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The present study examines by immunohistochemistry Dpl expression in brain samples from 10 patients with Alzheimer's disease (AD), three patients with Pick's disease, four patients with Parkinson's disease, eight patients with diffuse Lewy body disease (DLBD), six patients with sporadic Creutzfeldt\u2013Jakob disease (CJD) methionine\/methionine at the codon 129, two patients with sporadic CJD methionine\/valine at the codon 129 and numerous kuru plaques in the cerebellum, one patient with fatal familial insomnia (FFI), and 10 age\u2010matched controls. In the adult human brain, Dpl immunoreactivity was restricted to scattered granule cells of the cerebellum and scattered small granules in the cerebral cortex. Dpl immunoreactivity was seen around \u03b2A4 amyloid deposits in neuritic plaques, but not in diffuse plaques, AD and the common form of DLBD. Neurofibrillary tangles, Pick bodies and Lewy bodies were not stained with anti\u2010Dpl antibodies. No modifications in Dpl immunoreactivity were observed in CJD excepting those associated with accompanying senile plaques. No Dpl\u2010positive deposits were seen in FFI. Whether Dpl in neuritic plaques may attenuate amyloid\u2010induced oxidative stress and participate in the glial response around amyloid cores is discussed in light of the few available data on Dpl functions.<\/jats:p>","DOI":"10.1111\/j.1365-2990.2003.00534.x","type":"journal-article","created":{"date-parts":[[2004,12,27]],"date-time":"2004-12-27T18:02:32Z","timestamp":1104170552000},"page":"329-337","source":"Crossref","is-referenced-by-count":10,"title":["Selective PrP\u2010like protein, doppel immunoreactivity in dystrophic neurites of senile plaques in Alzheimer's disease"],"prefix":"10.1111","volume":"30","author":[{"given":"I.","family":"Ferrer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Freixas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Blanco","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Carmona","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B.","family":"Puig","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2,6]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0002-9440(10)64782-7"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1999.3108"},{"key":"e_1_2_6_4_2","doi-asserted-by":"crossref","first-page":"26834","DOI":"10.1016\/S0021-9258(19)61451-1","article-title":"Doppel is an N\u2010glycosylated, glycosylphosphophatidylinositol\u2010anchored protein. 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