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β ‐amyloid decreases detectable endothelial nitric oxide synthase in human erythrocytes: a role for membrane acetylcholinesterase
Author(s) -
Misiti Francesco,
CarelliAlinovi Cristiana,
Sampaolese Beatrice,
Giardina Bruno
Publication year - 2012
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.2822
Subject(s) - enos , acetylcholinesterase , nitric oxide synthase , nitric oxide , red blood cell , medicine , biology , biochemistry , endocrinology , amyloid beta , chemistry , microbiology and biotechnology , enzyme , peptide
Until few years ago, many studies of Alzheimer's disease investigated the effects of this syndrome in the central nervous system. Only recently, the detection of amyloid beta peptide (A β ) in the blood has evidenced the necessity to extend studies on extraneuronal cells, particularly on erythrocytes. A β is also present in brain capillaries, where it interacts with the erythrocytes, inducing several metabolic and functional alterations. Recently, functionally active endothelial type nitric oxide synthase (eNOS) was discovered in human erythrocytes. The goal of the present study was to evidence the effect of A β on erythrocyte eNOS. We found that A β following to 24‐h exposure causes a decrease in the immune staining of erythrocyte eNOS. Concurrently, A β alters erythrocyte cell morphology, decreases nitrites and nitrates levels, and affects membrane acetylcholinesterase activity. Propidium, an acetylcholinesterase inhibitor, was able to reverse the effects elicited by A β . These events could contribute to the vascular alterations associated with Alzheimer's disease disease. Copyright © 2012 John Wiley & Sons, Ltd.