keyword
https://read.qxmd.com/read/31396101/antisickling-drugs-targeting-%C3%AE-cys93-reduce-iron-oxidation-and-oxidative-changes-in-sickle-cell-hemoglobin
#21
JOURNAL ARTICLE
Tigist Kassa, Francine Wood, Michael Brad Strader, Abdu I Alayash
Sickle cell disease is a genetic blood disorder caused by a single point mutation in the β globin gene where glutamic acid is replaced by valine at the sixth position of the β chain of hemoglobin (Hb). At low oxygen tension, the polymerization of deoxyHbS into fibers occurs in red blood cells (RBCs) leading to an impaired blood vessel transit. Sickle cell hemoglobin (HbS), when oxidized with hydrogen peroxide (H2 O2 ), stays longer in a highly oxidizing ferryl (Fe4+ ) form causing irreversible oxidation of βCys93 to a destabilizing cysteic acid...
2019: Frontiers in Physiology
https://read.qxmd.com/read/31176765/antibacterial-activity-of-erythrocyte-from-grass-carp-ctenopharyngodon-idella-is-associated-with-phagocytosis-and-reactive-oxygen-species-generation
#22
JOURNAL ARTICLE
Zhendong Qin, Sarath Babu Vijayaraman, Hanzuo Lin, Yunjia Dai, Lijuan Zhao, Jungang Xie, Weiqiang Lin, Zaohe Wu, Jun Li, Li Lin
Red blood cells (RBCs) are widely accepted as their primary function in respiration. Recent studies in mammals have revealed a vital role in immune responses of RBCs; however, little is known about immune function of teleost erythrocytes. Here we demonstrated that RBCs from grass carp (Ctenopharyngodon idella) were capable of binding and aggregating the bacteria with apparent morphological alterations. The phagocytosis by teleost RBCs (erythrophagocytosis) was visualized by confocal, scanning and transmission electron microscopy...
September 2019: Fish & Shellfish Immunology
https://read.qxmd.com/read/31035002/epr-detection-of-sulfanyl-radical-during-sulfhemoglobin-formation-influence-of-catalase
#23
JOURNAL ARTICLE
Augustin C Mot, Cristina Puscas, Sorin Aurel Dorneanu, Radu Silaghi-Dumitrescu
Hemoglobin in its ferryl form oxidizes hydrogen sulfide and is transformed to sulfhemoglobin, where the sulfur is inserted covalently at the heme edge. Shown here is evidence that-as previously proposed by others-this process involves oxidation of hydrogen sulfide to a sulfanyl radical detectable by spin-trapping in electron paramagnetic resonance (EPR) spectroscopy. The yields and rates of formation of sulfhemoglobin as well as of the sulfanyl radical are affected by the same factors that affect the reactivity of hemoglobin ferryl, in bovine hemoglobin and in phytoglobins as well...
June 2019: Free Radical Biology & Medicine
https://read.qxmd.com/read/30630954/substitutions-in-the-%C3%AE-subunits-of-sickle-cell-hemoglobin-improve-oxidative-stability-and-increase-the-delay-time-of-sickle-cell-fiber-formation
#24
JOURNAL ARTICLE
Fantao Meng, Tigist Kassa, Michael Brad Strader, Jayashree Soman, John S Olson, Abdu I Alayash
After reacting with hydrogen peroxide (H2 O2 ), sickle-cell hemoglobin (HbS, βE6V) remains longer in a highly oxidizing ferryl form (HbFe4+ =O) and induces irreversible oxidation of "hot-spot" amino acids, including βCys-93. To control the damaging ferryl heme, here we constructed three HbS variants. The first contained a redox-active Tyr in β subunits (F41Y), a substitution present in Hb Mequon; the second contained the Asp (K82D) found in the β cleft of Hb Providence; and the third had both of these β substitutions...
