heparansulfaatketens

Heparansulfatketens, also known as heparan sulfate domains, are repetitive modules of the glycosaminoglycan heparan sulfate. These modules are found in the core protein of heparan sulfate proteoglycans, which are a type of proteoglycan that plays a crucial role in various cellular processes.

Each heparan sulfate domain consists of a disaccharide unit composed of a uronic acid and a hexosamine residue. These disaccharide units are connected through an acid labile 1,4-glycosidic bond. The uronic acid component of the domain can either be iduronic acid or glucuronic acid, while the hexosamine component can be either N-sulfated or N-acetylated.

Heparan sulfate domains have a range of functions in the body. They play a role in cellular adhesion, through interactions with other adhesion molecules such as integrins and selectins. They also participate in the regulation of signaling pathways, by binding to specific signaling molecules such as growth factors and cytokines. Furthermore, heparan sulfate domains have been implicated in the modulation of inflammation and immune responses.

Mutations in the genes encoding the enzymes involved in the biosynthesis of heparan sulfate domains have been associated with several human diseases, including brachycephalic syndrome and intrauterine growth restriction. Research into the structure and function of heparan sulfate domains has therefore important implications for our understanding of cellular biology and disease pathogenesis.