The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Alzheimer's β-Amyloid, Human Islet Amylin, and Prion Protein Fragment Evoke Intracellular Free Calcium Elevations by a Common Mechanism in a Hypothalamic GnRH Neuronal Cell Line
Open accessAbstract
A growing number of reports suggest that elevated levels of extracellular Alzheimer's beta-amyloid protein alter the homeostasis of free [Ca(2+)](i) in different cell types of the mammalian brain. In line with these results, we have previously shown that AbetaP[1-40] forms cation-selective channels (Ca(2+) included) across artificial planar bilayers formed from acidic phospholipids and across excised membrane patches from immortalized hypothalamic GnRH neurons (GT1-7 cells), suggesting that the nonregulated Ca(2+)-influx through these spontaneously formed "amyloid channels" may provide a mechanism to explain its toxicity (1). We have now found and report here that the application of AbetaP[1-40] to GT1-7 neurons consistently elevates [Ca(2+)](i) levels. We also found that human islet amylin and the prion protein fragment (PrP106-126), peptides that acquire beta-pleated sheet conformation in water solutions and have been reported to form ion channels across planar bilayer membranes, also increase cytosolic free calcium in GT1-7 neurons. Searching for protective agents, we found that soluble cholesterol, known to decrease the fluidity of the cell membrane, inhibits AbetaP[1-40]-evoked [Ca(2+)](i) rise. These results suggest that unregulated Ca(2+) entry across amyloid channels may be a common mechanism causing cell death, not only in diseases of the third age, including Alzheimer's disease and type 2 diabetes mellitus, but also in prion-induced diseases.
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Cites
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Scrapie prions aggregate to form amyloid-like birefringent rods
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Cited by
Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044
Different Species of α-Synuclein Oligomers Induce Calcium Influx and Seeding
Danzer, K. M., Haasen, D., Karow, A. R., Moussaud, S., Habeck, M., Giese, A., Kretzschmar, H., Hengerer, B., & Kostka, M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.2617-07.2007 · Cited by 765
Curtain, C. C., Ali, F., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 649
Amylin deposition in the brain: A second amyloid in Alzheimer disease?
Jackson, K., Barisone, G. A., Diaz, E., Jin, L., DeCarli, C., & Despa, F. (2013) · Annals of Neurology · doi:10.1002/ana.23956 · Cited by 340
Getting to the Heart of Alzheimer Disease
Tublin, J. M., Adelstein, J. M., del Monte, F., Combs, C. K., & Wold, L. E. (2019) · Circulation Research · doi:10.1161/circresaha.118.313563 · Cited by 188
Metadata
- Authors
- Kawahara, M., Kuroda, Y., Arispe, N., & Rojas, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 19
- Pages
- 14077-14083
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2098576607
- Cited by
- 294
- References
- 38
- FWCI
- 10.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Alzheimer's β-Amyloid, Human Islet Amylin, and Prion Protein Fragment Evoke Intracellular Free Calcium Elevations by a Common Mechanism in a Hypothalamic GnRH Neuronal Cell Line. https://app.cochat.ai/papers/10.1074/jbc.275.19.14077
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- Kawahara, M., Kuroda, Y., Arispe, N., & Rojas, E. (2000). Alzheimer's β-Amyloid, Human Islet Amylin, and Prion Protein Fragment Evoke Intracellular Free Calcium Elevations by a Common Mechanism in a Hypothalamic GnRH Neuronal Cell Line. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.19.14077
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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