{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Poole LG"],"funding":["National Institute of Environmental Health Sciences","National Institute of Diabetes and Digestive and Kidney Diseases","NIDDK NIH HHS","U.S. Department of Agriculture","NIEHS NIH HHS"],"pagination":["1182-1192"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9035112"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(5)"],"pubmed_abstract":["<h4>Background</h4>The blood coagulation factor fibrin(ogen) can modulate inflammation by altering leukocyte activity. Analyses of fibrin(ogen)-mediated proinflammatory activity have largely focused on leukocyte integrin binding activity revealed by conversion of fibrinogen to a stabilized fibrin polymer by blood coagulation enzymes. In addition to coagulation enzymes, fibrinogen is a substrate for tissue transglutaminase-2 (TG2), a widely expressed enzyme that produces unique fibrinogen Aα-γ chain cross-linked products.<h4>Objectives</h4>We tested the hypothesis that TG2 dependent cross-linking alters the proinflammatory activity of surface-adhered fibrinogen.<h4>Methods</h4>Mouse bone marrow-derived macrophages (BMDMs) were cultured on tissue culture plates coated with fibrinogen or TG2-"],"journal":["Journal of thrombosis and haemostasis : JTH"],"pubmed_title":["Cross-linking by tissue transglutaminase-2 alters fibrinogen-directed macrophage proinflammatory activity."],"pmcid":["PMC9035112"],"funding_grant_id":["F32DK121423","K99 DK129710","K99DK129710","R01 DK120289","F32 DK121423","R01DK120289","R01DK112778","R01ES017537","R01 ES017537"],"pubmed_authors":["Flick MJ","Kopec AK","Luyendyk JP","Poole LG"],"additional_accession":[]},"is_claimable":false,"name":"Cross-linking by tissue transglutaminase-2 alters fibrinogen-directed macrophage proinflammatory activity.","description":"<h4>Background</h4>The blood coagulation factor fibrin(ogen) can modulate inflammation by altering leukocyte activity. Analyses of fibrin(ogen)-mediated proinflammatory activity have largely focused on leukocyte integrin binding activity revealed by conversion of fibrinogen to a stabilized fibrin polymer by blood coagulation enzymes. In addition to coagulation enzymes, fibrinogen is a substrate for tissue transglutaminase-2 (TG2), a widely expressed enzyme that produces unique fibrinogen Aα-γ chain cross-linked products.<h4>Objectives</h4>We tested the hypothesis that TG2 dependent cross-linking alters the proinflammatory activity of surface-adhered fibrinogen.<h4>Methods</h4>Mouse bone marrow-derived macrophages (BMDMs) were cultured on tissue culture plates coated with fibrinogen or TG2-","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2025-04-27T04:21:30.653Z","creation":"2025-02-19T04:20:56.09Z"},"accession":"S-EPMC9035112","cross_references":{"pubmed":["35158413"],"doi":["10.1111/jth.15670"]}}