Relevant bibliographies by topics / HemoglobinS Polymerization

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'HemoglobinS Polymerization'

Author: Grafiati
Published: 5 June 2025
Last updated: 25 June 2025

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Journal articles on the topic "HemoglobinS Polymerization"

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Li, Xianfeng, Urooj A. Mirza, Brian T. Chait, and James M. Manning. "Systematic Enhancement of Polymerization of Recombinant Sickle Hemoglobin Mutants: Implications for Transgenic Mouse Model for Sickle Cell Anemia." Blood 90, no. 11 (1997): 4620–27. http://dx.doi.org/10.1182/blood.v90.11.4620.

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Abstract To provide quantitative information on the sites that promote polymerization of sickle hemoglobin (HbS) after formation of the initial hydrophobic bond involving Val-6(β) [E6V(β)] and also to provide hemoglobins with an enhanced polymerization that could be used in a mouse model for sickle cell anemia, we have expressed recombinant double, triple, and quadruple HbS mutants with substitutions on both the α- and β-chains, E6V(β)/E121R(β), D75Y(α)/E6V(β)/E121R(β) and D6A(α)/D75Y(α)/E6V(β)/E121R(β). These recombinant hemoglobins were extensively characterized by high-performance liquid chromatography analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, isoelectric focusing, amino acid analysis, and mass spectroscopy. They retained the functional properties of the Hb tetramer and polymerized in a linear manner at progressively lower Hb concentration as a function of the degree of substitution, suggesting that these remote sites (αD6A, αD75Y, and βE121R) on the α- and β-chains exhibit additive, enhanced polymerization properties. The quadruple mutant has a polymerization concentration close to that of the purified SAD hemoglobin from transgenic mouse red blood cells consisting of HbS, Hb Antilles, and Hb D-Punjab. Normal mouse Hb increases the polymerization concentration of each mutant. Thus, the general approach of using recombinant Hbs as described here should prove useful in elucidating the quantitative aspects of the mechanism of HbS polymerization and in identifying the contribution of individual sites to the overall process. The strategy described here demonstrates the feasibility of a systematic approach to achieve future recombinant HbS mutants that could provide a new generation of the transgenic mouse model for sickle cell anemia.
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Li, Xianfeng, Urooj A. Mirza, Brian T. Chait, and James M. Manning. "Systematic Enhancement of Polymerization of Recombinant Sickle Hemoglobin Mutants: Implications for Transgenic Mouse Model for Sickle Cell Anemia." Blood 90, no. 11 (1997): 4620–27. http://dx.doi.org/10.1182/blood.v90.11.4620.4620_4620_4627.

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To provide quantitative information on the sites that promote polymerization of sickle hemoglobin (HbS) after formation of the initial hydrophobic bond involving Val-6(β) [E6V(β)] and also to provide hemoglobins with an enhanced polymerization that could be used in a mouse model for sickle cell anemia, we have expressed recombinant double, triple, and quadruple HbS mutants with substitutions on both the α- and β-chains, E6V(β)/E121R(β), D75Y(α)/E6V(β)/E121R(β) and D6A(α)/D75Y(α)/E6V(β)/E121R(β). These recombinant hemoglobins were extensively characterized by high-performance liquid chromatography analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, isoelectric focusing, amino acid analysis, and mass spectroscopy. They retained the functional properties of the Hb tetramer and polymerized in a linear manner at progressively lower Hb concentration as a function of the degree of substitution, suggesting that these remote sites (αD6A, αD75Y, and βE121R) on the α- and β-chains exhibit additive, enhanced polymerization properties. The quadruple mutant has a polymerization concentration close to that of the purified SAD hemoglobin from transgenic mouse red blood cells consisting of HbS, Hb Antilles, and Hb D-Punjab. Normal mouse Hb increases the polymerization concentration of each mutant. Thus, the general approach of using recombinant Hbs as described here should prove useful in elucidating the quantitative aspects of the mechanism of HbS polymerization and in identifying the contribution of individual sites to the overall process. The strategy described here demonstrates the feasibility of a systematic approach to achieve future recombinant HbS mutants that could provide a new generation of the transgenic mouse model for sickle cell anemia.
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Riccio, Alessia, Gaetano Mangiapia, Daniela Giordano, et al. "Polymerization of hemoglobins in Arctic fish: Lycodes reticulatus and Gadus morhua." IUBMB Life 63, no. 5 (2011): 346–54. http://dx.doi.org/10.1002/iub.450.

