{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T00:21:52Z","timestamp":1781828512123,"version":"3.54.5"},"reference-count":70,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/501100001505","name":"Manatu Hauora | Health Research Council of New Zealand","doi-asserted-by":"publisher","award":["15\/333"],"award-info":[{"award-number":["15\/333"]}],"id":[{"id":"10.13039\/501100001505","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"Department of Health | National Health and Medical Research Council","doi-asserted-by":"publisher","award":["403911"],"award-info":[{"award-number":["403911"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2022,2,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Calprotectin is released by activated neutrophils along with myeloperoxidase (MPO) and proteases. It plays numerous roles in inflammation and infection, and is used as an inflammatory biomarker. However, calprotectin is readily oxidized by MPO-derived hypohalous acids to form covalent dimers of its S100A8 and S100A9 subunits. The dimers are susceptible to degradation by proteases. We show that detection of human calprotectin by ELISA declines markedly because of its oxidation by hypochlorous acid and subsequent degradation. Also, proteolysis liberates specific peptides from oxidized calprotectin that is present at inflammatory sites. We identified six calprotectin-derived peptides by mass spectrometry and detected them in the bronchoalveolar lavage fluid of children with cystic fibrosis (CF). We assessed the peptides as biomarkers of neutrophilic inflammation and infection. The content of the calprotectin peptide ILVI was related to calprotectin (r = 0.72, p = 0.01, n = 10). Four of the peptides were correlated with the concentration of MPO (r &amp;gt; 0.7, p \u2264 0.01, n = 21), while three were higher (p &amp;lt; 0.05) in neutrophil elastase\u2013positive (n = 14) than \u2013negative samples (n = 7). Also, five of the peptides were higher (p &amp;lt; 0.05) in the bronchoalveolar lavage fluid from children with CF with infections (n = 21) than from non-CF children without infections (n = 6). The specific peptides liberated from calprotectin will signal uncontrolled activity of proteases and MPO during inflammation. They may prove useful in tracking inflammation in respiratory diseases dominated by neutrophils, including coronavirus disease 2019.<\/jats:p>","DOI":"10.4049\/jimmunol.2001017","type":"journal-article","created":{"date-parts":[[2022,1,19]],"date-time":"2022-01-19T15:30:41Z","timestamp":1642606241000},"page":"979-990","source":"Crossref","is-referenced-by-count":13,"title":["Formation of Calprotectin-Derived Peptides in the Airways of Children with Cystic Fibrosis"],"prefix":"10.1093","volume":"208","author":[{"given":"Teagan S","family":"Edwards","sequence":"first","affiliation":[{"name":"Department of Paediatrics, University of Otago Christchurch , Christchurch,","place":["New Zealand"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2269-4595","authenticated-orcid":false,"given":"Nina","family":"Dickerhof","sequence":"additional","affiliation":[{"name":"Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch , Christchurch,","place":["New Zealand"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas J","family":"Magon","sequence":"additional","affiliation":[{"name":"Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch , Christchurch,","place":["New Zealand"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7055-5170","authenticated-orcid":false,"given":"Louise N","family":"Paton","sequence":"additional","affiliation":[{"name":"Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch , Christchurch,","place":["New Zealand"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6305-2201","authenticated-orcid":false,"given":"Peter D","family":"Sly","sequence":"additional","affiliation":[{"name":"Child Health Research Centre, University of Queensland , Brisbane,","place":["Australia"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8218-7766","authenticated-orcid":false,"given":"Anthony J","family":"Kettle","sequence":"additional","affiliation":[{"name":"Centre for Free Radical Research, Department of Pathology and Biomedical Science, University of Otago Christchurch , Christchurch,","place":["New Zealand"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,2,15]]},"reference":[{"key":"2025021008545758500_r1","doi-asserted-by":"crossref","first-page":"e00779-17","DOI":"10.1128\/IAI.00779-17","article-title":"Role of calprotectin in withholding zinc and copper from Candida albicans","volume":"86","author":"Besold","year":"2018","journal-title":"Infect. Immun."},{"key":"2025021008545758500_r2","doi-asserted-by":"crossref","first-page":"8828","DOI":"10.1021\/jacs.7b01212","article-title":"Nickel sequestration by the host-defense protein human calprotectin","volume":"139","author":"Nakashige","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"2025021008545758500_r3","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1038\/nchembio.1891","article-title":"Human calprotectin is an iron-sequestering host-defense protein","volume":"11","author":"Nakashige","year":"2015","journal-title":"Nat. Chem. Biol."