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Altered glycosylation pattern of proteins in Alzheimer disease.
- Source :
-
Journal of neuropathology and experimental neurology [J Neuropathol Exp Neurol] 1998 Oct; Vol. 57 (10), pp. 905-14. - Publication Year :
- 1998
-
Abstract
- 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.
- Subjects :
- Aged
Amyloid beta-Peptides metabolism
Biotin
Glycosylation
Hippocampus blood supply
Hippocampus metabolism
Hippocampus pathology
Histocytochemistry
Humans
Lectins
Microcirculation
Microscopy, Confocal
Middle Aged
Neurofibrillary Tangles metabolism
Neurofibrillary Tangles pathology
Plaque, Amyloid metabolism
Plaque, Amyloid pathology
tau Proteins metabolism
Alzheimer Disease metabolism
Nerve Tissue Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-3069
- Volume :
- 57
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Journal of neuropathology and experimental neurology
- Publication Type :
- Academic Journal
- Accession number :
- 9786241
- Full Text :
- https://doi.org/10.1097/00005072-199810000-00003