{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T13:46:15Z","timestamp":1791121575645,"version":"4.1.0"},"reference-count":42,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2006,10,9]],"date-time":"2006-10-09T00:00:00Z","timestamp":1160352000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Clin Investigation"],"published-print":{"date-parts":[[2006,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:bold>Background\u2002<\/jats:bold> Alzheimer's disease (AD) is an age\u2010related neurodegenerative disorder that is characterized by a progressive loss of higher cognitive functions. The brain of an individual with AD exhibits extracellular senile plaques (SPs) of aggregated amyloid\u2010beta peptide (A\u03b2) and intracellular neurofibrillary tangles (NFTs). Given the critical role of neuronal transport of both proteins and organelles, it is not surprising that perturbation of microtubule\u2010based transport may play a major role in the pathogenesis of AD.<\/jats:p><jats:p><jats:bold>Materials and methods\u2002<\/jats:bold> We used the cDNA subtraction methodology and <jats:italic>in vitro<\/jats:italic> neural cell culture analyses to study the meaning of the brain site\u2010specific gene expression pattern in cerebral tissue obtained from AD patients and also from control subjects at autopsy.<\/jats:p><jats:p><jats:bold>Results\u2002<\/jats:bold> We observed that cytoskeleton\u2010associated proteins were down\u2010regulated in AD subjects. We also noted an altered expression of the microtubule\u2010associated protein 1B (MAP1B), the heat\u2010shock protein (HSP)\u201090 (a key chaperone molecule), the tripartite motif\u2010containing proteins (TRIM)\u201032\/37 (an anti apoptotic enzyme with ubiquitin\u2010protein ligase activity) and the Reticulon\u20103 (a modulator of the amyloid\u2010precursor\u2010protein (APP) cleavage) in AD brains. Additional molecular\u2010 and cell\u2010biological studies revealed that small interfering RNA (siRNA)\u2010mediated down\u2010regulation of MAP1B expression leads to neuronal cell death <jats:italic>in vitro<\/jats:italic>.<\/jats:p><jats:p><jats:bold>Conclusion\u2002<\/jats:bold> Altered expression of MAP1B, HSP90, TRIM32\/37 and Reticulon\u20103 provides new clues by which the ubiquitin\u2010proteasome\u2010, the protein\u2010chaperon\u2010 and the APP\u2010processing systems are disturbed in AD, thus, leading to neuritic amyloid plaques and neurofibrillary tangles.<\/jats:p>","DOI":"10.1111\/j.1365-2362.2006.01722.x","type":"journal-article","created":{"date-parts":[[2006,10,9]],"date-time":"2006-10-09T16:52:36Z","timestamp":1160412756000},"page":"820-830","source":"Crossref","is-referenced-by-count":82,"title":["Brain site\u2010specific gene expression analysis in Alzheimer's disease 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