SEARCH · Search PubMed

Results for “SYNOVIAL FLUID”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 721 records · Page 40Linked to original sources

PubMed1991

Reproducibility of synovial fluid examination for crystals.

A quality assurance survey of synovial fluid examination for crystals was performed at six teaching hospitals. Aliquots of 12 different fluids (three with no crystals, one with betamethasone crystals, four with calcium pyrophosphate dihydrate (CPPD) crystals and four with monosodium urate monohydrate [urate] crystals) were examined by all six laboratories. Four laboratories performed well (10 or more correct out of 12) but two did poorly (50% or less correct). False positive crystal identification occurred in eight of 72 samples, but all false positive reports were from two laboratories. CPPD and urate crystals were missed in seven of 24 (29%) and five of 24 (21%) samples respectively. The standard of synovial fluid examination for crystals in Sydney teaching hospitals is not uniform and in some cases appears unsatisfactory.

Betamethasone↗

PubMed1994

Preliminary study of the tryptase levels in the synovial fluid of patients with inflammatory arthritis.

This study examined levels of tryptase, a specific mast cell product, in synovial fluid. Samples of synovial fluid from eight patients with rheumatoid arthritis and ten with other arthritides were measured in solid-phase immunoradiometric assays. Elevated concentrations of tryptase were present in samples from three patients with rheumatoid arthritis, one with psoriasis, and one with Reiter's syndrome. The data support the theory that mast cell activation is involved in the pathogenesis in some inflammatory joint diseases, but activation does not appear to be disease specific.

Adult↗

PubMed1993

Purification and characterization of hyaluronan from synovial fluid.

An easy and rapid method for the purification and characterization of hyaluronan from synovial fluid has been developed. Lipids were removed by filtration through a hydrophobic filter prior to the removal of proteins by phenol-chloroform extraction. The hyaluronan recovery was 95%, as measured by three different methods. The average molecular weight of hyaluronan did not change during the purification. Furthermore, it was found that an optimized enzymatic protein digestion of pathological human synovial fluid prior to filtration yielded up to five times more hyaluronan recovered. In addition, the molecular weight of hyaluronan from synovial fluid not digested with pronase E was apparently higher because of the presence of aggregates. After the purification of hyaluronan (ca. 15 min), a single size-exclusion chromatography step allowed the simultaneous determination of its concentration and the reasonable estimate of its average molecular weight and molecular weight distribution curve. The logarithm of the molecular weight showed a linear dependence on the size-exclusion chromatography elution volume for hyaluronan in the molecular weight range 2.0 x 10(6)-1.0 x 10(4). The removal of proteins allowed the determination of fairly low-molecular-weight fractions of hyaluronan, compared to untreated samples for which hyaluronan and protein peaks partially overlap.

Chromatography, Gel↗

PubMed1991

Neutrophils isolated from the synovial fluid of patients with rheumatoid arthritis: priming and activation in vivo.

The oxidative metabolism of neutrophils isolated from the bloodstream and synovial fluid of 16 patients with rheumatoid arthritis was compared by measuring the ability of neutrophils to generate luminol dependent chemiluminescence and to secrete O2-. Measurements of receptor mediated--that is, N-formyl-methionyl-leucyl-phenylalanine stimulated--activation or receptor and second message independent--that is phorbol myristate acetate stimulated--activation showed that synovial fluid neutrophils had biochemical characteristics to suggest that they had been either up-regulated (primed) or down-regulated (activated) in vivo. These conclusions were confirmed by comparison of these responses with the changes in oxidative metabolism observed during in vitro priming and activation of control neutrophils: synovial fluid neutrophils possessed lower levels of myeloperoxidase than paired bloodstream cells, and unlike bloodstream cells could not be primed in vitro. These data thus suggest that synovial fluid neutrophils have been exposed to both priming and activating agents within rheumatoid joints.

Adult↗

PubMed1975

Demonstration of boundary lubrication by synovial fluid.

