{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,3]],"date-time":"2026-06-03T13:21:53Z","timestamp":1780492913740,"version":"3.54.1"},"reference-count":80,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2017,9,8]],"date-time":"2017-09-08T00:00:00Z","timestamp":1504828800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>The biochemical properties of erythrocyte or human red blood cell (RBC) membrane acetylcholinesterase (AChE) and its applications on laboratory class and on research are reviewed. Evidence of the biochemical and the pathophysiological properties like the association between the RBC AChE enzyme activity and the clinical and biophysical parameters implicated in several diseases are overviewed, and the achievement of RBC AChE as a biomarker and as a prognostic factor are presented. Beyond its function as an enzyme, a special focus is highlighted in this review for a new function of the RBC AChE, namely a component of the signal transduction pathway of nitric oxide.<\/jats:p>","DOI":"10.3390\/molecules22091499","type":"journal-article","created":{"date-parts":[[2017,9,8]],"date-time":"2017-09-08T11:34:52Z","timestamp":1504870492000},"page":"1499","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":66,"title":["Human Erythrocyte Acetylcholinesterase in Health and Disease"],"prefix":"10.3390","volume":"22","author":[{"given":"Carlota","family":"Saldanha","sequence":"first","affiliation":[{"name":"Instituto de Bioqu\u00edmica, Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Professor Egas Moniz, 1649-028 Lisboa, Portugal"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,9,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3939","DOI":"10.1182\/blood-2008-07-161166","article-title":"Red cell membrane: Past, present, and future","volume":"112","author":"Mohandas","year":"2008","journal-title":"Blood"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.tracli.2006.02.013","article-title":"Target cell CD47 regulates macrophages activation and erythrophagocytosis","volume":"13","author":"Ollon","year":"2006","journal-title":"Transf. Clin. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/s00109-006-0123-8","article-title":"Suicidal erythrocytes death in sepsis","volume":"85","author":"Kempe","year":"2007","journal-title":"J. Mol. Med."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/ajh.23344","article-title":"Changes in the properties of normal human red blood cells during in vivo aging","volume":"88","author":"Franco","year":"2013","journal-title":"Am. J. Hematol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0024-3205(98)00258-6","article-title":"Acetylcholinesterase: An enzymatic marker of human red blood cell aging","volume":"63","author":"Prall","year":"1998","journal-title":"Life Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0005-2736(74)90162-X","article-title":"Acetycholinesterase as a probe for erythrocyte-membrane intactness","volume":"339","author":"Aloni","year":"1974","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3233\/CH-2011-1512","article-title":"Erythrocyte as a biological sensor","volume":"51","author":"Oliveira","year":"2012","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"81","DOI":"10.3233\/JCB-15008","article-title":"Instrumental analysis applied to erythrocyte properties","volume":"1","author":"Saldanha","year":"2015","journal-title":"J. Cell Biotechnol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2007","DOI":"10.1096\/fasebj.3.9.2545495","article-title":"Endothelium-derived relaxing and contracting factors","volume":"3","author":"Furchgott","year":"1989","journal-title":"FASEB J."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"H1027","DOI":"10.1152\/ajpheart.00226.2005","article-title":"Acetylcholine causes endothelium-dependent contraction of mouse arteries","volume":"289","author":"Zhou","year":"2005","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1074\/jbc.275.4.2342","article-title":"Erythrocytes possess an intrinsic barrier to nitric oxide consumption","volume":"275","author":"Vaughn","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"11771","DOI":"10.1073\/pnas.201276698","article-title":"Modulation of nitric oxide bioavailability by erythrocytes","volume":"98","author":"Huang","year":"2001","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1073\/pnas.0409876102","article-title":"Impaired vasodilation by red blood cells in sickle cell disease","volume":"102","author":"Pawloski","year":"2005","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1182\/blood.V100.1.276","article-title":"Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes","volume":"100","author":"Bordin","year":"2002","journal-title":"Blood"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1073\/pnas.0409741102","article-title":"Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane","volume":"102","author":"Campanella","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","first-page":"183","article-title":"Modulation of erythrocyte hemorheological properties by band 3 phosphorylation and dephosphorylation","volume":"36","author":"Saldanha","year":"2007","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s00232-009-9162-8","article-title":"Modulation of erythrocytes acetylcholinesterase activity and its association with G protein. Band 3 interactions","volume":"228","author":"Carvalho","year":"2009","journal-title":"J. Membr. