Monensin is a monovalent metal ionophore that affects the intracellular translocation of secretory proteins at the level of trans-Golgi cisternae. Exposure of endothelial cells to rnonensin results in the synthesis of heparan sulfate and chondroitin sulfate with a lower degree of sulfation. The inhi
Heparin stimulates the synthesis and modifies the sulfation pattern of heparan sulfate proteoglycan from endothelial cells
β Scribed by Helena B. Nader; Vincenzo Buonassisi; Patricia Colburn; Carl P. Dietrich
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 605 KB
- Volume
- 140
- Category
- Article
- ISSN
- 0021-9541
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β¦ Synopsis
Heparin stimulates 2-3-fold, in a concentration-dependent manner, the synthesis of heparan sulfate secreted by cultured endothelial cells. The increase in synthetic rate takes place immediately after exposure of the cells to heparin, affects only heparan sulfate, and i s specific for the endothelial cell. No stimulation by other glycosaminoglycans was observed. Analysis of the disaccharide products formed by the action of heparitinases reveals a higher degree of sulfation of the uronic acid residues in the heparan sulfate of cells exposed to heparin.
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## Abstract Primary cultures of rat hepatocytes maintained as monolayer in a serumβfree medium synthesise and secrete sulphated proteoglycans. Nearly 5% of the total ^35^(S)βsulphated material was obtained in a soluble form from beneath the cell layer. A shift in gel filtration pattern on Ξ²βelimina