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ABSTRACT: Abstract
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
SUBMITTER: Biswas I
PROVIDER: S-EPMC11907474 | biostudies-literature | 2025 Mar
REPOSITORIES: biostudies-literature