{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T23:22:06Z","timestamp":1790637726226,"version":"4.1.0"},"reference-count":63,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2022,3,29]],"date-time":"2022-03-29T00:00:00Z","timestamp":1648512000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP1099991"],"award-info":[{"award-number":["APP1099991"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Eunice Kennedy Shiver National Institute of Child Health and Human Development","award":["R01HD084628"],"award-info":[{"award-number":["R01HD084628"]}]},{"name":"Flinders Foundation","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}]},{"name":"Australian Institute of Nuclear Science and Engineering (AINSE) Post-graduate Research Award","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Plasminogen activator inhibitor type-2 (PAI-2), a member of the serpin family, is dramatically upregulated during pregnancy and in response to inflammation. Although PAI-2 exists in glycosylated and non-glycosylated forms in vivo, the majority of in vitro studies of PAI-2 have exclusively involved the intracellular non-glycosylated form. This study shows that exposure to inflammation-associated hypochlorite induces the oligomerisation of PAI-2 via a mechanism involving dityrosine formation. Compared to plasminogen activator inhibitor type-1 (PAI-1), both forms of PAI-2 are more resistant to hypochlorite-induced inactivation of its protease inhibitory activity. Holdase-type extracellular chaperone activity plays a putative non-canonical role for PAI-2. Our data demonstrate that glycosylated PAI-2 more efficiently inhibits the aggregation of Alzheimer\u2019s disease and preeclampsia-associated amyloid beta peptide (A\u03b2), compared to non-glycosylated PAI-2 in vitro. However, hypochlorite-induced modification of non-glycosylated PAI-2 dramatically enhances its holdase activity by promoting the formation of very high-molecular-mass chaperone-active PAI-2 oligomers. Both PAI-2 forms protect against A\u03b2-induced cytotoxicity in the SH-SY5Y neuroblastoma cell line in vitro. In the villous placenta, PAI-2 is localised primarily to syncytiotrophoblast with wide interpersonal variation in women with preeclampsia and in gestational-age-matched controls. Although intracellular PAI-2 and A\u03b2 staining localised to different placental cell types, some PAI-2 co-localised with A\u03b2 in the extracellular plaque-like aggregated deposits abundant in preeclamptic placenta. Thus, PAI-2 potentially contributes to controlling aberrant fibrinolysis and the accumulation of misfolded proteins in states characterised by oxidative and proteostasis stress, such as in Alzheimer\u2019s disease and preeclampsia.<\/jats:p>","DOI":"10.3390\/cells11071152","type":"journal-article","created":{"date-parts":[[2022,3,29]],"date-time":"2022-03-29T21:40:14Z","timestamp":1648590014000},"page":"1152","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["A Novel Role for Plasminogen Activator Inhibitor Type-2 as a Hypochlorite-Resistant Serine Protease Inhibitor and Holdase Chaperone"],"prefix":"10.3390","volume":"11","author":[{"given":"Jordan H.","family":"Cater","sequence":"first","affiliation":[{"name":"Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia"},{"name":"School of Chemistry and Biomolecular Science, University of Wollongong, Wollongong 2522, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noralyn B.","family":"Ma\u00f1ucat-Tan","sequence":"additional","affiliation":[{"name":"Flinders Health and Medical Research Institute and College of Medicine and Public Health, Flinders University, Bedford Park 5042, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1196-6674","authenticated-orcid":false,"given":"Demi K.","family":"Georgiou","sequence":"additional","affiliation":[{"name":"Flinders Health and Medical Research Institute and College of Medicine and Public Health, Flinders University, Bedford Park 5042, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guomao","family":"Zhao","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Illinois at Chicago College of Medicine, Chicago, IL 60611, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irina A.","family":"Buhimschi","sequence":"additional","affiliation":[{"name":"Department of Obstetrics and Gynaecology, University of Illinois at Chicago College of Medicine, Chicago, IL 60611, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amy R.","family":"Wyatt","sequence":"additional","affiliation":[{"name":"Flinders