scholarly journals Identification of tissue inhibitor of metalloproteinase-2 (TIMP-2)-progelatinase complex as the third metalloproteinase inhibitor peak in rheumatoid synovial fluid.

1993 ◽  
Vol 52 (3) ◽  
pp. 177-181 ◽  
Author(s):  
T E Cawston ◽  
H F Bigg ◽  
I M Clark ◽  
B L Hazleman
Keyword(s):  
Synovial Fluid ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Tissue Inhibitor ◽  
Metalloproteinase Inhibitor ◽  
The Third ◽  
Rheumatoid Synovial Fluid

Matrix metalloproteinase and tissue inhibitor of metalloproteinase in serum and synovial fluid of osteoarthritic dogs

2006 ◽  
Vol 19 (01) ◽  
pp. 49-55 ◽  
Author(s):  
J. K. Roush ◽  
T. Schermerhorn ◽  
K. E. Mitchell ◽  
B. J. Salinardi
Keyword(s):  
Mass Spectrometry ◽  
Synovial Fluid ◽  
Matrix Metalloproteinase ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor ◽  
Matrix Metalloproteinase 1 ◽  
Early Oa

SummaryTo better understand the mechanisms responsible for the pathological processes of osteoarthritis (OA) and to potentially identify a profile of changes that could be predictive of early OA, matrix metalloproteinase-1 (MMP-1) and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in the synovial fluid and serum of normal and osteoarthritic dogs were examined. The concentration of MMP-1 in the synovial fluid of osteoarthritic dogs (0.62 ± 0.16), as measured by densitometry, was significantly higher than that found in control dogs (0.42 ± 0.19) (P = 0.03). The concentration of MMP-1 in the serum of osteoarthritic dogs (0.74 ± 0.16) was significantly less than that found in control dogs (0.87 ± 0.08) (P = 0.05). The concentration of TIMP-2 in the synovial fluid of osteoarthritic dogs (46.2 ± 21.9 ng/ml) was significantly less than that of control dogs (122.0 ± 66.5 ng/ml) (P = 0.009). The concentration of TIMP-2 in the serum of osteoarthritic dogs (116.2 ± 43.1 ng/ml) was not significantly different than that of control dogs (95.1 ± 94.4 ng/ml) (P = 0.554). In addition, a phospho-tyrosine immunoprecipitation and mass spectrometry were used to isolate and identify interferonalpha in canine synovial fluid.

scholarly journals Purification of a metalloproteinase inhibitor from human rheumatoid synovial fluid

1985 ◽  
Vol 231 (3) ◽  
pp. 505-510 ◽  
Author(s):  
E Mercer ◽  
T E Cawston ◽  
M de Silva ◽  
B L Hazleman
Keyword(s):  
Synovial Fluid ◽  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Serine Proteinase ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Metalloproteinase Inhibitor ◽  
Bacterial Collagenase ◽  
Rheumatoid Synovial Fluid

A metalloproteinase inhibitor present in human rheumatoid synovial fluid was purified by a combination of heparin-Sepharose chromatography, concanavalin A-Sepharose chromatography, ion-exchange chromatography and gel filtration. The Mr of the purified inhibitor was 28000 by SDS/polyacrylamide-gel electrophoresis and 30000 by gel filtration. The inhibitor blocked the activity of the metalloproteinases collagenase, gelatinase and proteoglycanase, but not thermolysin or bacterial collagenase. The serine proteinase trypsin was not inhibited. The inhibitory activity was lost after treatment with trypsin (0.5 micrograms/ml) at 37 degrees C for 30 min, 4-aminophenylmercuric acetate (1 mM) at 37 degrees C for 3 h, after incubation for 30 min at 90 degrees C and by reduction and alkylation. These properties suggest that the inhibitor closely resembles the tissue inhibitor of metalloproteinases (‘TIMP’) recently purified from connective-tissue culture medium.

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