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Multiple cAMP-induced signaling cascades regulate prolactin expression in T cells
S Gerlo1, P Verdood, E L Hooghe-Peters
1Neuroendocrine Immunology Research Group, Department of Pharmacology, Free University of Brussels (VUB), Laarbeeklaan 103, 1090 Brussels, Belgium.
Cellular and Molecular Life Sciences : CMLS
|December 27, 2005
Summary
Cyclic adenosine monophosphate (cAMP) stimulates prolactin (PRL) transcription in human T lymphocytes. This process involves both protein kinase A (PKA) and EPAC-mediated pathways, impacting immune function.
Area of Science:
- Immunology
- Molecular Biology
- Endocrinology
Background:
- Prolactin (PRL), a pituitary hormone, plays a key role in reproduction and exhibits immunomodulatory functions.
- The precise molecular mechanisms by which PRL influences T lymphocyte function are not fully understood.
Purpose of the Study:
- To investigate the role of cyclic adenosine monophosphate (cAMP) in regulating prolactin (PRL) transcription in primary human T lymphocytes.
- To elucidate the signaling pathways involved in cAMP-mediated PRL expression.
Main Methods:
- Primary human T lymphocytes were treated with cAMP.
- Inhibition of protein kinase A (PKA) and p38 mitogen-activated protein kinase (MAPK) was performed.
- Phosphorylation of p38 and cAMP response element-binding protein (CREB) was analyzed.
- A methylated cAMP analogue activating EPAC was used.
Main Results:
- cAMP significantly stimulates PRL transcription in human T lymphocytes.
- Inhibition of PKA and p38 MAPK partially reduced cAMP-induced PRL expression.
- cAMP-induced p38 phosphorylation occurred independently of PKA and could be mediated by EPAC.
- CREB phosphorylation was dependent on PKA.
Conclusions:
- cAMP induces PRL expression in T lymphocytes through a dual signaling mechanism.
- One pathway involves PKA, leading to CREB phosphorylation.
- The second pathway is PKA-independent, involves EPAC, and leads to p38 phosphorylation, contributing to PRL expression.