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  • Immunosuppression and metalloproteinases  (1)
  • Inhibitors  (1)
  • 1
    ISSN: 1432-2277
    Keywords: Immunosuppression and metalloproteinases ; Metalloproteinases and immunosuppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The concentration of the metalloproteinases type I collagenase and gelatinase was measured in isolated polymorphonuclear leukocytes (PMNLs) of renal transplant recipients treated either with cyclosporin A (CyA) and prednisolone (Pr) (n=8) or azathioprine (Aza) and Pr (n=8), and of healthy subjects (n=12). PMNLs of CyA- and Aza-treated transplant patients displayed markedly higher gelatinase content (2427±489 and 3284±357 ng/107 cells) than PMNLs of controls (528±83 ng/107 cells). There was also a higher content of type I collagenase in PMNLs (3374±292 ng/107 cells) of Aza-treated patients and significantly elevated levels in PMNLs of patients receiving CyA (3625±229 ng/107 cells) compared with healthy subjects (2878±151 ng/107 cells). In contrast, neutrophil lactoferrin content was lower in transplant patients. Thus, immunosuppressive drugs may reduce the release of leukocyte proteinases, which are known for their deleterious role in proteolytic tissue and matrix breakdown. In vitro, the effects of different immunosuppressive drugs on the release of lactoferrin, collagenase and gelatinase were investigated on FMLPNTL-stimulated PMNLs isolated from healthy subjects. CyA but not Aza or Pr caused inhibition of gelatinase, collagenase and lactoferrin release.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 13 (1974), S. 10-28 
    ISSN: 0570-0833
    Keywords: Inhibitors ; Inhibitors ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The natural inhibitors of proteolytic enzymes are proteins. These inhibitors associate reversibly with the enzymes to form stoichiometric protein-protein complexes, in which substrate-analogous association at the active center of the enzyme results in competitive inhibition of all catalytic functions. The very widespread occurrence of inhibitors in the animal and plant kingdoms underlines their biological importance in the intermediate metabolism, which can be understood as an extension of the possibilities for temporary and local limitations of enzyme activities. Existing knowledge includes a series of covalent structures, detailed kinetic data on the reversible protein-protein interaction, the processes involved in inactivation, and chemical methods for the modification of these proteins. Early X-ray structural data for an inhibitor and its enzyme complex provide an insight into the molecular structure of the latter and the interactions involved in the association to form the complex.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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