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Krzyszczyk, Paulina, Kishan Patel, Yixin Meng, et al. "Macrophage modulation by polymerized hemoglobins: Potential as a wound-healing therapy." TECHNOLOGY 07, no. 03n04 (2019): 84–97. http://dx.doi.org/10.1142/s2339547819500055.

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Chronic skin wounds are hypoxic and are stalled in a pro-inflammatory state. Hemoglobin (Hb)-based oxygen carriers have shown potential in increasing oxygen delivery to aid wound healing. Macrophages also take up Hb, thus altering their phenotype and the regulation of inflammation. Herein, we compared the effect of Hb and polymerized Hbs (PolyHbs) on the phenotype of human macrophages. Macrophages were incubated with Hb or different forms of PolyHbs, and the inflammatory secretion profile was analyzed. PolyHbs were produced by polymerizing Hb in the relaxed (R) or tense (T) quaternary state and by varying the molar ratio of the glutaraldehyde crosslinking agent to Hb. Hb decreased the secretion of most measured factors. PolyHb treatment led to generally similar secretion profiles; however, Hb had more similar trends to R-state PolyHb. Ingenuity pathway analysis predicted positive outcomes in wound healing and angiogenesis for T-state PolyHb prepared with a 30:1 (glutaraldehyde:Hb) polymerization ratio. When tested in diabetic mouse wounds, T-state PolyHb resulted in the greatest epidermal thickness and vascular endothelial CD31 staining. Thus, the effects of PolyHb on macrophages are affected by the polymerization ratio and the quaternary state, and T-state PolyHb yields secretion profiles that are most beneficial in wound healing.
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Adachi, K., E. Rappaport, H. S. Eck, P. Konitzer, J. Kim та S. Surrey. "Polymerization and Solubility of Recombinant Hemoglobins α2β26VAL(HB S) and α2β26LEU(HB LEU)". Hemoglobin 15, № 5 (1991): 417–30. http://dx.doi.org/10.3109/03630269108998861.

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Petersen, Asbjørn G., Steen V. Petersen, Sebastian Frische, et al. "Hemoglobin polymerization via disulfide bond formation in the hypoxia-tolerant turtle Trachemys scripta: implications for antioxidant defense and O2 transport." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 314, no. 1 (2018): R84—R93. http://dx.doi.org/10.1152/ajpregu.00024.2017.

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The ability of many reptilian hemoglobins (Hbs) to form high-molecular weight polymers, albeit known for decades, has not been investigated in detail. Given that turtle Hbs often contain a high number of cysteine (Cys), potentially contributing to the red blood cell defense against reactive oxygen species, we have examined whether polymerization of Hb could occur via intermolecular disulfide bonds in red blood cells of freshwater turtle Trachemys scripta, a species that is highly tolerant of hypoxia and oxidative stress. We find that one of the two Hb isoforms of the hemolysate HbA is prone to polymerization in vitro into linear flexible chains of different size that are visible by electron microscopy but not the HbD isoform. Polymerization of purified HbA is favored by hydrogen peroxide, a main cellular reactive oxygen species and a thiol oxidant, and inhibited by thiol reduction and alkylation, indicating that HbA polymerization is due to disulfide bonds. By using mass spectrometry, we identify Cys5 of the αA-subunit of HbA as specifically responsible for forming disulfide bonds between adjacent HbA tetramers. Polymerization of HbA does not affect oxygen affinity, cooperativity, and sensitivity to the allosteric cofactor ATP, indicating that HbA is still fully functional. Polymers also form in T. scripta blood after exposure to anoxia but not normoxia, indicating that they are of physiological relevance. Taken together, these results show that HbA polymers may form during oxidative stress and that Cys5αA of HbA is a key element of the antioxidant capacity of turtle red blood cells.
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Adachi, K., P. Konitzer, J. Kim, N. Welch, and S. Surrey. "Effects of beta 6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast." Journal of Biological Chemistry 268, no. 29 (1993): 21650–56. http://dx.doi.org/10.1016/s0021-9258(20)80591-2.

