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PubMed1989

Increased carbonyl content of proteins in synovial fluid from patients with rheumatoid arthritis.

The carbonyl content of proteins in the synovial fluid (SF) of patients with rheumatoid arthritis was significantly (p less than or equal to 0.10) elevated over levels in the SF of patients with osteoarthritis (OA). Other indicators of oxidative damage including catalse, ceruloplasmin, ferritin and superoxide dismutase also showed statistically significant differences (p less than or equal to 0.05) compared to patients with OA.

Arthritis, Rheumatoid↗
PubMedDate not supplied

Clinical significance of synovial fluid total hemolytic complement activity.

Total hemolytic complement (CH50) was measured in 174 synovial fluids (SF) to determine its diagnostic and and prognostic value. SF CH50 was reduced relative to serum CH50 in 61% of patients with rheumatoid arthritis and 60% of patients with crystal-induced arthritis. There was no correlation of SF CH50 levels with disease duration, SF leukocyte count, presence of IgM rheumatoid factor, or radiologic evidence of erosions.

Arthritis, Reactive↗
PubMed1988

Synovial fluid collagenase in patients with destructive arthritis of the shoulder joint.

We studied synovial fluid (SF) collagenase in 10 women with severe rheumatoid arthritis (RA), 10 with pyrophosphate arthropathy, and 10 with idiopathic destructive disease of the shoulder conforming to a pattern recently described. SF cell counts were highest in the RA group. Particles were detected by polarized light microscopy and alizarin red staining. Crystals were seen in fluids from all 3 groups; pyrophosphate predominated in the pyrophosphate arthropathy group and alizarin red-positive particles in the idiopathic disease group. Collagenase and tissue inhibitor of metalloproteinase levels were estimated in SF after gel filtration. Tissue inhibitor of metalloproteinase activity was detected in all fluids, but tended to be highest in the RA group. Collagenase activity was detected in 3 RA fluids only. In no sample was collagenase found in an active form. These findings support the clinical concept of an aggressive destructive process which sometimes occurs in the shoulder joints of elderly women. Because we were not able to detect free collagenase in SF from any of the patients with idiopathic shoulder disease, the data suggest that high levels of active collagenase are not characteristic of this group of patients.

Apatites↗
PubMed1999

Value of direct smears of synovial fluid in the diagnosis of canine joint disease.

Assessments of direct smears of synovial fluid by four clinicians were compared with the results obtained with a Coulter counter. Estimates of total white cell counts by the clinicians were inaccurate and generally higher than the Coulter counter results. The method had a low sensitivity and specificity for the identification of degenerative joint disease and normal joints in comparison with the identification of inflammatory joint disease. There were marked variations in the results obtained by the four clinicians for all the analyses in the study.

Animals↗
PubMed1984

Elevations in synovial fluid plasminogen activator in patients with rheumatoid arthritis.

Plasminogen activator (PA) activity in synovial fluid (SF) obtained from patients with rheumatoid arthritis (RA) is elevated when compared to SF obtained from patients with osteoarthritis (OA). Immunological studies and lack of evidence for a decrease in PA inhibitors, or an increase in PA stimulators, suggest that elevations in RA SF PA activity reflect increases in PA level. Although the origin(s) of SF PA was not identified, the enzyme resembles urokinase and RA synovium may be a contributing source. These observations are consistent with a possible active role of PA in the pathogenesis of RA.

Adult↗
PubMedDate not supplied

Binding of synovial fluid proteins to monosodium urate crystals in vitro.

Sodium dodecylsulfate polyacrylamide gel electrophoresis (SDS PAGE) and western blot techniques were used to analyze proteins adsorbed in vitro to synthetic monosodium urate crystals (MSUC) from a variety of gouty biologic fluids. Distinct differences in adsorbed proteins were found in comparing synovial fluid (SF) with serum or plasma, particularly at 220 kD and below 19 kD. Further studies should consider the importance of the synovial milieu. Patterns of proteins adsorbed to MSUC from the SF of all 12 patients with gout were similar. A considerable number of polypeptides appeared to be selectively adsorbed. Of these, polypeptides associated with fibronectin, C1q and IgM were identified by immunotransblotting. The experiments also demonstrated that the overall polypeptide patterns obtained by SDS PAGE of eluates from MSUC exposed to SF were unaffected by heating MSUC to 180 degrees C, as well as by the volume of SF in the incubation mixture.

Adsorption↗
PubMed1985

IgG with a deviant conformation in serum and synovial fluid from rheumatoid arthritis patients.

