Heparan sulfate and heparin glycosaminoglycan chains (HS/Hep GAGs)

Heparan sulfate (HS) and heparin are complex, linear polysaccharides belonging to the glycosaminoglycan (GAG) family, typically found attached to core proteins as proteoglycans on cell surfaces and in the extracellular matrix (Gallagher & Lyon, 2000). They are characterized by repeating disaccharide units of uronic acid and glucosamine, which undergo extensive sulfation and epimerization, creating highly negatively charged domains that interact with a vast array of proteins, including growth factors, chemokines, and antithrombin (NCBI, 2022). In physiology, they regulate blood coagulation, cell signaling, and tissue morphogenesis by acting as co-receptors or sequestration sites for ligands. Pathologically, HS/heparin chains are exploited by various viruses, such as SARS-CoV-2 and Herpes Simplex Virus, for initial cell attachment and entry (Clausen et al., 2020). They also play significant roles in tumor angiogenesis, metastasis, and the stabilization of amyloid fibrils in neurodegenerative diseases. Therapeutic intervention often involves using exogenous heparin as an anticoagulant or developing HS mimetics to block pathological protein-GAG interactions (StatPearls, 2023).

Other names

Heparan sulfateHeparinHSHepHeparan sulfate glycosaminoglycanHS-GAGHeparin GAG

Potentiation of antithrombin III-mediated inhibition of Factor Xa and thrombin; competitive inhibition of growth factor and chemokine binding to their receptors; blockade of viral attachment to cell surface proteoglycans (StatPearls, 2023; NCBI, 2022).