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Schaer, Dominik J., Christian A. Schaer, Paul W. Buehler, et al. "CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin." Blood 107, no. 1 (2006): 373–80. http://dx.doi.org/10.1182/blood-2005-03-1014.

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AbstractCD163 mediates the internalization of hemoglobin-haptoglobin (Hb-Hp) complexes by macrophages. Because Hp binding capacity is exhausted during severe hemolysis, an Hp-independent Hb-clearance pathway is presumed to exist. We demonstrate that Hb interacts efficiently with CD163 in the absence of Hp. Not only is Hb internalized into an endosomal compartment by CD163 as a result of active receptor-dependent endocytosis; it also inhibits the uptake of Hb-Hp complexes, suggesting a common receptor-binding site. Free Hb further induces heme oxygenase mRNA expression in CD163+ HEK293 cells, but not in CD163- cells. Additional evidence for Hp-independent Hb-CD163 interaction is provided by the demonstration that CD163 mediates the uptake of αα-DBBF crosslinked Hb, a chemically modified Hb that forms minimal Hp complexes. Moreover, certain modifications to Hb, such as polymerization or the attachment of specific functional groups (3 lysyl residues) to the β-Cys93 can reduce or enhance this pathway of uptake. In human macrophages, Hp-complex formation critically enhances Hb uptake at low (1 μg/mL), but not at high (greater than 100 μg/mL), ligand concentrations, lending support for a concentration-dependent biphasic model of macrophage Hb-clearance. These results identify CD163 as a scavenger receptor for native Hb and small-molecular-weight Hb-based blood substitutes after Hp depletion.
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Barnikol, W. K. R. "Influence of the Polymerization Step Alone on Oxygen Affinity and Cooperative During Production of Hyperpolymers from Native Hemoglobins with Crosslinkers." Artificial Cells, Blood Substitutes, and Biotechnology 22, no. 3 (1994): 725–31. http://dx.doi.org/10.3109/10731199409117904.

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Prabin, Kumar Jani, Mishra Swati, Ranjan Mishra Sruti, et al. "SICKLE CELL ANEMIA DISEASE TREATMENT ONGENETICS MOLECULAR LEVEL IN BASTER, CHHATTISGARH, A REVIEW." COMMUNITY PRACTITIONER 20, no. 09 (2023): 329–38. https://doi.org/10.5281/zenodo.8385187.

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<strong>Abstract </strong> SCA is a hereditary blood disorder considered by irregular haemoglobin causing in the production of sickle shaped red blood cell. Baster in Chhattisgarh a state in central Indian faces a significant problems of sickle cell anemia with a high prevalence among tribal population. This abstract highlight the genetic molecular level treatment methods in baster, Chhattisgarh to take SCA. The advent of molecular biology and genetic research has covered the way for innovatives therapeutics strategies for SCA. Which involve nucleotide substitution in beta globin gene. The genetics molecular level treatment is hematotropoietics stem cell transplantation also known as bone marrow transplantation in baster, Chhattisgarh. Effort are proceeding to expand the availability and accessibiIity of (HSCT) for a sickle cell anemia patients with an emphasis on increasing the number of suitable donor through awareness campaign. Conclusion genetics molecular level treatment approaches for a SCA in baster, Chhattisgarh are gaining momentum and hold great promises foe the management and potentials cure of this unbearable disease the addition of hematopoietics, stem cell transplantation gene therapy, along with continual research effort. Contributed for individual with SCA in baster, chhattisgarh and beyond.
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Dissertations / Theses on the topic "HemoglobinS Polymerization"

