Decreased thrombin affinity of cell-surface thrombomodulin following treatment of cultured endothelial cells with β-D-xyloside

John F. Parkinson, Joe G.N. Garcia, Nils U. Bang

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Thrombomodulin, an endothelial cell-surface anticoagulant, has been postulated to contain a glycosaminoglycan. Thrombomodulin function was therefore studied in endothelial cells treated with β-D-xyloside, an inhibitor of glycosaminoglycan attachment to proteoglycan core proteins. β-D-xyloside caused a reproducible 3 to 5-fold increase in the Km of thrombomodulin for thrombin and a 20-30% decrease in the rate of protein C activation by the thrombin-thrombomodulin complex. These results support a role for glycosaminoglycans in thrombomodulin function and suggest that β-D-xylosides can be used to investigate both the anticoagulant mechanisms and the biosynthesis of cell-surface thrombomodulin.

Original languageEnglish (US)
Pages (from-to)177-183
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume169
Issue number1
DOIs
StatePublished - May 31 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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