Distribution pattern of matrix metalloproteinases 1, 2, 3, and 9, tissue inhibitors of matrix metalloproteinases 1 and 2, and α2-macroglobulin in cases of generalized AA- and AL amyloidosis
作者： D. Müller , A. Roessner , C. Röcken
关键词: Extracellular matrix 、 AL amyloidosis 、 Amyloid 、 Protease 、 AA amyloidosis 、 Matrix metalloproteinase 、 Pathology 、 Biology 、 Amyloidosis 、 Connective tissue
摘要: Matrix metalloproteinases (MMPs) degrade basement membranes and connective tissue play an essential role in the homeostasis of extracellular matrix which is disrupted by deposition amyloid. This immunohistochemical study investigated distribution pattern (MMP-1, -2, -3, -9) their inhibitors [α2-macroglobulin (α2-M), MMPs (TIMP)-1, TIMP-2] human AA- AL amyloid deposits. Specimens liver, kidney, spleen from 22 autopsy cases were investigated. Nine patients had suffered generalized AA amyloidosis, eight five rheumatoid arthritis or tuberculosis with no histological evidence In all amyloidotic non-amyloidotic patients, each protease inhibitor was detected almost every organ cases, there indication that a specific absent expressed, but difference observed spatial patterns. The most noticeable found immunostaining Only MMP-1, α2-M present deposits, only TIMP-1 TIMP-2 deposits first to show -3 are They may be involved remodeling proteolysis precursor fibril proteins.
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