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A Serine Proteinase as a “Trigger” for Human Natural Killer Lymphocyte-Mediated Cytolysis

  • Dorothy Hudig
  • Lory Minning
  • Doug Redelman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 187)

Abstract

The nature of the lesion created by cytotoxic lymphoyctes is not yet known. However, current evidence is consistent with insertion of a hydrophobic pore or channel into the membrane of the target cell. The sieving properties (1, 2) and morphological appearance (3, 4, 5) of the membranes of dead target cells are similar but not identical to the properties of erythrocyte membranes after complement attack. Efforts to determine whether or not the lymphocyte-mediated lesions could be composed of complement or complement-like proteins have been negative (6, 7) or substantially inconclusive (8). We approached the problem in a different manner, reasoning that if there were similarities between complement- and lymphocyte-mediated lesions, then a serine dependent proteinase cascade could regulate the lymphocyte system in a manner similar to the regulation characterized by complement proteinases D and Bb or Clr, Cls, and C2a.

Keywords

K562 Cell Serine Proteinase Activity Active Site Serine Proteinase Active Site Basic Pancreatic Trypsin Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Dorothy Hudig
    • 1
  • Lory Minning
    • 1
    • 2
  • Doug Redelman
    • 1
  1. 1.Department of Microbiology School of MedicineUniversity of Nevada, RenoRenoUSA
  2. 2.UC San Diego Cancer CenterLa JollaUSA

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