Novel regulator of transcription factor AP-1 in human trophoblast cells: FKBP52

CAMISAY MF, DE LEO SA, GALIGNIANA MD, ERLEJMAN AG

Congreso; LXII Reunión Anual de SAIC; 2017

FK506 binding protein 52 (FKBP52) is a cochaperone that modulates steroid receptors function and has peptidylprolyl-isomerase (PPIase) activity. Low FKBP52 protein level has been detected in placentas from preeclampsia (PE) as well as alteration in a component of AP-1, c-fos protein, expression and trophoblast invasiness. The aim of this work was to investigate the effect of FKBP52 on AP-1 signalling in trophoblast cells. BeWo cells were used as trophoblastic in vitro model. Cells were transfected with wild type FKBP52 or its PPIase mutants, and then, stimulated by PMA. AP-1 signalling was evaluated by analyzing endogenous c-fos expression and stability (Western blot:WB), pERK/ERK ratio along time (WB) and c-fos sublocalization (immunofluorescence). AP-1 transcriptional activity was evaluated by luciferase assays and endogenous biological target as IL-6 secretion (ELISA) and MMP-2 proteolytic activity (zymography). In presence of FKBP52, we observed a higher pERK/ ERK level for a longer time, also greater c-fos nuclear translocation, stability and protein abundance (1.9 ± 0,2 fold). Furthermore, FKBP52 stimulated AP-1 transcriptional activity on a concentration dependent manner (p