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Endothelial cells release casein kinase II-like activity capable of phosphorylating fibrinogen in response to thrombin

Authors
Journal
Thrombosis Research
0049-3848
Publisher
Elsevier
Publication Date
Volume
72
Issue
4
Identifiers
DOI: 10.1016/0049-3848(93)90140-j
Keywords
  • Fibrinogen
  • Endothelial Cells
  • Thrombin
  • Casein Kinase Ii
Disciplines
  • Biology

Abstract

Abstract Rat liver endothelial cells cultivated in the absence of serum and activated with thrombin released up to 10 % of the total protein kinase activity into the cell medium using casein or fibrinogen as the phosphate acceptor protein. The activity was partly inhibited by heparin, indicating that it was of the casein kinase II type. The release of kinase started directly after the addition of thrombin (2 NIH U/ml) to the media with two maxima; one after about 10 min and the second after around 30 min. The phosphorylating activity of media from cells incubated for longer times was less dependent on thrombin-induction which probably indicated the start of destruction of the cells. The results reported suggest that phosphorylation of fibrinogen could occur in the blood under acute phase conditions.

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