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Baron, J. F.

doi:10.1186/cc365

Cited by 20 publications

(2 citation statements)

References 25 publications

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“…The very first beginnings of hemoglobin application in biomedicine are related to its use as a blood substitute, i.e., more precisely as oxygen carriers (hemoglobin-based oxygen carriers, HBOCs) [ 32 , 42 , 43 , 44 ] ( Figure 2 ). The first HBOC was hemoglobin isolated from lysed erythrocytes given to patients intravenously.…”

Section: Exogenous Administration Of Extracellular Hemoglobinmentioning

confidence: 99%

“…Due to hemoglobin dimer precipitation in proximal tubules, nephrotoxic action occurs. Additionally, outside of erythrocytes, hemoglobin quickly oxidizes to methemoglobin, which cannot bind oxygen; instead, it releases heme, which participates in the creation of free radicals that exert harmful effects on surrounding cells [ 43 , 44 , 48 , 49 ]. After such reports on outcomes of extracellular hemoglobin administration, researchers have focused on obtaining recombinant hemoglobin by mutagenesis with desired features and reduced side effects.…”

Section: Exogenous Administration Of Extracellular Hemoglobinmentioning

confidence: 99%

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Extracellular Hemoglobin: Modulation of Cellular Functions and Pathophysiological Effects

et al. 2022

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Hemoglobin is essential for maintaining cellular bioenergetic homeostasis through its ability to bind and transport oxygen to the tissues. Besides its ability to transport oxygen, hemoglobin within erythrocytes plays an important role in cellular signaling and modulation of the inflammatory response either directly by binding gas molecules (NO, CO, and CO2) or indirectly by acting as their source. Once hemoglobin reaches the extracellular environment, it acquires several secondary functions affecting surrounding cells and tissues. By modulating the cell functions, this macromolecule becomes involved in the etiology and pathophysiology of various diseases. The up-to-date results disclose the impact of extracellular hemoglobin on (i) redox status, (ii) inflammatory state of cells, (iii) proliferation and chemotaxis, (iv) mitochondrial dynamic, (v) chemoresistance and (vi) differentiation. This review pays special attention to applied biomedical research and the use of non-vertebrate and vertebrate extracellular hemoglobin as a promising candidate for hemoglobin-based oxygen carriers, as well as cell culture medium additive. Although recent experimental settings have some limitations, they provide additional insight into the modulatory activity of extracellular hemoglobin in various cellular microenvironments, such as stem or tumor cells niches.

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Section: Exogenous Administration Of Extracellular Hemoglobinmentioning

confidence: 99%

Section: Exogenous Administration Of Extracellular Hemoglobinmentioning

confidence: 99%

Extracellular Hemoglobin: Modulation of Cellular Functions and Pathophysiological Effects

et al. 2022

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Blood Component Replacement Therapy

Sacks¹

2004

Critical Care Obstetrics

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Recognition of human hemoglobin with macromolecularly imprinted polymeric nanoparticles using non‐covalent interactions

Aylaz

Andaç

Deni̇zli̇

et al. 2021

J of Molecular Recognition

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Hemoglobin (Hb) is the most abundant protein in the blood. It is vital for the living as oxygen carriers. Some of the very pure Hb‐containing biological fluids are currently under clinical trial. However, the removal and purification of Hb from the blood are quite difficult, especially when it is at a low concentration level. In this study, the molecularly imprinted polymeric nanoparticles (MIPNs) were prepared using N‐methacryloyl‐histidine methyl ester (MAH) by mini‐emulsion polymerization technique for specific binding of human hemoglobin (HHb). MIPNs in monosize form have a size of 152 ± 4 nm. They also have a high binding capacity (32.33 mg/g) of HHb. MIPNs retain 84% of the re‐binding capacity for HHb after 10 cycles. The nanoparticles have 16 and 5 times higher binding capacity of HHb, respectively, in the presence of bovine serum albumin and lysozyme. Thanks to their high binding capacity and selectivity, MIPNs will allow them to be detected selectively for different target molecules. According to molecular docking, the main binding forces depend on hydrogen bonds and Van der Waals forces in the interaction within 5 Å around MAH molecule are observed through the amino acid residues of HHb at β1 and β2 subunit. The statistical mechanical analysis of docking showed that the free energy (ΔG) is −2732.14 kcal/mol, which indicates the interaction between MAH and HHb is energetically favorable at 298.15°K.

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Untitled

Cited by 20 publications

References 25 publications

Extracellular Hemoglobin: Modulation of Cellular Functions and Pathophysiological Effects

Extracellular Hemoglobin: Modulation of Cellular Functions and Pathophysiological Effects

Blood Component Replacement Therapy

Recognition of human hemoglobin with macromolecularly imprinted polymeric nanoparticles using non‐covalent interactions

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