acid-phosphatase and Arthritis

Arthritogenic alphaviruses including Ross River virus (RRV), Sindbis virus, and chikungunya virus cause worldwide outbreaks of musculoskeletal disease. The ability of alphaviruses to induce bone pathologies remains poorly defined. Here we show that primary human osteoblasts (hOBs) can be productively infected by RRV. RRV-infected hOBs produced high levels of inflammatory cytokine including IL-6. The RANKL/OPG ratio was disrupted in the synovial fluid of RRV patients, and this was accompanied by an increase in serum Tartrate-resistant acid phosphatase 5b (TRAP5b) levels. Infection of bone cells with RRV was validated using an established RRV murine model. In wild-type mice, infectious virus was detected in the femur, tibia, patella, and foot, together with reduced bone volume in the tibial epiphysis and vertebrae detected by microcomputed tomographic (µCT) analysis. The RANKL/OPG ratio was also disrupted in mice infected with RRV; both this effect and the bone loss were blocked by treatment with an IL-6 neutralizing antibody. Collectively, these findings provide previously unidentified evidence that alphavirus infection induces bone loss and that OBs are capable of producing proinflammatory mediators during alphavirus-induced arthralgia. The perturbed RANKL/OPG ratio in RRV-infected OBs may therefore contribute to bone loss in alphavirus infection.

Topics: Acid Phosphatase; Adult; Alphavirus Infections; Animals; Antibodies, Neutralizing; Arthritis; Bone and Bones; Bone Resorption; Female; Growth Plate; Humans; Inflammation Mediators; Interleukin-6; Isoenzymes; Male; Mice; Mice, Inbred C57BL; Neutralization Tests; Osteoblasts; Osteoclasts; Osteogenesis; Osteoprotegerin; Phenotype; RANK Ligand; Ross River virus; Synovial Fluid; Tartrate-Resistant Acid Phosphatase; Virus Replication; X-Ray Microtomography

Rheumatoid arthritis (RA) is a chronic inflammatory disease characterized by bone erosion and cartilage destruction in the joints. Many of the conventional antiarthritic drugs are effective in suppressing inflammation, but they do not offer protection against bone damage. Furthermore, the prolonged use of these drugs is associated with severe adverse reactions. Thus, new therapeutic agents that can control both inflammation and bone damage but with minimal side effects are sought. Celastrus is a Chinese herb that has been used for centuries in folk medicine for the treatment of various inflammatory diseases. However, its utility for protection against inflammation-induced bone damage in arthritis and the mechanisms involved therein have not been examined. We tested celastrus and its bioactive component celastrol for this attribute in the adjuvant-induced arthritis model of RA. The treatment of arthritic rats with celastrus/celastrol suppressed inflammatory arthritis and reduced bone and cartilage damage in the joints as demonstrated by histology and bone histomorphometry. The protective effects against bone damage are mediated primarily via the inhibition of defined mediators of osteoclastic bone remodeling (e.g. receptor activator of nuclear factor-κB ligand (RANKL)), the deviation of RANKL/osteoprotegerin ratio in favor of antiosteoclastic activity, and the reduction in osteoclast numbers. Furthermore, both the upstream inducers (proinflammatory cytokines) and the downstream effectors (MMP-9) of the osteoclastogenic mediators were altered. Thus, celastrus and celastrol controlled inflammation-induced bone damage by modulating the osteoimmune cross-talk. These natural products deserve further consideration and evaluation as adjuncts to conventional therapy for RA.

Topics: 3T3 Cells; Acid Phosphatase; Animals; Arthritis; Autoimmune Diseases; Bone and Bones; Celastrus; Cell Line; Fibroblasts; Immune System; Inflammation; Isoenzymes; Macrophages; Mice; Pentacyclic Triterpenes; Plant Extracts; Rats; Rats, Inbred Lew; Synovial Membrane; Tartrate-Resistant Acid Phosphatase; Triterpenes

Extract of the whole plant, Ajuga decumbens (KE) has long been used in China as a medication for the relief of joint pain. Previously, we proved that KE up-regulated the synthesis of collagen in false aged model rats. In this paper we examined the effects of KE on nitric oxide (NO) production, expression of inducible nitric oxide synthase (iNOS), osteoblast and osteoclast activity. We also investigated whether KE had any anti-osteoporosis or anti-arthritic activity by using ovariectmized mice and adjuvant induced arthritic rats. KE exhibited down-regulation of differentiation into osteoclast and up-regulation of mineralization in osteoblast-like MC3T3-E1 cells in a concentration-dependent manner. NO synthesized by iNOS plays important roles in inflammatory disease and imbalance between bone resorption and bone formation caused by estrogen depletion. KE inhibited expression of iNOS which caused concentration dependent inhibition of NO production. Furthermore, KE prevented brittle bones in ovariectomized mice and swelling of the left hind ankle in adjuvant induced arthritic rats. Therefore, KE improved the balance of bone resorption and bone formation, showing anti-inflammatory effects. Consequently, KE is beneficial for sufferers of bone and joint disease.

