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Thrombin Disintegrates Cell Surface Urokinase Focal Adhesion Plaques and Decreases Cell Extension: Implications for Axonal Growth

  • Caroline A. Hébert
  • Joffre B. Baker
Part of the NATO ASI Series book series (NSSA, volume 191)

Abstract

In addition to its function as the ultimate protease in the coagulation cascade thrombin has several hormone-like effects on cells in vitro. This serine protease is a potent mitogen for fibroblastic cells from several species.1,2 In addition, like other growth factors,3 thrombin can modulate cellular differentiation. Thrombin or a closely related protease present on neuroblastoma cells antagonizes formation of neurite extensions.4 Furthermore thrombin has recently been identified as the primary serum inhibitor of neurite extension in neuroblastoma cell cultures.5 In the present paper we show that thrombin, but not other growth factors tested, causes the disappearance on human fibroblasts of linear strands of cell surface urokinase-type plasminogen activator, strands which have recently been shown to colocalize with cell-to-substratum focal adhesion plaques (FAPs)6,7 Disappearance or gross alteration of FAPs in fact accompanies the thrombin-mediated dissolution of the cell surfaced urokinase strands.

Keywords

Platelet Derive Growth Factor Phorbol Myristate Acetate Phorbol Myristate Acetate Focal Contact Neurite Extension 
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 1990

Authors and Affiliations

  • Caroline A. Hébert
    • 1
  • Joffre B. Baker
    • 1
  1. 1.Department of BiochemistryUniversity of KansasLawrenceUSA

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