[PubMed] [Google Scholar] 16

[PubMed] [Google Scholar] 16. Lack of FSB labeling of PrP\positive Rabbit Polyclonal to Integrin beta1 plaques in non\AD brains. No co\localization of FSB with PrP\positive plaques was observed, similarly to the ThS staining pattern. (A) FSB staining (blue) was co\localized with neuritic plaques (arrowheads). (B) Conversely, FSB staining revealed no PrP\positive plaques (arrowheads). Bar: 50?m BPA-31-e12941-s001.jpg (559K) GUID:?014B54C5-E0FA-4250-ADEE-36059CDA011E FIGURE S5 Unfavorable ThS labeling of PrP accumulating diffuse plaque while positive ThS of neuritic plaque with a very small amyloid core. A diffuse plaque was not labeled by ThS and labeled by 3F4 antibody (arrows), while a neuritic plaque with a very small amyloid core was labeled by both ThS and 3F4 antibodies (arrowheads) from a representative 74\12 months\old patient without dementia. Bar: 100m BPA-31-e12941-s008.jpg (544K) GUID:?8C9B85E8-D991-49DB-9DEE-93011430E067 FIGURE S6. Low immunoreactivity of PrP antibodies in amyloid plaques of advanced AD brain tissue. (A, D) Compared to the immunoreactivity of A antibody 6E10 in Physique 6A, fainter labeling of PrP antibodies 3H2 (A) and T4 (D) are evident in serial sections of advanced AD brain tissue (arrows). (B, C) Almost no immunoreactivity is obvious in plaques in advanced AD with PrP antibodies, 6H4 (B) and 12F10 (C). Bar: 250?m BPA-31-e12941-s006.jpg (827K) GUID:?259FA10A-C7E2-4870-9E18-7F209F1E9DBF FIGURE S7 No PrP\plaque was detected from young and aged brain tissues without dementia. (A, B) The deposition of amyloid plaques was not detected by A antibody 6E10 in these cases (A), and (B) no PrP accumulating plaques were observed in the brain tissue of a 49\12 months\old patient. (C, D) Even in the brain tissue from an 85\12 months\old patient without dementia or amyloid plaque deposition (C), no PrP\positive plaque was detected (D). Intraneuronal A/APP immunoreactivity was observed as granular dots by the 6E10 antibody in (A, C) and at higher magnification (C, inset). (E, F) In spite of the amazing amyloid deposition and large numbers of amyloid deposits (E, inset) in an 85\12 months\old patient with an old infarction but without dementia (E), no PrP\immunoreactivity was detected. Bars: 250?m, (inset, E 25?m) BPA-31-e12941-s005.jpg (973K) GUID:?C4EE2B48-3EE3-4816-A1F3-0D0C4E8D6DA6 FIGURE S8 Localization of PrP in neurites and cell bodies of neurons. With higher magnification of Physique S7D, the ubiquitous localization of PrP immunoreactivity by antibody 3F4 is usually obvious along neurites, which appear like lines in parallel (arrows). Additionally, PrPC Tanshinone IIA sulfonic sodium is seen in cell body of neurons obvious by stronger brownish labeling (asterisks). Bar: 200?m BPA-31-e12941-s004.jpg (762K) GUID:?A973EF28-28DF-4C2E-BF8F-CDB9A92EEEAE Data Availability StatementAll data provided in this study are available from your corresponding author upon affordable requirement. Abstract Alzheimers disease (AD) is the main cause of dementia, and \amyloid (A) is usually a central factor in the initiation and progression of the disease. Different forms of A have been identified as monomers, oligomers, and amyloid fibrils. Many proteins have been implicated as putative receptors of respective forms of A. Distinct forms of A oligomers are considered to be neurotoxic species that trigger the pathophysiology of AD. It was reported that cellular prion protein (PrPC) is one of the most selective and high\affinity binding partners of A oligomers. The conversation of A oligomers with PrPC is usually important to synaptic dysfunction and loss. The binding of A oligomers to PrPC has mostly been analyzed with synthetic peptides, cell culture, and murine models of AD by biochemical and biological methods. However, the molecular mechanisms underlying the relationship between A oligomers and PrPC remain unclear, especially in the human brain. We immunohistochemically investigated the relationship between A oligomers and PrPC in human brain tissue with and without amyloid pathology. We histologically demonstrate that PrPC accumulates with aging in human brain Tanshinone IIA sulfonic sodium tissue even prior to AD mainly within diffuse\type amyloid plaques, which are composed of more soluble A oligomers without stacked \sheet fibril structures. Our Tanshinone IIA sulfonic sodium results suggest that PrPC accumulating plaques are associated with more soluble A oligomers, and appear even prior to AD. The investigation of PrPC accumulating plaques may provide new insights into AD. Keywords: amyloid plaque, A oligomer, human brain, neuropathology, PrPC PrPC accumulates within a subset.