Topics: 3T3 Cells; Acid Phosphatase; Ajuga; Animals; Anthraquinones; Arthritis; Arthritis, Experimental; Bone Resorption; Calcium; Coculture Techniques; Collagen; Coloring Agents; Female; Freund's Adjuvant; Isoenzymes; Male; Mice; Nitric Oxide; Nitric Oxide Synthase Type II; Osteoclasts; Osteoporosis; Ovariectomy; Phytotherapy; Plant Extracts; Rats; Rats, Inbred Lew; Tartrate-Resistant Acid Phosphatase

Large osteoclasts (>or=10 nuclei) predominate at sites of pathological bone resorption. We hypothesized this was related to increased resorptive activity of large osteoclasts and have demonstrated previously that larger osteoclasts are 8-fold more likely to be resorbing than small osteoclasts (2-5 nuclei). Here we ask whether these differences in resorptive activity can be explained by differences in expression of factors involved in osteoclast signaling, fusion, attachment, and matrix degradation. Authentic rabbit osteoclasts and osteoclasts derived from RAW264.7 cells showed similar increases in c-fms expression (1.7- to 1.8-fold) in large osteoclasts suggesting that RAW cells are a viable system for further analysis. We found 2- to 4.5-fold increases in the expression of the integrins alpha(v) and beta(3), the proteases proMMP9, matMMP9 and pro-cathepsinK, and in activating receptors RANK, IL-1R1, and TNFR1 in large osteoclasts. In contrast, small osteoclasts had higher expression of the fusion protein SIRPalpha1 and the decoy receptor IL-1R2. The higher expression of activation receptors and lower expression of IL-1R2 in large osteoclasts suggest they are hyperresponsive to extracellular factors. This is supported by the observation that the resorptive activity in large osteoclasts was more responsive to IL-1beta, and that this increased activity was inhibited by the IL-1 receptor antagonist, IL-1ra. This increased responsiveness of large osteoclasts to IL-1 may, in part, explain the pathological bone loss noted in inflammatory diseases. The heterogeneity in receptor expression and the differential response to cytokines and their antagonists could prove useful for selective inhibition of large osteoclasts actively engaged in pathological bone loss.

Topics: Acid Phosphatase; Animals; Arthritis; Cell Line; Cytokines; Enzyme Precursors; Immunoblotting; Inflammation; Integrin alpha1beta1; Interleukin 1 Receptor Antagonist Protein; Interleukin-1beta; Isoenzymes; Macrophage Colony-Stimulating Factor; Matrix Metalloproteinase 9; Mice; Osteoclasts; Rabbits; RANK Ligand; Receptor Activator of Nuclear Factor-kappa B; Receptor, Macrophage Colony-Stimulating Factor; Receptors, Immunologic; Reverse Transcriptase Polymerase Chain Reaction; Tartrate-Resistant Acid Phosphatase; Tumor Necrosis Factor-alpha

Peri-articular bone resorption is a feature of arthritis due to crystal deposition and rheumatoid disease. Under these conditions, the synovial fluid contains numerous inflammatory cells that produce cytokines and growth factors which promote osteoclast formation. The aim of this study was to determine whether inflammatory synovial fluid stimulates the formation of osteoclasts. Synovial fluid from rheumatoid arthritis (RA), pyrophosphate arthropathy (PPA) and osteoarthritis (OA) patients was added to cultures (n=8) of human peripheral blood mononuclear cells (PBMCs) in the presence and absence of macrophage colony-stimulating factor (M-CSF) and the receptor activator of NF-kappaB ligand (RANKL). Osteoclast formation was assessed by the formation of cells positive for tartrate-resistant acid phosphatase (TRAP) and vitronectin receptor (VNR) and the extent of lacunar resorption. The addition of 10% OA, RA and PPA synovial fluid to PBMC cultures resulted in the formation of numerous multinucleated or mononuclear TRAP(+) and VNR(+) cells which were capable of lacunar resorption. In contrast to PBMC cultures incubated with OA synovial fluid, there was marked stimulation of osteoclast formation and resorption in cultures containing inflammatory RA and PPA synovial fluid which contained high levels of tumour necrosis factor alpha, a factor which is known to stimulate RANKL-induced osteoclast formation.

