| Autor: |
Laskay G; Institute of Medical Chemistry, Albert Szent-Györgyi Medical University, Szeged, Hungary. laskayg@mdche.szote.u-szeged.hu, Zarándi M, Varga J, Jost K, Fónagy A, Torday C, Latzkovits L, Penke B |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1997 Jun 27; Vol. 235 (3), pp. 479-81. |
| DOI: |
10.1006/bbrc.1997.6806 |
| Abstrakt: |
Comparative fluorimetric studies on the long-term (8-hour) action of beta[1-42]amyloid and its shorter fragments beta[1-40], beta[25-35] and beta[31-35] on the steady-state intracellular Ca2+ concentration in primary cultures of rat astroglial cells using the Ca2+-sensitive fluorescent probe Fura-2 AM revealed higher 340/380 fluorescence excitation ratios in the treated cells as compared to the untreated controls. All the peptides were found to induce similar cellular effects, suggesting the [31-35] region as the putative active centre of the molecule. No significant alteration was detectable in Fura-2 fluorescence using the Ca2+-insensitive excitation wavelength of 367 nm, indicating that the observed changes reflect a real alteration in the Ca2+ concentration of the cells. Moreover, no considerable difference was observed in the total protein content of treated and untreated cells. Co-treatment of the cells with Pr-Ile-Ile-Gly-Leu-NH2 (Pr-IIGL) peptide, an analogue of the [31-34] region of beta[1-42]-amyloid, was found to effectively antagonize the beta[1-42]-amyloid-induced elevation of the fluorescence excitation ratio, leaving the 367-nm fluorescence unaffected. To the best of the authors' knowledge, this is the first report on an analogue of beta-amyloid peptide capable of blocking one of its physiological effects, thereby raising the possibility that this sequence could prove to be a lead compound for designing effective beta-amyloid antagonists. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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