An account is given of an oscillatory rotating friction measurement apparatus which can be used for demonstration of boundary lubrication by synovial fluid when rubber and glass are employed as rubbing surfaces. A technical description of the apparatus is given. The greatest importance is placed on getting the apparatus to demonstrate reproducible results when saline and normal bovine synovial fluid are used as lubricant. The greatest variations are caused by differences in the cleaning of the rubber and in its tension. On the basis of bovine synovial fluid from ten different hock joints investigations were made of individual variations and changes occurring during storage at 4 degrees C. The individual variations were found to be of no importance; a decrease in the lubricating effect was observed only after storage for two months. Addition of trypsin confirmed that boundary lubrication by synovial fluid can be related to the protein component. The conclusion is that the apparatus is considered suitable for clinical investigations of boundary lubrication in connection with different joint diseases.

Animals↗

PubMed1987

In vitro protein binding of diclofenac sodium in plasma and synovial fluid.

The in vitro protein binding behavior of diclofenac sodium (sodium[o-(2,6-dichloroanilino)phenyl]acetate) in plasma and synovial fluid was investigated by equilibrium dialysis. The drug was highly protein bound (approximately 99.5%) and the extent of binding remained constant for drug concentrations of 2-10 micrograms/mL. Comparable results were obtained with human serum albumin solution (45 g/L) indicating that albumin is probably the responsible protein. The extent of binding remained relatively constant for drug concentrations of 0.25-10 micrograms/mL when albumin concentrations were greater than 25 g/L. For albumin concentrations less than 10 g/L, the extent of binding tended to decrease with increased drug concentration. This concentration (10 g/L) is substantially lower than that usually observed in plasma or synovial fluid of arthritic patients. Curvature of the Scatchard plot indicated the existence of two classes of sites. Excellent results were obtained from fitting of the data according to two classes of sites (r2 greater than 0.999). Parameter estimates (SEM) of the number of binding sites, n1 and n2, and the corresponding association constants, k1 and k2, were 2.26 (0.55), 10.20 (0.69), and 1.32 (0.54) X 10(5) M-1, and 3.71 (1.11) X 10(3) M-1, respectively. Simultaneous samples obtained from arthritic patients indicate considerably higher total protein and albumin concentrations in plasma compared with synovial fluid, but the albumin:total protein ratios were essentially the same. There was very little difference in plasma binding in arthritic patients compared with normal subjects. The extent of binding in synovial fluid samples was consistently lower than that for plasma samples (mean +/- SD of 99.5 +/- 0.2% versus 99.7 +/- 0.1%, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)

Albumins↗

PubMed1990

Tumour necrosis factor in serum and synovial fluid of patients with active and severe rheumatoid arthritis.

Fifteen serum samples and 29 synovial fluids of patients with rheumatoid arthritis (RA) were examined for the presence of tumour necrosis factor (TNF). The assay for TNF was based on the cytotoxic activity of this cytokine for human melanoma cells in tissue culture. High concentrations of TNF were found in serum samples of patients with severe RA, who had increased erythrocyte sedimentation rate and serum alpha 2 macroglobulin, but decreased haemoglobin and serum iron concentrations. Tumour necrosis factor was also found in the synovial fluid of 16 out of 29 patients. High TNF concentrations were found in fluids with greater than 10(10) leucocytes/l. Tumour necrosis factor was not detected in the serum of normal subjects or in synovial fluid of patients with osteoarthritis. A mediator of inflammation, such as TNF, may contribute to the severity of RA.

Arthritis, Rheumatoid↗

PubMed1994

[Fibronectin in the synovium and synovial fluid in rheumatoid arthritis and in osteoarthritis].

