PMC:7381711 / 2953-4886 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7381711","sourcedb":"PMC","sourceid":"7381711","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7381711","text":"HEPARIN STRUCTURE AND FUNCTION\nHeparin is a heterogeneous preparation of long, linear highly sulfated heparan sulfate (HS) glycosaminoglycans purified from porcine intestines (see Fig. 1). The sulfated nature of its constituent HS glycosaminoglycan chains confers heparin with the highest negative charge density of any known biomolecule (43). This charge allows heparin to strongly and selectively interact with an immense number of proteins, the most classic being its interaction with serine protease inhibitor antithrombin-III (AT3) that provides its anticoagulant activity. This anticoagulant activity is dependent on the presence of a precise pentasaccharide sequence within longer HS chains that allows for AT3 binding as shown in Fig. 1. Beyond AT3, hundreds of biologically relevant, heparin-protein interactions have been described, which has led to the recognition of an immense number of potential off-target (both positive and negative) effects of heparin of unknown clinical importance.\nFig. 1. Structure and function of heparin. Heparins are a heterogeneous mix of heparan sulfate (HS) glycosaminoglycans. Each HS strand is composed of repeating disaccharide units of N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcA) or iduronic acid (IdoA). GlcNAc can be sulfated at three distinct sites (-6S, -NS, and -3S) and IdoA at one (-2S). Unfractionated heparin is composed of HS chains that are \u003e30 saccharides in length, whereas low-molecular weight heparin constituent HS chains are 22 saccharides or less (3). The charge distribution of heparin imparted by the presence of the precise pentasaccharide sequence shown allows for the binding of heparin to serine protease inhibitor antithrombin-III (AT3), conferring its primary anticoagulant effect. Innumerable other sulfation sequences are found in heparin preparations, which leads to binding and biologically relevant activity modulation of many other 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