Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0003873 (rheumatoid arthritis)
 53,068 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Paired samples of peripheral blood and synovial fluid (SF) aspirated from inflamed knee joints from 15 adult patients with classical rheumatoid arthritis, as well as peripheral blood obtained from 15 healthy subjects, were anticoagulated with ACD. Peripheral blood platelets were separated from other plasma constituents by gel filtration of platelet-rich plasma on Sepharose 2B. When using this technique on SF, it was found that platelets could be isolated from other SF constituents, and that each of the SF's gave a high yield of eluted platelets. Direct immunofluorescent staining for human fibronectin was performed with isolated and suspended platelets obtained from the three different sources. Aliquots of both intact and permeabilized platelets were stained. Intact peripheral platelets from all patients and normal subjects revealed a weakly positive staining, whereas the staining of intact SF platelets from all patients was clear and bright. The fluorescence of intact cells was surface-located and speckled. For permeabilized platelets, the staining had a punctate intracellular pattern, with a varying number of discrete and bright fluorescent foci per cell. Counting of the foci in each platelet specimen revealed that this number, which was also found in peripheral platelets from all patients and normal subjects, was distinctly greater than the number of foci in all the SF platelet specimens. No relationship was found between the various staining results and medical treatment or Waaler-Rose serology of the patients. The findings indicate that the SF platelets had large amounts of surface-bound and small amounts of intracellular fibronectin, whereas the converse was found in the case of peripheral platelets from the patients and normal subjects.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Demonstration of fibronectin associated with platelets in synovial fluid from patients with rheumatoid arthritis. 639 22

Immune complexes (IC) present in sera from patients with Hodgkin's disease (HD) were isolated using three different affinity columns: C1q-degalan, anti-C1q sepharose and conglutinin (K)-degalan. The isolated IC were analysed by immunoprecipitation, SDS-PAGE and sucrose density gradients and compared with IC similarly isolated from patients with rheumatoid arthritis (RA), systemic lupus erythematosus (SLE) and in vitro prepared BSA-anti-BSA complexes. Isolated material from each disease, and BSA-anti-BSA complexes contained proteins compatible with true immune complexes--IgM, IgG, C1q and C3 breakdown components. Albumin, fibronectin and CRP, whose affinity for IgM, C1q and C3 are known, were co-isolated along with IC material. The size of isolated IC in HD ranged from 8-40S on sucrose density gradients. Despite the operational difference in detecting and isolating HD complexes via the C1q ligand (C1q-degalan or anti-C1q column) and C3bi (K-degalan), material purified by both methods showed remarkable similarity on SDS-PAGE and immunoprecipitation analysis. Although IC isolated from different diseases showed disparate banding patterns on SDS-PAGE this was attributed to a variation in the relative concentrations of constituent proteins--IgM, IgG and C3 breakdown products. IgM, IgG and C3 bind loosely, and non-specifically, to macromolecular aggregates formed around immune complexes. Using the anti-C1q column, most of this material could be eluted using 0.02M EDTA. Least protein, yet the most specific for antigen and antibody was eluted at pH 3.0.
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PMID:Immune complexes in Hodgkin's disease: isolation, immunochemical and physico-chemical analysis. 641 1

Synovial fluid fibronectin from normal subjects and from patients who have rheumatic inflammatory diseases has been studied and compared with plasma fibronectin. The average fibronectin concentration in synovial fluids from normal subjects was 172 +/- 69 micrograms/ml; it was 721 +/- 315 and 556 +/- 349 micrograms/ml in synovial fluids from patients with rheumatoid arthritis and osteoarthritis, respectively. This is the first report on fibronectin concentrations in normal synovial fluids. Synovial fluid fibronectin from healthy subjects and patients with rheumatoid arthritis or osteoarthritis showed a molecular weight identical to that of plasma fibronectin. All normal and pathologic synovial fluid fibronectins showed a remarkably lower electrophoretic mobility compared with that of plasma fibronectin, when separated according to net molecular charge on agarose gel. Peptides from thermolysin digests of fibronectin from plasma and synovial fluid, when compared on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, showed distinct differences. These data demonstrate that synovial fluid fibronectin represents a molecular form which is structurally different from that of plasma fibronectin. This suggests that synovial fluid fibronectin is locally synthesized, possibly by a cell type which differs from that responsible for the production of the plasmatic fibronectin pool.
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PMID:Characterization of synovial fluid fibronectin from patients with rheumatic inflammatory diseases and healthy subjects. 646 96

