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Alterations in the ryanodine receptor calcium release channel correlate with Alzheimer's disease neurofibrillary and β-amyloid pathologies

Kelliher, M., Fastbom, J., Cowburn, R.F., Bonkale, W., Ohm, T.G., Ravid, R., Sorrentino, V., O'Neill, C.·1999·Neuroscience
DOI 10.1016/s0306-4522(99)00042-1
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Abstract

Investigation of the integrity of the ryanodine receptor in Alzheimer's disease is important because it plays a critical role in the regulation of calcium release from the endoplasmic reticulum in brain, impairment of which is believed to contribute to the pathogenesis of Alzheimer's disease. The present study compared ryanodine receptor levels and their functional modulation in particulate fractions from control and Alzheimer's disease temporal cortex, occipital cortex and putamen. Relationships between ryanodine receptor changes and the progression of Alzheimer's disease pathology were determined by examining autoradiographic [3H]ryanodine binding in entorhinal cortex/anterior hippocampus sections from 22 cases that had been staged for neurofibrillary changes and beta-amyloid deposition. A significant (P < 0.02) 40% decrease in the Bmax for [3H]ryanodine binding and significantly higher IC50 values for both magnesium and Ruthenium Red inhibition of [3H]ryanodine binding were detected in Alzheimer's disease temporal cortex particulate fractions compared to controls. Immunoblot analyses showed Type 2 ryanodine receptor holoprotein levels to be decreased by 20% (P < 0.05) in these Alzheimer's disease cases compared to controls. No significant differences were detected in [3H]ryanodine binding comparing control and Alzheimer's disease occipital cortex or putamen samples. The autoradiography study detected increased [3H]ryanodine binding in the subiculum, CA2 and CA1 regions in…

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Metadata

Authors
Kelliher, M., Fastbom, J., Cowburn, R. F., Bonkale, W., Ohm, T. G., Ravid, R., Sorrentino, V., & O'Neill, C.
Venue
Neuroscience
Publisher
Elsevier BV
Published
1999-05
Volume
92
Issue
2
Pages
499-513
ISSN
0306-4522
DOI
10.1016/s0306-4522(99)00042-1
Cited by
129
References
4
Language
en
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