| Autor: |
Sadler, Isobel I. J., Smith, David W., Shearman, Mark S., Ragan, C. Ian, Tailor, Vipula J., Pollack, Scott J. |
| Zdroj: |
NeuroReport; December 1995, Vol. 7 Issue: 1 p49-53, 5p |
| Abstrakt: |
AGENTS that interfere with the toxic effects of β-amyloid protein may be therapeutically useful against Alzheimer's disease. We reported recently that several sulphated glycosaminoglycans and sulphonated dyes attenuate the toxic effects of β-amyloid fragments β25–35 and β1–40 in two clonal cell lines. We now demonstrate that this protective effect is due to interference with β-amyloid cell association rather than effects on β-amyloid structure. Using an enzyme-linked immunoabsorbance assay to detect cell-associated β1–40, we found in a range of compounds a strong correlation between inhibition of HeLa cell association of β1–40 and attenuation of cellular toxicity as measured by inhibition of 3-[4,5-dimethylthia-zol-2-yl]-2,5-diphenyltetrazolium bromide (MTT) reduction. In contrast, effects on peptide structure, as measured by Congo red binding, were generally inconsistent with the attenuating effects of the compounds on cellular toxicity. These results suggest that by binding β-amyloid these agents prevent its interaction with cells. |
| Databáze: |
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