{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(5)"],"submitter":["Biswas I"],"pubmed_abstract":["<h4>Abstract</h4>Antithrombin (AT) is an anticoagulant serpin involved in the regulation of proteolytic activities of coagulation proteases. AT also possesses a direct anti-inflammatory function. The anticoagulant function of AT is mediated through its reactive center loop-dependent inhibition of coagulation proteases, but anti-inflammatory function of AT is mediated via its D-helix-dependent interaction with vascular glycosaminoglycans (GAGs). In vitro assays have established that therapeutic heparins promote the anticoagulant function of AT by binding D-helix and activating the serpin, however, the contribution of vascular GAGs to D-helix-dependent anticoagulant function of AT has remained poorly understood in vivo. Here, we explored this question by using 2 AT mutants, (AT-4Mut), which "],"journal":["Blood advances"],"pagination":["966-978"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11907474"],"repository":["biostudies-literature"],"pubmed_title":["Physiological significance of antithrombin D-helix interaction with vascular GAGs."],"pmcid":["PMC11907474"],"pubmed_authors":["Lupu F","Biswas I","Rezaie AR","Panicker SR"],"additional_accession":[]},"is_claimable":false,"name":"Physiological significance of antithrombin D-helix interaction with vascular GAGs.","description":"<h4>Abstract</h4>Antithrombin (AT) is an anticoagulant serpin involved in the regulation of proteolytic activities of coagulation proteases. AT also possesses a direct anti-inflammatory function. The anticoagulant function of AT is mediated through its reactive center loop-dependent inhibition of coagulation proteases, but anti-inflammatory function of AT is mediated via its D-helix-dependent interaction with vascular glycosaminoglycans (GAGs). In vitro assays have established that therapeutic heparins promote the anticoagulant function of AT by binding D-helix and activating the serpin, however, the contribution of vascular GAGs to D-helix-dependent anticoagulant function of AT has remained poorly understood in vivo. Here, we explored this question by using 2 AT mutants, (AT-4Mut), which ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2025-04-05T22:06:03.221Z","creation":"2025-04-05T22:06:03.221Z"},"accession":"S-EPMC11907474","cross_references":{"pubmed":["39671300"],"doi":["10.1182/bloodadvances.2024014756"]}}