A circulating high-molecular-weight glycoprotein called fibronectin plays a part in cell adhesion and migration before phagocytosis and in morphology, differentiation, and metabolism in inflammatory synovial effusions of patients with rheumatic diseases. A technique of nephelometric immunoassay, based on the measurement of an antigen-antibody reaction, was applied to the analysis of fibronectin concentrations in synovial fluids from 20 patients with rheumatoid arthritis (RA) and other diseases (non-RA). RA synovial fluids have a significantly higher concentration than the specimens obtained from Yersinia arthritis patients (n = 12). The mean concentration of other synovial fluids, from 12 patients with osteoarthritis of the knees, did not significantly differ from the synovial fluids of control values obtained from patients who underwent meniscectomy. There was a considerably negative correlation between fibronectin levels and overall indices of inflammatory activity, such as Ritchie articular indices or a whole number of painful rheumatoid arthritis joints. However, a particularly distinct correlation was obtained when raised fibronectin levels were compared with the inflammatory activity of the knee joint, from which the specimen was aspirated. Thus, these findings suggest that the measurements of fibronectin in synovial fluid may be of some differential-diagnostic value in rheumatoid variants, but may only serve as an indicator of inflammatory activity if the joint, from which the specimen is obtained, is taken into account.
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PMID:Different synovial fluid fibronectin levels in rheumatoid variants. 648 13

The authors report the results of an assay of plasma fibronectin and synovial fluid fibronectin conducted in 104 patients with arthropathy, including 26 cases of rheumatoid arthritis, 43 cases of mechanical arthropathy and 35 cases of non-rheumatoid arthritis. The plasma fibronectin levels do not vary significantly between the different groups of patients, but the mean value for the whole group of patients is significantly lower than that of a control population. The mean value of synovial fluid fibronectin was significantly higher in the patients with rheumatoid arthritis (583 +/- 76 mg/1) than in the patients with non-rheumatoid arthritis (379 +/- 58 mg/1) or mechanical arthropathy (367 +/- 32 mg/1). The assay of synovial fibronectin could therefore provide useful information for the aetiological diagnosis of inflammatory arthropathies. The local origin, from the synovial membrane itself, of the fibronectin in the synovial fluid is suggested by the fact that the synovial concentration of this protein is superior to the serum concentration in 50 to 90 per cent of cases, depending on the disease.
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PMID:[Plasma and synovial fibronectin. Results of personal research]. 649 78

An extension of the C1q-binding assay for the detection of immune-aggregate-mediated and non-immune-aggregate-mediated C1q binding is reported. The assay involves the use of two different C1q preparations, one radioiodinated by means of lactoperoxidase (LPO-125I-C1q) and the other by means of chloramine-T (CT-125I-C1q). The treatment with CT for 20 min at room temperature before iodination for 1 min led to abolishment of the C1q-binding capacities to complexed IgG: approximately 50% of LPO-125I-C1q but only 2% of CT-125I-C1q bound to 80 micrograms/ml of IgG forming part of tetanus toxoid/anti-tetanus toxoid complexes or to 200 micrograms/ml of heat-aggregated human gamma globulin. Similar results were obtained with staphylococcal protein-A-aggregated IgG. CT-treated C1q was haemolytically inactive. In contrast to the results with complexed IgG, CT treatment did not markedly reduce binding capacities of C1q to heparin: approximately 55% of LPO- and CT-125I-C1q were bound by 127 U/ml of commercial heparin in normal human serum. Both C1q preparations bound to a comparable extent to fibronectin, fibrinogen, and various bacterial endotoxins. When the LPO- and CT-125I-C1q-binding patterns obtained on serum samples from patients with systemic lupus erythematosus, rheumatoid arthritis, or essential mixed cryoglobulinaemia were compared with binding patterns observed using laboratory reactants, an immediate detection of non-immune-aggregate-mediated C1q binding became possible.
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PMID:An extended C1q-binding assay using lactoperoxidase- and chloramine-T-iodinated C1q. Immediate distinction between immune-aggregate-mediated and non-immune-aggregate-mediated C1q binding. 660 19