Specific rabbit antisera were prepared against an IgG with a special conformation (IgG spec.) previously detected in some sera from patients with rheumatoid arthritis. The antibodies had no affinity to normal human IgG and were not anti-idiotypic to human rheumatoid factor. The affinity of IgG spec. to the antibodies could not be explained by an antiglobulin activity to rabbit IgG. The amount of protein with affinity to immobilized specific IgG F(ab')2 of the antibodies was determined in serum and synovial fluid from patients with various joint diseases. A relationship between the content of IgG spec. and the diagnosis of seropositive rheumatoid arthritis was found on analysis of serum samples. IgG spec. also occurred in synovial fluid from some individuals with seropositive rheumatoid arthritis. Differences in the serum content of IgG spec. could not be explained by differences in the normal IgG content. Circular dichroism analysis of isolated IgG spec. showed that in the region(s) close to tyrosine residue(s) this polyclonal protein had similarities to heat-aggregated IgG.

Antibodies, Anti-Idiotypic↗
PubMed1994

Increased expression of VLA-5 adhesion molecules on synovial fluid T lymphocytes in chronic polyarthritis: a consequence of T-cell activation.

This study focuses on the consequences of T-lymphocyte activation in chronic polyarthritis in terms of expression of cell surface receptors interacting with extracellular matrix (ECM). The expression of the VLA group of integrins was studied on in vitro-stimulated peripheral-blood T cells, and on peripheral-blood and synovial-fluid mononuclear cells (MNC) of patients with polyarthritis. The VLA expression was measured by flow cytometry using monoclonal antibodies (MoAbs) against alpha-subunits of the VLA family. VLA-alpha 4 and VLA-alpha 5, but not VLA-alpha 1, were expressed on a major fraction of unstimulated peripheral-blood T cells both in the patients with polyarthritis and in healthy individuals. Two distinct populations, VLA-alpha 5-high and VLA-alpha 5-low, were found in resting peripheral-blood T lymphocytes. Two days after stimulation by phorbol 12-myristate 13-acetate (PMA) and concanavalin A, most T cells became VLA-alpha 5-high. In patients with chronic polyarthritis, the expression of VLA-alpha 1 and VLA-alpha 5 was always higher on synovial-fluid T cells than on peripheral-blood T cells. These results give further support to the hypothesis that upon activation the induction of the VLA adhesion-molecule expression may be a factor contributing to the accumulation of T cells in the inflamed synovium.

Adult↗
PubMed1993

Increased levels of leukemia inhibitory factor in synovial fluid from patients with rheumatoid arthritis and other inflammatory arthritides.

OBJECTIVE: To examine synovial fluid (SF) from patients with arthritis, for the presence of the cytokine leukemia inhibitory factor (LIF). METHODS: SF from 152 subjects was examined for LIF, using a radioreceptor competition assay. RESULTS: LIF was present at concentrations of 1-43 ng/ml in the SF of 23% of patients with rheumatoid arthritis (RA) or other inflammatory or infectious arthritides but in only 1 of 29 patients with osteoarthritis (P < 0.01). In the RA patients, the SF LIF concentration correlated significantly with the peripheral blood white blood cell count (WBC) (P < 0.05) and the SF WBC count (P < 0.01), but not with other clinical or radiologic parameters of disease activity or progression. CONCLUSION: LIF is implicated as a potential mediator of the local or systemic inflammatory response or the joint destruction seen in inflammatory arthritis.

Arthritis↗
PubMed1984

Spontaneous and induced immunoglobulin secretion by synovial fluid B lymphocytes in rheumatoid arthritis.

The functional properties of B lymphocytes in synovial fluid (SF) from patients with rheumatoid arthritis (RA) were analysed by means of a reverse haemolytic plaque forming cell (PFC) assay. SF mononuclear cells spontaneously secreted IgG, but little IgM or IgA. The SF cells failed to respond to the polyclonal B cell activators pokeweed mitogen (PWM) and Epstein-Barr virus. However, SF B cells cocultured with autologous T lymphocytes from the blood and stimulated with PWM secreted IgG but little IgM or IgA. The PFC responses of blood B cells cocultured with autologous SF T cells in the presence of PWM were low; irradiation of the T cells increased the blood B lymphocyte responses, but the differences were not statistically significant. It is concluded that suppressor SF T cells may be partly responsible for the poor response of SF B cells to PWM.

Adult↗
PubMed1992

Microscopic rice bodies in rheumatoid synovial fluid sediments.

To determine the clinical significance of the microscopic study of the synovial fluid (SF) sediment, 306 sediments were examined from 216 patients with the most frequently occurring acute and chronic arthropathies. The SF was obtained using a fine gauge needle. Microscopic rice bodies were seen in 53 (17.3%) of the samples studied. Forty-five (84.9%) of the samples in which rice bodies were observed were from patients with rheumatoid arthritis (RA) (p < 0.001); 34.9% of the 129 RA samples were found to contain rice bodies. The specificity of finding rice bodies in RA was 95.5%. Most rice bodies were composed of partly or totally hyalinized fibrinous material; in their interior, mononuclear cells were predominantly observed--most of them macrophagic in appearance. With less frequency the rice bodies exhibited central areas of fibrosis. Our results suggest that microscopic rice bodies are fibrinous particles derived from the entrapping of cells in the dense fibrin network present in inflammatory SF.

