Altered glycosylation pattern of proteins in Alzheimer disease
Por:
Guevara J., Espinosa B., Zenteno E., Vázquez L., Luna J., Perry G., Mena R.
Publicada:
1 ene 1998
Resumen:
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 Ga1?1,3GaINAc? 1,0 Ser/Thr or GalNAc? 1,0 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.
Filiaciones:
Guevara J.:
Program of Molecular Biomedicine, CINVESTAV, México, Mexico
Espinosa B.:
Department of Biochemistry, INER, México, Mexico
Zenteno E.:
Department of Biochemistry, Faculty of Medicine, UNAM, México, Mexico
Vázquez L.:
Lectins Laboratory, UAEM, Cuernavaca, Morelos, Mexico
Luna J.:
Dept. Physiol., Biophys. Neurosci., CINVESTAV, México, Mexico
Perry G.:
Institute of Pathology, Case Western Reserve University, Cleveland, OH, United States
Mena R.:
Dept. Physiol., Biophys. Neurosci., CINVESTAV, México, Mexico
Dept. of Physiol. and Neurosciences, CINVESTAV-IPN, PO. Box 14-740, 07000, México D.F., Mexico
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