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1006\/niox.2001.0397","article-title":"Protein thiols and glutathione influence the nitric oxide-dependent regulation of the red blood cell F metabolism","volume":"6","author":"Galli","year":"2002","journal-title":"Nitric Oxide"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/abbi.2000.1825","article-title":"Redox capacity of cells affects inactivation of glutathione reductase by nitrosative stress","volume":"378","author":"Fujii","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0021-9258(18)73318-8","article-title":"Cholinesterases in the blood of man","volume":"133","author":"Alles","year":"1940","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/0005-2744(72)90053-8","article-title":"Human erythrocyte acetylcholinesterase purification, properties and kinetic behavior","volume":"284","author":"Cilliv","year":"1972","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1016\/0005-2736(84)90411-5","article-title":"Selective solubilization by melittin of glycophorin A and acetylcholinesterase from human erythrocyte ghosts","volume":"778","author":"Maulet","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/0304-4157(85)90016-4","article-title":"Membrane acetylcholinesterases: Purification, molecular properties and interactions with amphiphilic environments","volume":"822","author":"Ott","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_24","unstructured":"Saldanha, C. (1986). Acetilcolinesterase-Contribui\u00e7\u00e3o Para o estUdo Cin\u00e9tico da Enzima Eritrocit\u00e1ria de Homem. [Ph.D. Thesis, Universidade Nova de Lisboa]."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0005-2736(81)90559-9","article-title":"Interaction of human red cell membrane acetylcholinesterase with phospholipids","volume":"640","author":"Brodbeck","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"6991","DOI":"10.1021\/bi8006324","article-title":"The Glycosylphosphatidylinositol Anchor: A complex membrane-anchoring structure for proteins","volume":"47","author":"Paulick","year":"2008","journal-title":"Biochemistry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1182\/blood.V81.3.815.815","article-title":"Human erythrocyte acetylcholinesterase bears the Yta blood group antigen and is reduced or absent in the Yt(a-b-) phenotype","volume":"81","author":"Rao","year":"1993","journal-title":"Blood"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1042\/bj3290329","article-title":"Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration","volume":"15","author":"Marcel","year":"1998","journal-title":"Biochem. J."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1515\/znc-2002-11-1221","article-title":"Kinetics and mechanism of hydrolysis of acetylthiocholine by butyrylcholine esterase","volume":"57","author":"Komersa","year":"2002","journal-title":"Z. Naturforsch."},{"key":"ref_30","unstructured":"Reis, M.F., Miguel, J.M.P., Machado, A.A., and Abdulla, M. (1995). 7-Inhibition of purified human acetylcholinesterase activity by zinc and copper. Trace Elements in Medicine, Health and Atherosclerosis, Smith-Gordon Co."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1590\/S1678-91992012000200014","article-title":"Enzymatic and biochemical characterization of bungarus sindanus snake venom acetylcholinesterase","volume":"18","author":"Ahmed","year":"2012","journal-title":"J. Venom. Anim. Toxins Trop. Dis."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0005-2736(87)90126-X","article-title":"Modulation of erythrocyte vesiculation by amphiphilic drugs","volume":"901","author":"Brodbeck","year":"1987","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1002\/bmb.2004.494032040374","article-title":"A colorimetric process to visualize erythrocyte exovesicles aggregates","volume":"32","author":"Saldanha","year":"2004","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s00232-002-1025-5","article-title":"Fluorescent probes DPH, TMA-DPH and C17-HC induce erythrocyte exovesiculation","volume":"190","author":"Saldanha","year":"2002","journal-title":"J. Membr. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1385\/CBB:43:3:419","article-title":"Gramicidin D and dithiothreitol effects on erythrocyte exovesiculation","volume":"42","author":"Santos","year":"2005","journal-title":"Cell Biochem. Biophys."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1006\/bbrc.1994.1130","article-title":"Oxidative stress transforms acetylcholinesterase to a molten-globule-like state","volume":"198","author":"Weiner","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"6731","DOI":"10.1073\/pnas.0909533107","article-title":"Measurement of red blood cell mechanics during morphological changes","volume":"15","author":"Parka","year":"2010","journal-title":"Proc. Nat. Acad. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1248\/bpb.b110671","article-title":"Membrane perturbations induced by new analogs of neocryptolepine","volume":"35","author":"Jaromin","year":"2012","journal-title":"Biol. Pharm."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1203\/00006450-197304000-00024","article-title":"A Review: Human erythrocyte acetylcholinesterase","volume":"7","author":"Herz","year":"1973","journal-title":"Pediatr. Res."