Distinct tumor specific expression of TGFB4 ebaf a novel human gene of the TGF- szlig nbsp superfamily

10.2741/a158 ◽  
1997 ◽  
Vol 2 (1) ◽  
pp. a18-25 ◽  
Author(s):  
Siamak Tabibzadeh

Genetics ◽  
2016 ◽  
Vol 204 (3) ◽  
pp. 1057-1064 ◽  
Author(s):  
Eun Yong Kang ◽  
Lisa J. Martin ◽  
Serghei Mangul ◽  
Warin Isvilanonda ◽  
Jennifer Zou ◽  
...  




2000 ◽  
Vol 38 ◽  
pp. S126
Author(s):  
K Nakahira
Keyword(s):  


1992 ◽  
Vol 68 (05) ◽  
pp. 539-544 ◽  
Author(s):  
Catherine Lenich ◽  
Ralph Pannell ◽  
Jack Henkin ◽  
Victor Gurewich

SummaryWe previously found that human pro-UK expressed in Escherichia coli is more active in fibrinolysis than recombinant human pro-UK obtained from mammalian cell culture media. To determine whether this difference is related to the lack of glycosylation of the E. coli product, we compared the activity of E. coli-derived pro-UK [(-)pro-UK] with that of a glycosylated pro-UK [(+)pro-UK] and of a mutant of pro-UK missing the glycosylation site at Asn-302 [(-) (302) pro-UK]. The latter two pro-UKs were obtained by expression of the human gene in a mammalian cell. The nonglycosylated pro-UKs were activated by plasmin more efficiently (≈2-fold) and were more active in clot lysis (1.5-fold) than the (+)pro-UK. Similarly, the nonglycosylated two-chain derivatives (UKs) were more active against plasminogen and were more rapidly inactivated by plasma inhibitors than the (+)UK.These findings indicate that glycosylation at Asn-302 influences the activity of pro-UK/UK and could be the major factor responsible for the enhanced activity of E. coli-derived pro-UK.





2013 ◽  
Author(s):  
AL Bookout ◽  
Y Jeong ◽  
M Downes ◽  
RT Yu ◽  
RM Evans ◽  
...  


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