31 research outputs found

    THE ACTIVATION OF HUMAN NEUTROPHIL GELATINASE

    No full text
    SOPATA I, MICHAELIS J, Tschesche H. THE ACTIVATION OF HUMAN NEUTROPHIL GELATINASE. In: Acta Biochim Pol. ACTA BIOCHIMICA POLONICA. Vol 37. ACTA BIOCHIMICA POLONICA; 1990: 181-185

    EFFECT OF IMMUNOSUPPRESSIVE DRUGS ON THE RELEASE OF METALLOPROTEINASES FROM HUMAN POLYMORPHONUCLEAR LEUKOCYTES

    No full text
    HEMPELMANN U, HAAGWEBER M, HORL WH, Tschesche H. EFFECT OF IMMUNOSUPPRESSIVE DRUGS ON THE RELEASE OF METALLOPROTEINASES FROM HUMAN POLYMORPHONUCLEAR LEUKOCYTES. TRANSPLANT INTERNATIONAL. 1991;4(1):26-30.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/10(7) cells) than PMNLs of controls (528 +/- 83 ng/10(7) cells). There was also a higher content of type I collagenase in PMNLs (3374 +/- 292 ng/10(7) cells) of Aza-treated patients and significantly elevated levels in PMNLs of patients receiving CyA (3625 +/- 229 ng/10(7) cells) compared with healthy subjects (2878 +/- 151 ng/10(7) 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

    EVIDENCE FOR THE TISSUE INHIBITOR OF METALLOPROTEINASES-1 (TIMP-1) IN HUMAN POLYMORPHONUCLEAR LEUKOCYTES

    No full text
    TRIEBEL S, BLASER J, GOTE T, et al. EVIDENCE FOR THE TISSUE INHIBITOR OF METALLOPROTEINASES-1 (TIMP-1) IN HUMAN POLYMORPHONUCLEAR LEUKOCYTES. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1995;231(3):714-719.A tissue inhibitor of metalloproteinases (TIMP)-1 was isolated from human polymorphonuclear leukocytes (PMNL) in a complex with latent 95-kDa gelatinase (matrixmetalloproteinase, MMP-9). It was separated from the enzyme by gel fitration in the presence of SDS. Using a competitive ELISA procedure, we determined that 10% of the isolated gelatinase was complexed with TIMP-1. The presence of the inhibitor in isolated PMNL could also be demonstrated by indirect immunofluorescence using a specific antibody against TIMP-1. Cellular mRNA was isolated from PMNL, which were highly purified by separation via formylMet-Leu-Pro-stimulated chemotactic migration in a Boyden chamber. Using reverse-transcription PCR and Northern blotting, TIMP-1 mRNA was shown to be present in PMNL, suggesting that these cells are also capable of synthesizing TIMP-1
    corecore