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Biomedical subjects

J Wize

Publications and source records attributed to J Wize.

At least 19 recordsLinked to original sources
PubMed1998

Ligation of selectin L and integrin CD11b/CD18 (Mac-1) induces release of gelatinase B (MMP-9) from human neutrophils.

OBJECTIVE AND DESIGN: To examine whether ligation of the adhesive receptors - selectin L and Mac-1 on the neutrophil surface could induce gelatinase B exocytosis. MATERIALS: Neutrophils were isolated from fresh heparinized blood of human donors by Gradisol G centrifugation and hypotonic lysis of erythrocytes. METHODS: Integrin CD1 1b/CD18 and selectin L mediated adhesive interaction of human neutrophils were mimicked by binding antibodies to these receptors on the surface of isolated leukocytes. Neutrophils (5 x 10(6)/ml) were incubated with antibodies against selectin L (40/microg/ml) and CD18 or CDI 1b (10microg/ml). The secretion of gelatinase was examined by determination of enzyme activity and gelatin substrate zymography of cell supernatants. RESULTS: Ligation of selectin L, CD18 and CD11b integrin subunits by monoclonal antibodies induced a rapid release of 24.6+/-1.8% (p<0.005), 24.0+/-2.9% (p<0.001) and 22.7+/-2.0% (p < 0.005) of total neutrophil gelatinase, respectively as compared with 11.1+/-1.6% in the control. These values were equivalent to N-formyl-methionylleucyl-phenylalanine (fMLP)-stimulated secretion of gelatinase. Under these experimental conditions there was no significant beta-glucuronidase release from azurophilic granules. Gelatinase exocytosis elicited by selectin L and CD18 ligation was inhibited by 82.7+/-10.1% and 49.3+/-5.9%, respectively after preincubation of the neutrophils with 10 microM herbimycin A. CONCLUSIONS: Ligation of selectin L and integrin CD11b/ CD18 provides stimulatory signals to neutrophils which induce secretion of gelatinase B that may facilitate their transmigration into sites of inflammation.

Antigens, Surface↗
PubMed1995

Neutrophil gelatinase levels in plasma and synovial fluid of patients with rheumatic diseases.

To examine the clinical significance of neutrophil gelatinase in rheumatic diseases, plasma and synovial fluid (SF) gelatinase levels were determined in 62 patients with rheumatoid arthritis (RA), 12 patients with ankylosing spondylitis (AS), 18 patients with osteoarthritis (OA) and 17 healthy controls. The gelatinase level was measured by enzyme-linked immunoassay (ELISA). The assay had a sensitivity of 1 ng/ml and a working range of 5-25 ng/ml. Gelatinase levels were significantly higher in the plasma of patients with RA and of patients with RA complicated by amyloidosis or vasculitis as compared to those of healthy controls. Moreover, the mean value of gelatinase in the plasma of patients with RA complicated by vasculitis was found to be significantly higher than that of RA patients without vasculitis. A significant increase in gelatinase concentration was also observed in the plasma of AS patients but not in the plasma of patients with OA. The concentration of gelatinase in the RA SF samples was much higher (18-fold) than the level of the enzyme in the plasma of RA patients. There was also a higher concentration of gelatinase (four-fold) in OA SF compared with OA plasma. The results suggested that circulating gelatinase may reflect some degree of neutrophil activation in patients with inflammatory arthritis, especially in those with RA complicated by vasculitis. However, the results did not allow a differentiation between chronic and acute inflammation.

Adult↗
PubMed1993

Comparison of Delmée and Polish serogroup-specific Clostridium difficile strains.

In this study we compared Delmée and Polish serogroup-specific Clostridium difficile strains by slide agglutination, observation of flagella and SDS-PAGE protein patterns. Among Delmée serogroup specific strains we observed flagella in groups A, D and K. Among Polish serogroup-specific Clostridium difficile strains we did not observe flagella. The Polish serogroup-specific strains gave different protein patterns compared to Delmée strains. SDS-PAGE protein pattern analyses of Polish serogroup-specific strains divide these strains into 3 groups: 71, 88 and third embracing 18, 27, 70, 72, and 89.

Adult↗
PubMed1990

Some properties of latent collagenase from human synovial fluid.