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Harrington, Daniel John. "Crystallographic Studies of the Pathological Polymerization of Human Hemoglobin." eScholarship@UMMS, 1998. http://escholarship.umassmed.edu/gsbs_diss/211.

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Sickle cell disease is caused by the intracellular polymerization of human hemoglobin containing a mutation of a glutamic acid to a valine residue at the sixth position of the β chain. This substitution of a hydrophobic residue for a hydrophilic residue greatly decreases the solubility of the hemoglobin tetramer, promoting the formation of ordered fibers in deoxygenated red blood cells. These fibers are composed of double strands of hemoglobin tetramers, which effectively bury the valine side chain in a hydrophobic pocket, eliminating its unfavorable interaction with solvent. Inhibition of fiber formation would greatly alleviate the symptoms of sickle cell disease; therefore, the elucidation of the structure of the fiber is critical to developing treatments for the disease. In this thesis, an analysis of the crystal structures of the double strand component of the fibers formed by HbS and other site-directed mutants displaying altered sickling properties is undertaken. Structure of HbS at high resolution: The structure of HbS was solved at 2.05 Å resolution. This high-resolution analysis produced significant improvements in the previous 3.0 Å model. In particular, the accurate positioning of side chains, and the placement of more than 500 solvent molecules was achieved. Some side chains in the physiologically relevant contacts were moved by as much as 3.5 Å away from their locations in the lower resolution model. The structure also demonstrates that well ordered water molecules are located in both the axial and lateral contacts, some of which may be exploited in the design of sickling inhibitors. Structures of Hbβ6L and Hbβ6W: The crystal structures of two human hemoglobins with mutations at the β6 position that display altered sickling behavior were solved and refined at high resolution. Both mutants were crystallized under conditions similar to those used with HbS. Hbβ6L showed a greater tendency to polymerize, and displayed reduced delay times in aggregation assays. The refined structure was very similar to that of HbS, with changes confined mostly to the lateral contacts. However, the packing of Leu β6 in the linear crystalline double strands is sub-optimal. This has important ramifications for the differences between the crystalline double strands and those within the physiological HbS fiber. Hbβ6W, on the other hand, showed a reduced tendency to polymerize and shorter delay times in polymerization assays. The protein crystallized in a different space group from the other two mutants (HbS and Hbβ6L) under the same crystallization conditions, and formed fundamentally different double strands in the crystals. This structure demonstrates conserved interactions at the axial contacts, but very different interactions at the lateral contacts. The alternate double strand formed by this protein in the crystal may be useful as a model for tetramer interactions within the physiological fiber, or as a structural model for heterogeneous nucleation. The structures of each of these mutants help explain their altered polymerization behavior.
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Weng, Weijun Ferrone Frank A. "Universal metastability of sickle hemoglobin polymerization /." Philadelphia, Pa. : Drexel University, 2008. http://hdl.handle.net/1860/2832.

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Zakharov, Mikhail N. Ferrone Frank A. "A microrheological study of sickle hemoglobin polymerization /." Philadelphia, Pa. : Drexel University, 2009. http://hdl.handle.net/1860/3075.

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Baudin-Chich, Véronique. "Interactions entre les sous-unites d'hemoglobines humaines adultes et foetales : les variantes pathologiques de l'interface alpha 1 beta 1 et l'hemoglobine s." Paris 6, 1988. http://www.theses.fr/1988PA066045.

