{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T09:12:53Z","timestamp":1777281173805,"version":"3.51.4"},"reference-count":0,"publisher":"Cell Physiol Biochem Press GmbH and Co KG","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell Physiol Biochem"],"abstract":"<jats:p>Background\/Aims: Brominated flame retardants (BFRs) are a group of synthetic compounds widely used to reduce the flammability of various materials. Due to their large scale production and extensive industrial application, increasing concern has arisen regarding their persistence in the environment and potential toxicological effects. In an effort to identify novel biomarkers indicative of cellular dysfunction caused by BFRs exposure, the aim of the present study is to investigate the activity of acetylcholinesterase (AChE) in human erythrocytes exposed to selected compounds, including tetrabromobisphenol A (TBBPA), tetrabromobisphenol S (TBBPS), 2,4-dibromophenol (2,4-DBP), 2,4,6-tribromophenol (2,4,6-TBP), and pentabromophenol (PBP). Methods: AChE activity was determined spectrophotometrically using Ellman\u2019s method after incubation of erythrocytes with the tested compounds. Results: The obtained results demonstrated that both TBBPA and TBBPS induced significant alterations in AChE activity. A statistically significant increase in enzyme activity was observed at concentrations of 10 \u00b5g\/mL for TBBPA and 50 \u00b5g\/mL for TBBPS. In the case of bromophenols, significant changes were detected only for 2,4,6-TBP at 25 \u00b5g\/mL and PBP at 10 \u00b5g\/mL. Conclusion: The results indicate that the biological effects of BFRs depend on their chemical structure and concentration. Although erythrocyte AChE activity responds to BFR exposure, it should not be regarded as a highly sensitive biosensor, since detectable alterations occur at concentrations that simultaneously elicit other cellular effects, including lipid peroxidation, phosphatidylserine externalization, and modifications in membrane fluidity, as reported in previous studies.<\/jats:p>","DOI":"10.33594\/000000863","type":"journal-article","created":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T08:26:16Z","timestamp":1777278376000},"page":"213-222","source":"Crossref","is-referenced-by-count":0,"title":["Acetylcholinesterase Activity in Erythrocytes: a Functional Sensor of Environmental Toxicity from Brominated Flame Retardants"],"prefix":"10.33594","volume":"60","author":[{"given":"Monika","family":"Jarosiewicz","sequence":"first","affiliation":[{"name":"Department of Biophysics of Environmental Pollution, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141\/143, 90-236 Lodz, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bo\u017cena","family":"Bukowska","sequence":"additional","affiliation":[{"name":"Department of Biophysics of Environmental Pollution, Faculty of Biology and Environmental Protection, University of Lodz, Pomorska 141\/143, 90-236 Lodz, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"19235","published-online":{"date-parts":[[2026,4,27]]},"container-title":["Cellular Physiology and Biochemistry"],"original-title":[],"deposited":{"date-parts":[[2026,4,27]],"date-time":"2026-04-27T08:26:17Z","timestamp":1777278377000},"score":1,"resource":{"primary":{"URL":"https:\/\/cellphysiolbiochem.com\/Articles\/000863\/index.html"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4,27]]},"references-count":0,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2026,4,27]]}},"URL":"https:\/\/doi.org\/10.33594\/000000863","relation":{},"ISSN":["1015-8987","1421-9778"],"issn-type":[{"value":"1015-8987","type":"print"},{"value":"1421-9778","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,4,27]]}}}