Latent collagenase has been isolated in pure form from the rheumatoid synovial fluid. The final preparation, activated by trypsin, yielded a collagenase of specific activity 2,227 units/mg. Electrophoresis in sodium dodecyl sulfate polyacrylamide gels revealed a protein doublet of 54 and 50 kDa. Trypsin or HgCl2 activation resulted in disappearance of the doublet and emergence of a new doublet of 47 and 43 kDa. The latent collagenase could also be activated by leucocyte cathepsin G or plasmin. Neither the latent nor the active collagenase from synovial fluid showed any cross-reactivity with the antibodies against leucocyte collagenase. The trypsin activated collagenase degraded collagen type I, II, III giving typical cleavage products but did not degrade type IV and V collagen.

Electrophoresis, Polyacrylamide Gel↗
PubMed1989

Neutrophil enzyme activities in carrageenan-induced inflammation in rats.

During the course of carrageenan-induced inflammation in rats major changes were observed in the activities of neutrophil granule enzymes. The activities of three enzymes--gelatinase, collagenase and beta-glucuronidase, the markers of three different types of granules, have been measured and compared to those of a control group of animals. Total collagenase and gelatinase activities of control rats were 59.4 +/- 3.6 (mean +/- SD) and 23.0 +/- 2.9 units/mg protein, respectively. Significantly reduced levels of both collagenase (35.6 +/- 2.5 units) (p less than 0.05) and gelatinase (7.1 +/- 0.7 units) (p less than 0.001) were measured in the blood neutrophils of inflamed rats; and the collagenase activity of neutrophils derived from inflamed pleural exudate was also significantly decreased to a level of 19.7 +/- 1.8 units/mg protein (p less than 0.01). However, the gelatinase activity of exudate neutrophils did not differ from that of blood cells of inflamed rats. In contrast, no change was found for the beta-glucuronidase activity in blood neutrophils of control and inflamed rats. These observations support the concept that during the inflammatory response in rats, neutrophils in the circulation may become activated as judged by the extracellular secretion of collagenase and gelatinase. Therefore, neutrophils accumulating in acute inflammatory lesions contain decreased levels of collagenolytic enzymes and the significance of this observation is discussed.

Animals↗
PubMed1986

Collagen-derived peptides release mast cell histamine.

The effect of collagen degradation products by bacterial (BCDP) and synovial fluid collagenase (SCDP) on histamine release from peritoneal mast cells of rat was estimated. Some BCDP as well as SCDP released 60-80% of mast cell histamine. In BCDP fraction the most active were BCDP II (m.wt. 13 kD) and BCDP III (m.wt. 6 kD). The last contained the highest percentage of hydroxyproline. As compared with bradykinin, BCDP III was about 50 fold more active as histamine releaser.

Animals↗
PubMed1984

Latent collagenase of rheumatoid synovial fluid is not of granulocytic origin.

The physicochemical properties of three latent collagenases derived from rheumatoid synovial fluid, polymorphonuclear leucocytes and culture medium of rheumatoid synovium were compared. It has been shown that synovial fluid enzyme is similar to that of synovium collagenase from tissue culture and differs significantly in molecular size and protein charge from granulocyte collagenase. The results indicate that the latent, trypsin-activable collagenase present in rheumatoid synovial fluid is not of granulocytic origin and seems to derive from the synovial membrane.

Arthritis, Rheumatoid↗
PubMed1980

A latent collagenase from rheumatoid synovial fluid. Purification and partial characterization.

1. A latent collagenase (EC 3.4.24.3) has been isolated from rheumatoid synovial fluids and purified by (NH4)2SO4 precipitation and column chromatography, utilising Sephadex G-150, DEAE Sephadex A-50 and Sephadex G-100 superfine grade. 2. The final preparation activated by trypsin (EC 3.4.21.4) had a specific activity against thermally reconstituted collagen fibrils of 259 micrograms collagen degraded/min per mg enzyme protein, representing a nearly 800-fold increase over that of the original rheumatoid synovial fluid. 3. The latent collagenase preparation can be activated by trypsin and to some extent by HgCl2 but not by 3 M NaSCN, 3.5 M NaCl, 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) or p-chloromercuribenzoate. 4. Inhibition studies and the acrylamide gel electrophoretic pattern of collagen degradation products showed that the trypsin-activated enzyme has the essential features of a neutral collagenase. 5. The molecular weights, determined by calibrated gel filtration, were 52 000 and 43 000 for the latent and the activated enzyme, respectively. 6. The nature of the latency of synovial fluid collagenase is discussed.