},{"key":"ref_40","first-page":"89","article-title":"An in vitro study of adrenaline effect on human erythrocyte properties in both gender","volume":"28","author":"Saldanha","year":"2003","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1186\/1476-069X-13-98","article-title":"Pesticide use, erythrocyte acetylcholinesterase level and self-reported acute intoxication symptoms among vegetable farmers in Nepal: A cross-sectional study","volume":"13","author":"Neupane","year":"2014","journal-title":"Environ. Health"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.cbi.2016.04.008","article-title":"Activity and determinants of cholinesterases and paraoxonase-1 in blood of workers exposed to non-cholinesterase inhibiting pesticides","volume":"259","author":"Gil","year":"2016","journal-title":"Chem. Biol. Interact."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"135","DOI":"10.3233\/CHM-1998-074","article-title":"The effect of sodium fluorescein angiography on erythrocyte properties","volume":"18","author":"Sargento","year":"1998","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/BF01675356","article-title":"Plasma dopamine-beta-hydroxylase and erythrocyte acetylcholinesterase in a group of patients with Parkinson disease","volume":"42","author":"Coelho","year":"1978","journal-title":"J. Neur. Transm."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/BF01249194","article-title":"Erythrocyte acetylcholinesterase in essential hypertension","volume":"49","author":"Nogueira","year":"1980","journal-title":"J. Neural Transm."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/eye.1999.18","article-title":"Red blood cell membrane integrity in primary open angle glaucoma: Ex vivo and in vitro studies","volume":"13","author":"Zabala","year":"1999","journal-title":"Eye"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1038\/eye.1988.53","article-title":"Haematological changes in retinal vasculitis","volume":"2","author":"Ramalho","year":"1988","journal-title":"Eye"},{"key":"ref_48","first-page":"989","article-title":"Identification of erythrocyte biomarkers in amyotrophic lateral sclerosis","volume":"64","author":"Duarte","year":"2016","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_49","first-page":"79","article-title":"Role of erythrocyte acetylcholinesterase in the diagnosis of hirschsprung\u2019s Disease","volume":"3","author":"Chalkoo","year":"2013","journal-title":"J. Pioneer. Med. Stud."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1161\/HYPERTENSIONAHA.110.163576","article-title":"Inflammation, immunity, and hypertension","volume":"57","author":"Harrison","year":"2011","journal-title":"Hypertension"},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Gupta, V.K., Pal, R., Siddiqi, N.J., and Sharma, B. (2015). Acetylcholinesterase from human erythrocytes as a surrogate biomarker of lead induced neurotoxicity. Enzyme Res., 2015.","DOI":"10.1155\/2015\/370705"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1177\/1178630217704659","article-title":"Risk factors of pesticide poisoning and pesticide users\u2019 cholinesterase levels in cotton production areas: Glazou\u00e9 and sav\u00e8 townships, in central republic of benin","volume":"11","author":"Vikkey","year":"2017","journal-title":"Environ. Health Insights"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1136\/bjo.2003.028357","article-title":"Nitric oxide proxies and ocular perfusion pressure in primary open angle glaucoma","volume":"88","author":"Galassi","year":"2004","journal-title":"Br. J. Ophtalmol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1021\/ar300234c","article-title":"Protein tyrosine nitration: Biochemical mechanisms and structural basis of its functional effects","volume":"46","author":"Rafael","year":"2013","journal-title":"Acc. Chem. Res."},{"key":"ref_55","first-page":"214","article-title":"Acetylcholinesterase and butyrylcholinesterase as possible markers of low-grade systemic inflammation","volume":"12","author":"Das","year":"2007","journal-title":"Med. Sci. Monit."},{"key":"ref_56","first-page":"195","article-title":"Effects of acetylcholine on an animal model of inflammation","volume":"53","author":"Saldanha","year":"2013","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_57","first-page":"803","article-title":"Evolving of endothelium cells in inflammation","volume":"7","author":"Pober","year":"2007","journal-title":"Nat. Rev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1007\/s00281-011-0290-8","article-title":"Fibrinogen as a key regulator of inflammation in disease","volume":"34","author":"Davalos","year":"2012","journal-title":"Semin. Immunopathol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0163-7258(99)00071-6","article-title":"Extraneuronal cholinergic system in lymphocytes","volume":"86","author":"Kawashima","year":"2000","journal-title":"Pharmacol. Ther."