The amyloid (V624M) similarly accumulated serum amyloid P-component and clusterin but also a C-terminal fragment of TGFBIp containing residues Y571-R588 derived from the fourth fasciclin-1 domain (FAS1-4), apolipoprotein E and apolipoprotein A-IV.
SAP recognizes carbohydrates, nuclear substances, and amyloid fibrils and thus participates in the resolution of infectious diseases, autoimmunity, and amyloidosis.
123I-labeled human SAP was injected intravenously into 20 controls and 189 consecutive patients with histologically proven amyloidosis: of AA type in 60 cases, AL type in 80, hereditary ATTR type in 27, and localized amyloidosis in 22 cases.
We then examined the persistence of splenic AA amyloid fibrils in SAP-deficient and wild-type mice to assess potential ways of treating individuals with amyloidosis.
This first demonstration of the participation of SAP in pathogenesis of amyloidosis in vivo confirms that inhibition of SAP binding to amyloid fibrils is an attractive therapeutic target in a range of serious human diseases.
A DNA polymorphic site, 5' to the serum amyloid P component gene, has been found to be significantly associated with amyloidosis in juvenile arthritic patients.