Immune complexes were precipitated with polyethylene glycol (PEG) from sera of patients with rheumatoid arthritis (RA), psoriatic arthritis and systemic lupus erythematosus. Precipitates were tested for their capacity to consume complement and for the presence of fibronectin (Fn) and specific autoantibodies rheumatoid factor (RF, anti-DNA). The results showed enrichment of autoantibody activity in the precipitates. In RA, RF was especially enriched in 2.5% PEG precipitates, while IgM anti-DNA activity was more evident in 3.5% precipitates. IgG anti-DNA antibody was detected only in 3.5% precipitates from lupus sera. Complement consumption activity of precipitates was mainly related to IgM autoantibodies. There was a strong correlation between the presence of RF activity and Fn in the PEG precipitates. Nephelometric studies revealed direct interaction between the Fn and IgM RF or heat aggregated gammaglobulin. It may be possible to monitor the serum levels of immune complex material using PEG precipitation.
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PMID:Immunochemical analyses of components of immune complexes in the sera of patients with autoimmune diseases. 666 92

Fibronectin is a glycoprotein found in body fluids, loose connective tissue matrix and in basement membranes. Fibronectin in rheumatoid arthritis synovial fluid was immunologically indistinguishable from the plasma form, as shown by double-diffusion analysis. Fibronectin isolated from rheumatoid synovial fluid by affinity chromatography on gelatin--Sepharose had a polypeptide pattern similar to that of plasma fibronectin in SDS--polyacrylamide gel electrophoresis. In fifty-one patients with rheumatoid arthritis and related diseases fibronectin concentrations is synovial fluid were 445 +/- 103 micrograms/ml (mean +/- SD) and within normal range, 335 +/- 52 micrograms/ml, in plasma. Immunofluorescence staining showed a prominent increase of fibronectin in the proliferating synovial connective tissue in rheumatoid arthritis as compared to normal synovial membrane. The results suggest an increased local production of fibronectin in rheumatoid synovial tissue.
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PMID:Fibronectin in synovial fluid and tissue in rheumatoid arthritis. 679 40

Fibronectin, a high molecular weight glycoprotein that binds to glycosaminoglycans, fibrinogen or fibrin, and collagen, was identified and quantitated in synovial fluid from patients with various rheumatic diseases. Fibronectin concentration was significantly higher in synovial fluids from patients with rheumatoid arthritis (RA) (697 microgram/ml) than in other synovial fluids. In RA, synovial fluid fibronectin concentration exceeded that in plasma and did not directly correlate with synovial fluid concentrations of albumin, total protein, or fibrinogen. Synovial fluid fibronectin concentration correlated directly with synovial fluid white blood cell count (r = 0.50, P less than 0.005). Fibronectin was present in cryoprotein formed from four rheumatoid synovial fluids.
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PMID:Detection and quantitation of fibronectin in synovial fluid from patients with rheumatic disease. 697 31

Fibronectin is a glycoprotein secreted by connective tissue cells into their environment and into the blood. Plasma fibronectin has been isolated and used to prepare an antiserum. This has been shown to be specific for fibronectin and unreactive with fibrin(ogen) and collagen, to which fibronectin binds in vitro. The antiserum has been used to examine the distribution of this protein in the synovium in health, in rheumatoid arthritis, and in osteoarthrosis, and to estimate levels in plasma and synovial fluid. The results suggest that fibronectin is synthesised by synovial cells, and the synovial fluid level of fibronectin was found to be about twice the plasma level in rheumatoid arthritis. In long-standing arthritis fibronectin was also found to be codistributed with (presumably by adsorption upon) fibrin and immature collagen in intra-articular structures but was no longer demonstrable in areas where mature collagen had been formed in areas undergoing fibrosis. The possible significance of local fibronectin production within joints in relation to its possible effect on the resolution or continuance of arthritis is discussed.
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PMID:Significance of fibronectin in rheumatoid arthritis and osteoarthrosis. 701 19


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