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• W2253432203 abstract "Research Article1 August 1989free access Modulation of morphological differentiation of human neuroepithelial cells by serine proteases: independence from blood coagulation. R.J. Grand R.J. Grand Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author P.W. Grabham P.W. Grabham Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author M.J. Gallimore M.J. Gallimore Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author P.H. Gallimore P.H. Gallimore Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author R.J. Grand R.J. Grand Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author P.W. Grabham P.W. Grabham Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author M.J. Gallimore M.J. Gallimore Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author P.H. Gallimore P.H. Gallimore Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. Search for more papers by this author Author Information R.J. Grand1, P.W. Grabham1, M.J. Gallimore1 and P.H. Gallimore1 1Department of Cancer Studies, University of Birmingham, Medical School, Walmer, Kent, UK. The EMBO Journal (1989)8:2209-2215https://doi.org/10.1002/j.1460-2075.1989.tb08344.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have previously shown that a serum protein, termed differentiation reversal factor (DRF), is responsible for neurite retraction in differentiated cultures of an adenovirus 12 (Ad12) transformed human retinoblast cell line. Data is presented here to show that DRF is identical to the serine protease prothrombin. Both proteins have been immunoprecipitated using an antibody raised against purified prothrombin and have been shown to hydrolyse a specific thrombin substrate only after activation by the snake venom ecarin. Following addition to Ad12 HER 10 cells, which had previously been differentiated by culture in the presence of 2 mM dibutyryl cAMP in serum-free medium, thrombin and prothrombin caused half-maximal retraction of neurites at concentrations of 0.5 ng/ml and 20 ng/ml respectively. Interestingly, activation of prothrombin was shown to be unnecessary for biological activity. Using the inhibitor di-isopropylfluorophosphate (DIP), we have shown that abrogation of the proteolytic activity of thrombin also results in a loss (greater than 2000 fold) of differentiation reversal activity. Thrombin and its zymogen both stimulated the mitosis of differentiated Ad12 HER 10 cells to a similar extent. In addition, differentiation reversal was highly specific since, at physiologically significant concentrations, closely related serine proteases did not cause neurite retraction. Prothrombin and thrombin also reversed morphological differentiation in the SK-N-SH neuroblastoma cell line and in heterogeneous cultures of cells from various regions in the human foetal brain. Previous ArticleNext Article Volume 8Issue 81 August 1989In this issue RelatedDetailsLoading ..." @default.
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• W2253432203 title "Modulation of morphological differentiation of human neuroepithelial cells by serine proteases: independence from blood coagulation." @default.
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