Release of active peptidylarginine deiminase into the circulation during acute inflammation induced by coronary artery bypass surgery

References

• Proost P, Loos T, Mortier A, et al. Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation. J Exp Med. 2008;205:2085–2097. doi:10.1084/jem.2008030518710930
   PubMed Web of Science ®Google Scholar
• Moelants EA, Mortier A, Grauwen K, Ronsse I, Van DJ, Proost P. Citrullination of TNF-alpha by peptidylarginine deiminases reduces its capacity to stimulate the production of inflammatory chemokines. Cytokine. 2013;61:161–167. doi:10.1016/j.cyto.2012.09.01123075670
   PubMed Web of Science ®Google Scholar
• Nakayama-Hamada M, Suzuki A, Furukawa H, Yamada R, Yamamoto K. Citrullinated fibrinogen inhibits thrombin-catalysed fibrin polymerization. J Biochem. 2008;144:393–398. doi:10.1093/jb/mvn07918583356
   PubMed Web of Science ®Google Scholar
• Nemmara VV, Tilvawala R, Salinger AJ, et al. Citrullination inactivates nicotinamide-N-methyltransferase. ACS Chem Biol. 2018;13:2663–2672. doi:10.1021/acschembio.8b0057830044909
   PubMed Web of Science ®Google Scholar
• Sipila KH, Ranga V, Rappu P, et al. Extracellular citrullination inhibits the function of matrix associated TGF-beta. Matrix Biol. 2016. doi:10.1016/j.matbio.2016.02.008
   PubMed Web of Science ®Google Scholar
• Rondas D, Crevecoeur I, D’Hertog W, et al. Citrullinated glucose-regulated protein 78 is an autoantigen in type 1 diabetes. Diabetes. 2015;64:573–586. doi:10.2337/db14-062125204978
   PubMed Web of Science ®Google Scholar
• Schellekens GA, de Jong BA, van den Hoogen FH, van de Putte LB, van Venrooij WJ. Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies. J Clin Invest. 1998;101:273–281. doi:10.1172/JCI13169421490
   PubMed Web of Science ®Google Scholar
• Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays. 2003;25:1106–1118. doi:10.1002/bies.1035714579251
   PubMed Web of Science ®Google Scholar
• Asaga H, Nakashima K, Senshu T, Ishigami A, Yamada M. Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils. J Leukoc Biol. 2001;70:46–51.11435484
   PubMed Web of Science ®Google Scholar
• Damgaard D, Bjorn ME, Steffensen MA, Pruijn GJ, Nielsen CH. Reduced glutathione as a physiological co-activator in the activation of peptidylarginine deiminase. Arthritis Res Ther. 2016;18:102. doi:10.1186/s13075-016-1000-727149996
   PubMed Web of Science ®Google Scholar
• Zhou Y, Di PT, Sims GP, Mittereder N, Mustelin T. Characterization of the hypercitrullination reaction in human neutrophils and other leukocytes. Mediators Inflamm. 2015;2015:236451. doi:10.1155/2015/12538026078491
   PubMed Web of Science ®Google Scholar
• Spengler J, Lugonja B, Jimmy YA, et al. Release of active peptidyl arginine deiminases by neutrophils can explain production of extracellular citrullinated autoantigens in rheumatoid arthritis synovial fluid. Arthritis Rheumatol. 2015;67:3135–3145. doi:10.1002/art.3931326245941
   PubMed Web of Science ®Google Scholar
• Damgaard D, Senolt L, Nielsen M, Pruijn G, Nielsen CH. Demonstration of extracellular peptidylarginine deiminase (PAD) activity in synovial fluid of patients with rheumatoid arthritis using a novel assay for citrullination of fibrinogen. Arthritis Res Ther. 2014;16:498. doi:10.1186/s13075-014-0498-925475141
   PubMed Web of Science ®Google Scholar
• Damgaard D, Bjorn ME, Jensen PO, Nielsen CH. Reactive oxygen species inhibit catalytic activity of peptidylarginine deiminase. J Enzyme Inhib Med Chem. 2017;32:1203–1208. doi:10.1080/14756366.2017.136850528933232
   PubMed Web of Science ®Google Scholar
• Klareskog L, Padyukov L, Alfredsson L. Smoking as a trigger for inflammatory rheumatic diseases. Curr Opin Rheumatol. 2007;19:49–54. doi:10.1097/BOR.0b013e32801127c817143096
   PubMed Web of Science ®Google Scholar