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Exploration de l'interface entre les sousunites de l'hemoglobine d'un meme dimere et de la surface externe en utilisant cinq variants de l'interface alpha 1 beta 1 et l'hemoglobine s. Il a ete trouve une instabilite moleculaire pour ces variants. Le comportement electrophoretique de ces variants est proche de celui de l'hemoglobine a suggerant un masquage dans cette region. Etude des interactions entre l'hemoglobine foetale et l'hemoglobine s modulant l'expression phenotypique de la drepanocytose
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Medkour, Terkia. "Modélisation mathématique et simulation numérique de la polymérisation de l’hémoglobine drépanocytaire." Thesis, Paris Est, 2008. http://www.theses.fr/2008PEST0044/document.

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La drépanocytose, ou anémie falciforme, présente une variabilité interindividuelle considérable, conditionnée par de multiples facteurs, dynamiques et interactifs, depuis le niveau moléculaire jusqu’au niveau du patient. L’hémoglobine drépanocytaire, ou hémoglobine S (HbS, tétramère a2bS 2), est un mutant de l’hémoglobine A (a2b2) : elle possède à sa surface une valine (hydrophobe) substituant un acide glutamique natif (négativement chargé). Cette mutation entraîne l’agrégation de l’HbS désoxygénée en polymères, ainsi que l’altération des propriétés de l’érythrocyte -dont sa rhéologie et ses interactions avec les différentes cellules vasculaires. C’est pourquoi la polymérisation de l’HbS constitue un facteur étiologique clef, sinon le primum movens, de la drépanocytose, et une hypothèse thérapeutique (étayée par l’observation) postule que la réduction des fibres intra-érythrocytaires de HbS pourrait améliorer le statut clinique des patients en abaissant la fréquence et la sévérité des crises vasoocclusives. Dans l’optique de mieux comprendre et de mieux gérer la variabilité individuelle drépanocytaire, il apparaît donc indispensable de disposer, en premier lieu, d’une description réaliste de la polymérisation de l’HbS. L’objectif de ce travail de thèse est la mise en place et la validation d’un modèle mathématique de la polymérisation de l’HbS désoxygénée, en tant que processus cinétiquethermodynamique, sous l’influence de la concentration et de la température –les deux facteurs modulateurs les plus importants. A partir d’un modèle existant, mais linéaire et incomplet (Ferrone et al., 1985), nous avons procédé à son implémentation, à sa correction et à sa mise à jour, ainsi qu’à l’évaluation quantitative de ses performances dynamiques, par intégration complète et simulation numérique (Simulink©). Ceci nous a permis de réaliser un diagnostic et d’effectuer un certain nombre de raffinements, concernant en particulier (i) la voie de nucléation hétérogène (formation de néo-fibres sur les fibres préexistantes), (ii) la non-idéalité de la solution protéique de HbS, induite par le volume exclus des fibres polymères (coefficients d’activité calculé à partir de la « théorie des particules convexes »), ainsi que (iii) la structuration spatiale des polymères en domaines. Le modèle développé dans ce travail servira de base pour une description (i) de l’influence dynamique de l’oxygénation et des hémoglobines non-polymérisantes sur la polymérisation de HbS, puis (ii) des polymères de HbS sur les propriétés membranaires et rhéologiques de l’érythrocyte drépanocytaire<br>Sickle cell disease pathology exhibits a strong interindividual variability, which depends upon multiple, dynamic and interacting factors, from the molecular to the patient level. Sickle hemoglobin, hemoglobin S (HbS, a2bS 2 tetramer), is a mutant of HbA (a2b2), with a surface valine (hydrophobic) substituting a native glutamic acid (negatively charged). Such a mutation endows deoxygenated HbS with the propensity to agregate into polymers, altering erythrocyte properties –including its rheology and its interactions with vascular and circulatory cells. Thus HbS polymerization is a key etiological factor of sickle cell disease, if not the primum movens. Indeed, one therapeutical hypothesis (supported by observation) postulates that the reduction of intra-erythrocytic HbS fibers could improve patients clinical status by lowering the frequency and the severity of vasooclusive crisis. In order to better understand and manage sickle cell disease variability, it is essential to have a realistic description of HbS polymerization. This work aims at developing and validating a mathematical model of deoxygenated HbS polymerization, as a kinetic and thermodynamic process under the influence of concentration and temperature –the two most important modulators. Building on an existing, but linearized and uncomplete (Ferrone et al., 1985) model, we have implemented, corrected and updated, and quantitatively evaluated its dynamical performances: this was done by full numerical integration using Simulink©. This allowed us to make several improvements, related in particular to : (i) the heterogeneous nucleation pathway (seeding and formation of new fibers from pre-existing ones), (ii) the non-ideality of the HbS protein solution, caused by polymer fibers excluded volume (activity coefficients were calculated with the CPT, Convex Particle Theory), and (iii) the spatial organization of polymers into domains. The model developped in this work will ground the description of the dynamic influence (i) oxygenation and non-polymerizing hemoglobins, (ii) HbS polymers interactions with membrane and consequences upon rheological properties of sickle cell erythrocyte
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Lee, Wen-Long, and 李文龍. "Polymerization of Hemoglobin by Genipin as Blood Substitute." Thesis, 1998. http://ndltd.ncl.edu.tw/handle/81494813122166358762.

