acid-phosphatase and Joint-Diseases

Topics: Acid Phosphatase; Acute Disease; Adult; Analgesics; Anti-Inflammatory Agents; Blood Coagulation Factors; Cathepsins; Chronic Disease; Cryoglobulins; Factor IX; Factor VIII; Freeze Drying; Hemarthrosis; Hemophilia A; Home Nursing; Humans; Joint Diseases; Male; Muscles; Radiography; Synovial Fluid; Synovial Membrane

Topics: Acid Phosphatase; Aged; Arthritis, Rheumatoid; Body Temperature; Calcinosis; Female; Humans; Inflammation; Joint Diseases; Kinins; Knee Joint; Lysosomes; Male; Middle Aged; Proteins; Psoriasis; Synovial Fluid

Matrix metalloproteinase (MMP) has been implicated in joint destruction of chronic arthritis diseases, such as rheumatoid arthritis. FR217840 (2R)-1-([5-(4-fluorophenyl)-2-thienyl]sulfonyl)-N-hydroxy-4-(methylsulfonyl)-2-piperazinecarboxamide is a potent, orally active synthetic MMP inhibitor that inhibits human collagenases (MMP-1, MMP-8 and MMP-13), gelatinases (MMP-2 and MMP-9) and membrane type MMP (MT-MMP) (MT1-MMP/MMP-14). FR217840 also inhibits rat collagenase and gelatinase. We studied the effect of FR217840 on a rat adjuvant induced arthritis model. Although oral administration (days 1-21) of FR217840 (3.2, 10, 32 mg/kg) to adjuvant injected Lewis rats did not affect inflammation, as indicated by both hind paw swelling and histological inflammatory infiltration, FR217840 suppressed both bone destruction and serum pyridinoline content in a dose-dependent manner. Also, FR217840 (32 mg/kg) reduced tartrate-resistant acid phosphatase (TRAP) cell number in the ankle joints of rats with arthritis. These results indicate that FR217840 successfully suppressed joint destruction and suggest that FR217840 may have potential as a novel anti-rheumatic drug.

Topics: Acid Phosphatase; Amino Acids; Animals; Ankle Joint; Arthritis, Experimental; Cell Line; Cells, Cultured; Collagenases; Disease Progression; Female; Humans; Isoenzymes; Joint Diseases; Matrix Metalloproteinase 1; Matrix Metalloproteinase 13; Matrix Metalloproteinase 8; Matrix Metalloproteinase 9; Matrix Metalloproteinase Inhibitors; Matrix Metalloproteinases; Piperazines; Protease Inhibitors; Radiography; Rats; Rats, Inbred Lew; Tartrate-Resistant Acid Phosphatase; Tumor Necrosis Factor-alpha

The findings are presented of a morphologic, quantitative, cytochemical and cytoenzymologic study of the mononucleated nonlymphoid cells in knee synovial fluids from osteoarthritis and various inflammatory diseases. The morphologic criteria allowed the identification of subtypes, including phagocytic subtypes, among synoviocytic and monocytic cells in the fluids. The quantitative study showed an important afflux of monocytes and a hyperexfoliation of synoviocytes in the inflammatory diseases. In fluids with intermediate cellularity, the ratio of monocytes to synoviocytes allowed the differential cytodiagnosis between osteoarthrosis and arthritis. All monocytic subtypes, especially the phagocytic one, were highly significantly increased in the inflammatory diseases. A lower increase was shown by the synoviocytic subtypes, except the phagocytic one, which was not changed. Giant multinucleated synoviocytes were found in every type of disease and thus do not constitute a cytodiagnostic marker. Alcian blue staining without hyaluronidase treatment showed hyaluronate in only a small percentage of the synoviocytes. Cytoenzymologic study showed that synoviocytes and monocytes were positive for all tested hydrolases (beta glucuronidase, acid phosphatase and alpha naphthyl acetate esterase), with the reactivities always higher in the synoviocytes. The synoviocytes were always negative with peroxidase, so this reaction, although it marks only a minority of the monocytic population, can be used as an extra cytologic criterion for the discrimination of mononucleated cells in synovial fluid. There was no significant quantitative difference at the cellular level between osteoarthrosis and arthritides in the reaction to these four enzymes. The lysosomal enzymatic activity in both monocytic and synoviocytic cells confirmed their heterophagic properties. However, synoviocytic heterophagy seems to be a physiologic process, either little or not affected by inflammatory events. On the other hand, monocytic heterophagy and then the macrophagic transformation of monocytes appears to be a major aspect of intrasynovial inflammatory reactions. The question remains as to why, if a large majority of exfoliated synoviocytes comes from type A synovial-lining cells and if they belong to mononuclear phagocytic system, do they so weakly, or not at all, participate as phagocytes in the inflammatory reaction.

