Activation of the MAPKs ERK1/2 by cell swelling in turbot hepatocytes

Autor: Hélène Ollivier, Audrey Fouchs, Karine Pichavant-Rafini, Stella Roy, Christophe Haond, Patrick Calvès
Přispěvatelé: Optimisation des régulations physiologiques (ORPHY (EA 4324)), Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO)-Université de Brest (UBO)-Centre Hospitalier Régional Universitaire de Brest (CHRU Brest)
Jazyk: angličtina
Rok vydání: 2010
Předmět:
MAPK/ERK pathway
MESH: Thapsigargin
MESH: Hepatocytes
chemistry.chemical_compound
Adenosine Triphosphate
0302 clinical medicine
MESH: Adenosine Triphosphate
MESH: Animals
Phosphorylation
Receptor
Egtazic Acid
MESH: Cell Size
Mitogen-Activated Protein Kinase 1
0303 health sciences
Mitogen-Activated Protein Kinase 3
Kinase
Purinergic receptor
General Medicine
MESH: Flatfishes
Cell biology
Hypotonic Solutions
MESH: Calcium
Flatfishes
Thapsigargin
MESH: Hypotonic Solutions
MESH: Mitogen-Activated Protein Kinase 3
MESH: Mitogen-Activated Protein Kinase 1
MESH: Enzyme Activation
MESH: Egtazic Acid
Biology
03 medical and health sciences
Osmotic Pressure
[SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO]
Animals
MESH: Receptors
Purinergic P2
Protein kinase A
Cell Size
030304 developmental biology
MESH: Phosphorylation
Receptors
Purinergic P2
Apyrase
Cell Biology
MESH: Osmotic Pressure
Molecular biology
Enzyme Activation
chemistry
Hepatocytes
Calcium
030217 neurology & neurosurgery
Zdroj: Biology of the Cell
Biology of the Cell, Wiley, 2010, 102 (8), pp.447-56. ⟨10.1042/BC20090154⟩
ISSN: 0248-4900
1768-322X
DOI: 10.1042/BC20090154⟩
Popis: International audience; BACKGROUND INFORMATION: Activation of MAPKs (mitogen-activated protein kinases), in particular ERK1/2 (extracellular-signal-regulated kinase 1/2), has been reported to take place in a large variety of cell types after hypo-osmotic cell swelling. Depending on cell type, ERK1/2 phosphorylation can then serve or not the RVD (regulatory volume decrease) process. The present study investigates ERK1/2 activation after aniso-osmotic stimulations in turbot hepatocytes and the potential link between phosphorylation of these proteins and RVD. RESULTS: In turbot hepatocytes, Western-blot analysis shows that a hypo-osmotic shock from 320 to 240 mOsm kg(-1) induced a rapid increase in ERK1/2 phosphorylation, whereas a hyper-osmotic shock from 320 to 400 mOsm kg(-1) induced no significant change in the phosphorylation of these proteins. The hypo-osmotic-induced ERK1/2 phosphorylation was significantly prevented when hypo-osmotic shock was performed in the presence of the specific MEK (MAPK/ERK kinase) inhibitor PD98059 (100 microM). In these conditions, the RVD process was not altered, suggesting that ERK1/2 did not participate in this process in turbot hepatocytes. Moreover, the hypo-osmotic-induced activation of ERK1/2 was significantly prevented by breakdown of extracellular ATP by apyrase (10 units ml(-1)), by inhibition of purinergic P2 receptors by suramin (100 microM) or by calcium depletion using EGTA (1 mM) and thapsigargin (1 microM). CONCLUSIONS: In turbot hepatocytes, hypo-osmotic swelling but not hyper-osmotic shrinkage induced the activation of ERK1/2. However, these proteins do not seem to be involved in the RVD process. Their hypo-osmotic-induced activation is partially due to cascades of signalling events triggered by the binding of released ATP on purinergic P2 receptors and requires the presence of calcium.
Databáze: OpenAIRE
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