Topics: Acid Phosphatase; Aged; Arthritis; Bone Resorption; Cell Differentiation; Cells, Cultured; Female; Humans; Integrin alphaVbeta3; Isoenzymes; Leukocytes, Mononuclear; Male; Middle Aged; Osteoclasts; Synovial Fluid; Tartrate-Resistant Acid Phosphatase

A study was made of the genetic variants (isoenzymes, phenotypes) of acid erythrocytic phosphatase (AcP) in 120 patients with rheumatic fever. There were 78 women and 42 men aged 16 to 57 years. The population data concerned with distribution of the AcP variants among the population of Moscow were used as control. As compared with control, the patients suffering from rheumatic fever demonstrated the accumulation of the rarely occurring variants of AcP (AC, BC and CC, in particular). A significant direct correlation was established between the activity of isoenzymes and relative risk of rheumatic fever incidence. The definite regularities in the distribution of AcP variants were found to depend on the disease clinical patterns (the articular syndrome, the times of the formation of heart diseases, the character of recurrent rheumocarditis). The data obtained can used for distinguishing the rheumatic fever risk groups and forecasting the rheumatic process (to a certain degree of probability).

Topics: Acid Phosphatase; Adolescent; Adult; Arthritis; Erythrocytes; Female; Humans; Isoenzymes; Male; Middle Aged; Phenotype; Rheumatic Fever; Risk Factors

The relative contributions of cellular and humoral immunity to cartilage destruction in chronic arthritis has been investigated in a model of chronic synovitis in the rabbit. In this model, antigen-induced arthritis, immunization with ovalbumin in Freund's complete adjuvant (FCA) followed by intra-articular injection of this protein produces a chronic synovitis associated with loss of proteoglycan from articular cartilage. In addition, the synovial lining cell population is metabolically activated. Similar treatment of animals immunized with ovalbumin in Freund's incomplete adjuvant (FIA) produced a resolving arthritis which initially (over the first 7 days) appears to be identical to that in FCA-immunized animals, apart from the lack of activation of synovial lining cells. Following this initial synovitis the joints return to apparent normality apart from a persistent 'low grade' synovitis consisting mainly of a plasma cell infiltrate. The most striking finding in the FIA-immunized animals is the rapid loss (greater than 30% by day 7) and recovery of proteoglycan from the matrix of articular cartilage. These findings show that the perpetuation of chronic destructive synovitis in the rabbit requires the presence of active cellular immunity.

Topics: Acid Phosphatase; Animals; Antibodies; Arthritis; Arthritis, Experimental; Cartilage, Articular; Female; Guinea Pigs; Hypersensitivity, Delayed; Immunity, Cellular; Male; Ovalbumin; Proteoglycans; Rabbits; Synovial Fluid; Synovitis

The use of unfixed and undecalcified cryostat sections of mouse knee joints is described for the study of enzyme histochemical reactions. Non-inflamed knee joints and knee joints of mice with antigen induced arthritis have been used. Joints were embedded in gelatin and subsequently cut at low speed with a motor-driven cryostat fitted with a tungsten carbide knife at an obtuse angle (10 degrees). The sections were attached to transparent tape to keep the integrity of the tissue intact. The following histochemical reactions were carried out successfully: the tetrazolium salt reaction for dehydrogenase and reductase activity, the post-azo-coupling method for acid phosphatase and cathepsin B activity and the simultaneous azo-coupling method for esterase activity. In all cases the morphology and integrity of the sections were well kept and serial sections were obtained without any difficulty. Nonspecific staining of the tape did not occur. The localization of the final reaction product was meeting criteria for specific and precise histochemical methods with the exception of the metal salt method because of nonspecific staining of undecalcified bone. Cytophotometry of the final reaction product appeared to be reproducible and valid as demonstrated by reaction for glucose-6-phosphate dehydrogenase activity in synoviocytes from knee joints with induced arthritis. End point measurements as well as kinetic measurements of the formazan production were performed and linear relationships were found between the specific formazan formation and section thickness or incubation time, respectively. It is concluded that cryostat sections attached to transparent tape are an excellent tool for the study of the metabolism in tissues adjacent to bone matrix.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Arthritis; Arthritis, Experimental; Cathepsin B; Histocytochemistry; Joints; Male; Mice; Mice, Inbred C57BL; Naphthol AS D Esterase; Oxidoreductases

