Cortisol decreases the synthesis of hyaluronic acid by human aortic smooth muscle cells in culture. - PubMed - NCBI
The effect of cortisol on the synthesis of glycosaminoglycans (GAGs) was studied in cultured human aortic smooth muscle cells. Cortisol, at a level slightly exceeding the physiological concentration (10(-6) M), decreased the synthesis of hyaluronic acid (HA) by 50% but had no significant effect on the synthesis of sulphated GAGs. The ratio of HA to sulphated GAGs decreased by 47%. These effects were most marked in the fraction secreted into the culture medium. Cortisol neither affected the activity of the hyaluronic acid synthesizing enzyme complex in a cell-free system nor the molecular weight distribution of hyaluronic acid. We suggest that the atherogenity of cortisol and stress may be associated with their effect on the synthesis of HA by the smooth muscle cells of the arterial wall.
Effect of glucocorticoids on glycosaminoglycan metabolism in cultured human skin fibroblasts. - PubMed - NCBI
Human skin fibroblasts were exposed to 3 anti-inflammatory steroids in order to study their effects on the glycosaminoglycan metabolism. The potent glucocorticoids, fluocinolone acetonide and budesonide, even at low concentrations strongly reduced the accumulation of hyaluronic acid and sulfated glycosaminoglycans in the medium, at the cell surface, and in the cells. Hydrocortisone had considerably less effect. The 3 compartments were not influenced to the same extent and the least inhibition was noted in the cell surface pool. Dermatan sulfate was decreased to the same relative extent in all 3 compartments, while hyaluronic acid and heparan sulfate were specifically retained at the cell surface, explaining why this compartment was less affected than the others. Dermatan sulfate was studied in more detail regarding effects on its copolymeric structure. Glucocorticoid treatment changed the uronosyl composition of the polysaccharides so that a relative decrease of glucuronic acid residues and a relative increase of iduronic acid residues were noted. This change was most evident in dermatan sulfate of the medium and of the cell surface. Thus, glucocorticoid treatment not only reduces the quantity of various glycosaminoglycans but also changes the distribution, the relative proportion, and the structure of connective tissue proteoglycans. These effects probably contribute to the development of skin atrophy, which often is observed after long-term treatment with potent glucocorticoids.
The effect of cortisol on the synthesis of glycosaminoglycans (GAGs) was studied in cultured human aortic smooth muscle cells. Cortisol, at a level slightly exceeding the physiological concentration (10(-6) M), decreased the synthesis of hyaluronic acid (HA) by 50% but had no significant effect on the synthesis of sulphated GAGs. The ratio of HA to sulphated GAGs decreased by 47%. These effects were most marked in the fraction secreted into the culture medium. Cortisol neither affected the activity of the hyaluronic acid synthesizing enzyme complex in a cell-free system nor the molecular weight distribution of hyaluronic acid. We suggest that the atherogenity of cortisol and stress may be associated with their effect on the synthesis of HA by the smooth muscle cells of the arterial wall.
Effect of glucocorticoids on glycosaminoglycan metabolism in cultured human skin fibroblasts. - PubMed - NCBI
Human skin fibroblasts were exposed to 3 anti-inflammatory steroids in order to study their effects on the glycosaminoglycan metabolism. The potent glucocorticoids, fluocinolone acetonide and budesonide, even at low concentrations strongly reduced the accumulation of hyaluronic acid and sulfated glycosaminoglycans in the medium, at the cell surface, and in the cells. Hydrocortisone had considerably less effect. The 3 compartments were not influenced to the same extent and the least inhibition was noted in the cell surface pool. Dermatan sulfate was decreased to the same relative extent in all 3 compartments, while hyaluronic acid and heparan sulfate were specifically retained at the cell surface, explaining why this compartment was less affected than the others. Dermatan sulfate was studied in more detail regarding effects on its copolymeric structure. Glucocorticoid treatment changed the uronosyl composition of the polysaccharides so that a relative decrease of glucuronic acid residues and a relative increase of iduronic acid residues were noted. This change was most evident in dermatan sulfate of the medium and of the cell surface. Thus, glucocorticoid treatment not only reduces the quantity of various glycosaminoglycans but also changes the distribution, the relative proportion, and the structure of connective tissue proteoglycans. These effects probably contribute to the development of skin atrophy, which often is observed after long-term treatment with potent glucocorticoids.