},{"key":"2025021008545758500_r4","doi-asserted-by":"crossref","first-page":"18089","DOI":"10.1021\/ja307974e","article-title":"Calcium ion gradients modulate the zinc affinity and antibacterial activity of human calprotectin","volume":"134","author":"Brophy","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"2025021008545758500_r5","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.pharmthera.2016.07.015","article-title":"S100A8\/A9: from basic science to clinical application","volume":"167","author":"Pruenster","year":"2016","journal-title":"Pharmacol. Ther."},{"key":"2025021008545758500_r6","doi-asserted-by":"crossref","first-page":"13462","DOI":"10.1016\/S0021-9258(18)98862-9","article-title":"Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14","volume":"266","author":"Teigelkamp","year":"1991","journal-title":"J. Biol. Chem."},{"key":"2025021008545758500_r7","doi-asserted-by":"crossref","first-page":"245","DOI":"10.33549\/physiolres.930448","article-title":"Calprotectin\u2014a pleiotropic molecule in acute and chronic inflammation","volume":"53","author":"Str\u00edz","year":"2004","journal-title":"Physiol. Res."},{"key":"2025021008545758500_r8","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1074\/jbc.272.14.9496","article-title":"Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway","volume":"272","author":"Rammes","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2025021008545758500_r9","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1136\/mp.51.3.143","article-title":"Chemotaxins C5a and fMLP induce release of calprotectin (leucocyte L1 protein) from polymorphonuclear cells in vitro","volume":"51","author":"Hetland","year":"1998","journal-title":"Mol. Pathol."},{"key":"2025021008545758500_r10","doi-asserted-by":"crossref","first-page":"101202","DOI":"10.1016\/j.redox.2019.101202","article-title":"Oxidative cross-linking of calprotectin occurs in vivo, altering its structure and susceptibility to proteolysis","volume":"24","author":"Hoskin","year":"2019","journal-title":"Redox Biol."},{"key":"2025021008545758500_r11","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1136\/adc.74.2.136","article-title":"Calprotectin as a marker of inflammation in cystic fibrosis","volume":"74","author":"Golden","year":"1996","journal-title":"Arch. Dis. Child."},{"key":"2025021008545758500_r12","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.jcf.2010.01.005","article-title":"Sputum and serum calprotectin are useful biomarkers during CF exacerbation","volume":"9","author":"Gray","year":"2010","journal-title":"J. Cyst. Fibros."},{"key":"2025021008545758500_r13","doi-asserted-by":"crossref","first-page":"760","DOI":"10.3899\/jrheum.140628","article-title":"Calprotectin as a biomarker for rheumatoid arthritis: a systematic review","volume":"42","author":"Abildtrup","year":"2015","journal-title":"J. Rheumatol."},{"key":"2025021008545758500_r14","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1177\/1741826711421078","article-title":"Plasma calprotectin levels reflect disease severity in patients with chronic heart failure","volume":"19","author":"Jensen","year":"2012","journal-title":"Eur. J. Prev. Cardiol."},{"key":"2025021008545758500_r15","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.jneuroim.2009.09.006","article-title":"Calprotectin levels in the cerebrospinal fluid reflect disease activity in multiple sclerosis","volume":"216","author":"Berg-Hansen","year":"2009","journal-title":"J. Neuroimmunol."},{"key":"2025021008545758500_r16","first-page":"931","article-title":"Elevated serum calprotectin levels in HIV-infected patients: the calprotectin response during ZDV treatment is associated with clinical events","volume":"7","author":"M\u00fcller","year":"1994","journal-title":"J Acquir Immune Defic Syndr (1988)"},{"key":"2025021008545758500_r17","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1080\/003655201750065979","article-title":"Fecal excretion of calprotectin in colorectal cancer: relationship to tumor characteristics","volume":"36","author":"Kristinsson","year":"2001","journal-title":"Scand. J. Gastroenterol."},{"key":"2025021008545758500_r18","doi-asserted-by":"crossref","first-page":"e0127318","DOI":"10.1371\/journal.pone.0127318","article-title":"Serum calprotectin, CD26 and EGF to establish a panel for the diagnosis of lung cancer","volume":"10","author":"Blanco-Prieto","year":"2015","journal-title":"PLoS One"},{"key":"2025021008545758500_r19","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.dld.2008.05.008","article-title":"Questions and answers on the role of faecal calprotectin as a biological marker in inflammatory bowel disease","volume":"41","author":"Gisbert","year":"2009","journal-title":"Dig. Liver Dis."},{"key":"2025021008545758500_r20","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3109\/00365548.2014.974206","article-title":"High faecal calprotectin levels in intestinal tuberculosis are associated with granulomas in intestinal biopsies","volume":"47","author":"Larsson","year":"2015","journal-title":"Infect. Dis. (Lond.)"