Various histochemical changes were found in spinal segments L4-L5 of rats with adjuvant arthritis, predominantly 30 days after inoculation. A slight to marked increase of substance P immunoreactivity occurred in laminae I, II and X. FRAP activity was enhanced in lamina II. Serotonin immunoreactivity was heavier in laminae I, VIII and IX in a few animals. The intensity of the histoenzymological reaction for succinic dehydrogenase increased in certain laminae VIII and X neurons. At day 15 of the disease the increase of substance P and FRAP activities was chiefly restricted to the medial portion of the superficial dorsal horn. There was a significant positive correlation between the scratching behaviour of arthritic rats and the substance P immunoreactivity in laminae X and I. If one accepts that scratching is pain-related, the data are consistent with a possible role of substance P in the chronic pain associated with adjuvant arthritis. They leave undetermined the significance of the other histochemical changes.

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Behavior, Animal; Fluorides; Histocytochemistry; Isoenzymes; Male; Rats; Rats, Inbred Strains; Serotonin; Spinal Cord; Substance P; Succinate Dehydrogenase; Time Factors

Topics: Acid Phosphatase; Arthritis; Genetic Markers; Haptoglobins; HLA Antigens; HLA-A Antigens; HLA-B Antigens; Humans; Immunoglobulin Allotypes; Immunoglobulin G; Isoenzymes; Phosphoglucomutase; Psoriasis

Adjuvant arthritis was induced in rats by the injection of Mycobacterium tuberculosis, and its severity was scored according to the macroscopic findings of the legs, tail, and ears. The average score so obtained was lower in SOD-injected rats than in the control group. The depression of albumin/globulin ratio was inhibited significantly in rats treated with 10.0 mg/kg of SOD. The levels of acid phosphatase and beta-glucuronidase were elevated after the administration of an adjuvant, and these lysosomal enzymes showed a remarkable increase in the control rats, while the elevation was inhibited in rats injected with 10.0 mg/kg of SOD. The levels of TBA-reactive substances in the sera and synovia were elevated at 2 weeks after the injection of adjuvant and decreased thereafter. In rats injected with 5.0 mg/kg or 10.0 mg/kg of SOD, the increase in both serum and synovial levels of TBA reactants was inhibited significantly. These observations suggest that the aggravation of adjuvant arthritis may be associated with lipid peroxidation due to superoxide, and that SOD may be beneficial for the treatment of arthritis.

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Blood Proteins; Body Weight; Female; Glucuronidase; Lipid Peroxides; Rats; Rats, Inbred Strains; Superoxide Dismutase; Thiobarbiturates

Monoarticular arthritis in the rabbit has been used to study the effect of intra-articular administration of cortisol-21-phosphate and alpha-1-proteinase inhibitor. The preparations were administered both separately and in combination. All treatments improved parameters associated with joint biochemistry and histopathology, but the greatest effect was found when steroid was combined with anti-proteinase. Cortisol-21-phosphate had both an anti-inflammatory and anti-arthritic action, whereas alpha-1-proteinase inhibitor showed little anti-inflammatory action but had some anti-arthritic effect. Alpha-1-proteinase inhibitor had no anti-inflammatory action against carrageenan induced oedema in the rat, but was anti-arthritic against adjuvant induced arthritis in the rat where it reduced both primary and secondary arthritis.

Topics: Acid Phosphatase; alpha 1-Antitrypsin; Animals; Arthritis; Arthritis, Experimental; Blood Proteins; Disease Models, Animal; Edema; Hydrocortisone; Injections, Intra-Articular; Proteins; Rabbits; Rats; Rats, Inbred Strains; Synovial Fluid

Adjuvant arthritis was induced in rats by the injection of Mycobacterium tuberculosis, and its severity was scored according to the macroscopic findings of the legs, tails, and ears. The average score so obtained was lower when the rats also received indomethacin (1.5 mg/kg/day). The depression of the albumin/globulin ratio was inhibited significantly by the administration of indomethacin. The levels of acid phosphatase and beta-glucuronidase were elevated after the injection of an adjuvant, but they decreased to some extent in rats administered indomethacin. The levels of thiobarbituric acid (TBA)-reactive substances in the sera and synovia were elevated at 2 weeks after the injection of adjuvant and decreased thereafter. In rats administered 1.5 mg/kg of indomethacin, the increase in both serum and synovial levels of TBA reactants was inhibited significantly. These observations suggest that the aggravation of adjuvant arthritis may be associated with lipid peroxidation and that indomethacin may, in part, exert its anti-inflammatory effect by preventing lipid peroxide-induced damage of the synovial membrane.