March 15, 2019: Journal of Biological Chemistry
https://read.qxmd.com/read/30594736/engineering-tyrosine-residues-into-hemoglobin-enhances-heme-reduction-decreases-oxidative-stress-and-increases-vascular-retention-of-a-hemoglobin-based-blood-substitute
#25
JOURNAL ARTICLE
Chris E Cooper, Gary G A Silkstone, Michelle Simons, Badri Rajagopal, Natalie Syrett, Thoufieq Shaik, Svetlana Gretton, Elizabeth Welbourn, Leif Bülow, Nélida Leiva Eriksson, Luca Ronda, Andrea Mozzarelli, Andras Eke, Domokos Mathe, Brandon J Reeder
Hemoglobin (Hb)-based oxygen carriers (HBOC) are modified extracellular proteins, designed to replace or augment the oxygen-carrying capacity of erythrocytes. However, clinical results have generally been disappointing due to adverse side effects, in part linked to the intrinsic oxidative toxicity of Hb. Previously a redox-active tyrosine residue was engineered into the Hb β subunit (βF41Y) to facilitate electron transfer between endogenous antioxidants such as ascorbate and the oxidative ferryl heme species, converting the highly oxidizing ferryl species into the less reactive ferric (met) form...
December 27, 2018: Free Radical Biology & Medicine
https://read.qxmd.com/read/30385713/hemoglobin-oxidation-dependent-reactions-promote-interactions-with-band-3-and-oxidative-changes-in-sickle-cell-derived-microparticles
#26
JOURNAL ARTICLE
Sirsendu Jana, Michael Brad Strader, Fantao Meng, Wayne Hicks, Tigist Kassa, Ivan Tarandovskiy, Silvia De Paoli, Jan Simak, Michael R Heaven, John D Belcher, Gregory M Vercellotti, Abdu I Alayash
The contribution of intracellular hemoglobin (Hb) oxidation to RBC-derived microparticle (MP) formation is poorly defined in sickle cell disease (SCD). Here we report that sickle Hb (HbS) oxidation, coupled with changes in cytosolic antioxidative proteins, is associated with membrane alterations and MP formation in homozygous Townes-sickle cell (Townes-SS) mice. Photometric and proteomic analyses confirmed the presence of high levels of Hb oxidation intermediates (ferric/ferryl) and consequent β-globin posttranslational modifications, including the irreversible oxidation of βCys93 and the ubiquitination of βLys96 and βLys145...
November 2, 2018: JCI Insight
https://read.qxmd.com/read/30193183/site-directed-mutagenesis-of-cysteine-residues-alters-oxidative-stability-of-fetal-hemoglobin
#27
JOURNAL ARTICLE
Karin Kettisen, Michael Brad Strader, Francine Wood, Abdu I Alayash, Leif Bülow
Redox active cysteine residues including βCys93 are part of hemoglobin's "oxidation hotspot". Irreversible oxidation of βCys93 ultimately leads to the collapse of the hemoglobin structure and release of heme. Human fetal hemoglobin (HbF), similarly to the adult hemoglobin (HbA), carries redox active γCys93 in the vicinity of the heme pocket. Site-directed mutagenesis has been used in this study to examine the impact of removal and/or addition of cysteine residues in HbF. The redox activities of the recombinant mutants were examined by determining the spontaneous autoxidation rate, the hydrogen peroxide induced ferric to ferryl oxidation rate, and irreversible oxidation of cysteine by quantitative mass spectrometry...
October 2018: Redox Biology
https://read.qxmd.com/read/30178349/novel-redox-active-tyrosine-mutations-enhance-the-regeneration-of-functional-oxyhemoglobin-from-methemoglobin-implications-for-design-of-blood-substitutes
#28
JOURNAL ARTICLE
G G A Silkstone, M Simons, B S Rajagopal, T Shaik, B J Reeder, C E Cooper
Heme mediated oxidative toxicity has been linked to adverse side effects in Hemoglobin Based Oxygen Carriers (HBOC), initiated by reactive ferryl (FeIV ) iron and globin based free radical species. We recently showed that the addition of a redox active tyrosine residue in the beta subunit (βF41Y) of recombinant hemoglobin had the capability to decrease lipid peroxidation by facilitating the reduction of FeIV iron by plasma antioxidants such as ascorbate. In order to explore this functionality further we created a suite of tyrosine mutants designed to be accessible for both reductant access at the protein surface, yet close enough to the heme cofactor to enable efficient electron transfer to the FeIV ...