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/bios4010001","article-title":"Application of a nitric oxide sensor in biomedicine","volume":"4","author":"Saldanha","year":"2014","journal-title":"Biosensors"},{"key":"ref_61","first-page":"111","article-title":"The modulation of cyclic nucleotide levels and PKC activity by acetylcholinesterase effectors in human erythrocytes","volume":"9","author":"Almeida","year":"2008","journal-title":"Acta Bioqu\u00edmica"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1042\/bj20020359","article-title":"Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3","volume":"368","author":"Zipser","year":"2002","journal-title":"Biochem. J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"4592","DOI":"10.1016\/S0021-9258(18)61234-7","article-title":"Tyrosine phosphorylation of band 3 inhibits peripheral protein binding","volume":"262","author":"Low","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_64","first-page":"3","article-title":"Timolol modulates erythrocyte nitric oxide bioavailability","volume":"4","author":"Saldanha","year":"2013","journal-title":"J. Clin. Exp. Optalmol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S0079-6603(00)66031-2","article-title":"Regulation and function of the cyclic nucleotide phosphodiesterase (PDE3) gene family","volume":"66","author":"Shakur","year":"2001","journal-title":"Prog. Nucleic Acid Res. Mol. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"207","DOI":"10.3233\/CH-2008-1130","article-title":"Non-neuronal cholinergic system and signal transduction pathways mediated by band 3 in red blood cells","volume":"40","author":"Carvalho","year":"2008","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1002\/jat.993","article-title":"Acetylcholine and choline effects on erytrocytes nitrite and nitrate levels","volume":"24","author":"Carvalho","year":"2004","journal-title":"J. Appl. Toxicol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.cellbi.2008.11.012","article-title":"Redox thiol status plays a central role in the mobilization and metabolism of nitric oxide in human red blood cells","volume":"33","author":"Carvalho","year":"2009","journal-title":"Cell Biol. Int."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1007\/s00232-015-9776-y","article-title":"Acetylcholinesterase conformational states influence nitric oxide mobilization in the erythrocyte","volume":"248","author":"Teixeira","year":"2015","journal-title":"J. Membr. Biol."},{"key":"ref_70","first-page":"407","article-title":"Evidence that the degree of band 3 phosphorylation modulates human erythrocytes nitric oxide efflux-in vitro model of hyperfibrinogenemia","volume":"49","author":"Saldanha","year":"2011","journal-title":"Clin. Hemorh. Microc."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.lfs.2012.06.035","article-title":"Fibrinogen effects on erythrocyte nitric oxide mobilization in presence of acetylcholine","volume":"91","author":"Saldanha","year":"2012","journal-title":"Life Sci."},{"key":"ref_72","first-page":"28","article-title":"Fibrinogen signaling in erythrocyte nitric oxide mobilization in presence of PI3-K and adenylyl cyclase inhibitors","volume":"3","author":"Freitas","year":"2016","journal-title":"Eur. J. Biomed. Pharm. Sci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.bbamem.2011.10.028","article-title":"Integrin-associated protein (CD47) is a putative mediator for soluble fibrinogen interaction with human red blood cells membrane","volume":"1818","author":"Calado","year":"2012","journal-title":"Biochem. Biophys. Acta"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1007\/s00232-009-9204-2","article-title":"Fibrinogen-dependent signaling in microvascular erythrocyte function: Implications on nitric oxide efflux","volume":"231","author":"Saldanha","year":"2009","journal-title":"J. Membr. Biol."},{"key":"ref_75","unstructured":"Saldanha, C., and Silva-Herdade, A.S. (2017, January 3\u20135). Casein kinase effects on nitric oxide metabolism and deformability of human erythocytes, XI. Proceedings of the Abstract Book of International Conference on Hemorheology and Microcirculation, Yaroslavl, Russia."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Saldanha, C., and Silva-Herdade, A.S. (2017). Physiological properties of erythrocytes in inflammation. J. Cell. Biotechnol., 3.","DOI":"10.3233\/JCB-179003"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1089\/jop.2015.0121","article-title":"Oral administration of forskolin, homotaurine, carnosine, and folic acid in patients with primary open angle glaucoma: Changes in intraocular pressure, pattern electroretinogram amplitude and foveal sensitivity","volume":"32","author":"Mutolo","year":"2016","journal-title":"J. Ocul. Pharmacol. Ther."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"369","DOI":"10.3233\/CH-152029","article-title":"Oxidative stress in the red blood cells of patients with primary open-angle glaucoma","volume":"62","author":"Rokicki","year":"2016","journal-title":"Clin. Hemorheol. Microcirc."},{"key":"ref_79","first-page":"989","article-title":"Erythrocyte nitric oxide in glaucoma patients\u2014Ex vivo study","volume":"64","author":"Esteves","year":"2016","journal-title":"Clin. Hemorh. Microcirc."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1038\/35054560","article-title":"Export by red blood cells of nitric oxide bioactivity","volume":"409","author":"Pawloski","year":"2001","journal-title":"Nature"}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/22\/9\/1499\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:44:28Z","timestamp":1760208268000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/22\/9\/1499"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,9,8]]},"references-count":80,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2017,9]]}},"alternative-id":["molecules22091499"],"URL":"https:\/\/doi.org\/10.3390\/molecules22091499","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,9,8]]}}}