It has been observed that the designs of Bcl 2 and Bax expression in the mouse do not often overlap w51x, and this, along with different areas of Bcl 2 and Bax within the cell, suggests that in certain cells these proteins aren’t managing each other, and that other proteins are involved. Moreover, exercise of the proteins may be changed by, like, phosphorylation. It’s been shown that Bcl 2 is inactivated by phosphorylation w36x, if Bax is similarly regulated this might explain why Bax can be present in large amounts through the brain without killing cells. Quantities of Bax protein were selectively increased in CA1 neurons destined to die after HI and then declined in a manner that correlated with cell loss. The induction of Bax might be linked to the induction of c Jun in these nerves. These results show that cells undergoing apoptosis may be under the control of cell specific and specific genetic checkpoints, which may involve any number of the bcl 2 associated proteins. We also discovered basal expression of Bax in control human hippocampi, which was lost within the granule cells in AD brains. This may be linked to success of these cells in AD. Bax was observed to be concentrated in senile plaques in AD hippocampi, which may be related to t amyloid toxicity in AD brains, along with astrocytes and tangles, indicating that Bax may play a part in the pathogenesis of AD. Neuronal cell death is extremely common all through normal development of the vertebrate nervous system and at AP26113 least 5-0 of the nerves are eventually lost w30x. That neuronal cell death is apoptotic in nature and is thought to be induced primarily with a loss or paid down expression of targetderived trophic factors, which act on the distal nerve endings. In adult and neonatal animals, even though natural neuronal cell death doesn’t occur usually, axon destruction fundamentally results in neuronal cell death.