2018: Advances in Experimental Medicine and Biology
https://read.qxmd.com/read/29802155/comparison-of-the-oxidative-reactivity-of-recombinant-fetal-and-adult-human-hemoglobin-implications-for-the-design-of-hemoglobin-based-oxygen-carriers
#29
JOURNAL ARTICLE
Michelle Simons, Svetlana Gretton, Gary G A Silkstone, Badri S Rajagopal, Victoria Allen-Baume, Natalie Syrett, Thoufieq Shaik, Nelida Leiva-Eriksson, Luca Ronda, Andrea Mozzarelli, Michael B Strader, Abdu I Alayash, Brandon J Reeder, Chris E Cooper
Hemoglobin (Hb)-based oxygen carriers (HBOCs) have been engineered to replace or augment the oxygen carrying capacity of erythrocytes. However, clinical results have generally been disappointing, in part due to the intrinsic oxidative toxicity of Hb. The most common HBOC starting material is adult human or bovine Hb. However, it has been suggested that fetal Hb may offer advantages due to decreased oxidative reactivity. Large-scale manufacturing of HBOC will likely and ultimately require recombinant sources of human proteins...
August 31, 2018: Bioscience Reports
https://read.qxmd.com/read/29414908/the-reaction-of-oxy-hemoglobin-with-nitrite-mechanism-antioxidant-modulated-effect-and-implications-for-blood-substitute-evaluation
#30
JOURNAL ARTICLE
Denisa Hathazi, Florina Scurtu, Cristina Bischin, Augustin Mot, Amr A A Attia, Jacob Kongsted, Radu Silaghi-Dumitrescu
The autocatalytic reaction between nitrite and the oxy form of globins involves free radicals. For myoglobin (Mb), an initial binding of nitrite to the iron-coordinated oxygen molecule was proposed; the resulting ferrous-peroxynitrate species was not detected, but its decay product, the high-valent ferryl form, was demonstrated in stopped-flow experiments. Reported here are the stopped flow spectra recorded upon mixing oxy Hb (native, as well as chemically-derivatized in the form of several candidates of blood substitutes) with a supraphysiological concentration of nitrite...
February 7, 2018: Molecules: a Journal of Synthetic Chemistry and Natural Product Chemistry
https://read.qxmd.com/read/29305213/interaction-of-glossoscolex-paulistus-extracellular-hemoglobin-with-hydrogen-peroxide-formation-and-decay-of-ferryl-hbgp
#31
JOURNAL ARTICLE
Silvia H Libardi, Fernanda R Alves, Marcel Tabak
The giant extracellular hemoglobin from earthworm Glossoscolex paulistus (HbGp) reacts with hydrogen peroxide, displaying peroxidase activity in the presence of guaiacol. The formation of ferryl-HbGp (compound II) from the peroxidase cycle was studied in the present work. The hypervalent ferryl-HbGp species was formed directly by the reaction of oxy-HbGp and hydrogen peroxide. The oxy-HbGp heme groups (144) under different excess of H2 O2 , relative to heme, showed an influence in the total amount of ferryl-HbGp at the end of the reaction...
May 2018: International Journal of Biological Macromolecules
https://read.qxmd.com/read/29158890/oxidation-of-pyrrole-by-dehaloperoxidase-hemoglobin-chemoenzymatic-synthesis-of-pyrrolin-2-ones
#32
JOURNAL ARTICLE
Nikolette L McCombs, Tatyana Smirnova, Reza A Ghiladi
The use of oxidoreductases as biocatalysts in the syntheses of functionalized, monomeric pyrroles has been a challenge owing to, among a number of factors, undesired polypyrrole formation. Here, we have investigated the ability of dehaloperoxidase (DHP), the coelomic hemoglobin from the terebellid polychaete Amphitrite ornata , to catalyze the H2 O2 -dependent oxidation of pyrroles as a new class of substrate for this enzyme. Substrate oxidation was observed for all compounds employed (pyrrole, N-methylpyrrole, 2-methylpyrrole, 3-methylpyrrole and 2,5-dimethylpyrrole) under both aerobic and anaerobic conditions...
