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26 April 2024

» pubmed » pmid12015594

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Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
M B Pepys ; J Herbert ; W L Hutchinson ; G A Tennent ; H J Lachmann ; J R Gallimore ; L B Lovat ; T Bartfai ; A Alanine ; C Hertel ; T Hoffmann ; R Jakob-Roetne ; R D Norcross ; J A Kemp ; K Yamamura ; M Suzuki ; G W Taylor ; S Murray ; D Thompson ; A Purvis ; S Kolstoe ; S P Wood ; P N Hawkins ;
Date:	16 May 2002
Journal:	Nature, 417 (6886), 254-9
Abstract:	The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. This palindromic compound also crosslinks and dimerizes SAP molecules, leading to their very rapid clearance by the liver, and thus produces a marked depletion of circulating human SAP. This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer’s disease and type 2 diabetes.
Source:	PubMed, pmid12015594 doi: 10.1038/417254a
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