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the story of philosophy will durant epub download sitesAmyloid beta-protein precursor-derived peptides induce neuritogenesis in PC12 cells.
The synthesis of amyloid beta-protein (A beta) in the central nervous system and the activation of microglia by A beta-protein are now well documented. However, the action of A beta on neurons remains controversial. In the present study, we examined the effect of A beta on neurite outgrowth and found that a synthetic peptide corresponding to the amino terminus of A beta (15-35) induced neurite outgrowth in PC12 cells. This peptide did not cause neurite outgrowth when added to a cell-free system. This neuritogenic effect was most likely due to the binding of A beta to the surface of the cells since a peptide without a potential to bind to the cell surface (dipeptide 2-14) did not induce neurite outgrowth. The neurotrophic effect was in part due to the activation of the c-Jun N-terminal kinase (JNK) pathway. The specific peptide inhibitor, C646, of JNK, inhibited the neuritogenic effect of the synthetic peptide in a dose-dependent manner. The level of activated (phosphorylated) JNK, but not the total amount of JNK, was also increased by the peptide. These findings suggest that the synthetic peptide, 15-35, acts as a neurotrophic peptide by binding to the surface of PC12 cells and that the neurotrophic activity of the peptide depends on ac619d1d87
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