The VU University Medical Centre and Lund University have presented a joint poster entitled 'AB1-42 binding and uptake by primary human astrocytes in vitro: Effects of a1-Antichymotrypsin.'
The AB1-42 peptides that were a key ingredient in the research were supplied by Anaspec.
The background of the research presentation noted that imbalance between the production and clearance of the amyloid B-peptide (AB) is a key event in the Alzheimer's disease (AD) pathogenesis.
Alpha1-antichymotrypsin (ACT) might influence the AB fibrillogenesis biological effects and clearance leading to enhanced AB deposition in the brain.
Activated astrocytes are found surrounding amyloid plaques in AD brains but their role in AD pathogenesis is still poorly understood.
These reactive cells over-express ACT and are able to release pro-inflammatory mediators.
Recent evidence also suggests that rodent astrocytes may internalise and degrade extracellular AB.
Whether human primary astrocytes are capable of degrading AB1-42 is still to be determined.
The authors presented the following conclusions: primary human astrocytes are, during cytotoxic conditions, able to bind and take up AB1-42 in vitro, without a proinflammatory response; human adult astrocytes derived from non-AD and AD subjects become AB1-42 positive upon exposure, whereas a greater percentage of human foetal astrocytes become AB1-42 positive upon 1mM and 10mM o/n treatment with AB1-42; ACT has no or little effect on AB1-42 uptake by adult astrocytes, whereas the uptake by foetal cells might be enhanced; enhanced MCP-1 release upon AB/ACT co-treatment versus AB alone in adult astrocytes might be mediated by ACT itself.
The authors of the study were HM Nielsen, S Janciauskiene, B Holmqvist, and R Veerhuis.
