Activation of PKC epsilon induces lactotroph proliferation through ERK1/2 in response to phorbol ester
Autor: | Alicia Inés Torres, Claudia Mariela Palmeri, Ana Lucía De Paul, Jorge Humberto Mukdsi, Silvina Gutiérrez, Juan Pablo Petiti |
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Rok vydání: | 2007 |
Předmět: |
MAPK/ERK pathway
medicine.medical_specialty Lactotrophs MAP Kinase Signaling System Protein Kinase C-epsilon Biochemistry chemistry.chemical_compound Endocrinology Internal medicine medicine Animals Rats Wistar Molecular Biology Protein kinase C Cells Cultured Cell Proliferation Mitogen-Activated Protein Kinase 3 Kinase Cell biology Rats Enzyme Activation Protein Transport chemistry Tetradecanoylphorbol Acetate Phorbol Phosphorylation Female Intracellular |
Zdroj: | Molecular and cellular endocrinology. 289(1-2) |
ISSN: | 0303-7207 |
Popis: | The aim of this investigation was to contribute to current knowledge about intracellular mechanisms that are involved in lactotroph cell proliferation, by evaluating the role of PKCalpha, PKCepsilon and extracellular-signal regulated kinase (ERK) 1/2 in response to phorbol 12-myristate13-acetate (PMA). In primary pituitary cultures, the activation of protein kinase C (PKC) by PMA for 15 min stimulated lactotroph proliferation; whereas a prolonged activation for 3-8h diminished this proliferative effect. The use of PMA for 15 min-activated PKCepsilon and ERK1/2, whereas incubation with PMA for 3 h induced PKCalpha activation and attenuated the PMA-triggered phosphorylation of ERK1/2. The following inhibitors: PKCs (bisindolylmaleimide I), PKCepsilon (epsilonV1 peptide) and ERK1/2 (PD98059) prevented the mitogenic activity induced by PMA for 15 min. Lactotroph cells stimulated with PMA for 15 min showed a translocation of PKCepsilon to membrane compartment and nucleus. These results thus establish that PKCepsilon plays an essential role in the lactotroph proliferation induced by PMA by triggering signals that involve ERK1/2 activation. |
Databáze: | OpenAIRE |
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