Health and Medical Research Institute and College of Medicine and Public Health, Flinders University, Bedford Park 5042, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5570-9645","authenticated-orcid":false,"given":"Marie","family":"Ranson","sequence":"additional","affiliation":[{"name":"Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong 2522, Australia"},{"name":"School of Chemistry and Biomolecular Science, University of Wollongong, Wollongong 2522, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,3,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1055\/s-0031-1276589","article-title":"Forty years later and the role of plasminogen activator inhibitor type 2\/SERPINB2 is still an enigma","volume":"37","author":"Lee","year":"2011","journal-title":"Semin. Thromb. Hemost."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1111\/j.1432-1033.1988.tb14162.x","article-title":"Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator by plasminogen-activator inhibitor type 1 and type 2","volume":"175","author":"Thorsen","year":"1988","journal-title":"Eur. J. Biochem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.yexcr.2004.03.030","article-title":"Kinetic analysis of plasminogen activator inhibitor type-2: Urokinase complex formation and subsequent internalisation by carcinoma cell lines","volume":"297","author":"Croucher","year":"2004","journal-title":"Exp. Cell Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1160\/TH10-02-0121","article-title":"Differential endocytosis of tissue plasminogen activator by serpins PAI-1 and PAI-2 on human peripheral blood monocytes","volume":"104","author":"Lee","year":"2010","journal-title":"Thromb. Haemost."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4858","DOI":"10.1111\/j.1742-4658.2005.04879.x","article-title":"The undecided serpin. The ins and outs of plasminogen activator inhibitor type 2","volume":"272","author":"Medcalf","year":"2005","journal-title":"FEBS J."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1615\/CritRevImmunol.v31.i1.20","article-title":"The role of SerpinB2 in immunity","volume":"31","author":"Schroder","year":"2011","journal-title":"Crit. Rev. Immunol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1879","DOI":"10.1111\/j.1538-7836.2005.01420.x","article-title":"PAI-1 and atherothrombosis","volume":"3","author":"Vaughan","year":"2005","journal-title":"J. Thromb. Haemost."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1055\/s-2007-996035","article-title":"Significance of the plasminogen activator inhibitor of placental type (PAI-2) in pregnancy","volume":"24","author":"Astedt","year":"1998","journal-title":"Semin. Thromb. Hemost."},{"key":"ref_9","first-page":"e0130136","article-title":"SerpinB2 (PAI-2) modulates proteostasis via binding misfolded proteins and promotion of cytoprotective inclusion formation","volume":"10","author":"Lee","year":"2015","journal-title":"Public Libr. Sci. One"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1016\/0006-291X(90)90909-7","article-title":"Plasminogen activator inhibitor 2 (PAI-2) is not inactivated by exposure to oxidants which can be released from activated neutrophils","volume":"166","author":"Baker","year":"1990","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"13852","DOI":"10.1016\/S0021-9258(18)92780-8","article-title":"The oxidative inactivation of plasminogen activator inhibitor type 1 results from a conformational change in the molecule and does not require the involvement of the P1\u2019methionine","volume":"266","author":"Strandberg","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1182\/blood.V69.2.460.460","article-title":"Fibrinolysis in pregnancy: A study of plasminogen activator inhibitors","volume":"69","author":"Kruithof","year":"1987","journal-title":"Blood"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1084\/jem.165.2.320","article-title":"Plasminogen activator-specific inhibitors produced by human monocytes\/macrophages","volume":"165","author":"Wohlwend","year":"1987","journal-title":"J. Exp. Med."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1159\/000366365","article-title":"The Chaperone Activity of Clusterin is Dependent on Glycosylation and Redox Environment","volume":"34","author":"Rohne","year":"2014","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_15","first-page":"5150","article-title":"Glycosylation of SPARC is Critical for Binding to Extracellular Matrix Proteins and Protection from Matrix Metalloproteinase Degradation","volume":"60","author":"Fox","year":"2019","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1093\/toxsci\/kfq206","article-title":"Glycosylation Protects Proteins against Free Radicals Generated from Toxic Xenobiotics","volume":"117","author":"Frei","year":"2010","journal-title":"Toxicol. Sci."