Crosstalk between estradiol and NFκB signaling pathways on placental leptin expression.

Pregnancy success requires a proper fetal maternal interaction at the establishment of implantation. Leptin has been described as a multitasking cytokine in pregnancy, particularly in the placenta, where it acts as an autocrine hormone. The expression of leptin in normal trophoblastic cells is regulated by different endogenous signals.

Regulation of NF-κB signalling cascade by immunophilins.

The fine regulation of signalling cascades is a key event required to maintain the appropriate functional properties of a cell when a given stimulus triggers specific biological responses. In this sense, cumulative experimental evidence during the last years has shown that high molecular weight immunophilins possess a fundamental importance in the regulation of many of these processes. It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90.

Biological relevance of Hsp90-binding immunophilins in cancer development and treatment.

Immunophilins are a family of intracellular receptors for immunosuppressive drugs. Those immunophilins that are related to immunosuppression are the smallest proteins of the family, i.e.

NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.

Hsp90 binding immunophilins FKBP51 and FKBP52 modulate steroid receptor trafficking and hormone-dependent biological responses. With the purpose to expand this model to other nuclear factors that are also subject to nuclear-cytoplasmic shuttling, we analyzed whether these immunophilins modulate NF-κB signaling. It is demonstrated that FKBP51 impairs both the nuclear translocation rate of NF-κB and its transcriptional activity.