},{"key":"2025021008545758500_r21","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.freeradbiomed.2015.05.022","article-title":"Oxidation of calprotectin by hypochlorous acid prevents chelation of essential metal ions and allows bacterial growth: relevance to infections in cystic fibrosis","volume":"86","author":"Magon","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r22","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.freeradbiomed.2012.12.012","article-title":"S100A8 and S100A9-oxidant scavengers in inflammation","volume":"58","author":"Gomes","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r23","doi-asserted-by":"crossref","first-page":"17444","DOI":"10.1021\/jacs.8b06354","article-title":"Oxidative post-translational modifications accelerate proteolytic degradation of calprotectin","volume":"140","author":"Stephan","year":"2018","journal-title":"J. Am. Chem. Soc."},{"key":"2025021008545758500_r24","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1080\/13510002.1997.11747085","article-title":"Myeloperoxidase: a key regulator of neutrophil oxidant production","volume":"3","author":"Kettle","year":"1997","journal-title":"Redox Rep."},{"key":"2025021008545758500_r25","doi-asserted-by":"crossref","first-page":"2190","DOI":"10.1016\/j.freeradbiomed.2011.09.019","article-title":"Spectral and kinetic evidence for reaction of superoxide with compound I of myeloperoxidase","volume":"51","author":"Kettle","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r26","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1016\/j.micinf.2003.09.008","article-title":"Neutrophil granules and secretory vesicles in inflammation","volume":"5","author":"Faurschou","year":"2003","journal-title":"Microbes Infect."},{"key":"2025021008545758500_r27","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1111\/1751-2980.12540","article-title":"Potential roles of neutrophils in regulating intestinal mucosal inflammation of inflammatory bowel disease","volume":"18","author":"Zhou","year":"2017","journal-title":"J. Dig. Dis."},{"key":"2025021008545758500_r28","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.freeradbiomed.2017.09.028","article-title":"Oxidative stress in early cystic fibrosis lung disease is exacerbated by airway glutathione deficiency","volume":"113","author":"Dickerhof","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r29","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/S0889-857X(21)00463-4","article-title":"The neutrophil in rheumatoid arthritis","volume":"21","author":"Pillinger","year":"1995","journal-title":"Rheum. Dis. Clin. North Am."},{"key":"2025021008545758500_r30","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1161\/01.ATV.0000163262.83456.6d","article-title":"Myeloperoxidase and cardiovascular disease","volume":"25","author":"Nicholls","year":"2005","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"2025021008545758500_r31","doi-asserted-by":"crossref","first-page":"1618","DOI":"10.1093\/rheumatology\/keq045","article-title":"Neutrophil function in inflammation and inflammatory diseases","volume":"49","author":"Wright","year":"2010","journal-title":"Rheumatology (Oxford)"},{"key":"2025021008545758500_r32","doi-asserted-by":"crossref","first-page":"1963","DOI":"10.1056\/NEJMoa1301725","article-title":"Risk factors for bronchiectasis in children with cystic fibrosis","volume":"368","author":"Sly","year":"2013","journal-title":"N. Engl. J. Med."},{"key":"2025021008545758500_r33","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1186\/s12931-019-1145-4","article-title":"Neutrophil elastase as a biomarker for bacterial infection in COPD","volume":"20","author":"Thulborn","year":"2019","journal-title":"Respir. Res."},{"key":"2025021008545758500_r34","doi-asserted-by":"crossref","first-page":"2314","DOI":"10.1016\/j.chest.2020.06.044","article-title":"BAL inflammatory markers can predict pulmonary exacerbations in children with cystic fibrosis","volume":"158","author":"Ishak","year":"2020","journal-title":"Chest"},{"key":"2025021008545758500_r35","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0021-9258(19)50881-X","article-title":"A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase","volume":"195","author":"Beers","year":"1952","journal-title":"J. Biol. Chem."},{"key":"2025021008545758500_r36","doi-asserted-by":"crossref","first-page":"e0192952","DOI":"10.1371\/journal.pone.0192952","article-title":"A myeloperoxidase precursor, pro-myeloperoxidase, is present in human plasma and elevated in cardiovascular disease patients","volume":"13","author":"Khalilova","year":"2018","journal-title":"PLoS One"},{"key":"2025021008545758500_r37","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1111\/j.1745-7270.2007.00343.x","article-title":"Human calprotectin: effect of calcium and zinc on its secondary and tertiary structures, and role of pH in its thermal stability","volume":"39","author":"Yousefi","year":"2007","journal-title":"Acta Biochim. Biophys. Sin. (Shanghai)"},{"key":"2025021008545758500_r38","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/0003-2697(85)90190-3","article-title":"Mechanism of dye response and interference in the Bradford protein assay","volume":"151","author":"Compton","year":"1985","journal-title":"Anal. Biochem."