Fibronectin (FN) in the rheumatoid, and osteoarthritic, synovium was examined by light microscopy using immunostaining by fluorescein-labeled anti-fibronectin, or by peroxidase-labeled anti-fibronectin. Immunofluorescent FN was found more in the rheumatoid synovium than in the osteoarthritic synovium. The mean fluorescence intensity in a given area of the synovium including the synovial surface in rheumatoid arthritis was significantly higher than in osteoarthritis. As there was a significant correlation between the fluorescence intensity in the synovium and the number of synovial lining cells immunostained with peroxidase-labeled anti-fibronectin, the fluorescence intensity appeared to depend on the number of synovial lining cells containing FN. FN in the rheumatoid synovium and synovial fluid cells was examined by electron microscopy after immunoperoxidase staining. Immunoelectron microscopy of the rheumatoid synovium demonstrated FN on the surface of both type-A and type-B cells, the collagen fibers, and within the mitochondria, in the endoplasmic reticulum of type-B cells, and in the intercellular contact zone. These findings suggested that FN was mainly produced in the type-B cells, and played a role in maintaining the synovial structure. Immunoelectron microscopy of the rheumatoid synovial fluid cells confirmed the presence of FN on their surfaces. This suggested that FN opsonized by adhering debris to FN on the cell surfaces in the synovial fluid. The concentration of FN in the rheumatoid, and osteoarthritic, synovial fluids was measured by single radial immunodiffusion. The FN concentration in the rheumatoid synovial fluids was significantly higher than in the osteoarthritic synovial fluids. However, it was not significantly correlated with the indices of inflammatory activity such as with the C-reactive protein, the erythrocyte sedimentation rate, or catalase activity measured by a gasometry, or with the number of polymorphonucleated cells.

Adult↗

PubMed1979

The significant reduction of high molecular weight-kininogen in synovial fluid of patients with active rheumatoid arthritis.

It has been proposed that kinin system was implicated in inflammatory joint diseases such as rheumatoid arthritis. Our present work provides further support on the involvement of the kinin system. In osteoarthritis patients, the total, high molecular weight (HMW)-, and low molecular weight (LMW)-kininogen levels in synovial fluid were not different from those in plasma. On the contrary, in rheumatoid patients, HMW-kininogen level in synovial fluid was significantly lower than that in plasma, whereas LMW-kininogen level in synovial fluid was not different from that in plasma. The reduction of HMW-kininogen level in synovial fluid was much more marked in active cases of those who showed high blood sedimentation rate and high C-reactive protein value. Furthermore, the reduction was closely related to the clinical severity. In active rheumatoid patients, HMW-kininogen level was further reduced in the synovial fluid after withdrawal of indomethacin.

Adult↗

PubMed1992

Determination of total protein concentration and viscosity of synovial fluid from the tibiotarsal joints of horses.

Viscosity of synovial fluid (SF) from 29 clinically normal horses was determined by use of a rotational cone and plate microviscosimeter. Total protein concentration in the SF of the 29 horses, as measured with a refractometer, was less than 2.5 g/dl. When the Coomassie brilliant blue test was used to determine total protein concentration in SF for 15 horses, the mean value was 1,088 mg/dl. Viscosity values at 60, 30, 12, 6, 3, and 1.5 revolutions/min (rpm) spindle speed were 4.41 +/- 1.54 centipoise (cp), 5.29 +/- 1.94 cp, 6.76 +/- 2.76 cp, 8.52 +/- 4.27 cp. 10.41 +/- 6.30 cp, and 13.07 +/- 9.05 cp, respectively. Synovial fluid viscosity increased with decreasing rpm and shear rate, but the shape of the curve for each horse fitted the asymptotic curve. The rotational cone and plate microviscosimeter was an accurate instrument in measuring SF viscosity at multiple rpm or shear rates in horses. The values obtained on clinically normal horses in this study will serve as a baseline for comparison in the evaluation of horses with joint disease.

Animals↗

PubMed1985

An assay for estimating the cytotoxicity of synovial fluid from patients with rheumatoid arthritis.

