Changes in functions of intermediate filaments in alzhaimer cell

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The fibroblasts were cultured from the cutaneous tissue of patients with familial Alzheimer's disease and non-familial Alzheimer's disease. In the process of collecting many clones of fibroblasts, a clone with a mutation in amyloid beta-protein precursor gene was found. The mutation was the same as reported by Goat et al, i. e. a substitution of Val to Ile at 717 of amyloid beta-protein precursor. The distribution of vimentin fibers in the cultured fibroblasts were studied, showing the drastic derangement in vimentin distribution in Alzheimer cells. The derangement was most obviously noticed with the cells with the mutation. The vimentin molecule showed no changes but the fodrin showed the increased accumulation in fibroblasts from Alzheimer patients. It was found that fodrin degradation in Alzheimr cells is inhibited. Considering the possibility that fodrin is degraded by Calcium-activated neutral protease (CANP), the calcium level and mobilization in Alzheimer cells was investigated. The results showed that calcium mobilization is significantly suppressed in Alzheimer fibroblasts. It is highly speculated that metabolism of cytoskeletal proteins such as fodrin is altered in Alzheimer cells which is closely related with the pathological processes observed in Alzheimer brain.