Topics: Acid Phosphatase; Glucuronidase; Histocytochemistry; Humans; Isoenzymes; Joint Diseases; Monocytes; Naphthol AS D Esterase; Peroxidase; Peroxidases; Synovial Fluid

Topics: Acid Phosphatase; Alkaline Phosphatase; Cartilage, Articular; Glucuronidase; Glycosaminoglycans; Histocytochemistry; Humans; Hydrolysis; Joint Diseases

This paper describes a morphologic, quantitative, cytochemical study of mononuclear non lymphoid cells in knee synovial fluid in osteoarthritis and various arthritides. Morphologic criteria allow to identify among these cells various synoviocytic and monocytic subtypes with in both types, phagocytic subtypes. Quantitative study shows in arthritides an important afflux of monocytes and a hyperexfoliation of synoviocytes. In fluids with intermediate cellularity, Monocytes/Synoviocytes ratio allows the differential cytodiagnosis between osteoarthrosis and arthritis. All monocytic subtypes and especially the phagocytic one are highly significantly increased in arthritides. Synoviocytic subtypes show a lower increase, except the phagocytic one, which is not changed. Giant multinuclear synoviocytes are found in every type of disease and cannot constitute a cytodiagnosis marker. Alcian Blue and hyaluronidase treatment show hyaluronate in a few percentage of Synoviocytes. Cytoenzymologic study shows that synoviocytes and monocytes are positive in all tested hydrolases: beta Glucuronidase, Acid Phosphatase, alpha Naphthyl Acetate Esterase, these activities being always higher in synoviocytes. With peroxidase, synoviocytes are always negative, so this reaction although it marks only a minority of monocytic population can be used as an extra cytologic criterion for discrimination of mononuclear cells in synovial fluid. In these four enzymes there is no significant quantitative difference at cellular level between osteoarthrosis and arthritides. Lysosomal enzymatic activity in both monocytic and synoviocytic cells confirms their heterophagic properties. However synoviocytic heterophagy seems to be a physiological process not or few affected by inflammatory events. On the opposite, monocytic heterophagy and then macrophagic transformation of monocytes appears as a major aspect of intrasynovial inflammatory reaction. If a large majority of exfoliated synoviocytes comes from A type synovial lining cells and if they belong to Mononuclear Phagocyte System, why do they so weakly, or not, participate as phagocytes to inflammatory reaction.

Topics: Acid Phosphatase; Arthritis, Reactive; Arthritis, Rheumatoid; Chondrocalcinosis; Glucuronidase; Gout; Humans; Joint Diseases; Knee Joint; Naphthol AS D Esterase; Peroxidases; Spondylitis, Ankylosing; Synovial Fluid

The synovium and synovial fluid have been studied in a patient with multicentric reticulohistiocytosis. Previously unreported histochemical, immunocytochemical and ultrahistochemical findings are presented and their relevance to the aetiology and pathogenesis are discussed. The synovial fluid analysis in this disease is characteristic and may be helpful in its early diagnosis.

Topics: Acid Phosphatase; Aged; Arylsulfatases; Humans; Joint Diseases; Leukocyte Count; Lymphatic Diseases; Male; Microscopy, Electron; Synovial Fluid; Synovial Membrane

In 30 cases of disease of the knee joint (9 cases of rheumatoid arthritis, 14 arthroses and 7 cases of posttraumatic postoperative synovitis), the quantitative changes of the four lysosomal enzymes (acid phosphatase, lactic acid dehydrogenase, cathepsin and proteins) was observed in the course of intra-articular treatment with Gordox. It was evident from the analysis of the enzyme determinations conducted within 5--30 days at various times, and from the clinical results of the treatment, that in the cured or improved cases, all four enzymes were reduced (6 patients), whereas, in 16 cases, three of the enzyme levels had decreased. The enzyme titer remained unchanged in those patients who had been treated without success. Although these results do not as yet allow any final conclusions with regard to the mechanisms of action of Gordox administered intraarticularly, they do indicate that further and even more thorough studies in this direction should be conducted.

Topics: Acid Phosphatase; Adult; Aged; Cathepsins; Glucuronidase; Humans; Hydrolases; Injections, Intra-Articular; Joint Diseases; L-Lactate Dehydrogenase; Middle Aged; Protease Inhibitors; Synovial Fluid

In order to analyze the presence of alkaline and acid phosphatase activity in osteoarthrotic subchondral bone frozen sections from 24 femoral heads were prepared for semiquantitative analysis, using the enzyme-histochemical methods described by Burstone and by Barka and Anderson. Different areas of the subchondral bone, viz. weight-bearing, nonweight-bearing and osteophytes as well as central regions were analyzed. Furthermore, the cartilagenous changes were determined by histological-histochemical grading. There were wide variations within the same femoral head with significantly greater activity of both alkaline and acid phosphatase in weight-bearing than in nonweight-bearing areas and in subchondral bone than in central regions. Osteophytes excluded, the enzyme activities correlated directly with the severity of the cartilage lesions. These enzyme activities presumably reflect the degree of bone regeneration and bone resorption respectively.

