0000000000607540
AUTHOR
R Carrotta
CONCANAVALIN A AGGREGATION AND TOXICITY ON NEUROBLASTOMA LAN5 CELL CULTURES
Amyloid beta-peptide aggregation and interaction with yeast cells membranes
Protein misfolding, aggregation and conversation...
Naïve Hsp60, similarly to GroEL, oligomerizes to build heptameric and tetradecameric structures.
Insulin activated Akt rescues Aβ oxidative stress-induced cell death by orchestrating molecular trafficking.
Increasing evidence indicates that Alzheimer's disease, one of the most diffused aging pathologies, and diabetes may be related. Here, we demonstrate that insulin signalling protects LAN5 cells by amyloid-β42 (Aβ)-induced toxicity. Aβ affects both activation of insulin receptors and the levels of phospho-Akt, a critical signalling molecule in this pathway. In contrast, oxidative stress induced by Aβ can be antagonized by active Akt that, in turn, inhibits Foxo3a, a pro-apoptotic transcription factor activated by reactive oxygen species generation. Insulin cascade protects against mitochondrial damage caused by Aβ treatment, restoring the mitochondrial membrane potential. Moreover, we show t…
Entrapment of Aβ(1-40) peptide in unstructured aggregates
Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…