Amyloidosis is a disorder of protein conformation and metabolism that results in the deposition of insoluble amyloid fibrils in tissues, which causes organ dysfunction; systemic amyloidosis is characterized by failure of multiple organs and the presence of amyloid precursor protein in the serum [1-3]. Reactive amyloid A (AA) amyloidosis is one of the most severe complications of several chronic disorders, particularly rheumatoid arthritis (RA) [4], and indeed, most patients with reactive AA amyloidosis have an underlying rheumatic disease. An extra-articular complication of RA, AA amyloidosis is a serious, potentially life-threatening disorder caused by deposition in organs of AA amyloid fibrils, which derive from the circulatory acute-phase reactant, serum amyloid A protein (SAA) [5]. AA amyloidosis secondary to RA is thus one of the intractable conditions found in patients with collagen vascular diseases and is an uncommon yet important complication of RA [6]. However, the actual pathological mechanisms that are responsible for the relationship between SAA and AA amyloidosis have not been fully elucidated. With new biological therapies, both treatment and understanding of the roles of cytokines and inflammatory cellular events in RA have seen considerable progress. Biologics are recommended for patients with RA who have a suboptimal response or an intolerance to traditional disease-modifying anti-rheumatic drugs (DMARDs), such as methotrexate (MTX). Early diagnosis and rapidly subsequent treatment are essential because patients with advanced disease can't usually undergo intensive therapy. Specific treatment of AA amyloidosis caused by RA aims to stop SAA production. Cytotoxics such as chlorambucil and cyclophosphamide (CYC) and biologics such as anti-tumor necrosis factor (TNF)α inhibitors and anti-interleukin (IL)-6 receptor antibody are reportedly useful for both RA and AA amyloidosis [7, 8]. By the way, the genetic predisposition allele SAA1.3, one of SAA1 gene