{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T13:48:05Z","timestamp":1787060885311,"version":"build-2736575974"},"reference-count":49,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2025,4,2]],"date-time":"2025-04-02T00:00:00Z","timestamp":1743552000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Med."],"abstract":"<jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>Carbamylation involves the non-enzymatic binding of isocyanic acid to the amino groups of proteins, making it associated with many pathological conditions, including inflammation, aging, arteriosclerosis, and renal failure. However, there are no data on protein carbamylation in patients with COVID-19. Our study is the first to evaluate the association between blood inflammation and protein carbamylation in patients who died from COVID-19 compared to COVID-19 survivors.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>The study included 50 patients admitted to Dr. Tytus Cha\u0142ubi\u0144ski Specialist Hospital in Radom, Poland. Twenty-five of them were COVID-19 survivors (15 men, 10 women), and 25 were COVID-19 deceased patients (15 men, 10 women). The number of subjects was based on a pilot study assuming a significance level of 0.05 and a test power of 0.8. Plasma\/serum samples were assayed for carbamyl-lysine (CBL) and inflammatory biomarkers (CRP, procalcitonin, D-dimer, IL-6, and WBC). The concentration of CBL was measured using an enzyme-linked immunosorbent assay (ELISA). Statistical analysis was performed using the Mann-Whitney U test and Spearman rank correlation. Receiver Operating Characteristic (ROC) analysis was used to assess the diagnostic utility of serum CBL.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Serum CBL levels were significantly higher in patients who died from COVID-19 compared to COVID-19 survivors (\n                      <jats:italic>p<\/jats:italic>\n                      = 0.0011). There was a positive correlation of serum CBL with IL-6, D-dimer, and WBC. Serum CBL levels &amp;gt;101 ng\/mL, with moderate sensitivity and specificity, differentiate COVID-19 deceased from recovered patients (area under the curve 0.76).\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>In conclusion, COVID-19 is associated with excessive protein carbamylation. Inflammation may be a source of higher CBL production in COVID-19. A thorough understanding of the consequences of increased protein carbamylation may clarify the consequences of COVID-19 complications.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.3389\/fmed.2025.1561670","type":"journal-article","created":{"date-parts":[[2025,4,2]],"date-time":"2025-04-02T02:57:27Z","timestamp":1743562647000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":3,"title":["Association of inflammation and protein carbamylation in patients with COVID-19"],"prefix":"10.3389","volume":"12","author":[{"given":"Jolanta","family":"Smykiewicz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryszard","family":"Tomasiuk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roman","family":"Cemaga","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jakub","family":"Buczkowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mateusz","family":"Maciejczyk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2025,4,2]]},"reference":[{"key":"B1","year":"2024","journal-title":"COVID-19 Epidemiological Update."},{"key":"B2","doi-asserted-by":"publisher","first-page":"8155","DOI":"10.3390\/IJMS25158155","article-title":"Comprehensive review of COVID-19: epidemiology, pathogenesis, advancement in diagnostic and detection techniques, and post-pandemic treatment strategies.","volume":"25","author":"Chung","year":"2024","journal-title":"Int J Mol Sci."},{"key":"B3","doi-asserted-by":"publisher","first-page":"2255","DOI":"10.1056\/NEJMra2026131","article-title":"Cytokine storm.","volume":"383","author":"Fajgenbaum","year":"2020","journal-title":"New Eng J Med"},{"key":"B4","doi-asserted-by":"publisher","first-page":"647","DOI":"10.1107\/S2059798324007794","article-title":"Post-translational modifications in the protein data bank.","volume":"80","author":"Schofield","year":"2024","journal-title":"Acta Crystallogr D Struct Biol"},{"key":"B5","doi-asserted-by":"publisher","first-page":"e261","DOI":"10.1002\/MCO2.261","article-title":"Protein posttranslational modifications in health and diseases: functions, regulatory mechanisms, and therapeutic implications.","volume":"4","author":"Zhong","year":"2023","journal-title":"MedComm"},{"key":"B6","doi-asserted-by":"publisher","first-page":"1240115","DOI":"10.3389\/fonc.2023.1240115","article-title":"Post-translational modifications and their implications in cancer.","volume":"13","author":"Dutta","year":"2023","journal-title":"Front Oncol"},{"key":"B7","doi-asserted-by":"publisher","first-page":"102464","DOI":"10.1016\/j.coph.2024.102464","article-title":"Effects of protein glycation and protective mechanisms against glycative stress.","volume":"76","author":"Najjar","year":"2024","journal-title":"Curr Opin Pharmacol"},{"key":"B8","doi-asserted-by":"publisher","first-page":"1213802","DOI":"10.3389\/fonc.2023.1213802","article-title":"Could circulating biomarkers of nitrosative stress and protein glycoxidation be useful in patients with gastric cancer?","volume":"13","author":"Dorf","year":"2023","journal-title":"Front Oncol"},{"key":"B9","doi-asserted-by":"publisher","first-page":"101920","DOI":"10.1016\/j.redox.2021.101920","article-title":"Protein glycation - biomarkers of metabolic dysfunction and early-stage decline in health in the era of precision medicine.","volume":"42","author":"Rabbani","year":"2021","journal-title":"Redox Biol"},{"key":"B10","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1016\/j.jprot.2013.05.012","article-title":"Protein glycation during aging and in cardiovascular disease.","volume":"92","author":"Simm","year":"2013","journal-title":"J Proteomics"},{"key":"B11","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/J.JNS.2012.02.018","article-title":"Advanced glycation end products and neurodegenerative diseases: mechanisms and perspective.","volume":"317","author":"Li","year":"2012","journal-title":"J Neurol Sci"},{"key":"B12","doi-asserted-by":"publisher","first-page":"2","DOI":"10.1093\/GLYCOB\/CWZ073","article-title":"Advanced glycation end products (AGEs), protein aggregation and their cross talk: new insight in tumorigenesis.","volume":"30","author":"Haque","year":"2019","journal-title":"Glycobiology"},{"key":"B13","doi-asserted-by":"publisher","first-page":"107806","DOI":"10.1016\/j.intimp.2021.107806","article-title":"Advanced glycation end products (AGEs) and its receptor, RAGE, modulate age-dependent COVID-19 morbidity and mortality. 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