Affiliations: [a] Department of Human Sciences, Society and Health, University of Cassino and Southern Latium, V. S. Angelo Th., Polo Didattico della Folcara, Cassino (FR), Italy
| [b] Institute of Biochemistry and Clinical Biochemistry, Catholic University, School of Medicine, Rome, Italy
| [c]
Institute for the Structure of the Matter (ISM), National Research Council (CNR), Rome, Italy
Correspondence:
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Corresponding author: Prof. Francesco Misiti, Department of Human Sciences, Society and Health University of Cassino and Southern Lazio V. S.Angelo-Polo didattico della Folcara Cassino (FR) 03043, Italy. Tel.: +39 7762994423; E-mail: f.misiti@unicas.it.
Abstract: Our attention is focused on the study of a new model based on the red blood cell (RBC) and on its interaction with amyloid beta peptide 1-42 (Aβ). RBC are highly deformable to assist blood flow in the microcirculation. For this reasons RBC abnormalities could contribute to Alzheimer’s disease (AD) by obstructing oxygen delivery to brain, causing hypoxia. In our work, considering that RBC membrane contains, among blood elements, higher acetylcholinesterase (AChE) levels, we can assume that in blood occurs a mechanism similar to the one which occurs at the neuronal level leading to an increase of Aβ toxicity mediated by its binding with AChE, located on the RBC external face. Furthermore, since mechanical properties of RBC membrane are regulated by a number of molecular components of signalling and/or regulatory pathways, of these, particular interest has been addressed toward Nitric Oxide (NO) metabolism, due to its dependence to AChE.
Keywords: Amyloid beta peptide, red blood cell, nitric oxide synthase, acetylcholinesterase, NO metabolites, Alzheimer disease