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"311","DOI":"10.3109\/10715769709065769","article-title":"Effect of active oxygen radicals on protein and carbohydrate moieties of recombinant human erythropoietin","volume":"27","author":"Uchida","year":"1997","journal-title":"Free Radic. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1038\/labinvest.3780263","article-title":"Myeloperoxidase-dependent generation of hypochlorite-modified proteins in human placental tissues during normal pregnancy","volume":"81","author":"Hammer","year":"2001","journal-title":"Lab. Investig."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1182\/blood.V74.4.1332.1332","article-title":"Changes in the plasma levels of type 1 and type 2 plasminogen activator inhibitors in normal pregnancy and in patients with severe preeclampsia","volume":"74","author":"Estelles","year":"1989","journal-title":"Blood"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1111\/j.1471-0528.1993.tb12982.x","article-title":"Plasminogen activator inhibitors (PAI-1 and PAI-2) in normal pregnancies, pre-eclampsia and hydatidiform mole","volume":"100","author":"Reith","year":"1993","journal-title":"Br. J. Obstet. Gynaecol. Int. J. Obstet. Gynaecol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1055\/s-0038-1650657","article-title":"Decreased expression of PAI-2 mRNA and protein in pregnancies complicated with intrauterine fetal growth retardation","volume":"76","author":"Grancha","year":"1996","journal-title":"Thromb. Haemost."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"245ra292","DOI":"10.1126\/scitranslmed.3008808","article-title":"Protein misfolding, congophilia, oligomerization, and defective amyloid processing in preeclampsia","volume":"6","author":"Buhimschi","year":"2014","journal-title":"Sci. Transl. Med."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"4069","DOI":"10.1016\/S0021-9258(18)53581-X","article-title":"Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages","volume":"268","author":"Heinecke","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_24","first-page":"1","article-title":"The CD-loop of PAI-2 (SERPINB2) is redundant in the targeting, inhibition and clearance of cell surface uPA activity","volume":"9","author":"Cochran","year":"2009","journal-title":"BioMed Cent. Biotechnol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1080\/10715760000301011","article-title":"Plasma protein carbonyls in nonpregnant, healthy pregnant and preeclamptic women","volume":"33","author":"Zusterzeel","year":"2000","journal-title":"Free Radic. Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1053\/plac.2000.0606","article-title":"Protein carbonyls in decidua and placenta of pre-eclamptic women as markers for oxidative stress","volume":"22","author":"Zusterzeel","year":"2001","journal-title":"Placenta"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1172\/JCI119379","article-title":"3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima","volume":"99","author":"Hazen","year":"1997","journal-title":"J. Clin. Investig."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"012056","DOI":"10.1088\/1742-6596\/291\/1\/012056","article-title":"Peroxidase-induced degradation of single-walled carbon nanotubes: Hypochlorite is a major oxidant capable of in vivo degradation of carbon nanotubes","volume":"291","author":"Vlasova","year":"2011","journal-title":"J. Phys. Conf. Ser."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1056\/NEJM198902093200606","article-title":"Tissue destruction by neutrophils","volume":"320","author":"Weiss","year":"1989","journal-title":"New Engl. J. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1016\/j.yexcr.2013.02.018","article-title":"Secretion of SerpinB2 from endothelial cells activated with inflammatory stimuli","volume":"319","author":"Boncela","year":"2013","journal-title":"Exp. Cell Res."