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Blood Proteins; Female; Glucuronidase; Indomethacin; Lipid Peroxides; Mycobacterium tuberculosis; Rats; Rats, Inbred Strains; Synovial Membrane; Time Factors

Anti-arthritic action of superoxide dismutase (SOD) was studied in rabbits. Arthritis was induced by intraarticular injections of lambda-carrageenin (1%, 1 ml) into the knee joint weekly for two weeks. In this experimental arthritis, acid phosphatase activity, quantities of protein, uronic acid and lipid peroxide, and leukocyte counts in the synovial fluid increased; and the quantity of uronic acid in the articular cartilage decreased. Microscopic findings of the synovial membrane showed a proliferative synovitis. The responses of the left and right knee joint to carrageenin were much to the same in degree, so that the anti-arthritic action of SOD by intraarticular injections was evaluated on one knee joint, referring to the other joint as a control (saline injections). Two injections of SOD (350 SOD unit = 0.1 mg), one a week, suppressed the inflammatory changes in the biochemical parameters of the synovial fluid and the articular cartilage; particularly, significant inhibitory effects on acid phosphatase, lipid peroxide and leukocyte were observed. The microscopic findings of the synovial membrane also revealed that SOD was efficacious. On the other hand, 0.1 mg of denatured SOD, prepared by reducing the S-S bond or heating under an alkaline condition, did not show any anti-arthritic activity. These results suggest that the anti-arthritic action of SOD actually depends on the enzymatic activity of superoxide dismutase.

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Arthritis, Experimental; Carrageenan; Cartilage; Leukocyte Count; Lipid Peroxides; Male; Proteins; Rabbits; Superoxide Dismutase; Synovial Fluid; Synovial Membrane; Uric Acid

Adjuvant arthritis was induced in rats fed a diet deficient in or supplemented with vitamin E, and its severity was scored according to the macroscopic findings of their legs, tails, and ears. The average score so obtained was higher in the vitamin E-deficient diet group than in the group of rats supplemented with vitamin E. Whereas the A/G ratio remained depressed in vitamin E-deficient rats, rats on a vitamin E-supplemented diet showed a fast recovery from A/G-ratio depression. The serum levels of beta-glucuronidase and acid phosphatase were elevated after administration of an adjuvant. The serum levels of these lysosomal enzymes showed a remarkable increase in rats fed a vitamin E-deficient diet, while the elevation in lysosomal enzyme levels in rats fed a vitamin E-supplemented diet was inhibited. The levels of thiobarbituric acid (TBA) reactants in the synovia were elevated at 2 weeks after exposure to the adjuvant and were decreased thereafter. In rats maintained on a diet supplemented with vitamin E, on the other hand, the increase in synovial level of TBA reactive substances was inhibited. These observations suggest that the aggravation of adjuvant arthritis may be associated with lipid peroxidation and that antioxidants, such as vitamin E, may be beneficial for arthritis.

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Body Weight; Female; Glucuronidase; Lipid Peroxides; Rats; Rats, Inbred Strains; Synovial Fluid; Vitamin E; Vitamin E Deficiency

Sesquiterpene lactones containing an alpha-methylene-gamma-lactone moiety were shown to be potent inhibitors of carrageenan-induced edema and chronic adjuvant-induced arthritis in rodents at 2.5 mg/kg/day. The mode of action of sesquiterpene lactones as anti-inflammatory agents appeared to be at multiple sites; for example, at 5 X 10(-4) M, the sesquiterpene lactones effectively uncoupled the oxidative phosphorylation of human polymorphonuclear neutrophils and elevated the cyclic adenosine monophosphate levels of rat neutrophils and rat and mouse liver cells. Free and total lysosomal enzymatic activity was inhibited by these agents at 5 X 10(-4) M in both rat and mouse liver and rat and human neutrophils. Furthermore, the structure-activity relationships for the stabilization of lysosomal membrane for rat liver cathepsin activity followed the same structural requirement necessary for anti-inflammatory activity; i.e., the alpha-methylene-gamma-lactone moiety contributed the most activity, whereas the beta-unsubstituted cyclopentenone and alpha-epoxycyclopentanone contributed only minor activity. Human polymorphonuclear neutrophil chemotaxis was inhibited at low concentrations (i.e., 5 X 10(-5) and 5 X10(-6) M), whereas prostaglandin synthetase activity was inhibited at a higher concentration (i.e., 10(-3) M) by the sesquiterpene lactones.

