VEGF controls microglial phagocytic response to amyloid-β.

Microglial cells are well known to be implicated in the pathogenesis of Alzheimer's disease (AD), due to the impaired clearance of amyloid-β (Aβ) protein. In AD, Aβ accumulates in the brain parenchyma as soluble oligomers and protofibrils, and its aggregation process further give rise to amyloid plaques. Compelling evidence now indicate that Aβ oligomers (Aβo) are the most toxic forms responsible for neuronal and synaptic alterations.

A novel peptide derived from vascular endothelial growth factor prevents amyloid beta aggregation and toxicity.

Amyloid-β oligomers (Aβo) are the most pathologically relevant Aβ species in Alzheimer's disease (AD), because they induce early synaptic dysfunction that leads to learning and memory impairments. In contrast, increasing VEGF (Vascular Endothelial Growth Factor) brain levels have been shown to improve learning and memory processes, and to alleviate Aβ-mediated synapse dysfunction. Here, we designed a new peptide, the blocking peptide (BP), which is derived from an Aβo-targeted domain of the VEGF protein, and investigated its effect on Aβ-associated toxicity.

Effect of the hydration status of the smear layer on the wettability and bond strength of a self-etching primer to dentin.

Purpose: To evaluate the microtensile bond strength (MTBS) of a resin-based composite to smear layer-covered dentin using a self-etching primer, Clearfil SE Bond (CSEB), under two different hydration states. Surface roughness and wettability (contact angle measurements) of water and the CSEB primer were also evaluated on this substrate.

Methods: Contact angle (CA) measurements were performed on four caries-free extracted human third molars.