Determination of Cathepsins B and H in Sera and Synovial Fluids of Patients with Different Joint Diseases

Synovial fluids and sera of patients with inflammatory and metabolic joint diseases contain different cysteine proteinases. The quantities of cathepsins B and H were determined by newly developed specific enzyme-linked immunoassay tests (ELISA), with detection limits of 0.5 microgram/l for cathepsin B and 3 micrograms/l for cathepsin H. The values of cathepsin B in normal sera ranged from 0.6 microgram/l to 2 micrograms/l, whereas in sera of patients with joint diseases they ranged from 1.7 micrograms/l to 18 micrograms/l. Cathepsin H was not found in sera (values below 3 micrograms/l), but was measurable in patients' synovial fluids. Patients with rheumatoid arthritis have on average the highest values of cathepsin B in synovial fluids, whereas patients with undifferentiated arthritis have the highest values of cathepsin H. The results show that cathepsins B and H are present in arthritic synovial fluids, where they may be implicated in destructive processes. There is yet no clear correlation between the quantity of each cathepsin released in synovia and the clinical diagnosis or the stage of the disease.

[1]  J. Peter-Katalinic,et al.  Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases. , 1988 .

[2]  J. Kos,et al.  A new purification procedure of human kidney cathepsin H, its properties and kinetic data. , 1988, Biological chemistry Hoppe-Seyler.

[3]  B. Lenarčič,et al.  Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases. , 1988, Biological chemistry Hoppe-Seyler.

[4]  V. Turk,et al.  The mammalian cysteine proteinase inhibitors. Structural diversity and evolutionary origin , 1986 .

[5]  V. Turk,et al.  Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens , 1986 .

[6]  H. Tschesche.  Proteinases in Inflammation and Tumor Invasion , 1986 .

[7]  T. Tsukahara,et al.  Distribution of cathepsins B and H in rat tissues and peripheral blood cells. , 1985, Journal of biochemistry.

[8]  A. Poole,et al.  Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH. , 1984, Arthritis and rheumatism.

[9]  R. Timpl,et al.  Monoclonal antibodies used as probes for the structural organization of the central region of fibronectin , 1983, FEBS letters.

[10]  Y. Sinha,et al.  Production of antibodies by inoculation into lymph nodes. , 1983, Methods in enzymology.

[11]  J. Mort,et al.  A radioimmunoassay for total human cathepsin B. , 1982, Clinica chimica acta; international journal of clinical chemistry.

[12]  N. Katunuma,et al.  Immunological studies on cathepsins B and H from rat liver. , 1982, Journal of biochemistry.

[13]  T. Ono,et al.  Characterization of porcine plasma fibronectin and its fragmentation by porcine liver cathepsin B. , 1981, Journal of Biochemistry (Tokyo).

[14]  A. Poole,et al.  Immunofluorescent localization of cathepsins B and D in human fibroblasts. , 1981, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[15]  N. Hadler,et al.  Protease inhibitors in inflammatory synovial effusions. , 1981, Annals of the rheumatic diseases.

[16]  Alan J. Barrett,et al.  [41] Cathepsin B, cathepsin H, and cathepsin L , 1981 .

[17]  A. Schuurs,et al.  3,3',5,5' - Tetramethylbenzidine as an Ames test negative chromogen for horse-radish peroxidase in enzyme-immunoassay. , 1981, Journal of immunoassay.

[18]  A. Barrett,et al.  Cathepsin B, Cathepsin H, and cathepsin L. , 1981, Methods in enzymology.

[19]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[20]  J Carlsson,et al.  Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyldithio)propionate, a new heterobifunctional reagent. , 1978, The Biochemical journal.

[21]  C. Jenkin,et al.  Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. , 1978, Immunochemistry.

[22]  A. Barrett,et al.  The degradation of cartilage proteoglycans by tissue proteinases. Proteoglycan structure and its susceptibility to proteolysis. , 1977, The Biochemical journal.

[23]  D. Etherington.  The purification of bovine cathepsin B1 and its mode of action on bovine collagens. , 1974, The Biochemical journal.

[24]  A. Barrett,et al.  Cathepsin B1. A lysosomal enzyme that degrades native collagen. , 1974, The Biochemical journal.

[25]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[26]  G. A. Bennett,et al.  1958 Revision of diagnostic criteria for rheumatoid arthritis. , 1959, Bulletin on the rheumatic diseases.