scholarly journals Chondromucoprotein-degrading neutral protease activity in rheumatoid synovial fluid.

1971 ◽  
Vol 30 (1) ◽  
pp. 73-77 ◽  
Author(s):  
G C Wood ◽  
R H Pryce-Jones ◽  
D D White ◽  
G Nuki
Keyword(s):  
Synovial Fluid ◽  
Protease Activity ◽  
Neutral Protease ◽  
Rheumatoid Synovial Fluid

Neutral Protease from the Polymorphonuclear Leucocytes of Human Rheumatoid Synovial Fluid

1974 ◽  
Vol 47 (5) ◽  
pp. 403-414
Author(s):  
R. H. Pryce-Jones ◽  
J. Saklatvala ◽  
G. C. Wood
Keyword(s):  
Ionic Strength ◽  
Synovial Fluid ◽  
Protease Activity ◽  
Degradation Products ◽  
Neutral Protease ◽  
Polymorphonuclear Leucocytes ◽  
Bovine Articular Cartilage ◽  
Rheumatoid Synovial Fluid ◽  
Synovial Fluids ◽  
Low Ionic Strength

1. The cartilage-proteoglycan-degrading activity of synovial fluid cells from rheumatoid patients is primarily due to neutral protease activity; hyaluronidase does not contribute significantly. Evidence for these conclusions is adduced from electrophoresis of degradation products, from comparison of the proteoglycan-degrading and protease activities of extracts and from the effects of activators and inhibitors. 2. Most of the neutral protease activity is insoluble in buffer of low ionic strength and may thus be separated from small amounts of other, soluble, proteoglycan-degrading enzymes. This ‘insoluble’ protease dissolves in KCl (1 mol/l) and has appreciable solubility even at physiological ionic strength. 3. The protease has optimum activity between pH 7.5 and pH 10, with little or no activity below pH 6.0. 4. The enzyme hydrolyses a number of substrates including elastin and two synthetic substrates for elastase. Hydrolysis of the latter is inhibited by dilutions of synovial fluids and serum and it thus differs from the elastase-like esterase activity of synovial fluid and serum. 5. The ‘insoluble’ enzyme fraction caused loss of staining and release of hexuronate from slices of bovine articular cartilage at salt concentrations near physiological and these effects were almost completely inhibited by cell-free synovial fluids. 6. The properties of the synovial fluid cell neutral protease are compared with those of the similar enzyme activity found in granulocytes from blood and it is concluded that the synovial fluid enzyme is probably derived from granulocytes.

Elevated neutral protease activity in myelin from brains of patients with multiple sclerosis

1984 ◽  
Vol 15 (3) ◽  
pp. 264-267 ◽  
Author(s):  
Shuzo Sato ◽  
Richard H. Quarles ◽  
Roscoe O. Brady ◽  
Wallace W. Tourtellotte
Keyword(s):  
Multiple Sclerosis ◽  
Protease Activity ◽  
Neutral Protease

The Primary Plasmin Inhibitor in Rheumatoid Synovial Fluid

1977 ◽  
Vol 20 (7) ◽  
pp. 1354-1358 ◽  
Author(s):  
Inge Clemmensen ◽  
René Donde ◽  
R. Bach Andersen
Keyword(s):  
Synovial Fluid ◽  
Rheumatoid Synovial Fluid ◽  
Plasmin Inhibitor
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