Molecular and Chemical Neuropathology

, Volume 27, Issue 3, pp 249–258

The in vitro formation of recombinant τ polymers

Effect of phosphorylation and glycation
  • Maria Dolores Ledesma
  • Miguel Medina
  • Jesus Avila
Original Articles

DOI: 10.1007/BF02815107

Cite this article as:
Ledesma, M.D., Medina, M. & Avila, J. Molecular and Chemical Neuropathology (1996) 27: 249. doi:10.1007/BF02815107

Abstract

τ Isolated from paired helical filaments, aberrant structures that appear in Alzheimer disease (AD) patients’ brains, show at least two posttranslational modifications: phosphorylation (Grundke-Iqbal et al., 1986; Ihara et al., 1986) and glycation (Ledesma et al., 1994; Yan et al., 1994). To test whether these modifications could affect the capacity of τ to self-aggregate, recombinant τ was phosphorylated and glycated, and its capacity to form polymers analyzed. Our results indicate that on phosphorylation and glycation, the capacity of τ to form aggregates increases, and that glycation of τ could stabilize the assembled polymers and could facilitate formation of bundles from these polymers.

Index Entries

Alzheimer disease τ protein paired helical filaments phosphorylation glycation aggregation 

Copyright information

© Humana Press Inc 1996

Authors and Affiliations

  • Maria Dolores Ledesma
    • 1
  • Miguel Medina
    • 1
  • Jesus Avila
    • 1
  1. 1.Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM)Universidad Autónoma de MadridMadridSpain