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Antiapoptotic effects of vasopressin in the neuronal cell line H32 involve protein kinase Cα and β
Author(s) -
Chen Jun,
Liu Ying,
Soh JaeWon,
Aguilera Greti
Publication year - 2009
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2009.06219.x
Subject(s) - protein kinase c , kinase , mapk/erk pathway , protein kinase b , protein kinase a , microbiology and biotechnology , phosphorylation , signal transduction , pi3k/akt/mtor pathway , chemistry , biology
Activation of V1 vasopressin (VP) receptors prevents serum deprivation‐induced apoptosis in neuronal H32 cells, partially through mitogen‐activated protein kinase (MAPK) mediated Bad phosphorylation. In this study, we investigated the role of protein kinases C (PKC) and B (PKB) mediating VP‐induced antiapoptosis in H32 cells. Serum deprivation increased PKCδ but not PKCα or PKCβ activity, while VP increased PKCα and PKCβ without affecting PKCδ activity. Inhibition of PKCδ prevented caspase 3 activation, indicating that PKCδ mediates the pro‐apoptotic actions of serum deprivation. Simultaneous inhibition of PKCα and β and MAPK abolished VP‐induced Bad phosphorylation, but it only partially prevented caspase 3 inhibition. Complete abolition of the protective effect of VP on serum deprivation‐induced caspase 3 activity required additional blockade of phosphoinositide 3 kinase (PI3K)/protein kinase B. The data demonstrate that VP exerts antiapoptosis through multiple pathways; while PKCα and β together with extracellular signal‐regulated kinases/MAPK activation mediates Bad phosphorylation (inactivation), the full protective action of VP requires additional activation of PKB (PI3K/protein kinase B) pathway.