Antiapoptotic effects of vasopressin in the neuronal cell line H32 involve protein kinase Calpha and beta.
Article
Chen, Jun, Liu, Ying, Soh, Jae-Won et al. (2009). Antiapoptotic effects of vasopressin in the neuronal cell line H32 involve protein kinase Calpha and beta.
. Journal of Neurochemistry, 110(4), 1310-1320. 10.1111/j.1471-4159.2009.06219.x
Chen, Jun, Liu, Ying, Soh, Jae-Won et al. (2009). Antiapoptotic effects of vasopressin in the neuronal cell line H32 involve protein kinase Calpha and beta.
. Journal of Neurochemistry, 110(4), 1310-1320. 10.1111/j.1471-4159.2009.06219.x
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 PKCdelta but not PKCalpha or PKCbeta activity, while VP increased PKCalpha and PKCbeta without affecting PKCdelta activity. Inhibition of PKCdelta prevented caspase 3 activation, indicating that PKCdelta mediates the pro-apoptotic actions of serum deprivation. Simultaneous inhibition of PKCalpha and beta 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 PKCalpha and beta 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.
