Dec 10, 1998

Tau glycation is involved in aggregation of the protein but not in the formation of filaments

Cellular and Molecular Biology
M D LedesmaJ Avila

Abstract

A tau peptide, peptide 2R, with capacity for self assembly into filaments was used as a model to test the role of glycation on tau assembly or aggregation. Our results indicate that glycation of that peptide facilitates dimer formation but not assembly into filaments. However, glycation of tau results in the bundling of the tau filaments formed by glycosaminoglycan-induced polymerisation. These results suggest a role of glycation in the formation of covalent links among pre-formed filaments but not in the assembly of those filaments.

  • References
  • Citations

References

  • We're still populating references for this paper, please check back later.
  • References
  • Citations

Citations

  • This paper may not have been cited yet.

Mentioned in this Paper

Familial Alzheimer Disease (FAD)
Covalent Interaction
Glycosaminoglycans
Neurofibrillary Degeneration (Morphologic Abnormality)
Aggregation
Microtubules
Polymers
Electron Microscopy
Protein Glycosylation
Tau Proteins

About this Paper

Related Feeds

Alzheimer's Disease: Tau & TDP-43

Alzheimer's disease is a chronic neurodegenerative disease. This feed focuses on the underlying role of Tau proteins and TAR DNA-binding protein 43, as well as other genetic factors, in Alzheimer's.

Related Papers

Biochimica Et Biophysica Acta
I DalleDonneR Colombo
Current Biology : CB
K R Fath, D R Burgess
European Journal of Vascular and Endovascular Surgery : the Official Journal of the European Society for Vascular Surgery
W M P F BosmanM J Jacobs
© 2020 Meta ULC. All rights reserved