Several therapies for Alzheimer's Disease (AD) are currently under investigation. Some studies have reported that concentration of vitamins in biological fluids are lower in AD patients compared to control subjects and clinical evidence has shown the therapeutic potential of vitamin C and E in delaying AD progression. However, the molecular mechanism(s) that are engaged upon their administration in the APP metabolism in vitro or in vivo still need clarifying. Here, we investigate the effects of vitamin C supplementation, at physiological concentration, in skin fibroblasts obtained from SAD and FAD patients. This study shows that SAD patients' fibroblasts exhibited the exclusive appearance of C-terminal fragments, derived from APP processing, without giving rise to the beta-amyloid peptide, other than corresponding decreased levels of lysosomal enzymes, such as beta-hexosaminidase, alpha-mannosidase and cathepsins B, L, and D.
Costanzi, E., Martino, S., Persichetti, E., Tiribuzi, R., Massini, C., Bernardi, G., et al. (2008). Effects of Vitamin C on Fibroblasts from Sporadic Alzheimer’s Disease Patients. NEUROCHEMICAL RESEARCH, 33(12), 2510-2515 [10.1007/s11064-007-9539-y].
Effects of Vitamin C on Fibroblasts from Sporadic Alzheimer’s Disease Patients
BERNARDI, GIORGIO;ORLACCHIO, ANTONIO;
2008-12-01
Abstract
Several therapies for Alzheimer's Disease (AD) are currently under investigation. Some studies have reported that concentration of vitamins in biological fluids are lower in AD patients compared to control subjects and clinical evidence has shown the therapeutic potential of vitamin C and E in delaying AD progression. However, the molecular mechanism(s) that are engaged upon their administration in the APP metabolism in vitro or in vivo still need clarifying. Here, we investigate the effects of vitamin C supplementation, at physiological concentration, in skin fibroblasts obtained from SAD and FAD patients. This study shows that SAD patients' fibroblasts exhibited the exclusive appearance of C-terminal fragments, derived from APP processing, without giving rise to the beta-amyloid peptide, other than corresponding decreased levels of lysosomal enzymes, such as beta-hexosaminidase, alpha-mannosidase and cathepsins B, L, and D.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