2017: Catalysis Science & Technology
https://read.qxmd.com/read/29134657/mechanisms-involved-in-hemoglobin-mediated-oxidation-of-lipids-in-washed-fish-muscle-and-inhibitory-effects-of-phospholipase-a2
#33
JOURNAL ARTICLE
Nantawat Tatiyaborworntham, Mark P Richards
BACKGROUND: Hemoglobin (Hb) is a lipid oxidation promoter in fish muscle. Phospholipase A2 (PLA2; EC 3.1.1.4) is linked to an increased resistance to lipid oxidation of frozen-thawed cod fillets via an unknown mechanism. The present study aimed to investigate the mechanism of Hb-mediated lipid oxidation with a focus on ferryl Hb and methemoglobin (metHb), the pro-oxidative Hb species, and to examine how porcine pancreatic PLA2 inhibits Hb-mediated lipid oxidation in washed cod muscle (WCM)...
May 2018: Journal of the Science of Food and Agriculture
https://read.qxmd.com/read/28863941/potential-role-of-ferric-hemoglobin-in-ms-pathogenesis-effects-of-oxidative-stress-and-extracellular-methemoglobin-or-its-degradation-products-on-myelin-components
#34
JOURNAL ARTICLE
Vladimir V Bamm, Mary E L Henein, Shannon L J Sproul, Danielle K Lanthier, George Harauz
There is a well-documented relationship between cerebral vasculature and multiple sclerosis (MS) lesions: abnormal accumulations of iron have been found in the walls of the dilated veins in cerebral MS plaques. The source of this iron is unknown, but could be related to the recognized phenomenon of capillary and venous hemorrhages leading to blood extravasation. In turn, hemorrhaging leading to hemolysis results in extracellular release of hemoglobin, a reactive molecule that could induce local oxidative stress, inflammation, and tissue damage...
November 2017: Free Radical Biology & Medicine
https://read.qxmd.com/read/28829595/factors-affecting-lipid-oxidation-due-to-pig-and-turkey-hemolysate
#35
COMPARATIVE STUDY
Haizhou Wu, Jie Yin, Jianhao Zhang, Mark P Richards
Turkey hemolysate promoted lipid oxidation in washed muscle more effectively than pig hemolysate, which was partly attributed to the greater ability of H2O2 that formed during auto-oxidation to oxidize the avian hemoglobin (Hb). Turkey and pig hemolysate (2.5 μM Hb) exposed to 10 μM H2O2 oxidized to 48% and 4% metHb, respectively. Catalase activity, which converts H2O2 to water, was elevated in the pig hemolysate. The larger difference in Hb oxidation when comparing turkey and pig hemolysate in washed muscle (relative to their auto-oxidation rates) suggested that lipid oxidation products facilitated formation of metHb...
September 13, 2017: Journal of Agricultural and Food Chemistry
https://read.qxmd.com/read/28770911/targeting-%C3%AE-cys93-in-hemoglobin-s-with-an-antisickling-agent-possessing-dual-allosteric-and-antioxidant-effects
#36
JOURNAL ARTICLE
Tigist Kassa, M B Strader, Akito Nakagawa, Warren M Zapol, Abdu I Alayash
Sickle cell disease (SCD) is an inherited blood disorder caused by a β globin gene mutation of hemoglobin (HbS). The polymerization of deoxyHbS and its subsequent aggregation (into long fibers) is the primary molecular event which leads to red blood cell (RBC) sickling and ultimately hemolytic anemia. We have recently suggested that HbS oxidative toxicity may also contribute to SCD pathophysiology due to its defective pseudoperoxidase activity. As a consequence, a persistently higher oxidized ferryl heme is formed which irreversibly oxidizes "hotspot" residues (particularly βCys93) causing protein unfolding and subsequent heme loss...
