2 is highly and specifically expressed in early erythroid cells. Here the role of TRAK2 was studied among human CD34+ cells that were

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Trawick, J. D., N. Kraut, F. R. Simon, and R. O. Poyton. "Regulation of yeast COX6 by the general transcription factor ABF1 and separate HAP2- and heme-responsive elements." Molecular and Cellular Biology 12, no. 5 (1992): 2302–14. http://dx.doi.org/10.1128/mcb.12.5.2302-2314.1992.

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Transcription of the Saccharomyces cerevisiae COX6 gene is regulated by heme and carbon source. It is also affected by the HAP2/3/4 transcription factor complex and by SNF1 and SSN6. Previously, we have shown that most of this regulation is mediated through UAS6, an 84-bp upstream activation segment of the COX6 promoter. In this study, by using linker scanning mutagenesis and protein binding assays, we have identified three elements within UAS6 and one element downstream of it that are important. Two of these, HDS1 (heme-dependent site 1; between -269 and -251 bp) and HDS2 (between -228 and -2

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Trawick, J. D., N. Kraut, F. R. Simon, and R. O. Poyton. "Regulation of yeast COX6 by the general transcription factor ABF1 and separate HAP2- and heme-responsive elements." Molecular and Cellular Biology 12, no. 5 (1992): 2302–14. http://dx.doi.org/10.1128/mcb.12.5.2302.

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Transcription of the Saccharomyces cerevisiae COX6 gene is regulated by heme and carbon source. It is also affected by the HAP2/3/4 transcription factor complex and by SNF1 and SSN6. Previously, we have shown that most of this regulation is mediated through UAS6, an 84-bp upstream activation segment of the COX6 promoter. In this study, by using linker scanning mutagenesis and protein binding assays, we have identified three elements within UAS6 and one element downstream of it that are important. Two of these, HDS1 (heme-dependent site 1; between -269 and -251 bp) and HDS2 (between -228 and -2

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Zhou, Suiping, David Gell, Yi Kong, et al. "Mechanisms of Alpha Hemoglobin Stabilizing Protein (AHSP) Actions." Blood 104, no. 11 (2004): 499. http://dx.doi.org/10.1182/blood.v104.11.499.499.

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Abstract Alpha hemoglobin stabilizing protein (AHSP) is an abundant erythroid factor that specifically binds and stabilizes free α hemoglobin (Kihm et al., Nature 417:758, Gell et al., JBC, 277:40602). In mice, AHSP deficiency causes oxidative stress, mild anemia, and reticulocytosis. Furthermore, loss of AHSP exacerbates α globin precipitation and anemia in a murine model for β thalassemia. These data suggest that AHSP operates as a molecular chaperone to stabilize free α hemoglobin and inhibit its ability to catalyze redox chemistry. We investigated how AHSP associates with α hemoglobin and

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Golonka, Rachel, Beng San Yeoh, and Matam Vijay-Kumar. "The Iron Tug-of-War between Bacterial Siderophores and Innate Immunity." Journal of Innate Immunity 11, no. 3 (2019): 249–62. http://dx.doi.org/10.1159/000494627.

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Iron is necessary for the survival of almost all aerobic organisms. In the mammalian host, iron is a required cofactor for the assembly of functional iron-sulfur (Fe-S) cluster proteins, heme-binding proteins and ribonucleotide reductases that regulate various functions, including heme synthesis, oxygen transport and DNA synthesis. However, the bioavailability of iron is low due to its insolubility under aerobic conditions. Moreover, the host coordinates a nutritional immune response to restrict the accessibility of iron against potential pathogens. To counter nutritional immunity, most commen

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Chen, Jane-Jane. "Heme-Regulated eIF2α Kinase in Erythropoiesis and Oxidative Stress". Blood 118, № 21 (2011): SCI—23—SCI—23. http://dx.doi.org/10.1182/blood.v118.21.sci-23.sci-23.

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Abstract SCI-23 Besides serving as a prosthetic group for hemoglobin, heme also regulates translation by inhibiting the kinase activity of heme-regulated translational inhibitor (HRI). HRI is the only known protein kinase that senses the intracellular heme concentration and does so through its two heme-binding domains. HRI is activated in heme deficiency by autophosphorylation, and phosphorylates the α-subunit of eukaryotic initiation factor 2 (eIF2α), which impairs the recycling of eIF2 for further translational initiation and results in cessation of protein synthesis. In this manner, HRI ser

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Pajarillo, Edward, Asha Rizor, Deok-Soo Son, Michael Aschner, and Eunsook Lee. "The transcription factor REST up-regulates tyrosine hydroxylase and antiapoptotic genes and protects dopaminergic neurons against manganese toxicity." Journal of Biological Chemistry 295, no. 10 (2020): 3040–54. http://dx.doi.org/10.1074/jbc.ra119.011446.

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Dopaminergic functions are important for various biological activities, and their impairment leads to neurodegeneration, a hallmark of Parkinson's disease (PD). Chronic manganese (Mn) exposure causes the neurological disorder manganism, presenting symptoms similar to those of PD. Emerging evidence has linked the transcription factor RE1-silencing transcription factor (REST) to PD and also Alzheimer's disease. But REST's role in dopaminergic neurons is unclear. Here, we investigated whether REST protects dopaminergic neurons against Mn-induced toxicity and enhances expression of the dopamine-sy

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Mikasa, Taisuke, Masami Kugo, Seigo Nishimura, Sigeru Taketani, Sumio Ishijima, and Ikuko Sagami. "Thermodynamic Characterization of the Ca2+-Dependent Interaction Between SOUL and ALG-2." International Journal of Molecular Sciences 19, no. 12 (2018): 3802. http://dx.doi.org/10.3390/ijms19123802.

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SOUL, a heme-binding protein-2 (HEBP-2), interacts with apoptosis-linked gene 2 protein (ALG-2) in a Ca2+-dependent manner. To investigate the properties of the interaction of SOUL with ALG-2, we generated several mutants of SOUL and ALG-2 and analyzed the recombinant proteins using pulldown assay and isothermal titration calorimetry. The interaction between SOUL and ALG-2 (delta3-23ALG-2) was an exothermic reaction, with 1:1 stoichiometry and high affinity (Kd = 32.4 nM) in the presence of Ca2+. The heat capacity change (ΔCp) of the reaction showed a large negative value (−390 cal/K·mol), whi

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Jones, Richard C., Joanna Deck, Ricky D. Edmondson, and Mark E. Hart. "Relative Quantitative Comparisons of the Extracellular Protein Profiles of Staphylococcus aureus UAMS-1 and Its sarA, agr, and sarA agr Regulatory Mutants Using One-Dimensional Polyacrylamide Gel Electrophoresis and Nanocapillary Liquid Chromatography Coupled with Tandem Mass Spectrometry." Journal of Bacteriology 190, no. 15 (2008): 5265–78. http://dx.doi.org/10.1128/jb.00383-08.

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ABSTRACT One-dimensional polyacrylamide gel electrophoresis followed by nanocapillary liquid chromatography coupled with mass spectrometry was used to analyze proteins isolated from Staphylococcus aureus UAMS-1 after 3, 6, 12, and 24 h of in vitro growth. Protein abundance was determined using a quantitative value termed normalized peptide number, and overall, proteins known to be associated with the cell wall were more abundant early on in growth, while proteins known to be secreted into the surrounding milieu were more abundant late in growth. In addition, proteins from spent media and cell

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