INVESTIGADORES
GALIGNIANA Mario Daniel
congresos y reuniones científicas
Título:
FK506 binding protein 52 modulated AP-1 functions in human trophoblast cells
Autor/es:
CAMISAY MF, DE LEO SA, FONTANA V, GALIGNIANA MD, ERLEJMAN AG
Lugar:
Puerto Varas
Reunión:
Congreso; International Congress of the Society for Maternal-Fetal Interaction & Placenta; 2017
Resumen:
FK506 binding protein 52 (FKBP52) is a cochaperone that influences steroid receptors function and has peptidylprolyl-isomerase (PPIase) activity. Reduced FKBP52 protein has been detected in placentas from preeclampsia (PE), also it has been suggested that c-fos is implicated in regulating invasive mechanism of trophoblast in PE as well as in placentas from normal gestations. Objective: The aim of this work was to investigate the effect of FKBP52 on the transcription factor activator protein 1 (AP-1) in trophoblast cells. Methods: BeWo were used as in vitro choriocarcinoma model. Cells were transfected with wild type FKBPs or their putative PPIase mutants, and then, stimulated by miristic-acetated phorbol ester 12-myristate 13-acetate (PMA). AP-1 signalling was evaluated by luciferase assays and Western blot, analyzing endogenous c-fos expression and monitoring phophorylated extracellular signal?regulated kinases 1 and 2 (pERK1/2)/total ERK ratio along time. Interleukin 6 (IL-6) secretion was measured by ELISA, and Matrix metalloproteinase 2 (MMP-2) proteolytic activity was determined by zymography. Results: After 30 min of PMA treatment ERK1/2 acquired its maximum phosphorylation level. In presences of FKBP52 pERK1/2 level remained increases along time (P