The joint is the prime site of involvement in rheumatoid arthritis: the synovium showing lymphocytic involvement and damage. The synovial fluid shows evidence of inflammation such as increased neutrophils and raised CRP. Application of a cell-free extract of serum or synovial fluid from patients with rheumatoid arthritis, or serum from normal individuals on to 111indium oxine radiolabelled endothelial cells and fibroblasts, promotes the release of the isotope as a result of cell damage and death (cytotoxicity). In paired samples, synovial fluid was consistently more cytotoxic than rheumatoid serum. There was no difference in the cytotoxicity of rheumatoid serum or normal serum. These results demonstrate the presence of soluble factors in synovial fluid, which are capable of destroying cells, typical of those found in the synovial cavity, in blood vessels and in connective tissue generally. This system may prove to be a useful model of inflammatory damage.

Arthritis, Rheumatoid↗

PubMed1993

Neutral endopeptidase (3.4.24.11) in plasma and synovial fluid of patients with rheumatoid arthritis. A marker of disease activity or a regulator of pain and inflammation?

In recent years the role of the peripheral nervous system has been focused on the pathogenesis of rheumatoid arthritis (RA). In particular, substance P (SP), released by the sensory terminals, has been demonstrated to be involved in cartilage breakdown [13]. The aim of our work was to study the levels of SP and its peptidases, neutral endopeptidase (3.4.24.11) (NEP) and angiotensin-converting enzyme (ACE), in the synovial fluid and plasma of 30 patients with RA and 14 patients with osteoarthritis (OA). ACE and NEP were determined with a fluorimetric assay and SP with a radioimmunoassay (RIA) method. ACE levels were normal in the plasma of patients with RA and OA (6.1 +/- 1.9 and 6.7 +/- 1.4 pmol/ml/min, respectively); we found no differences in the values, of ACE between RA and OA synovial fluid (5.7 +/- 4.2 and 5.5 +/- 4.1 pmol/ml/min, respectively). NEP levels were significantly increased in plasma (139.3 +/- 36 pmol/ml/min) and synovial fluid (133.8 +/- 32 pmol/ml/min) of patients with RA when compared to patients with OA (73.4 +/- 22 in plasma and 15.2 +/- 10.8 pmol/ml/min in synovial fluid) and healthy controls (89.7 +/- 14 pmol/ml/min in plasma). In synovial fluid, SP was significantly higher in RA patients (43.1 +/- 16.6 pg/ml) than in OA patients (12 +/- 13.1 pg/ml), while plasma levels did not show any difference (RA: 14.4 +/- 10.2; OA: 13.6 +/- 10.6; healthy subjects: 11.3 +/- 3.9 pg/ml). The only relationship detected in controls and in OA was among plasma NEP and ESR (P < 0.05) and synovial fluid NEP (P < 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1999

Increased levels of lactoferrin in synovial fluid but not in serum from patients with rheumatoid arthritis.

Lactoferrin is a multifunctional immunoregulatory protein, stored in specific granules of neutrophil granulocytes, from which it is released following cell activation. As activated neutrophils play a crucial role in the destruction of synovial joints in rheumatoid arthritis, we evaluated lactoferrin concentration in synovial fluid and sera from 21 patients with rheumatoid arthritis and 11 patients with osteoarthritis. We also measured lactoferrin levels in sera from 12 healthy controls. Lactoferrin was measured by a solid-phase inhibition immunoassay. Median lactoferrin levels were significantly higher in synovial fluid from rheumatoid arthritis than from osteoarthritis patients (P = 0.0002). In contrast, no significant difference was found between serum lactoferrin from patients with rheumatoid arthritis or osteoarthritis compared with normal controls. In patients with rheumatoid arthritis, lactoferrin concentrations were higher in synovial fluid than in sera (P = 0.036). In both rheumatoid arthritis and osteoarthritis no correlation was found between serum and synovial fluid lactoferrin (P = 0.51 and P = 0.5, respectively). In synovial fluid from patients with rheumatoid arthritis, lactoferrin concentrations correlated with neutrophil granulocyte count (P < 0.0001), but neither serum nor synovial lactoferrin levels correlated with disease activity (P = 0.32 and P = 0.25, respectively). In conclusion, lactoferrin is a reliable marker of neutrophil activation at sites of inflammation in rheumatoid synovitis, but does not represent a marker of disease activity.

