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

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Summary

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.Recent evidence also suggests that rodent astrocytes may internalize and degrade extracellular Aβ.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 About VU University Medical Centre The VU university medical centre has defined a number of clusters of research interest and patiënt care.With a vision for innovation through synergy, AnaSpec offers expertise in three primary technologies: peptides, detection reagents, and combinatorial chemistry.### San Jose, CA, August 31, 2008 --( PR.com )-- 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.

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