Preferential association of serum amyloid P component with fibrillar deposits in familial British and Danish dementias: similarities with Alzheimer's disease
| Autor: | Douglas Ng, Blas Frangione, Gordon T. Plant, Hans Brændgaard, Jordana L Meyerson, Tamas Revesz, Tammaryn Lashley, Jorge Ghiso, Marie Bojsen-Møller, Agueda Rostagno, Janice L. Holton |
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| Rok vydání: | 2007 |
| Předmět: |
Pathology
medicine.medical_specialty Amyloid Denmark Plaque Amyloid Fibril chemistry.chemical_compound mental disorders medicine Humans Senile plaques Benzothiazoles Serum amyloid P component Adaptor Proteins Signal Transducing Aged Amyloid beta-Peptides Membrane Glycoproteins biology Brain Membrane Proteins medicine.disease Immunohistochemistry Peptide Fragments Biochemistry of Alzheimer's disease Protein Subunits Serum Amyloid P-Component Thiazoles Neurology chemistry England biology.protein Neurofibrils Thioflavin Dementia Neurology (clinical) Cerebral amyloid angiopathy Alzheimer's disease Biomarkers Cerebral Amyloid Angiopathy Familial |
| Zdroj: | Journal of the neurological sciences. 257(1-2) |
| ISSN: | 0022-510X |
| Popis: | Two hereditary forms of cerebrovascular amyloidosis, familial British and Danish dementias (FBD and FDD), share striking similarities with Alzheimer's disease (AD) despite structural differences among their amyloid subunits (ABri in FBD, ADan in FDD, and A in AD). Neuropathological lesions in these disorders include neurofibrillary tangles, parenchymal amyloid and pre-amyloid deposits and overwhelming cerebral amyloid angiopathy co-localizing with reactive microglia and multiple amyloid associated proteins including activation products of the complement cascade. Immunohistochemical analysis of FBD and FDD brain lesions unveiled the presence of serum amyloid P-component (SAP) primarily associated with thioflavin positive amyloid deposits in spite of the significant pre-amyloid burden existing in both disorders. Using affinity chromatography and ELISA binding assays we demonstrated specific, calcium-dependent, saturable, high affinity binding interactions between SAP and ABri/ADan peptides, with dissociation constant values in the sub-nanomolar range and within the same order of magnitude as those resulting from the interaction of SAP with Alzheimer's A beta 1-40 and A beta 1-42. The preferential association of SAP with fibrillar amyloid lesions and not with non-fibrillar pre-amyloid deposits is puzzling, suggesting that SAP modulates the assembly and stability of the final fibril rather than participating in the early steps of protein misfolding and oligomerization. (c) 2007 Elsevier B.V. All rights reserved. |
| Databáze: | OpenAIRE |
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