Altered glycosylation pattern of proteins in Alzheimer disease

J Neuropathol Exp Neurol. 1998 Oct;57(10):905-14. doi: 10.1097/00005072-199810000-00003.


Post-translational modifications due to glycosylation of proteins in human brains from patients with Alzheimer disease (AD) were analyzed using lectin histochemistry. Results indicate a significant increase in the production of O-glycosylated (containing Galbeta1,3GalNAc alpha1,0 Ser/Thr or GalNAc alpha1,0 Ser/Thr) proteins in neuritic plaques and neurofibrillary tangles which are the major histopathological hallmarks of AD brains. These alterations were determined by positive labelling with lectins obtained from Amaranthus leucocarpus (ALL) and Macrobrachium rosenbergii (MRL) respectively. Immunohistochemistry indicated that the lectin-staining labelled specifically both neurofibrillary tangles and neuritic plaques. In contrast, lectins labelling was restricted to microvessels in normal control brains. These results provide evidence that modifications of the specific glycosylation patterns are closely related with the presence of the hallmark lesions of this disease, suggesting that an abnormal enzymatic processing of proteins may be an early event in the neuronal degeneration which characterises AD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Alzheimer Disease / metabolism*
  • Amyloid beta-Peptides / metabolism
  • Biotin
  • Glycosylation
  • Hippocampus / blood supply
  • Hippocampus / metabolism
  • Hippocampus / pathology
  • Histocytochemistry
  • Humans
  • Lectins
  • Microcirculation
  • Microscopy, Confocal
  • Middle Aged
  • Nerve Tissue Proteins / metabolism*
  • Neurofibrillary Tangles / metabolism
  • Neurofibrillary Tangles / pathology
  • Plaque, Amyloid / metabolism
  • Plaque, Amyloid / pathology
  • tau Proteins / metabolism


  • Amyloid beta-Peptides
  • Lectins
  • Nerve Tissue Proteins
  • tau Proteins
  • Biotin