16234245

Source:http://linkedlifedata.com/resource/pubmed/id/16234245

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0002716, umls-concept:C0006784, umls-concept:C0026045, umls-concept:C0162638, umls-concept:C0291573, umls-concept:C0521390, umls-concept:C0597304, umls-concept:C1314939, umls-concept:C1417003, umls-concept:C1417004, umls-concept:C1417006, umls-concept:C1749467
pubmed:issue	1
pubmed:dateCreated	2006-1-12
pubmed:abstractText	A growing body of evidence supports the notion that soluble oligomeric forms of the amyloid beta-peptide (Abeta) may be the proximate effectors of neuronal injuries and death in the early stages of Alzheimer disease. However, the molecular mechanisms associated with neuronal apoptosis induced by soluble Abeta remain to be elucidated. We recently demonstrated the involvement of an early reactive oxygen species-dependent perturbation of the microtubule network (Sponne, I., Fifre, A., Drouet, B., Klein, C., Koziel, V., Pincon-Raymond, M., Olivier, J.-L., Chambaz, J., and Pillot, T. (2003) J. Biol. Chem. 278, 3437-3445). Because microtubule-associated proteins (MAPs) are responsible for the polymerization, stabilization, and dynamics of the microtubule network, we investigated whether MAPs might represent the intracellular targets that would enable us to explain the microtubule perturbation involved in soluble Abeta-mediated neuronal apoptosis. The data presented here show that soluble Abeta oligomers induce a time-dependent degradation of MAP1A, MAP1B, and MAP2 involving a perturbation of Ca2+ homeostasis with subsequent calpain activation that, on its own, is sufficient to induce the proteolysis of isoforms MAP2a, MAP2b, and MAP2c. In contrast, MAP1A and MAP1B sequential proteolysis results from the Abeta-mediated activation of caspase-3 and calpain. The prevention of MAP1A, MAP1B, and MAP2 proteolysis by antioxidants highlights the early reactive oxygen species generation in the perturbation of the microtubule network induced by soluble Abeta. These data clearly demonstrate the impact of cytoskeletal perturbations on soluble Abeta-mediated cell death and support the notion of microtubule-stabilizing agents as effective Alzheimer disease drugs.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calpain, http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Casp9 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3, http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9, http://linkedlifedata.com/resource/pubmed/chemical/Caspases, http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mtap2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-40), http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (1-42), http://linkedlifedata.com/resource/pubmed/chemical/amyloid beta-protein (40-1)
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	0021-9258
pubmed:author	pubmed-author:BihainBernard EBE, pubmed-author:FifreAlexandreA, pubmed-author:KozielVioletteV, pubmed-author:KriemBadreddineB, pubmed-author:OlivierJean-LucJL, pubmed-author:OsterThierryT, pubmed-author:PillotThierryT, pubmed-author:SponneIsabelleI, pubmed-author:Yen PotinFrances TFT
pubmed:issnType	Print
pubmed:day	6
pubmed:volume	281
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	229-40
pubmed:dateRevised	2010-11-18
pubmed:meshHeading	pubmed-meshheading:16234245-Amyloid beta-Peptides, pubmed-meshheading:16234245-Animals, pubmed-meshheading:16234245-Apoptosis, pubmed-meshheading:16234245-Calcium, pubmed-meshheading:16234245-Calpain, pubmed-meshheading:16234245-Caspase 3, pubmed-meshheading:16234245-Caspase 9, pubmed-meshheading:16234245-Caspases, pubmed-meshheading:16234245-Cells, Cultured, pubmed-meshheading:16234245-Cerebral Cortex, pubmed-meshheading:16234245-Cytoskeleton, pubmed-meshheading:16234245-Homeostasis, pubmed-meshheading:16234245-Isomerism, pubmed-meshheading:16234245-Mice, pubmed-meshheading:16234245-Mice, Inbred C57BL, pubmed-meshheading:16234245-Microtubule-Associated Proteins, pubmed-meshheading:16234245-Neurons, pubmed-meshheading:16234245-Oxidative Stress, pubmed-meshheading:16234245-Peptide Fragments
pubmed:year	2006
pubmed:articleTitle	Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3.
pubmed:affiliation	Lipidomix, JeuneEquipe 2482, Laboratoire Médecine et Thérapeutique Moléculaire, Institut National Polytechnique de Lorraine, 54500 Vandoeuvre-lès-Nancy, France.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't