Mostrar el registro sencillo del ítem
dc.contributor.author
Patton, R. Lyle
dc.contributor.author
Kalback, Walter M.
dc.contributor.author
Esh, Chera L.
dc.contributor.author
Kokjohn, Tyler A.
dc.contributor.author
Van Vickle, Gregory D.
dc.contributor.author
Luehrs, Dean C.
dc.contributor.author
Kuo, Yu-Min
dc.contributor.author
Lopez, John
dc.contributor.author
Brune, Daniel
dc.contributor.author
Ferrer, Isidro
dc.contributor.author
Masliah, Eliezer
dc.contributor.author
Newel, Amanda J.
dc.contributor.author
Beach, Thomas G.
dc.contributor.author
Castaño, Eduardo Miguel
dc.contributor.author
Roher, Alex E.
dc.date.available
2018-03-22T19:43:20Z
dc.date.issued
2006-12
dc.identifier.citation
Patton, R. Lyle; Kalback, Walter M.; Esh, Chera L.; Kokjohn, Tyler A.; Van Vickle, Gregory D.; et al.; Amyloid-β peptide remnants in AN-1792-immunized Alzheimer's disease patients: A biochemical analysis; Amer Soc Investigative Pathology, Inc; American Journal Of Pathology; 169; 3; 12-2006; 1048-1063
dc.identifier.issn
0002-9440
dc.identifier.uri
http://hdl.handle.net/11336/39733
dc.description.abstract
Experiments with amyloid-β (Aβ)-42-immunized transgenic mouse models of Alzheimer's disease have revealed amyloid plaque disruption and apparent cognitive function recovery. Neuropathological examination of patients vaccinated against purified Aβ-42 (AN-1792) has demonstrated that senile plaque disruption occurred in immunized humans as well. Here, we examined tissue histology and quantified and biochemically characterized the remnant amyloid peptides in the gray and white matter and leptomeningeal/cortical vessels of two AN-1792-vaccinated patients, one of whom developed meningoencephalitis. Compact core and diffuse amyloid deposits in both vaccinated individuals were focally absent in some regions. Although parenchymal amyloid was focally disaggregated, vascular deposits were relatively preserved or even increased. Immunoassay revealed that total soluble amyloid levels were sharply elevated in vaccinated patient gray and white matter compared with Alzheimer's disease cases. Our experiments suggest that although immunization disrupted amyloid deposits, vascular capture prevented large-scale egress of Aβ peptides. Trapped, solubilized amyloid peptides may ultimately have cascading toxic effects on cerebrovascular, gray and white matter tissues. Anti-amyloid immunization may be most effective not as therapeutic or mitigating measures but as a prophylactic measure when Aβ deposition is still minimal. This may allow Aβ mobilization under conditions in which drainage and degradation of these toxic peptides is efficient.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Amer Soc Investigative Pathology, Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Alzheimer
dc.subject
Vaccination
dc.subject
Amyloid Beta
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Amyloid-β peptide remnants in AN-1792-immunized Alzheimer's disease patients: A biochemical analysis
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-15T15:21:43Z
dc.identifier.eissn
1525-2191
dc.journal.volume
169
dc.journal.number
3
dc.journal.pagination
1048-1063
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Philadelphia
dc.description.fil
Fil: Patton, R. Lyle. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Kalback, Walter M.. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Esh, Chera L.. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Kokjohn, Tyler A.. Midwestern University Glendale; Estados Unidos. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Van Vickle, Gregory D.. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Luehrs, Dean C.. National Cheng Kung University; China
dc.description.fil
Fil: Kuo, Yu-Min. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Lopez, John. Arizona State University; Estados Unidos
dc.description.fil
Fil: Brune, Daniel. Arizona State University; Estados Unidos
dc.description.fil
Fil: Ferrer, Isidro. Hospital Universitari de Bellvitge; España
dc.description.fil
Fil: Masliah, Eliezer. University of California at San Diego; Estados Unidos
dc.description.fil
Fil: Newel, Amanda J.. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Beach, Thomas G.. Banner Sun Health Research Institute; Estados Unidos
dc.description.fil
Fil: Castaño, Eduardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Roher, Alex E.. Banner Sun Health Research Institute; Estados Unidos
dc.journal.title
American Journal Of Pathology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0002-9440(10)62779-4
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.2353/ajpath.2006.060269
Archivos asociados