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Endothelial cells release casein kinase II like activity capable of phosphorylating fibrinogen in response to thrombin
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (ek pia)
1993 (English)In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 72, no 4, 315-320 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
1993. Vol. 72, no 4, 315-320 p.
Keyword [en]
fibrinogen, endothelial cells, thrombin, casein kinase II
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-173190DOI: 10.1016/0049-3848(93)90140-JPubMedID: 8303671OAI: oai:DiVA.org:uu-173190DiVA: diva2:516839
Available from: 2012-04-20 Created: 2012-04-20 Last updated: 2017-12-07Bibliographically approved

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Ekman, Pia

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