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Arylsulfatases; Cathepsins; Chemotaxis, Leukocyte; Cyclic AMP; Cyclooxygenase Inhibitors; Edema; Humans; In Vitro Techniques; Lactones; Liver; Lysosomes; Male; Mice; Neutrophils; Oxidative Phosphorylation; Rats; Sesquiterpenes; Structure-Activity Relationship; Uncoupling Agents

This paper reports on the incorporation of acid phosphatase histochemistry with a quantitative technique designed to measure the percentage of histochemically-localized enzyme-reactive cells found in adjuvant arthritic articular cartilage, synovial membrane and bone marrow. With the data presented and the comparisons made, this incorporation is validated and adjuvant arthritic acid phosphatase "lesions" established. In addition to discussing the importance of the histochemical data and its relationship with intra-articular lysosomes, the applicability of the reactive cell values to drug inhibition studies is discussed.

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Bone Marrow; Cartilage, Articular; Histocytochemistry; Histological Techniques; Humans; Male; Methods; Synovial Membrane

Topics: Acid Phosphatase; Animals; Arthritis; Arthritis, Experimental; Leukocyte Count; Leukocytes; Liver; Male; Neuraminidase; Rats

Protease, antiprotease, and acid phosphatase blood levels of adjuvant arthritic rats were determined. The protease levels appear to vary inversely with the antiprotease levels. Changes in the protease levels correspond closely to changes in the acid phosphatase levels. Thus it is likely that the lysosomes contribute to the proteases present in the blood. Administered cortisol appears to raise blood antiprotease levels in both normal and arthritic rats and this may reflect an anti-inflammatory action by this drug.

Topics: Acid Phosphatase; alpha 1-Antitrypsin; Animals; Arthritis; Arthritis, Experimental; Clinical Enzyme Tests; Edema; Exudates and Transudates; Granulation Tissue; Hydrocortisone; Peptide Hydrolases; Protease Inhibitors; Rats

The key to the pathogenesis of arthrosis lies in the mechanism responsible for the initial lesions. In this experimental work the possibility of producing arthrosic changes is demonstrated by activating lysosomal chondrocytic enzymes by the intra-articular injection of Vitamin A in rabbits. On the basis of the experimental results the authors discuss the possible role that activation of the lysosomal hydrolytic enzymes might play in producing primary and secondary arthrosis in humans. They advance the hypothesis that this mechanism may be the common final step in the degradation of the articular cartilage, whatever the aetiological factor.

Topics: Acid Phosphatase; Animals; Arthritis; Carbohydrate Dehydrogenases; Cartilage, Articular; Enzyme Activation; Glucuronidase; Injections, Intra-Articular; Knee Joint; L-Lactate Dehydrogenase; Lysosomes; Rabbits; Uridine Diphosphate Glucose Dehydrogenase; Vitamin A

Topics: Acid Phosphatase; Adjuvants, Immunologic; Alkaline Phosphatase; Aminopeptidases; Animals; Ankle Joint; Arthritis; Bordetella; Cartilage; Glucuronidase; Hindlimb; Histocytochemistry; Joints; Leucine; Male; Mycobacterium tuberculosis; Rats; Time Factors

1 Old English (OE) rabbits produced more severe monoarticular arthritis (MAA) after sensitization and intra-articular challenge with ovalbumin than did either New Zealand White (NZW) or Dutch rabbits. NZW rabbits were better responders than Dutch rabbits.2 The swelling of the joint in all three strains of rabbits was triphasic. There was an initial acute swelling which appeared to peak at 2-4 days after challenge. This was followed by a decrease in joint size, and then a secondary increase in size beginning 1-2 weeks after challenge.3 An investigation of MAA in OE rabbits showed that there was an increase in E-type prostaglandins, total leucocyte counts and free acid phosphatase activity in the synovial fluid of the challenged joints at 6 h, 19 h, 47 h, 7 days and 46 days following challenge. There were also histopathological changes at these times. In addition, there was an increase in the surface temperature of both the challenged and non-challenged knees, and a rise in the body temperature.4 Prostaglandin levels peaked at 19 h and were equivalent to 19 ng E(2) per joint. In a separate experiment, the prostaglandin present at 18 h was shown to be mainly E(1). Maximum levels of prostaglandin appeared to coincide with maximum joint temperature, but preceded maximum joint swelling and a significant rise in both the number of inflammatory cells and the free acid phosphatase activity in the synovial fluid, all of which occurred at 47 hours.5 Indomethacin, 7.5 mg/kg orally twice daily, almost completely inhibited the increase in prostaglandin levels in the challenged joints and produced a moderate reduction in joint swelling. It also reduced the increased surface temperature of both knee joints and the raised body temperature. However, indomethacin had no effect on the number of leucocytes present, the free acid phosphatase levels, or the histopathological changes in the joint.6 The mean plasma level of indomethacin ranged from 0.5 to 3 mug/ml at the time when the animals were killed.7 Lysosomal enzymes may be more important than prostaglandins in rabbit MAA, and the lack of effect of indomethacin on joint histopathology may be due to its inability to prevent the release of these enzymes.