Adult↗

PubMed1997

Neutrophils from the synovial fluid of patients with rheumatoid arthritis express the high affinity immunoglobulin G receptor, Fc gamma RI (CD64): role of immune complexes and cytokines in induction of receptor expression.

Neutrophils isolated from the synovial fluid of 16/24 patients with rheumatoid arthritis expressed Fc gamma RI (CD64), the high-affinity receptor for monomeric immunoglobulin G (IgG), on their cell surface. Receptor expression ranged from 17% to 168% of the level of expression obtained after incubation of control blood neutrophils with 100 U/ml interferon-gamma (IFN-gamma) for 24 hr in vitro. Similarly, mRNA for Fc gamma RI was detected in synovial fluid neutrophils from 12/15 patients and transcript levels ranged from 5% to 200% of the values obtained after treatment of blood neutrophils with IFN-gamma for 4 hr in vitro. No surface expression nor mRNA were detected in freshly isolated blood neutrophils from either patients or from healthy controls. Addition of cell-free synovial fluid to control blood neutrophils induced both mRNA and surface expression of Fc gamma RI to levels that were comparable to those achieved after addition of IFN-gamma. Neither soluble nor insoluble immune complexes appeared to be involved in induction of Fc gamma RI expression in spite of the ability of these complexes to induce protein biosynthesis. Synovial fluid-induced expression of Fc gamma RI was partially blocked by incubation with neutralizing IFN-gamma antibodies, whilst neutralizing interleukin (IL)-6 antibodies had little effect. Levels of IFN-gamma measured within these synovial fluids ranged from 0 to 2.7 U/ml, well within the range known to induce neutrophil Fc gamma RI expression. These data thus indicate that gene expression in synovial fluid neutrophils is selectively activated as the cells enter the diseased joint. Furthermore, these data indicate that induced expression of Fc gamma RI may alter the ability of infiltrating neutrophils to respond to IgG-containing immune complexes present in these joints.

Antigen-Antibody Complex↗

PubMed1997

Postmortem alcohol analysis of the synovial fluid and its availability in medico-legal practices.

Alcohol analyses using the synovial fluid of the knee joint (synovial alcohol concentration, SAC) as well as blood (BAC) and urine (UAC) were performed by the pulse heating-gas chromatographic method in 12 medico-legal autopsy cases. In 11 of the 12 cases, the regression analysis showed that BAC and UAC had a fairly linear relationship with SAC, and the average ratios of the BAC/SAC and UAC/SAC were 0.76 +/- 0.12 (range 0.60-0.94) and 1.03 +/- 0.11 (range 0.90-1.21), respectively. The measured BACs showed a difference of 11.8 +/- 9.4% (0.9-27.1%) when compared with the calculated BACs by means of the average BAC/SAC ratio. Between the measured UACs and the calculated UACs, there was an average difference of 7.9 +/- 6.0% (0.3-17.8%). The present study demonstrates that the synovial fluid is one of the available biological specimens for the prediction of BAC or UAC within a range in autopsy cases in which suitable blood and/or urine specimens cannot be obtained.

Adult↗

PubMed1985

Disease distribution of synovial fluid mast cells and cytophagocytic mononuclear cells in inflammatory arthritis.

Three hundred and twenty-one synovial fluids from the knees of patients with six different inflammatory arthropathies have been examined for the presence of cytophagocytic monocytes (CPM) and mast cells. Both cell types were seen independently in many of the fluids examined but were found together only in those patients with Reiter's disease, psoriatic arthritis, ankylosing spondylitis, and enteropathic arthritis. These four disease groups also contain the highest proportion of patients with mast cells in their synovial fluids and those individuals with the greatest number of synovial fluid CPM. Criteria have been developed from these observations which may be employed in the differential diagnosis of inflammatory arthropathies.

