Extracellular heparin

Heparin sulfate proteoglycans (HSPGs) are heavily glycosylated proteins that are part of the extracellular matrix. Interaction with HSPGs help to stabilize and localize extracellular Wnts. 

This molecule is present on many cell sur ces as a proteoglycan and is extracellular. It contains GlcN with fewer N-sulfates than heparin, and, unhke heparin, its predominant uronic acid is GlcUA. 

Polymeric carbohydrates are usually encountered as distributions, so high resolution is rarely important. Of all biological macromolecules, carbohydrates are particularly amenable to analysis by GPC because hydrophobic interactions are typically weak. A section below is devoted to the analyses of carboxymethylcellulose and xanthan. Other examples of polysaccharides of interest are hyaluronic acid,62 polymers of (l-glucose,121125 heparin,126127 cellulose and chitin,128 and Mucorales extracellular polysaccharides.129... 

Rusnati M, Tulipano G, Urbinati C, et al. The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists. J Biol Chem 1998 273(26) 16027-16037. 

Heparin has been found to bind a large number of proteins (Table 3). The biological activity of heparin and related polysaccharides is usually ascribed to their interaction with heparin-binding proteins. These proteins can be classified into classes including (1) enzymes, (2) protease inhibitors, (3) lipoproteins, (4) growth factors, (5) chemokines, (6) selectins, (7) extracellular matrix proteins, (8) receptor proteins, (9) viral coat proteins, (10) nuclear proteins, and (11) other proteins (1). Many heparin-binding proteins are enzymes and enzyme inhibitors. For example, proteases in the coagulation cascade, such as factors Ha, IXa, Xa, Xlla, and Villa, are heparin-... 

Unlike other GAGs that are extracellular compounds, heparin is an intracellular component of mast cells that line arteries, especially in liver, lungs, and skin. 

The structure of PTPo is consistent with its role in binding ligands on the surface of other cells or in the extracellular matrix. It interacts with heparin sulphate proteoglycan in the basement membrane (Sajnani-Perez et al. 2003). It may also bind to the C-terminal domain of cell surface-exposed nucleolin, a normally nuclear protein that is presented on the surface of developing muscle cells (Alete et al. 2006). However, these complexes seem to mediate structural or long-term regulatory interactions rather than short-term signaling to the neuronal secretory machinery. 

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