Antiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence.

ABSTRACT: A specific pentasaccharide sequence of heparin binds with high affinity to native antithrombin and induces a conformational change in the inhibitor by a previously described two-step interaction mechanism. In this work, the interactions of heparin with the antiangiogenic latent and cleaved antithrombin forms were studied. Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin. Rapid kinetic studies demonstrated that this pentasaccharide induced a conformational change also in latent and cleaved antithrombin. The binding affinities of these antithrombin forms for the pentasaccharide, as compared to native antithrombin, were approximately 30-fold lower due to two to three fewer ionic interactions, resulting in less stable conf

SUBMITTER: Schedin-Weiss S 

PROVIDER: S-EPMC2706396 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature