PKC Inhibition

PKC is a family of serine/threonine kinases that are involved in the transduction of signals for cell proliferation, differentiation, ► apoptosis, senescence, and an-giogenesis. The family is comprised of at least 12 isoforms, which are subdivided into three classes (classical/conventional, novel, and atypical) on the basis of calcium- and diacylglycerol (DAG) dependence. PKC isoforms differ in structure, subcellular localization, tissue specificity, mode of activation, and substrate specificity. Activation of PKC results in its translocation, and subcellular localization is thought to regulate accessibility to activators and substrates. PKC is activated by such varied upstream signals as ► G protein-coupled receptors (GPCRs), receptor tyrosine kinases (RTKs), and nonRTKs via DAG activation (Fig. 1). Several PKC isoforms are independently activated by the phospholipase C (PLC) and phosphoinositide-3 kinase (PI3K) pathways. Of PKC's numerous substrates, a major target is the MEK-ERK pathway, also thought to be involved in the activation of Rafl (Serova et al. 2006) (The Raf-MEK-ERK pathway is a signaling cascade - the first entirely mapped from the cell membrane with many substrates both in the cytosol and the nucleus). PKC has been identified as a potential target for the treatment of a number of medical diseases, including diabetes, cancer, and ► bipolar disorder. With respect to its potential role in bipolar disorder, it is significant that lithium and valproate bring about strikingly similar effects on the PKC signaling cascade (Manji and Lenox 1999), as discussed below.

Myo-inositol

Serotonin, norepinephrine, dopamine,

Myo-inositol

Serotonin, norepinephrine, dopamine,

Cytoskeletal proteins underlying long-term neuroplasticity

Cytoskeletal proteins underlying long-term neuroplasticity

Long-term alterations in synaptic plasticity and neuronal morphology

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