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Tsai, Ching Hsuan, and 蔡靚璇. "Polymerization of Hemoglobin by Genipin for Blood Substitute." Thesis, 1996. http://ndltd.ncl.edu.tw/handle/98281214161793759646.

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Budhiraja, Vikas. "Effect of hemoglobin polymerization on the oxygen transport in hemoglobin solutions and packed cells." Thesis, 1997. http://hdl.handle.net/1911/19139.

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The effect of hemoglobin polymerization on the facilitated transport of oxygen in systems containing polymerized hemoglobins has been studied experimentally. In part I of this work, the oxygen transport efficacy of a candidate blood substitute based on polymerized bovine hemoglobin was studied. The diffusion of dissolved oxygen in the polymerized hemoglobin samples was not different from that in the unaltered hemoglobin solutions. However, in the high oxygen tension gradient (HOTG) decreasing pO$\sb2$ experiments at 37$\sp\circ$C, while the augmented oxygen transport was almost double than that of the simple diffusive flux of oxygen in the case of the latter, it was only increased by 30% in the case of polymerized hemoglobin. The lower facilitated oxygen transport is due to the decreased diffusion coefficient as well as the decreased oxygen affinity of the polymerized hemoglobin. For lower pO$\sb2$ gradients in the range of physiological significance (constant, low oxygen tension gradient, CLOTG, experiments), the oxygen transport in the polymerized hemoglobin samples was approximately the same as in unpolymerized sample over a wide range of oxygen tensions. At lower oxygen tensions, there was a significant augmentation effect, less than in the HOTG experiment and less for the polymerized than for the unploymerized Hb. In order to further confirm the results of diffusion cell experiments, in part II of this work, the diffusion coefficients of various unpolymerized and polymerized hemoglobins were measured using the PFG NMR technique. The diffusion coefficient values were in good agreement with those estimated from the diffusion cell experiments. The effect of hemoglobin polymerization on oxygen transport in sickle erythrocytes at 37$\sp\circ$C was studied in part III of this work. HOTG and CLOTG decreasing pO$\sb2$ diffusion cell experiments conducted on packed sickle cells show negligible enhancement of oxygen transport by sickle hemoglobin. Diffusion coefficients of unpolymerized HbS in the solution phase of slowly deoxygenating sickle cells was measured using PFG NMR technique. After an initial decrease the hemoglobin diffusion coefficient stays constant suggesting that though the polymer does offer appreciable resistance, it is not very high so as to drastically reduce the diffusion of hemoglobin and oxygen.
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Book chapters on the topic "HemoglobinS Polymerization"

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Prouty, Muriel S. "Polymerization and Phase Transitions in Deoxy Sickle Cell Hemoglobin." In ACS Symposium Series. American Chemical Society, 1992. http://dx.doi.org/10.1021/bk-1992-0493.ch016.

