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  • 1
    Electronic Resource
    Electronic Resource
    Cathepsin G degrades denatured collagen (1989)
    Springer
    Inflammation 13 (1989), S. 137-145 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Neutrophils are known to contain several metalloproteinases that can damage collagen, a major structural component of the extracellular matrix. Here a neutrophil serine proteinase secreted from activated neutrophils was shown to cleave denatured collagen (gelatin). This serine proteinase was not inhibited by synthetic inhibitors of elastase (elastatinal or Me-O-suc-Ala-Pro-Val-CH2Cl). However, a synthetic inhibitor of cathepsin G (Z-Gly-Leu-Phe-CH2Cl) was able to inhibit the serine proteinase having gelatinolytic activity, indicating that cathepsin G, a major serine proteinase, from neutrophils is responsible for cleaving gelatin. Purified cathepsin G was also shown to degrade gelatin. In further experiments, oxidized glutathione was able to enhance the gelatinolytic activity of cathepsin G. These results show that cathepsin G is capable of cleaving denatured collagen, and its activity is enhanced or stabilized in the presence of gtutathione. The data support the concept that cathepsin G released from neutrophils could play a major role in degrading collagen during inflammation and may in part account for the degradation of extracellular matrix during inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00924785
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Activation of neutrophil collagenase by cathepsin G (1989)
    Springer
    Inflammation 13 (1989), S. 245-258 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Collagenase is secreted from neutrophils as a latent or proenzyme. In an effort to understand the mechanism of collagenase activation in inflammation, human peripheral neutrophils (PMNs) were isolated and incubated with the tumor promotor, phorbol myristate acetate (PMA), which induces the neutrophils to degranulate and secrete proteinases. Neutrophil media were then treated with various activators or inhibitors of collagenase and other proteinases, and the collagenase activity was measured. A serine proteinase secreted from neutrophils, cathepsin G, was found to activate latent collagenase, but it was also found to require activation itself. Both hypochlorous acid (HOCl) and oxidized glutathione (GSSG) were tested for their coilagenase-activating ability and were found to be successful only in the presence of active cathepsin G. A specific cathepsin G inhibitor (0.5 mM Z-Gly-Leu-Phe-CH2Cl) prevented the activation of latent collagenase by HOCl. To confirm these results, purified neutrophil cathepsin G was incubated with a neutrophil proteinase mixture which contained latent collagenase. The collagenase was shown to be activated upon incubation with purified cathepsin G. These results indicate that cathepsin G is a key mediator in neutrophil collagenase activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00914392
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Protein disulphide isomerase from human peripheral blood neutrophils (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 144 (1990), S. 280-286 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protein disulphide isomerase (PDI) is a 56 kDa resident polypeptide of the endoplasmic reticulum of many cell types. We evaluated the ability of human peripheral blood polymorphonuclear neutrophils (PMN) to synthesize both mRNA and proteins. Using in vitro [35S]-methionine labeling of purified PMN, followed by immunoprecipitation of cell lysates with immobilized polyclonal and monoclonal antibodies and analysis by gel electrophoresis, PMN were shown to synthesize many proteins, including actin. In contrast, incorporation of [35S]-methionine into PDI was not detected. Purification of total RNA from PMN and analysis by Northern blots demonstrated the presence in PMN of PDI-RNA. Western immunoblot evaluations of total PMN protein display an immunoreactive-PDI of 56 kDa. Indirect immunofluorescence studies suggest an abundance of immunoreactive-PDI throughout PMN. We therefore conclude that PDI is synthesized in precursor cells of the bone marrow. Phorbol 12-myristate 13-aceiate, a reagent known to affect the degranulation of specific granules, causes the release of immunoreactive-PDI into a post-centrifugation supernatant. PDI, a ubiquitous endoplasmic reticulum resident protein, is shown here to be associated with specific granules in a cell type which has lost its intracellular membrane network during terminal differentiation.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041440214
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    Paper (German National Licenses)
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