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β-Amyloid peptide induced cytoskeletal reorganization in cultured astrocytes

✍ Scribed by O. Salinero; M.T. Moreno-Flores; M.L. Ceballos; F. Wandosell


Publisher
John Wiley and Sons
Year
1997
Tongue
English
Weight
250 KB
Volume
47
Category
Article
ISSN
0360-4012

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✦ Synopsis


The effects of b-amyloid (25-35) (bA) on cultured astrocytes from rat cortex were studied and compared with those of a scrambled peptide and with untreated cultures. Single addition (from 5 to 200 mg/ml) of bA peptide induced a marked morphological change in astrocytes, changing their flat polygonal shape into stellate process-bearing morphology. The changes induced by bA were concentration and time-dependent. The addition of the scrambled peptide did not alter cell viability in comparison with untreated astrocyte cultures. However, cell viability was dose-dependently decreased by bA.

A subpopulation of bA-treated astrocytes showed an increase in glial fibrillary acidic protein (GFAP) and Vimentin (Vim) immunostaining while other reactive astrocyte markers such as S100b, MAP2, and ApoE remained unaltered or undetectable. The morphological changes in bA-treated astrocytes appeared to be mainly due to a cytoskeletal reorganization, since the total amounts of GFAP and Vim proteins were not essentially modified. These results strongly suggest that astrocytes are another cellular target of the effects of bA and this may be relevant to understanding the neuropathology of Alzheimer's disease. J.


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