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A functional prothrombin gene product is synthesized by human kidney cells

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Author

  • Leisa Stenberg
  • Mark A. Brown
  • Elise Nilsson
  • Otto Ljungberg
  • Johan Stenflo

Summary, in English

gamma -carboxylated polypeptides were detected in the human kidney by immunohistochemistry with a monoclonal antibody (M3B) specific for gamma -carboxyglutamyl residues. An similar to 70-kDa gamma -carboxylated protein, subsequently identified as prothrombin, was isolated from the intracellular compartment of cultured human embryonic kidney (HEK293) cells by immunoaffinity chromatography on M3B-coupled resin. Immunohistochemical analyses demonstrated that prothrombin and another vitamin K-dependent protein, the growth arrest-specific protein 6, were detectable in human kidney. As in the liver, the kidney synthesizes prothrombin as a zymogen that can be cleaved by ecarin to an amidolytically active serine protease that is inhibited by hirudin, This demonstrates for the first time the de novo synthesis of a full-length, gamma -carboxylated, and functional prothrombin gene product by human kidney cells.

Publishing year

2001

Language

English

Pages

1036-1041

Publication/Series

Biochemical and Biophysical Research Communications

Volume

280

Issue

4

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Keywords

  • kidney
  • prothrombin
  • γ-carboxyglutamate
  • HEK293 cells
  • growth arrest-specific protein 6
  • nephrolithiasis

Status

Published

Research group

  • Clinical Chemistry, Malmö
  • Pathology, Malmö

ISBN/ISSN/Other

  • ISSN: 1090-2104