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Endothelial protein c receptor-dependent inhibition of migration of human lymphocytes by protein c involves epidermal growth factor receptor

Academic Article
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Overview

authors

  • Feistritzer, C.
  • Mosheimer, B. A.
  • Sturn, D. H.
  • Riewald, Matthias
  • Patsch, J. R.
  • Wiedermann, C. J.

publication date

  • January 2006

journal

  • Journal of Immunology  Journal

abstract

  • The protein C pathway is an important regulator of the blood coagulation system. Protein C may also play a role in inflammatory and immunomodulatory processes. Whether protein C or activated protein C affects lymphocyte migration and possible mechanisms involved was tested. Lymphocyte migration was studied by micropore filter assays. Lymphocytes that were pretreated with protein C (Ceprotin) or activated protein C (Xigris) significantly reduced their migration toward IL-8, RANTES, MCP-1, and substance P, but not toward sphingosine-1-phosphate. The inhibitory effects of protein C or activated protein C were reversed by Abs against endothelial protein C receptor and epidermal growth factor receptor. Evidence for the synthesis of endothelial protein C receptor by lymphocytes is shown by demonstration of receptor mRNA expression and detection of endothelial protein C receptor immunoreactivity on the cells' surface. Data suggest that an endothelial protein C receptor is expressed by lymphocytes whose activation with protein C or activated protein C arrests directed migration. Exposure of lymphocytes to protein C or activated protein C stimulates phosphorylation of Tyr845 of epidermal growth factor receptor, which may be relevant for cytoprotective effects of the protein C pathway.

subject areas

  • Antigens
  • Antigens, CD
  • Apoptosis
  • Blood Coagulation Factors
  • Cell Movement
  • Cells, Cultured
  • Chemotaxis, Leukocyte
  • Endothelium, Vascular
  • Glycoproteins
  • Humans
  • In Vitro Techniques
  • Lymphocytes
  • Protein C
  • Receptor, Epidermal Growth Factor
  • Receptors, Cell Surface
  • Signal Transduction
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Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 16393989
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Additional Document Info

start page

  • 1019

end page

  • 1025

volume

  • 176

issue

  • 2

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