Proteinase inhibitors in human synovial fluid

Shtacher, Gad; Maayan, Rachel; Feinstein, Gad

doi:10.1016/0005-2795(73)90155-4

Cited by 46 publications

(8 citation statements)

References 16 publications

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“…In patients with deficient phenotypes, the serum level of AlPi is reduced, and since this level parallels the amount found in synovial fluid (17), the latter would be expected to be markedly reduced. Since the mechanism of inhibition of proteolytic activity involves formation of complexes between AlPi and proteases (18)(19)(20), low levels of AlPi could result in increased amounts of protease remaining unbound and active. Furthermore, we have shown that such unbound proteases can act upon formed complexes causing denaturation of AlPi.…”

Section: Resultsmentioning

confidence: 99%

Increased frequency of the MZ phenotype of alpha-1-protease inhibitor in juvenile chronic polyarthritis.

Arnaúd¹,

Galbraith²,

Faulk³

1977

J. Clin. Invest.

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A B S T R A C T Pi phenotypes of alpha-1-protease inhibitor were determined by isoelectric focusing and print immunofixation in 96 English children suffering from juvenile chronic polyarthritis. A significantly increased frequency of the MZ phenotype (10.41%) was found in comparison with a geographically matched control population (1.6%). The results of this study suggest that the possession of a Z-deficient allele of alpha-l-protease inhibitor could be a predisposing, aggravating, or perpetuating factor in the articular damage occurring in juvenile chronic polyarthritis.

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Section: Resultsmentioning

confidence: 99%

Increased frequency of the MZ phenotype of alpha-1-protease inhibitor in juvenile chronic polyarthritis.

Arnaúd¹,

Galbraith²,

Faulk³

1977

J. Clin. Invest.

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“…Previous studies have demonstrated that PMN incubation with cytokines, such as tumor necrosis factor or interleukin-1, may modify the neutrophil response (12,13); therefore, higher levels of SF cytokines (14,15) might explain some of the variation in both IgG and non-IgG-coated fibrils observed for the different PMN-SF mixtures. Variations in the concentration and activity of collagenase inhibitors in the SF, such as TIMP (tissue inhibitor of metalloproteinases) or a,-macroglobulin, might also account for some of the variability observed (16). Finally, antirheumatic drugs in the SF of some of the patients could have modulated some of the observed responses in this system.…”

Section: Discussionmentioning

confidence: 99%

Lysis of fibrillar collagen by neutrophils in synovial fluid. A Role for Surface‐Bound Immunoglobulins

Chatham

Heck

Blackburn

1990

Arthritis & Rheumatism

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Synovial fluids (SF) contain inhibitors capable of neutralizing the activity of proteases secreted by inflammatory cells and fibroblasts. To further define a potential role for SF polymorphonuclear neutrophils (PMN) in mediating joint destruction, peripheral blood PMN were suspended in SF and incubated with reconstituted collagen fibrils. Incubation of PMN-SF mixtures with collagen fibrils precoated with monomeric IgG resulted in significant lysis of the underlying fibrils relative to that seen with uncoated fibrils. Augmented fibril lysis by PMN-SF mixtures in which the PMN were activated with fluid-phase ligands such as phorbol myristate acetate or heat-aggregated IgG was not seen. Lysis of IgG-coated fibrils by PMN-SF was inhibited in the presence of EDTA or sodium azide. PMN-mediated resorption of fibrillar collagen occurred despite the presence of protease inhibitors in the SF at a concentration capable of neutralizing human neutrophil collagenase. These results suggest that the focal release and activation of human neutrophil collagenase during PMN

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“…The proteins chosen for quantitation (Table 1) are of the size of albumin with the exception of cr2M. Total protein values were comparable with accepted ranges [4,22] (Table 4). The acutephase reaction of increased al-acid glycoprotein in plasma with rheumatoid arthritis was not parallelled in the synovial fluids.…”

Section: Plasma Protein Contentsmentioning

confidence: 97%

“…In synovial fluids both active and inactive cc2M has been found in various joint diseases [4,5]. It has been suggested that enzymes entrapped by ~2M may function in the breakdown of peptides.…”

mentioning

confidence: 99%

Functionally active α2-macroglobulin and kinin release in synovial fluids of rheumatoid arthritis

1978

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The function of a2M (a2-macroglobulin) as a proteinase inhibitor in synovial fluid of rheumatoid arthritis was investigated. Low esterase activity was found in the 19S sieve fraction of Sephadex G-200 gel filtered synovial fluid samples, comparable with that obtained with normal human plasma. The molar binding ratio of uzM isolated from the synovial fluid and trypsin was estimated according to earlier established methods. The formation of an equimolar complex indicated that the synovial u2M was functionally intact.Esterase activities were measured on uN-tosyI-Larginine [3H]methyl ester. Synovial fluid samples were all found to contain proteinase enzyme which did not bind to the synovlal ohM nor to the added functionally intact, immunologically pure a2M prepared from normal human plasma.Albumin, uL-acid glycoprotein, a2HS-glyeoprotein , u2M and kininogen in synoviai fluids were determined by single radial immunodiffuslon. Only the ct2M contents were clearly lower than in normal human serum per ml.The higher than 1 ratio between the immunoreactive kininogen determined with monospeeific anti-human kininogen serum and the pharmacologically active klninogen indicated that klnin release had occurred possibly in the synovial membrane. Protelnase enzymes present in the synovial fluids and unbound to ohM caused further depletion of the active klnin Segment in synovlal kininogen. A model of the regulation by u2M of the synovlal klninogen-klnin system is given.

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Proteinase inhibitors in human synovial fluid

Cited by 46 publications

References 16 publications

Increased frequency of the MZ phenotype of alpha-1-protease inhibitor in juvenile chronic polyarthritis.

Increased frequency of the MZ phenotype of alpha-1-protease inhibitor in juvenile chronic polyarthritis.

Lysis of fibrillar collagen by neutrophils in synovial fluid. A Role for Surface‐Bound Immunoglobulins

Functionally active α2-macroglobulin and kinin release in synovial fluids of rheumatoid arthritis

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