AnaSpec Peptides Used in Latest Alzheimer’s Research Findings by VU University Medical Centre and Lund University

At the 2008 International Conference for Alzheimer’s Disease, the VU University Medical Centre and Lund University presented a joint poster entitled, “Aβ1-42 binding and uptake by primary human astrocytes in vitro: Effects of a1-Antichymotrypsin.” The authors of the study were H. M Nielsen, S. Janciauskiene, B. Holmqvist, and R. Veerhuis. The Aβ1-42 peptides that were a key ingredient in the research were supplied by AnaSpec, Inc.

The background of the research presentation noted that imbalance between the production and clearance of the amyloid β-peptide (Aβ) is a key event in the Alzheimer’s disease (AD) pathogenesis. Alpha1-antichymotrypsin (ACT) might influence the Aβ fibrillogenesis biological effects and clearance leading to enhanced Aβ 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 internalize and degrade extracellular Aβ. If also human primary astrocytes are capable of degrading Aβ 1-42, is still to be determined.

The authors presented the following conclusions:

• Primary human astrocytes are, during cytotoxic conditions, able to bind and take up Aβ1-42 in vitro, without a pro-inflammatory response
• Human adult astrocytes derived from non-AD and AD subjects become Aβ1-42 positive upon exposure, in a similar manner, whereas a greater percentage of human fetal astrocytes become Aβ1-42 positive upon 1 mM and 10 mM o/n treatment with Aβ1-42
• ACT has no or little effect on Aβ1-42 uptake by adult astrocytes whereas the uptake by fetal cells might be enhanced
• Enhanced MCP-1 release upon Aβ/ACT co-treatment versus Aβ alone in adult astrocytes, might be mediated by ACT itself