Arthritis, Rheumatoid↗
PubMed1973

Comparative study of the in vitro proliferative responses of blood and synovial fluid leukocytes of rheumatoid arthritis patients.

Lymphocyte-rich suspensions from blood and synovial fluid (SF) of 20 patients with rheumatoid arthritis (RA) and from blood of 12 normal subjects, were cultured with heat-aggregated, aggregate-free, and native human gamma globulin (HGG), with autologous IgG separated from RA-SF by anion-exchange chromatography and with phytohemagglutinin (PHA). No significant differences were noted between the in vitro proliferative responses of blood lymphocytes of RA and normal controls to any of these preparations. Significant differences were noted between blood and SF lymphocytes of RA patients with respect to their responses to the aggregate-free HGG and to PHA. Incubation of RA-SF cells but not RA-blood cells with aggregate-free HGG before their culture with the aggregated HGG markedly suppressed the in vitro proliferative response to the latter. The observed differences between blood and SF lymphocytes and the suppression of blastogenic response of SF cells by exposure to the aggregate-free preparation raise the possibility of modulating the immune and/or the inflammatory responses in RA.

Adult↗
PubMedDate not supplied

Purification and some properties of collagenase proenzyme activator from rheumatoid synovial fluid.

1. An activator of leucocyte latent collagenase has been extracted from rheumatoid synovial fluid by a preparative method consisting of six steps including precipitation by ammonium sulphate and chromatography on Sephadex G-100, QAE-Sephadex and SP-Sephadex C-50. The purification factor was nearly 1000 and the activator isolated could be shown to have a high degree of homogeneity.--2. Gel chromatography indicated a molecular weight of ca. 60 000.--3. Kinetic studies of the activation and inactivation of the activator during incubation at higher temperatures demonstrated its enzymic nature.--4. Activation of latent collagenase was partially inhibited by iPr2P-F and KCN. Soybean trypsin inhibitor, iodoacetamide, TosLysCH2Cl and TosPheCH2Cl had no effect.--5. Leucocyte latent collagenase was also activated by an excess of trypsin and p-hydroxymercuribenzenesulphonic acid, but only to the extent of about 40% of its activation capacity. Purified neutral protease from human leucocyte granules had no effect on latent collagenase.--6. Several typical substrates for proteases, peptidases, esterases and glycosidases were not attacked by the activator. The possibility that the activator is a known enzyme, such as kallikrein, urokinase or cathepsin B1, could be excluded.

Arthritis, Rheumatoid↗
PubMed2004

Hyaluronan in horses: physiological production rate, plasma and synovial fluid concentrations in control conditions and following sodium hyaluronate administration.

REASONS FOR PERFORMING STUDY: Hyaluronic acid (HA) is an endogenous glycosaminoglycan used in the treatment of joint diseases, but medication control is required by horseracing authorities. Therefore, a medication control policy needs to be established. OBJECTIVES: To establish physiological plasma HA concentrations in post race horses, determine the HA endogenous production rate and document the disposition of HA after i.v. and intra-articular hyaluronic acid administration at recommended therapeutic doses. METHODS: Hyaluronan concentrations in plasma were determined using an ELISA specific test; concentrations in synovial fluid were determined using a radiometric binding assay. RESULTS: The overall mean plasma HA concentration in 120 post competition horses was 89 ng/ml. In a group of 6 experimental horses, synovial fluid control concentration was 328+/-112 microg/ml. After i.v. sodium hyaluronate administration (37.8 mg in toto), the terminal half-life was very short (43+/-29 mins) and after a delay of 3 h, the plasma concentration returned to control values. The endogenous HA production rate was 33-164 mg in toto per day, i.e. 1-4 times the recommended i.v. daily dose. Twenty-four hours after intra-articular administration, HA concentration was not significantly different from control values (328+/-112 microg/ml). CONCLUSIONS AND POTENTIAL RELEVANCE: Due to the rapid disappearance of HA from plasma after i.v. administration and from the joint after intra-articular administration, long-term detection needs a more appropriate approach to be developed.

Analysis of Variance↗
PubMed1998

Identification of matrix metalloproteinases (MMPs) in synovial fluid from patients with temporomandibular disorder.

