title: [A review for recent advances in AA amyloid research and therapeutic approach to AA amyloidosis complicating rheumatoid arthritis].
abstract: AA amyloidosis is a life threatening clinical complication of chronic inflammatory diseases such as rheumatoid arthritis. It has been demonstrated biochemically that amyloidosis resulted from abnormal folding of proteins, which are deposited as insoluble fibrils in extracellular tissue, leading to the disruption of their normal function. In this regard, amyloidosis has been recognized as a conformation disorder. Interestingly, genetic polymorphisms of amyloid precursor protein (SAA) have been reported to associate with increased risk for AA amyloidosis. Also recent biochemical research revealed that SAA is synthesized under the influence of the proinflammatory cytokines, such as IL-6, TNF-alpha, IL-1. Additionally, it was suggested that amyloid deposits in extracellular tissue could reflect to the serum level of SAA in the reversible fashion, leading to the hypothesis that the control of the SAA synthesis could be beneficial to the treatment of amyloidosis. In this context, anti-cytokine therapies may be most effective. Especially the inhibition of IL-6 is critical to suppression of SAA production, so treatment with a humanized monoclonal antibody against human IL-6 receptor may not only ameliorate RA disease activity but also pave the way for the treatment of AA amyloidosis.
authors.affiliation: Department of Internal Medicine, Rheumatic diseases, Kin-ikyo-chuo Hospital.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Tamura
authors.forename: Kiminori
authors.initials: K
authors.lastname: Hasegawa
mesh_terms: D000686:Amyloidosis / Q000188:drug therapy* / Q000209:etiology; D001172:Arthritis, Rheumatoid / Q000150:complications*; D006801:Humans; D000685:Serum Amyloid A Protein / Q000378:metabolism*
chemical_list: D000685:Serum Amyloid A Protein