Laminin heparin binding

Sung, U., O Rear, J.J. and Yurchenco, P.D. (1993) Cell and heparin-binding sites in the distal long arm of laminin identification of active and cryptic sites with recombinant and hybrid glycoprotein. J. Cell Biol. 123 1255-1268. 

In addition to gangliosides, heparin related molecules have also been shown to be involved in fibronectin mediated cell adhesion. Heparin binding sites have been described on many cell adhesion proteins e.g., fibronectin (25-26), laminin (27), and vitronectin... 

Study of heparin binding to thrombin, 56 low-density lipoproteins, lipoprotein lipase, circulatory serine proteases, proteinase inhibitors, heparin-binding growth factors, blood vessel-associated proteins (fibronectin and laminin) and binding to cells and tissues. Study of anticoagulant activity and the modulation of the structure, function and metabolism of many proteins and en-2ymes. 

Charonis,. A.S., Skubitz, A.P.N., Koliakos, G.G., Reger, L.A., Dege, ]., Vogel, A.M., Wohlhneter, R. and Fnrcht, L.T, (1988), A novel synthetic peptide from the B1 chain of laminin widi heparin-binding and cell adhesion-promoting activities./. CellBiol., 107. 1253—1260. 

FN, fibronectin BSP, bone sialoprotain, HBP, heparin binding peptides LN, laminin PDL, poly-D-lysine VN, vitronectin... 

Fragment 3 (Mr 50K) possessed / structure, appeared globular in electron micrographs, and was found to bind to heparin. It was assumed to be the globular region at the end of the long arm of laminin. This site is one of the main heparin- and heparan sulfate-binding domains in laminin (Ott et al., 1982). 

Early attempts to functionalize biomaterial surfaces with biological molecules were focused on improving blood compatibility of cardiovascular devices, such as the artificial heart and synthetic blood vessels, by immobilizing heparin or albumin on polyurethane or Dacron . To enhance cell adhesion to biomaterial surfaces, entire extracellular matrix (ECM) proteins, such as fibronectin and laminin, have been used directly as coatings. However, because of the nonspecific manner of whole protein adsorption, most of the cell binding capability is often lost. Using a molecular templating technique, it may be possible to select which protein(s) to absorb on biomaterial surfaces. ... 

Hopf M, Gdhring W, Kohfeldt E, Yamada Y, Timpl R. Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibro-nectin, fibulin-2 and heparin. Eur J Biochem 1999 259 917-925. 

Laminin Trimer 850 kDa A-chain 400 kDa Bl-chain 215 kDa B2-chain 205 kDa Extracellular matrix Binds collagen, entactin, heparin and integrin Principal component of extracellular matrix... 

Heparin sulphate Low-density form 600-700 Extracellular matrix Binds laminin and Structural component of... 

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