PMID: 8947944Nov 1, 1996Paper

Aluminum-sensitive degradation of amyloid beta-protein 1-40 by murine and human intracellular enzymes

Neurotoxicology and Teratology
W A BanksA J Kastin

Abstract

Both amyloid beta protein (A beta) and aluminum (A1) have been implicated in Alzheimer's disease. Recently, A beta has been found to be produced by peripheral tissues as well as by the CNS and to cross and accumulate in the vascular bed of the brain, which comprises the blood-brain barrier (BBB). This raises the possibility that blood-borne A beta may be a source of A beta within the CNS. Al has been shown to alter the structure and function of A beta, to inhibit the class of enzymes (metalloproteases) associated with the processing and degradation of A beta, and to alter the permeability of the BBB to peptides of similar size to A beta. Therefore, Al could alter the access of blood-borne A beta to the CNS either by changing the permeability of the BBB or by affecting enzymatic degradation. We examined the effect of Al on both of these parameters and found that Al did not alter the permeability of the BBB to A beta radioactively labeled with 125I (I-A beta) ever after correction for in vivo degradation. However, Al did enhance clearance and degradation of I-A beta in the circulation but not in the brain. Alterations in clearance can indirectly affect the CNS accumulation of circulating substances by modifying their presentation...Continue Reading

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Citations

Mar 4, 2000·The Journal of Comparative Neurology·M Salvador-SilvaM P Villegas-Pérez
Nov 20, 1998·Journal of Neuroscience Research·V R LombardiR Cacabelos
Jul 12, 2002·Journal of Neuroscience Research·Jeffrey D SorbelDiana I Lurie
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Jan 21, 2006·Life Sciences·Eva Stefanovits-BányaiAnna Blázovics
Jun 22, 1999·The Journal of Biological Chemistry·R YaminC R Abraham

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