| First Author | González-Arenas A | Year | 2008 |
| Journal | Biochim Biophys Acta | Volume | 1783 |
| Issue | 2 | Pages | 253-62 |
| PubMed ID | 18166159 | Mgi Jnum | J:133451 |
| Mgi Id | MGI:3778586 | Doi | 10.1016/j.bbamcr.2007.11.014 |
| Citation | Gonzalez-Arenas A, et al. (2008) Regulation of LPA receptor function by estrogens. Biochim Biophys Acta 1783(2):253-62 |
| abstractText | 17beta-Estradiol induced LPA(1) receptor desensitization in C9 cells stably expressing LPA(1) receptors and transiently expressing estrogen receptor alpha. Such desensitization was evidenced by a reduction in lysophosphatidic acid-mediated Ca(2+)mobilization and it was associated to receptor phosphorylation and internalization. These effects of 17beta-estradiol were rapid (taking place over 5 min) and were blocked by the estrogen receptor antagonist ICI 182780. Similarly, inhibitors of phosphoinositide 3-kinase (wortmannin and LY294002) and of protein kinase C (staurosporine and Go 6976) blocked 17beta-estradiol-induced LPA(1) receptor desensitization and phosphorylation. Confocal microscopy evidenced LPA(1) receptor internalization in response to 17beta-estradiol treatment. Association between LPA(1) receptors and protein kinase C alpha was suggested by co-immunoprecipitation assays. Protein kinase C alpha was associated with LPA(1) receptors in the absence of stimulus and such association further increased in a dynamic fashion in response to 17beta-estradiol. The results demonstrated that in C9 cells estrogens modulate LPA(1) action through estrogen receptor alpha with the participation of protein kinase C alpha and phosphoinositide 3-kinase. |
