The objective of the proposed research plan is to study the mechanism by which heparan sulfate proteoglycans synthesized by endothelial cell cultures interact with certain proteins (blood factors) and inhibit their enzymatic activity. To this end, the heparan sulfate proteoglycans that are released into the supernatant growth medium will be isolated and characterized by various biochemical techniques, including the analysis of the structural features of the glycosaminoglycan chains with the use of various degradative enzymes and the elucidation of the primary structure of the protein core.
| Sampaio, L O; Dietrich, C P; Colburn, P et al. (1992) Effect of monensin on the sulfation of heparan sulfate proteoglycan from endothelial cells. J Cell Biochem 50:103-10 |
| Colburn, P; Crabb, J W; Buonassisi, V (1991) Enhanced inhibition of tissue factor by the extended form of an endothelial cell glycoprotein (an extrinsic pathway inhibitor). J Cell Physiol 148:320-6 |
| Nader, H B; Toma, L; Pinhal, M A et al. (1991) Effect of heparin and dextran sulfate on the synthesis and structure of heparan sulfate from cultured endothelial cells. Semin Thromb Hemost 17 Suppl 1:47-56 |
| Nader, H B; Buonassisi, V; Colburn, P et al. (1989) Heparin stimulates the synthesis and modifies the sulfation pattern of heparan sulfate proteoglycan from endothelial cells. J Cell Physiol 140:305-10 |
| Colburn, P; Buonassisi, V; Dietrich, C P et al. (1987) N-glycansulfated fibronectin: one of the several sulfated glycoproteins synthesized by endothelial cells in culture. Biochem Biophys Res Commun 147:920-6 |