},{"key":"2025021008545758500_r39","doi-asserted-by":"crossref","first-page":"3798","DOI":"10.1021\/j100884a007","article-title":"The acid ionization constant of HOCl from 5 to 35\u00b0","volume":"70","author":"Morris","year":"1966","journal-title":"J. Phys. Chem."},{"key":"2025021008545758500_r40","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1016\/j.freeradbiomed.2010.06.028","article-title":"Hypothiocyanous acid is a potent inhibitor of apoptosis and caspase 3 activation in endothelial cells","volume":"49","author":"Bozonet","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r41","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1042\/BJ20140612","article-title":"Potent inhibition of macrophage migration inhibitory factor (MIF) by myeloperoxidase-dependent oxidation of epicatechins","volume":"462","author":"Dickerhof","year":"2014","journal-title":"Biochem. J."},{"key":"2025021008545758500_r42","doi-asserted-by":"crossref","first-page":"6465","DOI":"10.1074\/jbc.M112.418970","article-title":"Ceruloplasmin is an endogenous inhibitor of myeloperoxidase","volume":"288","author":"Chapman","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2025021008545758500_r43","doi-asserted-by":"crossref","first-page":"975","DOI":"10.3109\/10715762.2012.667566","article-title":"Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids","volume":"46","author":"Pattison","year":"2012","journal-title":"Free Radic. Res."},{"key":"2025021008545758500_r44","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1164\/rccm.200311-1516OC","article-title":"Myeloperoxidase and protein oxidation in the airways of young children with cystic fibrosis","volume":"170","author":"Kettle","year":"2004","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"2025021008545758500_r45","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.cca.2006.03.027","article-title":"Pancreatic cancer-derived S-100A8 N-terminal peptide: a diabetes cause?","volume":"372","author":"Basso","year":"2006","journal-title":"Clin. Chim. Acta"},{"key":"2025021008545758500_r46","doi-asserted-by":"crossref","first-page":"9914","DOI":"10.1016\/S0021-9258(18)48021-0","article-title":"Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein","volume":"262","author":"Davies","year":"1987","journal-title":"J. Biol. Chem."},{"key":"2025021008545758500_r47","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1016\/0891-5849(93)90167-S","article-title":"Potential roles of hypochlorous acid and N-chloroamines in collagen breakdown by phagocytic cells in synovitis","volume":"15","author":"Davies","year":"1993","journal-title":"Free Radic. Biol. Med."},{"key":"2025021008545758500_r48","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0003-9861(91)90327-F","article-title":"Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl","volume":"285","author":"Vissers","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"key":"2025021008545758500_r49","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.cell.2008.09.024","article-title":"Bleach activates a redox-regulated chaperone by oxidative protein unfolding","volume":"135","author":"Winter","year":"2008","journal-title":"Cell"},{"key":"2025021008545758500_r50","doi-asserted-by":"crossref","first-page":"2701","DOI":"10.1016\/j.ijbiomac.2017.10.159","article-title":"Oxidation of C-reactive protein by hypochlorous acid leads to the formation of potent platelet activator","volume":"107","author":"Boncler","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"2025021008545758500_r51","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1021\/tx050207b","article-title":"Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function","volume":"18","author":"Hawkins","year":"2005","journal-title":"Chem. Res. Toxicol."},{"key":"2025021008545758500_r52","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1164\/rccm.201906-1190PP","article-title":"Targeting proteases in cystic fibrosis lung disease. paradigms, progress, and potential","volume":"201","author":"McKelvey","year":"2020","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"2025021008545758500_r53","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1021\/ac00227a007","article-title":"Direct potentiometric determination of chloride ion in whole blood","volume":"53","author":"Oka","year":"1981","journal-title":"Anal. Chem."},{"key":"2025021008545758500_r54","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jcf.2016.10.012","article-title":"Oxidized glutathione and uric acid as biomarkers of early cystic fibrosis lung disease","volume":"16","author":"Dickerhof","year":"2017","journal-title":"J. Cyst. Fibros."},{"key":"2025021008545758500_r55","doi-asserted-by":"crossref","first-page":"1801118","DOI":"10.1183\/13993003.01118-2018","article-title":"Myeloperoxidase oxidation of methionine associates with early cystic fibrosis lung disease","volume":"52","author":"Chandler","year":"2018","journal-title":"Eur. Respir. J."