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1006\/excr.1998.4118","article-title":"Secretion of plasminogen activator inhibitor 2 by human peripheral blood monocytes occurs via an endoplasmic reticulum\u2013golgi-independent pathway","volume":"242","author":"Ritchie","year":"1998","journal-title":"Exp. Cell Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1681\/ASN.2019101085","article-title":"SerpinB2 Regulates Immune Response in Kidney Injury and Aging","volume":"31","author":"Sen","year":"2020","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1016\/j.ajpath.2016.02.017","article-title":"SerpinB2 Deficiency Results in a Stratum Corneum Defect and Increased Sensitivity to Topically Applied Inflammatory Agents","volume":"186","author":"Schroder","year":"2016","journal-title":"Am. J. Pathol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2968","DOI":"10.1111\/jth.15054","article-title":"Deficiency of plasminogen activator inhibitor-2 results in accelerated tumor growth","volume":"18","author":"Westrick","year":"2020","journal-title":"J. Thromb. Haemost."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1161\/HYPERTENSIONAHA.107.107532","article-title":"Increased myeloperoxidase in the placenta and circulation of women with preeclampsia","volume":"52","author":"Gandley","year":"2008","journal-title":"Hypertension"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1177\/107602960501100415","article-title":"Coagulation and fibrinolysis in preeclampsia and neonates","volume":"11","author":"Tanjung","year":"2005","journal-title":"Clin. Appl. Thromb. Hemost. Off. J. Int. Acad. Clin. Appl. Thromb. Hemost."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1093\/abbs\/36.1.42","article-title":"Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1","volume":"36","author":"Fan","year":"2004","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1039\/B712728F","article-title":"Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity","volume":"4","author":"Wilson","year":"2008","journal-title":"Mol. Biosyst."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1412","DOI":"10.1021\/bi062082v","article-title":"Effects of glycosylation on the structure and function of the extracellular chaperone clusterin","volume":"46","author":"Stewart","year":"2007","journal-title":"Biochemistry"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1074\/jbc.REV118.002809","article-title":"Small heat shock proteins: Simplicity meets complexity","volume":"294","author":"Haslbeck","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"21920","DOI":"10.1074\/jbc.M109.033688","article-title":"Structural characterization of clusterin-chaperone client protein complexes","volume":"284","author":"Wyatt","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"E2081","DOI":"10.1073\/pnas.1403379111","article-title":"Hypochlorite-induced structural modifications enhance the chaperone activity of human alpha2-macroglobulin","volume":"111","author":"Wyatt","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.ebiom.2016.03.035","article-title":"The role of amyloid-\u03b2 oligomers in toxicity, propagation, and immunotherapy","volume":"6","author":"Sengupta","year":"2016","journal-title":"EBioMedicine"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0304-3940(93)90899-V","article-title":"Microglia express the type 2 plasminogen activator inhibitor in the brain of control subjects and patients with Alzheimer\u2019s disease","volume":"164","author":"Akiyama","year":"1993","journal-title":"Neurosci. Lett."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.placenta.2005.10.008","article-title":"Differential expression of the receptor tyrosine kinase EphB4 and its ligand Ephrin-B2 during human placental development","volume":"27","author":"Chennakesava","year":"2006","journal-title":"Placenta"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3882","DOI":"10.4049\/jimmunol.166.6.3882","article-title":"The Fc receptor for IgG expressed in the villus endothelium of human placenta is Fc gamma RIIb2","volume":"166","author":"Lyden","year":"2001","journal-title":"J. Immunol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.placenta.2008.04.007","article-title":"Novel HLA-G-binding leukocyte immunoglobulin-like receptor (LILR) expression patterns in human placentas and umbilical cords","volume":"29","author":"McIntire","year":"2008","journal-title":"Placenta"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1095\/biolreprod55.2.400","article-title":"Expression of the human p55 and p75 tumor necrosis factor receptors in primary villous trophoblasts and their role in cytotoxic signal transduction","volume":"55","author":"Yui","year":"1996","journal-title":"Biol. Reprod."