Amyloid-β peptide binds to microtubule-associated protein 1B (MAP1B)

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• 作者：Goar Gevorkian ; Alfonso Gonzalez-Noriega ; Gonzalo Acero ; Jorge Ordoñ ; ez ; Colette Michalak ; Maria Elena Munguia ; Tzipe Govezensky ; David H. Cribbs ; Karen Manoutcharian
• 关键词：Amyloid-beta peptide ; Phage displayed cDNA library ; Microtubule-associated protein 1B (MAP1B)
• 刊名：Neurochemistry International
• 出版年：2008
• 出版时间：May 2008
• 年：2008
• 卷：52
• 期：6
• 页码：1030-1036
• 全文大小：439 K

文摘

Extracellular and intraneuronal formation of amyloid-beta aggregates have been demonstrated to be involved in the pathogenesis of Alzheimer's disease. However, the precise mechanism of amyloid-beta neurotoxicity is not completely understood. Previous studies suggest that binding of amyloid-beta to a number of targets have deleterious effects on cellular functions. In the present study we have shown for the first time that amyloid-beta 1–42 bound to a peptide comprising the microtubule binding domain of the heavy chain of microtubule-associated protein 1B by the screening of a human brain cDNA library expressed on M13 phage. This interaction may explain, in part, the loss of neuronal cytoskeletal integrity, impairment of microtubule-dependent transport and synaptic dysfunction observed previously in Alzheimer's disease.