Evaluation of the effect of brominated flame retardants on hemoglobin oxidation and hemolysis in human erythrocytes

Jarosiewicz, Monika; Duchnowicz, Piotr; Włuka, Anna; Bukowska, Bożena

doi:10.1016/j.fct.2017.09.016

Cited by 32 publications

(12 citation statements)

References 32 publications

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“…Our previous study [9] demonstrated that analyzed BFRs even at relatively low (environmental relevant) concentrations, caused ROS production in human RBCs. BFRs studied also increased the methemoglobin level in human RBCs [11].…”

Section: Discussionmentioning

confidence: 74%

“…Considering the fact that BFRs are potentially able to be incorporated into RBC membrane, triggering eryptosis and hemolysis [9,11], the decision was made to analyze how they can directly affect basic (protein) membrane components. For this purpose, tryptophan fluorescence was measured in the membrane of RBC.…”

Section: Discussionmentioning

confidence: 99%

“…RBCs were isolated from buffy coat obtained from blood from healthy donors from the Regional Centre of Blood Donation and Blood Treatment (Lodz, Poland). The RBCs' isolation procedure was previously described by Jarosiewicz et al (2017) [11]. RBCs with hematocrit of 5% (about 630 mln cells/mL) were incubated with tested compounds at 37 • C for 48 h. The samples that contained the RBCs, Ringer buffer and DMSO (final concentration 0.4%) were used as negative controls and compared to the samples without DMSO, so it was possible to exclude its influence on RBCs.…”

Section: Erythrocyte and Erythrocyte's Membrane Isolationmentioning

confidence: 99%

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Evaluation of the Effect of Selected Brominated Flame Retardants on Human Serum Albumin and Human Erythrocyte Membrane Proteins

Jarosiewicz

Miłowska

Krokosz

et al. 2020

IJMS

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Brominated flame retardants (BFRs) have been using to reduce the flammability of plastics contained in many products, such as household articles, furniture, mattresses, textiles or insulation. Considering the fact that these compounds may be released into the environment leading to the exposure of living organisms, it is necessary to study their possible effects and mechanisms of action. Proteins play a crucial role in all biological processes. For this reason, a simple model of human serum albumin (HSA) was chosen to study the mechanism of BFRs’ effect on proteins. The study determined interactions between selected BFRs, i.e., tetrabromobisphenol A (TBBPA), tetrabromobisphenol S (TBBPS), 2,4-dibromophenol (2,4-DBP), 2,4,6-tribromophenol (2,4,6-TBP) and pentabromophenol (PBP), and HSA by measurement of fluorescence of intrinsic tryptophan and absorbance of circular dichroism (CD). In addition, in order to understand the possible effect of these compounds in their native environment, the effect of BFRs on membrane proteins of human erythrocytes (red blood cells, RBCs) was also assessed. Among bromophenols, PBP had the strongest oxidative effect on RBC membrane, and 2,4-DBP demonstrated the weakest fluorescence-quenching effect of both membrane tryptophan and HSA. By contrast to PBP, 2,4-DBP and 2,4,6-TBP caused spatial changes of HSA. We have observed that among all analyzed BFRs, TBBPA caused the strongest oxidation of RBC membrane proteins and the model HSA protein, causing reduction of fluorescence of tryptophan contained in them. TBBPA also changed albumin conformation properties, leading to impairment of the α-helix structure. However, TBBPS had the weakest oxidative effect on proteins among studied BFRs and did not affect the secondary structure of HSA.

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Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Erythrocyte and Erythrocyte's Membrane Isolationmentioning

confidence: 99%

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Evaluation of the Effect of Selected Brominated Flame Retardants on Human Serum Albumin and Human Erythrocyte Membrane Proteins

Jarosiewicz

Miłowska

Krokosz

et al. 2020

IJMS

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“…Hemolysis leads to a release of Hb from erythrocytes. This phenomenon can contribute to metHb 3+ formation, which is incapable of oxygen transport as it binds to oxygen very tightly and does not release it in tissues, even when the partial pressure of oxygen is low [ 38 , 53 , 54 , 55 ].…”

