A study of amyloid arthropathy in multiple myeloma. 1981

P Hickling, and M Wilkins, and G R Newman, and M H Pritchard, and J Jessop, and J Whittaker, and G Nuki

Forty-three patients with classical multiple myeloma were studied to assess the prevalence and characteristics of amyloid arthropathy using clinical, radiological, and histological methods. Two patients were found to have amyloid arthropathy, and a third case is described in detail. Complement and cryoprecipitate analysis of the synovial fluid, and electronmicroscopy of the synovium, synovial debris and cartilage were undertaken in an attempt to shed further light onto the pathogenesis of what has hitherto been regarded as a rare complication of multiple myeloma. Complement components were not depressed and no evidence of specific light chain containing immune complexes was found in synovial fluid cryoprecipitates. Histochemical and electron microscopic localization of amyloid in perichondrocytic lacunae as well as in synovial fluid debris, synovium and the articular cartilage surface suggest the possibility that chondrocytes and synovial macrophages may share a role in processing immunoglobulin components as a prelude to the formation of amyloid fibrils. Amyloid arthropathy occurs in about 5 per cent of patients with multiple myeloma. The clinical picture can resemble rheumatoid arthritis with median nerve compression in the carpal tunnel and symmetrical arthritis of the wrists and small joints of the hands. Diagnosis can be established by examination of Congo red stained synovial fluid sediments under polarized light even in the absence of other clinical features of amyloidosis and when rectal biopsy is negative.

UI MeSH Term Description Entries
D007592 Joint Diseases Diseases involving the JOINTS. Arthropathies,Arthropathy,Joint Disease
D008297 Male Males
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
D009101 Multiple Myeloma A malignancy of mature PLASMA CELLS engaging in monoclonal immunoglobulin production. It is characterized by hyperglobulinemia, excess Bence-Jones proteins (free monoclonal IMMUNOGLOBULIN LIGHT CHAINS) in the urine, skeletal destruction, bone pain, and fractures. Other features include ANEMIA; HYPERCALCEMIA; and RENAL INSUFFICIENCY. Myeloma, Plasma-Cell,Kahler Disease,Myeloma, Multiple,Myeloma-Multiple,Myelomatosis,Plasma Cell Myeloma,Cell Myeloma, Plasma,Cell Myelomas, Plasma,Disease, Kahler,Multiple Myelomas,Myeloma Multiple,Myeloma, Plasma Cell,Myeloma-Multiples,Myelomas, Multiple,Myelomas, Plasma Cell,Myelomas, Plasma-Cell,Myelomatoses,Plasma Cell Myelomas,Plasma-Cell Myeloma,Plasma-Cell Myelomas
D002358 Cartilage, Articular A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact. Articular Cartilage,Articular Cartilages,Cartilages, Articular
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000368 Aged A person 65 years of age or older. For a person older than 79 years, AGED, 80 AND OVER is available. Elderly
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D000686 Amyloidosis A group of sporadic, familial and/or inherited, degenerative, and infectious disease processes, linked by the common theme of abnormal protein folding and deposition of AMYLOID. As the amyloid deposits enlarge they displace normal tissue structures, causing disruption of function. Various signs and symptoms depend on the location and size of the deposits. Amyloidoses

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