Arthritis, Rheumatoid↗
PubMed1980

Biological effects of degradation products of collagen by bacterial collagenase.

1 Collagen degradation products (CDP) resulting from bacterial collagenase digestion were fractionated by gel filtration and their biological activities in rats were estimated. 2 CDP induced the following kinin-like effects: increase in permeability of skin blood vessels, contraction of the isolated intestine of the rat, depression of locomotor activity and of motor coordination. 3 The most active CDP fraction was CDP III containing peptides of mol. wt. < 1000 D with a high percentage of hydroxyproline. 4 As compared with bradykinin, CDP III was less active in the skin permeability test and was 15,000 to 20,000 fold less effective in induction of isolated intestine contraction. 5 Depression of the CNS induced by 30 microgram of CDP III administered into the brain ventricle was similar to that observed after 4 microgram of bradykinin given by the same route. 6 CDP III prolonged the duration of sleep evoked by thiopentone and enhanced the threshold of convulsion induced by pentazol. 7 The activity of CDP in comparison to other low molecular weight peptides is discussed.

Animals↗
PubMed1979

A latent gelatin specific proteinase of human leucocytes and its activation.

1. Gelatin specific proteinase (gelatinase) exists in human leucocytes extracts mainly in a latent form. 2. It is activated by different proteinases as well as by some chemicals (urea, NaSCN, HgCl2). 3. Non-proteolytic activation of latent gelatinase and the decreasing of its molecular weight associated with it strongly suggests that it is an enzyme-inhibitor complex.

Endopeptidases↗
PubMed1975

Hydroxyproline levels and collagenolytic activity in synovial fluids of patients with rheumatic diseases.

Free, total, and peptide hydroxyproline levels were determined in synovial fluid obtained from the knee joints of 60 patients with theumatoid arthritis (RA), and 26 patients with degenerative joint disease. In addition, in 160 synovial fluid samples obtained from 121 patients including 50 with degenerative joint disease, 60 with RA, 3 with Reiter's syndrome, 3 with hydarthrosis intermittens and 5 with ankylosing spondylitis, the collagenolytic activity was determined. The mean values of free and peptide hydroxyproline in the inflammatory and degenerative fluids were the same, but slight differences were found in the mean values of total hydroxyproline. No effect on the level of free and bound hydroxyproline was observed after treatment with intra-articular hydrocortisone and gold salts. The collagenolytic activity of synovial fluid was registered in 38% of cases of RA and in some cases of Reiter's syndrome and hydrarthrosis intermittens, but it was not found in 50 cases of degenerative joint disease or in cases of ankylosing spondylitis. During a longer observation of patients with inflammatory forms of RA a variability in the collagenolytic activity was observed in repeated examinations of the fluid obtained from the same patient; this activity appeared and disappeared. The incidence of collagenolytic activity and its values were higher in patients with active rheumatoid process and this activity was present more frequently in patients with a short history of the disease (up to 3 years). The collagenolytic activity of rheumatoid fluids was, to a high degree, inhibited by normal human serum. The problem of presence or lack of collagenolytic activity in rheumatoid fluids is discussed.

Adult↗
PubMed1975

Isolation, purification and properties of a factor from rheumatoid synovial fluid activating the latent forms of collagenolytic enzymes.

1. An activator catalysing specifically conversion of latent forms of human leucocyte collagenase and gelatin-specific protease into the active forms, has been isolated from rheumatoid synovial fluid and purified 55-fold with a yield of 16%. 2. Molecular weight of the activator is about 35 000. 3. The activator is thermolabile, and is irreversibly inactivated at pH below 5.5 or in the presence of low concentrations of trypsin or papain; it is resistant to the action of lysozyme, hyaluronidase, diisopropylfluorophosphate, soybean trypsin inhibitor, p-chloromercuribenzoate, iodoacetamide and dithiothreitol. 4. The activator did not show any activity towards collagen, gelatin, casein, haemoglobin, histones, elastin or p-phenylazobenzyloxycarbonyl-peptide.

Arthritis, Rheumatoid↗