Document Detail

AA-Amyloid is cleared by endogenous immunological mechanisms.
MedLine Citation:
PMID:  22900541     Owner:  NLM     Status:  In-Data-Review    
Objective: AA amyloidosis is a complication to longstanding inflammatory diseases, but reduction of amyloid mass has been reported as the inflammation ceases. Not much is known about the endogenous factors that contribute to this amyloid resolution. Herein, we describe the dynamics of amyloid degradation and resolution in experimental murine AA-amyloidosis. Methods: AA-amyloidosis was induced in mice with injections of amyloid enhancing factor (AEF) and by inflammation induced with injections of silver nitrate. Resolution of amyloid deposits was monitored over time. Results: Virtually all amyloid was cleared within 34 weeks. Using the ELISA-technique, antibodies directed against protein AA were detected in animals during amyloid clearance phase and macrophages were shown to internalize amyloid. Also, passive immunization with an amyloid specific monoclonal antibody, produced by a B-cell clone recovered from an animal with advanced AA-amyloidosis, reduced amyloid development in murine AA-amyloidosis. Conclusion: Immunoglobulins co-localize with amyloid deposits and can contribute to amyloid degradation by Fc-receptor mediated phagocytosis, and should be considered key players in the degradation process.
Sofia N Nyström; Gunilla T Westermark
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis     Volume:  19     ISSN:  1744-2818     ISO Abbreviation:  Amyloid     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-08-20     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9433802     Medline TA:  Amyloid     Country:  England    
Other Details:
Languages:  eng     Pagination:  138-45     Citation Subset:  IM    
Department of Clinical and Experimental Medicine, Division of Cell Biology, Linköping University , Linköping , Sweden.
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