Wyniki wyszukiwania

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Matrix degrading proteinases from human granulocytes: type I, II, III collagenase, gelatinase and type IV, V-collagenase. A survery of recent findings and inhibition by gamma-anticollagenase

100%

Tschesche H., Fedrowitz J., Kohnert U., Michaelis J., Macartney H. W.

Folia Histochemica et Cytobiologica

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1986

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tom 24

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nr 2

2

Modulation of testicular macrophage activity by collagenase

100%

Bryniarski K., Szczepanik M., Ptak M., Ptak W.

Folia Histochemica et Cytobiologica

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2005

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tom 43

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nr 1

3

Setaria cervi collagenase: IgG cleavage and inhibition by Wuchereria bancrofti infected sera

100%

Srivastava Y., Gupta S., Pokharel D. R., Rathaur S.

Acta Parasitologica

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2004

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tom 49

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nr 3

Significant protease activity has been detected in somatic extract of adults and microfilarial stage of Setaria cervi, using general protease substrates and collagen. The pH optima studies of the somatic extract of adult females showed two peaks at 7.0 and 5.0 for collagenase activity. Both forms were purified using sequential DEAE-sepharose and Sephadex G-100 column chromatography. The purified enzymes had the molecular masses of 175 and 20 kDa and pH optima at 7.0 and 5.0, respectively. The 175 kDa collagenase was more sensitive to metal chelators and serine protease inhibitors. However, 20 kDa collagenase was sensitive to cysteine protease inhibitors. The IgG antibodies from W. bancrofti infected human sera inhibited both enzymes. Further the purified collagenases were used to digest total human IgG at their respective pH and for different lengths of time. The 175 kDa protein was capable of cleaving human IgG. The digestion appeared to be restricted to a single cleavage point of H-chain within the hinge region of IgG molecule and produced fragments of similar molecular mass (27 kDa) indicating cleavage to Fab and Fc fragments. The degree of digestion was found to be proportional to the incubation time at 37°C. No further digestion of either fragments were observed. The L-chains were apparently resistant to collagenase digestion in all cases. Thus, the results suggest that S. cervi collagenase might be involved in the defense mechanisms of the parasite against the immune response of the host.

4

Immunoreactivity of chemically cross-linked gluten and hydrolysates of wheat flour

84%

Majak I., Leszczynska J., Lacka A.

Biotechnology and Food Science

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2011

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tom 75

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nr 2

5

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Biochemical characterisation of the tissue degrading enzyme, collagenase, in the spined soldier bug, Podisus maculiventris (Hemiptera: Pentatomidae)

84%

Ghamari M., Hosseininaveh V., Darvishzadeh A., Talebi K.

Journal of Plant Protection Research

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2014

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tom 54

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nr 2

Podisus maculiventris (Say) is a generalist predator attacking many insect species from different orders. The bug injects saliva into its prey's body. The ingested hemolymph and liquefied internal tissues pass through the bug's alimentary tract. Collagenase working on peptide bonds of collagen and basement membrane proteins, leads to the disintegration of the prey's internal organs. As yet, there is an almost complete lack of knowledge on the collagenase activity in P. maculiventris. The collagenase activity of the salivary glands and midgut was optimum at pH 8.0 which was congruent with the optimal pH of the total proteolytic activity of the salivary glands. More collagenolytic activity was determined in the posterior lobe of the salivary glands and anterior midgut. Significant inhibition of collagenolytic activity by ethylenediaminetetraacetic acid (EDTA) revealed the enzyme is a metalloproteinase. The collagenase activity notably decreased when the bug went hungry. The salivary gland collagenase is a vital enzyme in extra-oral digestion and facilitates the action of other digestive enzymes. The midgut collagenase may be involved in the digestion of the ingested muscle fibers. The collagenase probably acts as an intoxicating agent in the saliva (venom) of P. maculiventris. Paralysing toxins are present in the salivary gland secretion.

6

Fibronectin and fibrinogen degradation products stimulate PMN-leukocyte and mast cell degranulation

84%

Wojtecka-Lukasik E., Maslinski S.

Journal of Physiology and Pharmacology

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1992

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tom 43

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nr 2

The ability of various peptides cleaved by plasmin from human fibrinogen and fibronectin or fibrinogen- and fibronectin- related synthetic peptides to induce histamine release from mast cells and collagenase and elastase from PMN- leukocytes was examined. Low molecular weight fibrinogen degradation products showed dose dependent secretion of collagenase. These peptides (mol. wt. 1.4 kD) at the concentration of 10⁻⁵ M released about 47% of collagenase and 13% of elastase. Synthetic fib- rinopeptides A and В had a similar strong collagenase releasing potency and also released histamine from mast cells. Peptides from plasmin digestion of fibronectin containing cell attachment site with sequence Arg-Gly-Asp-Ser and also synthetic peptide reproducing this aminoacid sequence at the concentration of 1000 µg/ml released about 50% of collagenase and 55% of elastase from PMN-leukocytes. Moreover peptides containing cell attachment and gelatin binding site induced histamine release from mast cells. The association of fibrinogen and fibronectin degradation with activation of mast cells may motivate the treatment with antihistaminic drugs of all pathological conditions where the intensive protein degradation takes place.

7

Central activity of peptide Gly-Pro-Hyp-the main component of collagen degradation products mixture

67%

Wisniewski K., Artemowicz B., Lutostanska A., Mackowiak J., Koziolkiewicz W.

Acta Neurobiologiae Experimentalis

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1994

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tom 54

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nr 1

8

The activity of enzymes of different subcellular localization in the wall of aortic aneurysm and parietal thrombus

67%

Gacko M., Worowska A., Glowinski S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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2000

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tom 48

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nr 3

Ograniczanie wyników

Matrix degrading proteinases from human granulocytes: type I, II, III collagenase, gelatinase and type IV, V-collagenase. A survery of recent findings and inhibition by gamma-anticollagenase

Modulation of testicular macrophage activity by collagenase

Setaria cervi collagenase: IgG cleavage and inhibition by Wuchereria bancrofti infected sera

Immunoreactivity of chemically cross-linked gluten and hydrolysates of wheat flour

Biochemical characterisation of the tissue degrading enzyme, collagenase, in the spined soldier bug, Podisus maculiventris (Hemiptera: Pentatomidae)

Fibronectin and fibrinogen degradation products stimulate PMN-leukocyte and mast cell degranulation

Central activity of peptide Gly-Pro-Hyp-the main component of collagen degradation products mixture

The activity of enzymes of different subcellular localization in the wall of aortic aneurysm and parietal thrombus