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(American Journal of Pathology. 2001;158:1585-1591.)
© 2001 American Society for Investigative Pathology

Short Communications

FE65 in Alzheimer’s Disease

Neuronal Distribution and Association with Neurofibrillary Tangles

Benoît Delatour^*, Luc Mercken, Khalid H. El Hachimi, Marie-Anne Colle^*, Laurent Pradier and Charles Duyckaerts^*

From the Laboratoire de Neuropathologie Escourolle,^*
Inserm U106, Université Paris VI, Paris; the Neurodegenerative Disease Group,
Aventis Pharma, Paris; and Ecole Pratique des Hautes Etudes,
Inserm U106, Paris, France

FE65, a protein expressed in the nervous system, has the ability to bind the C-terminal domain of the amyloid precursor protein. This suggests a role for FE65 in the pathogenesis of Alzheimer’s disease (AD). The present study was conducted to find out if the distribution of FE65 immunoreactivity was affected during the course of AD, and to determine the degree of co-localization of FE65 with other proteins known to be involved in AD. Single immunoperoxidase-labeling experiments, conducted on six sporadic AD patients and six nondemented age-matched controls, showed that the proportion of volume occupied by FE65 immunoreactivity was not modified in the isocortex of AD patients. However, in hippocampal area CA4, increased FE65 immunoreactivity seemed to be associated with the severity of the disease. Double-immunofluorescent labeling did not show any clear co-localization of FE65 with the amyloid precursor protein. FE65 immunoreactivity was also absent from focal and diffuse deposits of the ß-amyloid peptide. Unexpectedly double labeling experiments showed a co-localization of FE65 and tau proteins in intracellular tangles. Ultrastructural observations confirmed that FE65 was associated with paired helical filaments.

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