Proteolytic enzymes with gelatinolytic activity in the synovial fluid (SF) of temporomandibular joint (TMJ) arthropathies were assayed by gelatin-impregnated gel enzymography. SF samples were collected from 10 TMJs in patients with closed lock (CL) condition and 5 TMJs from asymptomatic healthy volunteers. Two proteinases with gelatinolytic activities at 92 kDa and 72 kDa were detected in both the normal and the diseased TMJs. Also detected were weak bands at molecular weights of 83 kDa and 66 kDa. All of these proteinase activities were inhibited by EDTA and tissue inhibitor of metalloproteinases (TIMP), required Ca2+ for activation, and were detected with gelatin but not casein as substrate, suggesting that these enzymes were matrix metalloproteinases (MMPs). The 72 kDa and 66 kDa bands further reacted with anti-MMP-2 antibody by Western blot analysis, and the proteinases in the TMJ-SF could cleave type IV collagen in vitro without any activation. These four activities identified by enzymography were, therefore, identified as 92 kDa-gelatinase (proMMP-9), 83 kDa-gelatinase (active MMP-9), 72 kDa-gelatinase (proMMP-2) and 66 kDa-gelatinase (active MMP-2). Densitometric analyses of these bands revealed higher levels of the active form of MMP-9 in the CL patients compared to controls. These findings suggest that MMP-2 and -9 could be dominant proteinases in the TMJ-SF and possibly reflect TMJ pathology.

Adolescent↗
PubMed1987

Inhibitor of interleukin-2 synthesis and response in rheumatoid synovial fluid.

We studied the effects of a factor present in rheumatoid arthritis (RA) synovial fluid (SF) on interleukin-2 (IL-2)-dependent cell proliferation and on the production of IL-2 by mitogen-stimulated peripheral blood mononuclear cells. RA SF suppressed the responsiveness of a mouse T cell line (HT-2) to IL-2, indicating that it contained an inhibitor of the IL-2 response. When RA SF was fractionated by Sephadex G-200 gel filtration, the inhibitory activity was detected mainly in fractions with a molecular weight of approximately 150,000, but was also found in a 15-19-kd fraction. Removal of IgG from the 150-kd fraction, by means of an anti-IgG affinity column, did not reduce the activity of the fraction, nor was activity found in the eluted IgG. The inhibitory fractions reduced mouse thymocyte proliferative responses to IL-1 in the presence of phytohemagglutinin, and reduced the production of IL-2 by human peripheral blood mononuclear cells, but did not inhibit IL-1-induced human foreskin fibroblast proliferation; this suggests that the factor was not an IL-1 inhibitor. The inhibitory activity of the RA SF factor was blocked by an antibody against an inhibitor of IL-2 that was purified from a culture of the human monocytic leukemia cell line, THP-1. This finding also supports the conclusion that RA SF contains an IL-2 inhibitory factor. The observed inhibition of both IL-2 synthesis and IL-2 response suggests that the target of the inhibition was the T lymphocyte.

Animals↗
PubMed1993

Degradation of human articular cartilage by neutrophils in synovial fluid.

OBJECTIVE: To determine whether surface-adherent immunoglobulins are capable of mediating synovial fluid (SF) neutrophil degradation of proteoglycan and collagen in intact, normal human articular cartilage, and to define the respective roles of neutrophil serine proteases and metalloproteases in degrading these cartilage constituents. METHODS: Pellet explants of normal human articular cartilage pretreated with bovine serum albumin (BSA) or IgG were incubated with polymorphonuclear cells suspended in SF (PMN-SF), or with supernatants derived from neutrophils stimulated with surface-associated IgG. Proteoglycan degradation was measured by assaying release of 35S-proteoglycan fragments from cartilage explants prelabeled with 35S-sulfate. Collagen degradation was measured by assaying hydroxyproline content in the PMN-SF preparations or neutrophil supernatants following their incubation with unlabeled explants. RESULTS: Significant release of both 35S fragments and hydroxyproline was noted following incubation of PMN-SF with IgG-treated pellets, compared with pellets treated with BSA. IgG preparations derived from pooled normal serum or rheumatoid arthritis SF were equally efficacious in mediating PMN degradation of cartilage collagens. Explant release of 35S fragments during incubation with PMN supernatant was completely inhibited when serine proteases were inactivated by diisopropyl fluorophosphate (DFP); however, release of 35S fragments was enhanced when metalloprotease activity was present in the supernatant. Release of hydroxyproline during incubation of explants with PMN supernatant was comparable in the presence of DFP or EDTA, but was markedly enhanced when both serine and metalloprotease activity were present in the supernatant. CONCLUSION: Neutrophils in SF are capable of degrading both proteoglycans and collagens in intact human articular cartilage. Degradation of these cartilage constituents is facilitated by immunoglobulins adherent to the cartilage surface and by the synergistic action of PMN serine and metalloproteases released during activation of neutrophils with surface-associated immunoglobulin.

Arthritis, Rheumatoid↗