Topics: Acid Phosphatase; Aged; Alkaline Phosphatase; Female; Hip Joint; Humans; Joint Diseases; Male; Osteoarthritis

Topics: Acid Phosphatase; Diagnosis, Differential; Humans; Joint Diseases; Proteins; Synovial Fluid

Topics: Acid Phosphatase; Adult; Aged; Arthritis, Rheumatoid; Female; Humans; Joint Diseases; Male; Middle Aged; Synovial Fluid

An experimental model of degenerative joint disease on chondromalacia consists of a surgically-scarified articular surface of the adult dog knee joint. In 52 dogs, evaluated by histologic and enzymatic assays over a period of 1 to 110 weeks post-surgery, the levels of acid hydrolase activity varied on various areas of articular cartilage within the same joint. There was a transient rise in most of the acid hydrolases in the synovium as a response to arthrotomy of the knee joint. All of the acid hydrolases studied did not respond uniformly to surgically created trauma. There was evidence of repair of the cartilage lacerations even when the subchondral zone was not breached. Lacerations in the central portion of the patella rarely showed healing in contrast to those placed more to the periphery of the articular surface. There was no gross or histologic evidence of progressive degenerative joint disease up to 2 years post-surgery. Thus an injury inflicted to the surface of the articular cartilage may be in itself insufficient in severity to produce destructive changes in the joint. This should not be too surprising, since, clinically, all joint surface injury does not lead to degenerative arthritis. The joint seems to have an injury threshold whereby chondrocytes are capable of repairing surface injury if the damage is not massive or repetitive. Insofar as lacerations in the center of the patella rarely healed, while the peripheral ones showed consistent signs of healing, the site of injury, as well as the magnitude of injury, may be critical.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Arylsulfatases; Cartilage Diseases; Cartilage, Articular; Cathepsins; Deoxyribonucleases; Disease Models, Animal; Dogs; Glucuronidase; Joint Diseases; Knee Joint; Patella; Synovial Membrane; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Arthritis, Reactive; Behcet Syndrome; Buffers; Chondrocalcinosis; Gout; Histocytochemistry; Humans; Hydrarthrosis; Joint Diseases; Methods; Synovial Fluid; Ultracentrifugation

Topics: Acid Phosphatase; Arginase; Arthritis, Rheumatoid; Glycoside Hydrolases; Gout; Humans; Joint Diseases; Osteoarthritis; Peptide Hydrolases; Rheumatic Diseases; Synovial Fluid; Transaminases

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; Arthritis, Rheumatoid; Bursitis; Fructose-Bisphosphate Aldolase; Gout; Humans; Joint Diseases; Osteoarthritis; Phosphoric Monoester Hydrolases; Synovial Fluid; Transaminases

Topics: Acid Phosphatase; Cytodiagnosis; Esterases; Histocytochemistry; Humans; Joint Diseases; Synovial Fluid

Topics: Acid Phosphatase; Arthritis, Rheumatoid; C-Reactive Protein; Diagnosis, Differential; Gout; Histiocytes; Humans; Joint Diseases; Synovial Fluid; Synovitis; Uric Acid; Viscosity

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

Topics: Acid Phosphatase; Adrenal Cortex Hormones; Alanine Transaminase; Alkaline Phosphatase; Animals; Anti-Bacterial Agents; Aspartate Aminotransferases; Bacteriological Techniques; Blood Cell Count; Blood Chemical Analysis; Blood Glucose; Forelimb; Fructose-Bisphosphate Aldolase; Horse Diseases; Horses; Hydrarthrosis; Injections, Intra-Articular; Joint Diseases; Knee Joint; L-Lactate Dehydrogenase; Osteochondritis; Radiography; Synovial Fluid

Topics: Acid Phosphatase; Animals; Buffers; Cartilage, Articular; Catechols; Cathepsins; Disease Models, Animal; DNA; Enzyme Activation; Glucuronidase; Glycoside Hydrolases; Hydrolases; In Vitro Techniques; Joint Diseases; Joints; Knee Joint; Organ Size; Pressure; Rabbits; Sucrose; Sulfatases; Synovial Membrane

Topics: Acid Phosphatase; Glycoside Hydrolases; Humans; In Vitro Techniques; Joint Diseases; Leukocyte Count; Synovial Fluid

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