Topics: Acid Phosphatase; Animals; Arthritis; Body Temperature; Female; Immunization; Indomethacin; Knee Joint; Leukocyte Count; Lysosomes; Male; Mycobacterium; Ovalbumin; Prostaglandins; Rabbits; Species Specificity; Synovial Fluid; Time Factors

Topics: Acid Phosphatase; Animals; Antifungal Agents; Arthritis; Cartilage, Articular; Cathepsins; Cell Division; Endoplasmic Reticulum; Fatty Acids, Unsaturated; Glycoside Hydrolases; Histiocytes; Lactones; Lymphocytes; Lysosomes; Microscopy, Electron; Plasma Cells; Rabbits; Synovial Membrane

Topics: Acid Phosphatase; Animals; Arthritis; Clinical Enzyme Tests; Freund's Adjuvant; Hypersensitivity, Delayed; Rats; Rats, Inbred Strains

Topics: Acid Phosphatase; Adjuvants, Immunologic; Animals; Arthritis; Cell Membrane; Erythrocytes; Foot; Glucuronidase; Hemolysis; Hindlimb; Indomethacin; Liver; Lysosomes; Mycobacterium tuberculosis; Osmotic Fragility; Paramethasone; Phenylbutazone; Rats; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Arthritis; Dihydrolipoamide Dehydrogenase; Histocytochemistry; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Mycoplasma Infections; Succinate Dehydrogenase; Swine; Swine Diseases; Synovial Membrane

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Bradykinin; Carrageenan; Edema; Fluorides; Foot; Glucuronidase; Hindlimb; Lethal Dose 50; Liver; Lysosomes; Male; Rats; Rats, Inbred Strains; Serotonin; Triamcinolone Acetonide

Topics: Acid Phosphatase; Aminopeptidases; Animals; Arthritis; Freund's Adjuvant; Glucuronidase; Hindlimb; Liver; Lung; Lysosomes; Male; Naphthalenes; Proteins; Rats; Testis

Topics: Acid Phosphatase; Alkaline Phosphatase; Arteries; Arthritis; Blood Protein Electrophoresis; Blood Proteins; Diagnosis, Differential; Exudates and Transudates; Humans; Joint Diseases; Suppuration; Synovial Fluid; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Arthritis; Cartilage; Cathepsins; Fructose-Bisphosphate Aldolase; Glutathione Reductase; Humans; Joints; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Malate Dehydrogenase; Muramidase; Pyruvate Kinase; Spondylitis, Ankylosing; Synovial Fluid

Topics: Acetates; Acid Phosphatase; Animals; Arthritis; Female; Glucosamine; Glucuronidase; Glycoside Hydrolases; Hindlimb; Joints; Lysosomes; Male; Mycobacterium tuberculosis; Rats; Time Factors

Topics: Acid Phosphatase; Amino Acids; Animals; Arthritis; Aspirin; Chronic Disease; Disease Models, Animal; Freund's Adjuvant; Glucuronidase; Liver; Lysosomes; Male; Membranes; Phenylbutazone; Rats

Topics: Acid Phosphatase; Aminopeptidases; Animals; Arthritis; Glucuronidase; Liver; Lung; Lysosomes; Male; Naphthalenes; Rats; Testis

Topics: Acid Phosphatase; Alkaline Phosphatase; Arthritis; Arthritis, Rheumatoid; Humans; Joint Diseases; Rheumatic Fever; Rickets; Synovial Fluid; Synovitis

Topics: Acid Phosphatase; Animals; Arthritis; Cortisone; Depression, Chemical; Dexamethasone; Freund's Adjuvant; Glucocorticoids; Glucuronidase; Hindlimb; In Vitro Techniques; Indomethacin; Liver; Lysosomes; Male; Membranes; Neutrophils; Phenylbutazone; Rats; Temperature; Triamcinolone Acetonide; Vitamin E

