Activation of pro‐urokinase by the human T cell‐associated serine proteinase HuTSP‐1

FEBS Letters

Kramer, Michael D.²  Brunner, Georg³  Simon, Markus M.¹ 

[1] Max-Planck-Institute or Immunobiology, Stübeweg 51, 7800 Freiburg, FRG;Department of Dermatology, University of Heidelberg, Vossstr. 2, 6900 Heidelberg, FRG;German Cancer Research Centre, Institute of Immunology and Genetics, Im Neuenheimer Feld 280, 6900 Heidelberg, FRG

关键词: Plasminogen activator;    Urokinase;    Pro-urokinase;    Proenzyme activation;    T cell-associated serine proteinase-1;    PA;    plasminogen activator;    pro-uPA;    pro-urokinase;    rpro-uPA;    recombinant pro-urokinase;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    tPA;    tissue type plasminogen activator;    uPA;    urokinase type plasminogen activator;    HuTSP-1;    human T cell-associated serine proteinase-1;   

DOI  :  10.1016/0014-5793(90)80087-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The human T cell-associated serine proteinase-1 (HuTSP-1) is expressed by activated T lymphocytes and is exocytosed upon their interaction with target cells. Here, we report that HuTSP-1 is able to convert single-chain human pro-urokinase into the active two-chain enzyme. Time-dependent activation by HuTSP-1 of recombinant human pro-urokinase as well as natural pro-urokinase derived from human melanoma cells was demonstrated in a chromogenic assay specific for active urokinase type plasminogen activator and in immunoblotting experiments revealing the conversion of single-chain into two-chain urokinase. Control experiments excluded plasmin as the activating agent. These data suggest a novel pathway for plasmin generation during T cell-mediated processes such as immune responses and extravasation of immune cells.

【 授权许可】

Unknown