| Literature DB >> 18079022 |
Goar Gevorkian1, Alfonso Gonzalez-Noriega, Gonzalo Acero, Jorge Ordoñez, Colette Michalak, Maria Elena Munguia, Tzipe Govezensky, David H Cribbs, Karen Manoutcharian.
Abstract
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.Entities:
Mesh：
Substances：
Year: 2007 PMID： 18079022 PMCID： PMC2390996 DOI： 10.1016/j.neuint.2007.10.020
Source DB: PubMed Journal: Neurochem Int ISSN： 0197-0186 Impact factor: 3.921