Topics: Acid Phosphatase; Adjuvants, Immunologic; Animals; Arthritis; Female; Forelimb; Glucuronidase; Glycoproteins; Hindlimb; Hydrocortisone; Lysosomes; Microbial Collagenase; Mucoproteins; Penicillamine; Phenylbutazone; Rats; Stimulation, Chemical

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Cathepsins; Glucuronidase; Hexosaminidases; Humans; Lysosomes; Methods; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Arthritis, Reactive; Aspartate Aminotransferases; Bradykinin; Female; Glucuronidase; Humans; Hydrogen-Ion Concentration; Kinins; L-Lactate Dehydrogenase; Male; Muscle, Smooth; Osteoarthritis; Synovial Fluid; Uterus

Topics: Acid Phosphatase; Acute Disease; Aminocaproates; Animals; Arthritis; Cartilage, Articular; Chronic Disease; Glucuronidase; Hot Temperature; Hydrolases; Hypertrophy; Inflammation; Injections, Intra-Articular; Leukocytes; Lysosomes; Peptide Hydrolases; Rabbits; Skin; Synovial Membrane

Topics: Acid Phosphatase; Animals; Arthritis; Centrifugation, Density Gradient; Coliphages; Electron Transport Complex IV; Glucuronidase; Hydrolases; Inflammation; Joints; Liver; Lysosomes; Malate Dehydrogenase; Male; Mitochondria, Liver; Rabbits; Sulfatases; Thorium Dioxide

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Arthritis, Rheumatoid; Aspirin; Cathepsins; Depression, Chemical; Glucuronidase; Gold; Humans; Hydrocortisone; Hydrogen-Ion Concentration; Hydrolases; In Vitro Techniques; Indomethacin; Knee Joint; Liver; Lysosomes; Osteoarthritis; Phenylbutazone; Phosphoric Monoester Hydrolases; Rabbits; Sulfhydryl Compounds; Synovial Fluid

Topics: Acid Phosphatase; Antibodies, Antinuclear; Arthritis; Aspirin; Autoantibodies; Humans; Indomethacin; Phenylbutazone; Steroids; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Humans; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Electrophoresis; Humans; Isoenzymes; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Histocytochemistry; Humans; Knee Joint; Microscopy, Electron; Osteoarthritis; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Blood Chemical Analysis; Blood Protein Electrophoresis; Chemical Phenomena; Chemistry, Physical; Humans; Hyaluronoglucosaminidase; Latex Fixation Tests; Physical Examination; Rheumatoid Factor; Serum Albumin; Serum Globulins; Synovial Fluid; Ultrasonics; Viscosity

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Blood Cells; Cathepsins; Clinical Enzyme Tests; Glucuronidase; Humans; Immunodiffusion; Inclusion Bodies; Leukocytes; Phagocytosis; Precipitin Tests; Rheumatic Diseases; Rheumatoid Factor; Synovial Fluid

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Cytoplasm; Electrons; Histocytochemistry; Lysosomes; Microscopy; Microscopy, Electron; Mitochondria; Pathology; Synovial Membrane

Topics: Acid Phosphatase; Adolescent; Alkaline Phosphatase; Arthritis; Arthritis, Infectious; Arthritis, Rheumatoid; Chemistry Techniques, Analytical; Diagnosis; Geriatrics; Gout; Humans; Knee Injuries; Osteoarthritis; Phosphoric Monoester Hydrolases; Synovial Fluid; Synovitis; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Arthritis; Arthritis, Rheumatoid; Cartilage; Cytoplasmic Granules; Electrons; Histocytochemistry; Histological Techniques; Humans; Lysosomes; Microscopy; Microscopy, Electron; Synovial Membrane

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Arthritis; Aspartate Aminotransferases; D-Alanine Transaminase; Fructose-Bisphosphate Aldolase; Humans; Hydrarthrosis; Joint Diseases; L-Lactate Dehydrogenase; Synovial Fluid; Tuberculosis; Tuberculosis, Osteoarticular

Topics: Acid Phosphatase; Adenoma; Alkaline Phosphatase; Ameloblastoma; Arthritis; Bone Cysts; Bone Neoplasms; Chondrosarcoma; Fibroma; Fibrous Dysplasia of Bone; Geriatrics; Giant Cell Tumors; Humans; Neoplasm Metastasis; Osteitis Fibrosa Cystica; Osteoma; Osteosarcoma; Prognosis; Radiography; Sarcoma, Ewing; Tuberculosis; Tuberculosis, Osteoarticular