Induction Of Tissue-Type Plasminogen Activator By Ionizing Radiation In Human Malignant Melanoma Cells

Author(s):  
DAVID A. BOOTHMAN ◽  
MEIZHI WANG ◽  
SAMUEL W. LEE
1994 ◽  
Vol 56 (2) ◽  
pp. 214-218 ◽  
Author(s):  
Raymond Sawaya ◽  
Philip J. Tofion ◽  
Sanjeeva Mohanam ◽  
Francis Ali-Oosman ◽  
Lance A. Liotta ◽  
...  

1993 ◽  
Vol 53 (3) ◽  
pp. 395-400 ◽  
Author(s):  
Michel Houde ◽  
Georges De Bruyne ◽  
Marc Bracke ◽  
Magnus Ingelman-sundberg ◽  
GÓRan Skoglund ◽  
...  

1988 ◽  
Vol 19 (1) ◽  
pp. 107-110
Author(s):  
Tetsuhiro SAKAI ◽  
Kiyotaka OKADA ◽  
Hiroshi BANDO ◽  
Hideharu FUKAO ◽  
Shigeru UESHIMA ◽  
...  

1985 ◽  
Vol 54 (04) ◽  
pp. 788-791 ◽  
Author(s):  
D C Rijken ◽  
J J Emeis ◽  
G J Gerwig

SummaryTwo variants (I and II) of tissue-type plasminogen activator (t-PA) from human melanoma cells were separated by Lysine Sepharose chromatography. The carbohydrate compositions of the forms were determined by gas-liquid chromatography. Variant I contained 12.8 g and variant II 7.1 g of carbohydrate per 100 g protein. Both variants contained N-acetylgalactosamine, suggesting O-glycosylation in addition to N-glycosylation. The possible role of N-linked oligosaccharides for the biological activity of t-PA was studied using t-PA secreted by melanoma cells in the presence of tunicamycin, an inhibitor of N-glycosylation. The latter t-PA showed the same plasminogen activating and fibrin binding properties as normally glycosylated t-PA, indicating that N-linked carbohydrate is not involved in the fibrinolytic activity of t-PA.


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