Section: Discussionmentioning

confidence: 99%

Human Erythrocytes Exposed to Phthalates and Their Metabolites Alter Antioxidant Enzyme Activity and Hemoglobin Oxidation

Sicińska

Kik

Bukowska

2020

IJMS

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Phthalates used as plasticizers have become a part of human life because of their important role in various industries. Human exposure to these compounds is unavoidable, and therefore their mechanisms of toxicity should be investigated. Due to their structure and function, human erythrocytes are increasingly used as a cell model for testing the in vitro toxicity of various xenobiotics. Therefore, the purpose of our study was to assess the effect of selected phthalates on methemoglobin (metHb), reactive oxygen species (ROS) including hydroxyl radical levels, as well as the activity of antioxidative enzymes, such as superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GSH-Px), in human erythrocytes. Erythrocytes were incubated with di-n-butyl phthalate (DBP), butylbenzyl phthalate (BBP), and their metabolites, i.e., mono-n-butyl phthalate (MBP) and monobenzyl phthalate (MBzP), at concentrations ranging from 0.5 to 100 µg/mL for 6 or 24 h. This study shows that the analyzed phthalates disturbed the redox balance in human erythrocytes. DBP and BBP, at much lower concentrations than their metabolites, caused a statistically significant increase of metHb and ROS, including hydroxyl radical levels, and changed the activity of antioxidant enzymes. The studied phthalates disturbed the redox balance in human erythrocytes, which may contribute to the accelerated removal of these cells from the circulation.

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“…The haemoglobin oxidation was determined as the methaemoglobin level according to the method described previously 48 . Briefly, after incubation of RBCs with 10 −7 g/ml of h-BN-OH-n for 1 hour at 37 °C, cells were treated with deionized water (+4 °C for 2 hours) and centrifuged (3000 rpm for 10 min at 4 °C).…”

Section: Methodsmentioning

confidence: 99%

Non-cytotoxic hydroxyl-functionalized exfoliated boron nitride nanoflakes impair the immunological function of insect haemocytes in vivo

Czarniewska

Mrówczyńska

Jędrzejczak-Silicka

et al. 2019

Sci Rep

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To induce the water solubility of hexagonal boron nitride (h-BN), we exfoliated and functionalized bulk h-BN with hydroxyl groups (h-BN-OH-n). Short-term studies showed that h-BN-OH-n induced low cytotoxicity in different models: insect haemocytes (in vivo), human erythrocytes and mouse fibroblasts (in vitro). We also demonstrated that Alexa Fluor 647-h-BN-OH-n administered topically to the insects passed through the cuticle barrier and was phagocytosed by haemocytes. Nanoflakes did not affect the haemocyte cell membrane and did not interfere with the phagocytosis of latex beads. Long-term immunoassays showed that h-BN-OH-n, despite not inducing haemocytotoxicity, impaired nodulation, the most important cellular immune response in insects. The haemocytes exposed to h-BN-OH-n and then to bacteria differed in morphology and adhesiveness from the haemocytes exposed only to bacteria and exhibited the same morphology and adhesiveness as the control haemocytes. The h-BN-OH-n-induced decrease in nodulation can therefore result from the reduced ability of haemocytes to recognize bacteria, migrate to them or form microaggregates around them, which can lead to dysfunction of the immune system during pathogen infection. Long-term in vivo studies with animal models are still necessary to unambiguously confirm that h-BN is biocompatible and useful for application as a platform for drug delivery or for bioimaging.

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Evaluation of the effect of brominated flame retardants on hemoglobin oxidation and hemolysis in human erythrocytes

Cited by 32 publications

References 32 publications

Evaluation of the Effect of Selected Brominated Flame Retardants on Human Serum Albumin and Human Erythrocyte Membrane Proteins

Evaluation of the Effect of Selected Brominated Flame Retardants on Human Serum Albumin and Human Erythrocyte Membrane Proteins

Human Erythrocytes Exposed to Phthalates and Their Metabolites Alter Antioxidant Enzyme Activity and Hemoglobin Oxidation

Non-cytotoxic hydroxyl-functionalized exfoliated boron nitride nanoflakes impair the immunological function of insect haemocytes in vivo

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