},{"key":"2025021008545758500_r56","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1186\/s12931-017-0691-x","article-title":"Neutrophil elastase in bronchiectasis","volume":"18","author":"Gramegna","year":"2017","journal-title":"Respir. Res."},{"key":"2025021008545758500_r57","first-page":"1075","article-title":"Early pulmonary inflammation in infants with cystic fibrosis","volume":"151","author":"Khan","year":"1995","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"2025021008545758500_r58","doi-asserted-by":"crossref","first-page":"217","DOI":"10.3389\/fmed.2018.00217","article-title":"The role of neutrophils and neutrophil elastase in pulmonary arterial hypertension","volume":"5","author":"Taylor","year":"2018","journal-title":"Front. Med. (Lausanne)"},{"key":"2025021008545758500_r59","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/2052-0492-2-32","article-title":"Pathophysiology and biomarkers of acute respiratory distress syndrome","volume":"2","author":"Fujishima","year":"2014","journal-title":"J. Intensive Care"},{"key":"2025021008545758500_r60","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1089\/ars.2015.6317","article-title":"Clinical relevance of biomarkers of oxidative stress","volume":"23","author":"Frijhoff","year":"2015","journal-title":"Antioxid. Redox Signal."},{"key":"2025021008545758500_r61","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.bbagen.2013.07.004","article-title":"Measuring chlorine bleach in biology and medicine","volume":"1840","author":"Kettle","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"2025021008545758500_r62","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1378\/chest.104.4.1032","article-title":"General vs local anesthesia. Effect on bronchoalveolar lavage findings","volume":"104","author":"de Blasio","year":"1993","journal-title":"Chest"},{"key":"2025021008545758500_r63","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/1559-0275-11-23","article-title":"Deciphering the peptidome of urine from ovarian cancer patients and healthy controls","volume":"11","author":"Smith","year":"2014","journal-title":"Clin. Proteomics"},{"key":"2025021008545758500_r64","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1016\/j.cell.2020.08.002","article-title":"Elevated calprotectin and abnormal myeloid cell subsets discriminate severe from mild COVID-19","volume":"182","author":"Silvin","year":"2020","journal-title":"Cell"},{"key":"2025021008545758500_r65","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1080\/1744666X.2021.1905526","article-title":"Circulating calprotectin as a biomarker of COVID-19 severity","volume":"17","author":"Mahler","year":"2021","journal-title":"Expert Rev. Clin. Immunol."},{"key":"2025021008545758500_r66","doi-asserted-by":"crossref","first-page":"2831","DOI":"10.1111\/j.1572-0241.2000.03194.x","article-title":"Fecal calprotectin levels predict colorectal inflammation among patients with chronic diarrhea referred for colonoscopy","volume":"95","author":"Limburg","year":"2000","journal-title":"Am. J. Gastroenterol."},{"key":"2025021008545758500_r67","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1002\/ibd.20472","article-title":"Clinical role of calprotectin assay in determining histological relapses in children affected by inflammatory bowel diseases","volume":"14","author":"Diamanti","year":"2008","journal-title":"Inflamm. Bowel Dis."},{"key":"2025021008545758500_r68","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/s12876-016-0462-z","article-title":"Fecal calprotectin level correlated with both endoscopic severity and disease extent in ulcerative colitis","volume":"16","author":"Kawashima","year":"2016","journal-title":"BMC Gastroenterol."},{"key":"2025021008545758500_r69","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1097\/00054725-200606000-00013","article-title":"Role of fecal calprotectin as a biomarker of intestinal inflammation in inflammatory bowel disease","volume":"12","author":"Konikoff","year":"2006","journal-title":"Inflamm. Bowel Dis."},{"key":"2025021008545758500_r70","doi-asserted-by":"crossref","first-page":"7706","DOI":"10.1016\/S0021-9258(20)89506-4","article-title":"Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells","volume":"266","author":"Edgeworth","year":"1991","journal-title":"J. Biol. Chem."}],"container-title":["The Journal of Immunology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/jimmunol\/article-pdf\/208\/4\/979\/61466016\/ji2001017.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jimmunol\/article-pdf\/208\/4\/979\/61466016\/ji2001017.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,10]],"date-time":"2025-02-10T08:55:24Z","timestamp":1739177724000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jimmunol\/article\/208\/4\/979\/7924570"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2]]},"references-count":70,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2022,2,15]]}},"URL":"https:\/\/doi.org\/10.4049\/jimmunol.2001017","relation":{},"ISSN":["0022-1767","1550-6606"],"issn-type":[{"value":"0022-1767","type":"print"},{"value":"1550-6606","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2022,2]]},"published":{"date-parts":[[2022,2]]}}}