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Altered glycosylation of acetylcholinesterase in Creutzfeldt–Jakob disease
Author(s) -
Silveyra MaríaXimena,
CuadradoCorrales Natividad,
Marcos Alberto,
Barquero MaríaSagrario,
Rábano Alberto,
Calero Miguel,
SáezValero Javier
Publication year - 2006
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2005.03514.x
Subject(s) - acetylcholinesterase , glycosylation , aché , glycoprotein , alzheimer's disease , biology , enzyme , disease , biochemistry , medicine
Changes in the glycosylation pattern of brain proteins have been associated with Creutzfeldt–Jakob disease (CJD). We have investigated the glycosylation status of acetylcholinesterase (AChE) by lectin binding assay. Our data show that in lumbar CSF from definite and probable sporadic CJD cases AChE activity is lower compared with that in age‐matched controls. We also show, for the first time, that AChE glycosylation is altered in CJD CSF and brain. Unlike Alzheimer's disease, in which an alteration in both the glycosylation and levels of AChE molecular forms is observed, the abnormal glycosylation of AChE in CJD appears to be unrelated to changes in molecular forms of this enzyme. These findings suggest that altered AChE glycosylation in CJD may be a consequence of the general perturbation of the glycosylation machinery that affects prion protein, as well as other proteins. The diagnostic potential of these changes remains to be explored.