September 20, 2017: Metallomics: Integrated Biometal Science
https://read.qxmd.com/read/28501110/arachidonic-acid-causes-hidden-blood-loss-like-red-blood-cell-damage-through-oxidative-stress-reactions
#37
JOURNAL ARTICLE
Tao Yuan, Yu Cong, Jia Meng, Hong Qian, Wei Ye, Wen-Shuang Sun, Jian-Ning Zhao, Ni-Rong Bao
BACKGROUND: Hidden blood loss (HBL) often occurs in the prosthetic replacement for joint, but the mechanism is still not clear. MATERIALS AND METHODS: This study tried to establish an animal model of HBL by injecting arachidonic acid (AA) into the Sprague-Dawley rats. Different concentrations of AA were injected into the tail veins of the rats, and blood samples were collected before and after administration at 24, 48, and 72 h. A complete blood count was obtained by to find the hemoglobin (Hb) and red blood cell (RBC) count changes...
May 1, 2017: Journal of Surgical Research
https://read.qxmd.com/read/28323418/bioinspired-polydopamine-coated-hemoglobin-as-potential-oxygen-carrier-with-antioxidant-properties
#38
JOURNAL ARTICLE
Quan Wang, Ruirui Zhang, Mingzi Lu, Guoxing You, Ying Wang, Gan Chen, Caiyan Zhao, Zhen Wang, Xiang Song, Yan Wu, Lian Zhao, Hong Zhou
Oxidative side reaction is one of the major factors hindering the development of hemoglobin-based oxygen carriers (HBOCs). To avoid the oxidative toxicity, we designed and synthesized polydopamine-coated hemoglobin (Hb-PDA) nanoparticles via simple one-step assemblage without any toxic reagent. Hb-PDA nanoparticles showed oxidative protection of Hb by inhibiting the generation of methemoglobin (MetHb) and ferryl (Fe IV) Hb, as well as excellent antioxidant properties by scavenging free radicals and reactive oxygen species (ROS)...
April 10, 2017: Biomacromolecules
https://read.qxmd.com/read/28270376/antioxidants-attenuate-oxidative-stress-induced-hidden-blood-loss-in-rats
#39
JOURNAL ARTICLE
Hong Qian, Tao Yuan, Jian Tong, Wen Shuang Sun, Jiajia Jin, Wen Xiang Chen, Jia Meng, Nirong Bao, Jianning Zhao
OBJECTIVE: Hidden blood loss (HBL), commonly seen after total knee or hip arthroplasty, causes postoperative anemia even after reinfusion or blood transfusion based on the visible blood loss volume. Recent studies demonstrated that oxidative stress might be involved in HBL. However, whether the antioxidants proanthocyanidin (PA) or hydrogen water (HW) can ameliorate HBL remains poorly understood. The aim of this study was to evaluate the effects of PA and HW on HBL. MATERIALS AND METHODS: A rat HBL model was established through administration of linoleic acid with or without treatment with PA or HW...
December 1, 2017: Turkish Journal of Haematology: Official Journal of Turkish Society of Haematology
https://read.qxmd.com/read/28069451/determination-of-extinction-coefficients-of-human-hemoglobin-in-various-redox-states
#40
JOURNAL ARTICLE
Fantao Meng, Abdu I Alayash
The role of hemoglobin (Hb) redox forms in tissue and organ toxicities remain ambiguous despite the well-documented contribution of Hb redox reactivity to cellular and subcellular oxidative changes. Moreover, several recent studies, in which Hb toxicity were investigated, have shown conflicting outcomes. Uncertainties over the potential role of these species may in part be due to the protein preparation method of choice, the use of published extinction coefficients and the lack of suitable controls for Hb oxidation and heme loss...
March 15, 2017: Analytical Biochemistry
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