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MacDonald, Shirley L., and Duncan S. Pepper. "[19] Hemoglobin polymerization." In Hemoglobins Part B: Biochemical and Analytical Methods. Elsevier, 1994. http://dx.doi.org/10.1016/0076-6879(94)31021-1.

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Razynska, A., and E. Bucci. "Zero-link Polymerization: a New Class of Polymeric Hemoglobins." In Blood Substitutes, Present and Future Perspectives. Elsevier, 1998. http://dx.doi.org/10.1016/b978-044420524-7/50022-9.

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Eaton, William A., and James Hofrichter. "Sickle Cell Hemoglobin Polymerization." In Advances in Protein Chemistry. Elsevier, 1990. http://dx.doi.org/10.1016/s0065-3233(08)60287-9.

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Connes Philippe, Machado Roberto, Hue Olivier, and Reid Harvey. "Sickle Cell Anemia." In Biomedical and Health Research. IOS Press, 2010. https://doi.org/10.3233/978-1-60750-497-9-607.

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Sickle cell anemia (SCA or SS homozygous sickle cell disease) is an inherited blood disorder caused by single nucleotide substitution in the &amp;beta;-globin gene that renders their hemoglobin (HbS) much less soluble than normal hemoglobin (HbA) when deoxygenated. The polymerization of HbS upon deoxygenation is the basic pathophysiologic event leading to RBC sickling, hemolysis, vasoocclusion and ultimately to chronic organ damage.
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Ferrone, Frank A. "Hemoglobin S Polymerization, Just the Beginning." In Renaissance of Sickle Cell Disease Research in the Genome Era. PUBLISHED BY IMPERIAL COLLEGE PRESS AND DISTRIBUTED BY WORLD SCIENTIFIC PUBLISHING CO., 2007. http://dx.doi.org/10.1142/9781860947964_0009.

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Matsuhira, Takashi, Keizo Yamamoto, and Hiromi Sakai. "Ring-opening Polymerization of Hemoglobin Based on Supramolecular Chemistry." In Nanobiotherapeutic Based Blood Substitutes. WORLD SCIENTIFIC, 2022. http://dx.doi.org/10.1142/9789811228698_0016.

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Erhabor, Osaro, Teddy Charles Adias, Tosan Erhabor, Osaro Mgbere, Sadiya Usman, and Bibiana Nonye Egenti. "Role of Sociodemographic and Economic Variables in Predisposition to Vaso-Occlusive Crisis and Mortality in Patients with SCD: Case Study of Sub-Saharan Africa." In Sickle Cell Disease [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.105685.

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Sickle cell disease (SCD) is a major public health challenge. It is a common cause of acute and chronic illness and death, which results from a single amino acid substitution (glutamic acid to valine) at position 6 of the beta (β) chain of the hemoglobin molecule. The pathophysiology is based on the polymerization of deoxygenated hemoglobin S (HbS) and production of irreversibly sickled red cells and vaso-occlusive crisis (VOC). The disease is associated with recurrent episodes of acute pain and organ damage. This chapter highlights the role of SES on the predisposition to VOC and mortality among SCD patients. Findings from this review will enable the development and implementation of policies that can facilitate the effective management of SCD in the region. More awareness and education of parents of children and adults living with SCD are needed to identify factors that predispose patients to VOC and common-sense measures to prevent these triggers. SCD patients should be protected against malaria. The need for nutritional intervention, proper hydration, avoidance of dietary intake of sodium, strenuous physical activity, and extreme weather to reduce the incidence of VOC cannot be overemphasized. Protective immunization and access to effective prophylactic and therapeutic agents should be implemented.
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Bakker, J. C., W. K. Bleeker, H. J. H. Hens, P. T. M. Biessels, M. van Iterson, and A. Trouwborst. "Safety and Efficacy of Hemoglobin Modified by Crosslinking or Polymerization." In Blood Substitutes, Present and Future Perspectives. Elsevier, 1998. http://dx.doi.org/10.1016/b978-044420524-7/50019-9.

