[C-11]PIB-amyloid binding and levels of A beta 40 and A beta 42 in postmortem brain tissue from Alzheimer patients
2009 (English)In: Neurochemistry International, ISSN 0197-0186, E-ISSN 1872-9754, Vol. 54, no 5-6, 347-357 p.Article in journal (Refereed) Published
beta-Amyloid (A beta) deposits are one of the major histopathological hallmarks of Alzheimer's disease (AD). The amyloid-imaging positron emission tomography (PET) tracer [C-11]PIB (N-methyl[C-11]2-(4'-methylaminophenyl)-6-hydroxy-benzothiazole) is used in the assessment of A beta deposits in the human brain. [C-11]PIB-amyloid interaction and insoluble A beta 40 and A beta 42 peptide levels in the brain were quantified in postmortem tissue from nine AD patients and nine age-matched control subjects in the temporal, frontal and parietal cortices and the cerebellum. Autoradiographical studies showed significantly higher densities of specific [C-11]PIB-amyloid binding in gray matter in the temporal and parietal cortex (62 fmol/mg tissue) in AD patients as compared to control subjects, whereas the density was somewhat lower in the frontal cortex (56 fmol/mg tissue). No specific binding could be detected in the AD cerebellum or in the tissues from the control subjects (<= 5 fmol/mg tissue). Insoluble A beta 40 and total A beta levels (i.e. sum of A beta 40 and A beta 42) were significantly higher in patients than in controls in all measured cortical regions as determined using ELISA, which was confirmed using immunohistochemistry. The present findings show a more regional selective distribution of [C-11]PIB amyloid binding than previously reported. Moreover, it is suggested that some of the [C-11]PIB binding and insoluble A beta seen in control subjects may be amyloid in the blood vessels. (C) 2009 Elsevier Ltd. All rights reserved.
Place, publisher, year, edition, pages
2009. Vol. 54, no 5-6, 347-357 p.
Alzheimer's disease, Autoradiography, beta-Amyloid, [C-11]PIB, Immunohistochemistry, Radioligand assay
IdentifiersURN: urn:nbn:se:uu:diva-129135DOI: 10.1016/j.neuint.2008.12.016ISI: 000264912300010OAI: oai:DiVA.org:uu-129135DiVA: diva2:337713