Lipocortin-independent effect of dexamethasone on phospholipase activity in a thymic epithelial cell line.

In the cloned rat thymic endocrine epithelial cell line TEA3A1, treatment with dexamethasone leads to decreased levels of prostaglandin E2, prostaglandin F2 alpha, and thromboxane B2. Dexamethasone treatment also leads to a decrease of both calcium-dependent and calcium-independent phospholipase A2 activity measured in a cell-free assay. Dexamethasone-treated cells also have increased levels of lipocortin-I, a putative modulator of phospholipase A2 activity. The property of calcium-dependent binding of lipocortin to the particulate fraction was used to prepare cytosolic and particulate subcellular fractions which contained phospholiphase A2 activity but no lipocortin-I. Dexamethasone decreased phospholipase A2 activity in both cytosolic and particulate fractions even in the absence of lipocortin, suggesting the presence of a lipocortin-independent mechanism.