Alzheimer’s Disease (AD) is a chronic neurodegenerative disease commonly characterized by the aggregation and deposition of insoluble amyloid beta plaques throughout the brain, and by an associated neuroinflammatory response to these plaques involving astrocytes and microglia. Choline is an essential nutrient with diverse functional roles that has emerged as a promising candidate for the treatment of AD. Localized plaque regions in the polymorphic layer in the medial dentate gyrus of the hippocampus and in the cortex were examined in 9-month-old APP-NL-G-F knock-in AD model mice to determine the effects of perinatal choline supplementation on astrocytosis and gliosis associated with amyloid beta. The size of ionized calcium-binding adaptor molecule 1 (Iba1)-positive cells and clusters were larger in control diet APPNL-G-F mice, although the number and total area covered by Iba1+ cells/clusters were decreased compared to those of control diet C57BL6/J mice. In comparison, choline supplementation significantly reduced the size of Iba1+ cells/clusters in APPNL-G-F mice. These results suggest that perinatal choline supplementation ameliorates neuroinflammatory processes associated with amyloid plaques in these 9-month-old APPNL-G-F mice, and that dietary supplementation of choline might serve as an effective treatment for AD. / 2026-02-14T00:00:00Z

One of the most prevalent diseases acquired in older populations and currently the most common form of dementia, exists in the form of Alzheimer's [1]. Progressing over time, Alzheimer's begins intramolecularly through the buildup of amyloid precursor protein derived Aβ peptides which aggregate into neurotoxic fibrils. The fibrils result in damage to memory and cognitive systems, leading to depression of routine function and eventual death. There is currently no cure nor treatment by which this plaque buildup can be prevented or eliminated, and as such, significant work is being made towards this topic. It has been recently discovered that the human matriptase protein is capable of cleaving both the amyloid precursor protein from which Aβ peptides are made as well as the Aβ1-42 peptide itself, facilitating interest into its potential to reduce fibril formation [2][3]. In this study we set out to determine if the human matriptase serine protease domain can cleave Aβ fibrils or prevent the Aβ fibril formation in vitro. A recombinant matriptase serine protease domain (r-MatPD) was subcloned into a pET-28a-c(+) expressing vector, expressed, and purified via Ni-NTA affinity resin. The purified his-tagged r-MatPD was further auto-activated and incubated with the purified recombinant Aβ1-42 peptides. We observed that r-MatPD can cut polymerized Aβ1-42 into smaller fragments and prevent Aβ1-42 fibril formation. Effectively, this study suggested that the matriptase protease domain can be further investigated for its role in Aβ fibril clearance in vivo with a possibility of developing matriptase therapeutic potentials in treating Alzheimer's patients.

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