• Makrygiannakis D, Hermansson M, Ulfgren AK, et al. Smoking increases peptidylarginine deiminase 2 enzyme expression in human lungs and increases citrullination in BAL cells. Ann Rheum Dis. 2008;67:1488–1492. doi:10.1136/ard.2007.07519218413445
   PubMed Web of Science ®Google Scholar
• Damgaard D, Friberg Bruun NM, Quisgaard GM, Palarasah Y, Svane-Knudsen V, Nielsen CH. Smoking is associated with increased levels of extracellular peptidylarginine deiminase 2 (PAD2) in the lungs. Clin Exp Rheumatol. 2015;33:405–408.25897949
   PubMed Web of Science ®Google Scholar
• Lugli EB, Correia RE, Fischer R, et al. Expression of citrulline and homocitrulline residues in the lungs of non-smokers and smokers: implications for autoimmunity in rheumatoid arthritis. Arthritis Res Ther. 2015;17:9. doi:10.1186/s13075-015-0520-x25600626
   PubMed Web of Science ®Google Scholar
• Engstrom M, Eriksson K, Lee L, et al. Increased citrullination and expression of peptidylarginine deiminases independently of P. gingivalis and A. actinomycetemcomitans in gingival tissue of patients with periodontitis. J Transl Med. 2018;16:214. doi:10.1186/s12967-018-1588-230064459
   PubMed Web of Science ®Google Scholar
• Makrygiannakis D, af Klin E, Lundberg IE, et al. Citrullination is an inflammation-dependent process. Ann Rheum Dis. 2006;65:1219–1222. doi:10.1136/ard.2005.04940316540548
   PubMed Web of Science ®Google Scholar
• Jongman RM, Zijlstra JG, Kok WF, et al. Off-pump CABG surgery reduces systemic inflammation compared with on-pump surgery but does not change systemic endothelial responses: a prospective randomized study. Shock. 2014;42:121–128. doi:10.1097/SHK.000000000000019024727871
   PubMed Web of Science ®Google Scholar
• Andresen TK, Svennevig JL, Videm V. Soluble VCAM-1 is a very early marker of endothelial cell activation in cardiopulmonary bypass. Perfusion. 2002;17:15–21. doi:10.1191/0267659102pf531oa11817523
   PubMed Web of Science ®Google Scholar
• Toft P, Nielsen CH, Tonnesen E, Hansen TG, Hokland M. Changes in adhesion molecule expression and oxidative burst activity of granulocytes and monocytes during open-heart surgery with cardiopulmonary bypass compared with abdominal surgery. Eur J Anaesthesiol. 1998;15:345–353.9649997
   PubMed Web of Science ®Google Scholar
• Denizot Y, Leguyader A, Cornu E, et al. Release of soluble vascular endothelial growth factor receptor-1 (sFlt-1) during coronary artery bypass surgery. J Cardiothorac Surg. 2007;2:38. doi:10.1186/1749-8090-2-3817888151
   PubMed Web of Science ®Google Scholar
• Damgaard D, Palarasah Y, Skjodt K, et al. Generation of monoclonal antibodies against peptidylarginine deiminase 2 (PAD2) and development of a PAD2-specific enzyme-linked immunosorbent assay. J Immunol Methods. 2014;405:15–22. doi:10.1016/j.jim.2013.12.00824384061
   PubMed Web of Science ®Google Scholar
• Moriarty SE, Shah JH, Lynn M, et al. Oxidation of glutathione and cysteine in human plasma associated with smoking. Free Radic Biol Med. 2003;35:1582–1588.14680681
   PubMed Web of Science ®Google Scholar
• Mortier A, Van DJ, Proost P. Regulation of chemokine activity by posttranslational modification. Pharmacol Ther. 2008;120:197–217. doi:10.1016/j.pharmthera.2008.08.00618793669
   PubMed Web of Science ®Google Scholar
• Bennike TB, Ellingsen T, Glerup H, et al. Proteome analysis of rheumatoid arthritis gut mucosa. J Proteome Res. 2017;16:346–354. doi:10.1021/acs.jproteome.6b0059827627584
   PubMed Web of Science ®Google Scholar
• Zhou Y, Chen B, Mittereder N, et al. Spontaneous secretion of the citrullination enzyme PAD2 and cell surface exposure of PAD4 by neutrophils. Front Immunol. 2017;8:1200. doi:10.3389/fimmu.2017.0120028993780
   PubMed Web of Science ®Google Scholar
• Blachere NE, Parveen S, Fak J, Frank MO, Orange DE. Inflammatory but not apoptotic death of granulocytes citrullinates fibrinogen. Arthritis Res Ther. 2015;17:369. doi:10.1186/s13075-015-0890-026684871
   PubMed Web of Science ®Google Scholar