Amyloid-beta peptide binds to microtubule-associated protein 1B (MAP1B)
Por:
Gevorkian G., Gonzalez-Noriega A., Acero G., Ordonez, J, Michalak C., Munguia M.E., Govezensky T., Cribbs D.H., Manoutcharian K.
Publicada:
1 may 2008
Resumen:
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. (C) 2007 Elsevier Ltd. All rights reserved.
Filiaciones:
Gevorkian G.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Gonzalez-Noriega A.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Acero G.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Ordonez, J:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Michalak C.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Munguia M.E.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Govezensky T.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
Cribbs D.H.:
The Institute for Brain Aging and Dementia, Irvine, CA 92697-4540, United States
Department of Neurology, University of California Irvine, Irvine, CA 92697-4540, United States
Manoutcharian K.:
Univ Nacl Autonoma Mexico, Inst Invest Biomed, Mexico City 04510, DF, Mexico
All Open Access; Green
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