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Jain, Mr Ashutosh. "Haematological Disease-II." In Edited Book of Pathophysiology. Iterative International Publishers, Selfypage Developers Pvt Ltd, 2024. http://dx.doi.org/10.58532/nbennurebch8.

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Hematological diseases include various inherited disorders that affect the production and function of blood cells. Sickle cell anemia and thalassemia are two significant genetic blood disorders. Sickle cell anemia is characterized by the production of abnormal hemoglobin S, which causes red blood cells to become rigid and crescent-shaped. The pathophysiology involves the polymerization of hemoglobin S under low oxygen conditions, leading to vaso occlusive crises and hemolysis. Epidemiologically, sickle cell anemia predominantly affects individuals of African, Mediterranean, Middle Eastern, and Indian ancestry. Symptoms include severe pain episodes, anemia, swelling in the hands and feet, frequent infections, and delayed growth. Diagnosis is confirmed through hemoglobin electrophoresis. Treatment focuses on managing symptoms and preventing complications through pain management, hydroxyurea, blood transfusions, and bone marrow transplants. Complications can include stroke, acute chest syndrome, organ damage, and increased risk of infections. Prevention strategies involve genetic counseling and prenatal screening. Thalassemia is another inherited blood disorder characterized by reduced or absent production of one or more globin chains, leading to ineffective erythropoiesis and hemolysis. There are two main types: alpha and beta thalassemia, depending on which globin chain is affected. Epidemiologically, thalassemia is most common in individuals of Mediterranean, Middle Eastern, South Asian, and African descent. Symptoms vary depending on the severity and include anemia, fatigue, bone deformities, and growth delays. Severe forms, such as beta-thalassemia major, present early in life and require regular blood transfusions. Diagnosis involves blood tests showing microcytic hypochromic anemia and genetic testing. Treatment for severe thalassemia includes regular blood transfusions, iron chelation therapy to prevent iron overload, and bone marrow transplants. Complications can include heart and liver disease due to iron overload, growth retardation, and increased risk of infections. Prevention strategies include genetic counseling, carrier screening, and prenatal diagnosis to manage and reduce the incidence of these disorders
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Conference papers on the topic "HemoglobinS Polymerization"

1

Li, He, and George Lykotrafitis. "A Coarse-Grained Molecular Dynamics Model for Sickle Hemoglobin Fibers." In ASME 2010 International Mechanical Engineering Congress and Exposition. ASMEDC, 2010. http://dx.doi.org/10.1115/imece2010-37980.

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Abstract:
The intracellular polymerization of deoxy sickle cell hemoglobin (HbS) has been identified as the main cause of sickle cell disease. Therefore, the material properties and biomechanical behavior of polymerized HbS fibers have been a topic of intense research interest. A solvent-free coarse-grained molecular dynamics (CGMD) model has been developed and it represents a single hemoglobin fiber with four tightly bonded chains, each of which comprises soft particles. A harmonic spring potential, a bending potential, a torsional potential, and a Lennard-Jones potential are introduced along with a Langevin thermostat to simulate the behavior of a polymerized HbS fiber in the cytoplasm. The parameters of the potentials are identified via comparison of the simulation results with the experimentally measured values of bending and torsional rigidity of single HbS fibers. The proposed model is able to very efficiently simulate HbS fibers of 20 nm diameter and on the order of μm length-scale and μs time-scale. The model is validated by comparison with published experimental results and then it is used to investigate the interaction between two HbS fibers, and to study the fiber zippering process during heterogeneous fiber growth.
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