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- Title
Localization of Human Serum Amyloid P Component and Heparan Sulfate Proteoglycan in In Vitro-Formed Aβ Fibrils.
- Authors
Holm Nielsen; Nybo; Junker; Toftedal Hansen; Rasmussen; Svehag
- Abstract
Ultrastructural studies of the localization of serum amyloid P component (SAP) in amyloid fibrils have given divergent results. We here report for the first time that electron microscopy of SAP coincubated with Aβ[sub 1–42] peptides or with mature Aβ[sub 1–42] fibrils, revealed SAP molecules coating the surface of the mature fibrils and that protofibrils of Aβ[sub 1–42 ]did not bind SAP. Also when incubated with extracted amyloid light chain (AL)-fibrils the SAP molecules aligned on the fibril surface. Heparan sulfate proteoglycan bound to the surface of the Aβ fibrils with a spacing of about 50 nm. We conclude that SAP does not bind to protofibrils but to the surface of mature Aβ fibrils and that it may stabilize and protect the fibrils.
- Subjects
AMYLOID; PROTEOGLYCANS
- Publication
Scandinavian Journal of Immunology, 2000, Vol 52, Issue 2
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1046/j.1365-3083.2000.00775.x