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/s10571-015-0256-9","article-title":"Endothelial Dysfunction and Amyloid-\u03b2-Induced Neurovascular Alterations","volume":"36","author":"Koizumi","year":"2016","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6869","DOI":"10.4049\/jimmunol.166.11.6869","article-title":"Activation of human macrophages by amyloid-beta is attenuated by astrocytes","volume":"166","author":"Smits","year":"2001","journal-title":"J. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"6351","DOI":"10.1021\/bi00369a001","article-title":"Inactivation of plasminogen activator inhibitor by oxidants","volume":"25","author":"Lawrence","year":"1986","journal-title":"Biochemistry"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.1093\/emboj\/cdg178","article-title":"A redox-sensitive loop regulates plasminogen activator inhibitor type 2 (PAI-2) polymerization","volume":"22","author":"Wilczynska","year":"2003","journal-title":"EMBO J."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"0955","DOI":"10.1055\/s-0038-1656084","article-title":"PCR-RFLP Detection od PAI-2 Gene Variants: Prevelence in Ethnic Groups and Disease Relationship in patients Undergoing corony Angiography","volume":"77","author":"Foy","year":"1997","journal-title":"Thromb. Haemost."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1186\/s12944-015-0150-y","article-title":"Variant of PAI-2 gene is associated with coronary artery disease and recurrent coronary event risk in Chinese Han population","volume":"14","author":"Li","year":"2015","journal-title":"Lipids Health Dis."},{"key":"ref_55","first-page":"603","article-title":"Immunological evidence for hypochlorite-modified proteins in human kidney","volume":"150","author":"Malle","year":"1997","journal-title":"Am. J. Pathol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"e004918","DOI":"10.1161\/JAHA.116.004918","article-title":"Causal Effect of Plasminogen Activator Inhibitor Type 1 on Coronary Heart Disease","volume":"6","author":"Song","year":"2017","journal-title":"J. Am. Heart Assoc."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1600-051X.1989.tb01606.x","article-title":"Crevicular fluid myeloperoxidase at healthy, gingivitis and periodontitis sites","volume":"16","author":"Cao","year":"1989","journal-title":"J. Clin. Periodontol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"531","DOI":"10.4103\/0972-124X.162199","article-title":"Effect of nonsurgical periodontal therapy on salivary myeloperoxidase levels: A biochemical study","volume":"19","author":"Dagar","year":"2015","journal-title":"J. Indian Soc. Periodontol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.archoralbio.2016.05.016","article-title":"PAI-2\/SerpinB2 inhibits proteolytic activity in a P. gingivalis-dominated multispecies bacterial consortium","volume":"70","author":"Neilands","year":"2016","journal-title":"Arch. Oral. Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1007\/s12291-016-0584-7","article-title":"Increased Oxidatively Modified Forms of Albumin in Association with Decreased Total Antioxidant Activity in Different Types of Hypertensive Disorders of Pregnancy","volume":"32","author":"Harish","year":"2017","journal-title":"Indian J. Clin. Biochem."},{"key":"ref_61","first-page":"16","article-title":"Higher plasma AOPP is associated with increased proteinuria excretion and decreased glomerular filtration rate in pre-eclamptic women","volume":"3","author":"Huang","year":"2013","journal-title":"Pregnancy Hypertens. Int. J. Women\u2019s Cardiovasc. Health"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1678","DOI":"10.12688\/f1000research.19517.1","article-title":"Stress-induced chaperones: A first line of defense against the powerful oxidant hypochlorous acid","volume":"8","author":"Goemans","year":"2019","journal-title":"F1000Research"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"101847","DOI":"10.1016\/j.redox.2020.101847","article-title":"Hypochlorite-induced aggregation of fibrinogen underlies a novel antioxidant role in blood plasma","volume":"40","author":"Kaur","year":"2021","journal-title":"Redox Biol."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/7\/1152\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T22:45:41Z","timestamp":1760136341000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/11\/7\/1152"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,3,29]]},"references-count":63,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2022,4]]}},"alternative-id":["cells11071152"],"URL":"https:\/\/doi.org\/10.3390\/cells11071152","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,3,29]]}}}