Arthritis↗

PubMed1989

Pathogenesis of ovine lentivirus-induced arthritis: phenotypic evaluation of T lymphocytes in synovial fluid, synovium, and peripheral circulation.

Sheep and goats develop a chronic, progressive arthritis reminiscent of rheumatoid arthritis, but caused by lentiviruses related to human immunodeficiency virus. The distribution of T lymphocytes in peripheral circulation of two infected sheep with arthritis, one infected sheep with interstitial pneumonia, three asymptomatic sheep, and three uninfected sheep was evaluated. Sheep with clinical disease have depressed ratios of CD4/CD8 lymphocytes in peripheral circulation compared to asymptomatic and uninfected animals. In one sheep, the depressed ratio was due to an absolute increase in CD8-positive lymphocytes. The predominant lymphocyte populations in both synovial fluid and synovium from this animal were also CD8 positive. Macrophages were the other predominant cell population in synovial fluid and were infected with lentivirus. Little cell-free virus was detected in the synovial fluid, although 1 in 400 cells was infected as determined by infectious center assays. Infected cells in the synovial fluid had a reduction in virus gene expression compared to infected cells in peripheral circulation. This reduction in virus gene expression may be due to the presence of interferon-like activity in the synovial fluid.

Animals↗

PubMed1997

Nucleotide pyrophosphohydrolase in human synovial fluid.

OBJECTIVE: To identify the molecular forms of ectonucleotide pyrophosphohydrolase (NTPPHase) in human synovial fluid (SF). METHODS: We examined synovial fluids from 32 patients with various joint diseases [10 calcium pyrophosphate dihydrate (CPPD) deposition disease; 7 osteoarthritis (OA); 6 rheumatoid arthritis (RA); 3 after total knee arthroplasty (TKA); 6 olecranon bursa] and 3 normal joint fluids. Joint fluids were analyzed after sequential centrifugation for NTPPHase activity and by Western blot using polyclonal antibodies against 127 kDa porcine articular cartilage vesicle-associated NTPPHase and against PC-1 and 58 kDa, 2 other ecto-NTPPHases. Lysate from human synoviocytes, porcine chondrocytes, and their conditioned media were examined using antibodies to these ecto-NTPPHases. Radiographs of joints from which fluid was obtained were graded for degenerative changes 0-4 using a standard method. RESULTS: NTPPHase activity was found in all pathological and normal SF tested and correlated with the degree of radiographic degeneration (r = 0.55, p < 0.05). NTPPHase specific activity in ultracentrifugation pellets was highest in CPPD deposition disease fluids (p < 0.05). 127 kDa enzyme was found in both sedimentable and soluble fractions from CPPD, OA, TKA, and normal fluids, and was extensively degraded in all inflammatory fluids. Intact 115 kDa PC-1 was found only in the 2 CPPD fluids with the highest NTPPHase activity. 58 kDa enzyme was found in most fluids, predominantly in the soluble fraction. 127 kDa protein was identified in human synoviocyte conditioned media but not in cell lysate, while PC-1 and 58 kDa proteins were found in the cell lysate but not in the conditioned media. CONCLUSION: There was no disease specific association with any one ecto-NTPPHase. Total enzyme activity correlated with the degree of degenerative change. The specific activity of pelletable 127 kDa enzyme was higher in fluids containing CPPD crystals. All 3 ecto-NTPPHases or their presumed degradation products were detectable in some pathologic and normal fluids. A 200 kDa reactive band often accompanied reactivity to the 127 kDa enzyme. PC-1 and 127 kDa proteins were extensively degraded in inflammatory SF, while 58 kDa protein was not. The relative contribution of each of these enzymes to inorganic pyrophosphate production by human joint tissues remains unclear.

Animals↗