AI Article Synopsis
- The study investigates how Prostaglandin E (PGE2) activates signaling pathways in T cells from both healthy individuals and those with uveal melanoma.
- PGE2 activation involves phosphorylation of the cAMP responsive element-binding protein (CREB), partially mediated by protein kinase A, as confirmed by specific inhibitors.
- Immunoprecipitation studies show that upon PGE2 treatment, various CREB family proteins and the phosphorylated form of CREB interact with CREB-binding protein (CBP), with T cells from cancer patients showing delayed increases in this interaction compared to healthy subjects.
Article Abstract
Prostaglandin E-induced signal transduction pathways in human T cells from healthy and uveal melanoma-bearing subjects were studied. Transfection experiments showed that PGE2 was able to phosphorylate and activate the fusion trans-activator of the cAMP responsive element-binding protein (CREB). Phosphorylation was at least partially mediated by protein kinase A, as evidenced by the effects of specific kinase inhibitors. Western blotting experiments, which were performed to identify the CREB/ATF2 family members involved in the response to PGE2, revealed a modulation of proteins CREB1, CREB2 and ATF2 and phosphorylation of the 43 kDa form of CREB. Experiments of immunoprecipitation with CREB-binding protein (CBP) demonstrated that, after PGE2 treatment, all of the CREB/ATF isoforms studied, as well as the phosphorylated form of CREB (p-CREB), interacted with CBP. In basal conditions, T cells from patients with conjunctiva basal cell carcinoma showed the presence of p-CREB, which coimmunoprecipitated with CBP. CREB phosphorylation did not modify after PGE2 treatment whereas the p-CREB fraction bound to CBP increased in a delayed manner compared to normal subjects.
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| http://dx.doi.org/10.1046/j.1440-1711.2001.01034.x | DOI Listing |
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