scholarly journals Tyrosine 67 in the epidermal growth factor-like domain of tissue-type plasminogen activator is important for clearance by a specific hepatic receptor.

1992 ◽  
Vol 267 (14) ◽  
pp. 9668-9677 ◽  
Author(s):  
R Bassel-Duby ◽  
N.Y. Jiang ◽  
T Bittick ◽  
E Madison ◽  
D McGookey ◽  
...  
1990 ◽  
Vol 63 (03) ◽  
pp. 464-471 ◽  
Author(s):  
James Wilhelm ◽  
Narender K Kalyan ◽  
Shaw Guang Lee ◽  
Wah-Tung Hum ◽  
Ruth Rappaport ◽  
...  

SummaryΔ2−89 t-PA is a deletion mutant lacking the finger (F) and epidermal growth factor (EGF) domains; thus, the fibrin interaction of this molecule must be mediated solely by the kringle region. In the present study, the influence of the oligosaccharide side-chains on the activity of Δ2−89 t-PA has been investigated. Δ2−89 t-PA was secreted in two forms, designated I and II, which presumably differ by the lack of one asparagine-linked oligosaccharide in the kiiugle 2 domain of form TT, Forms I and II of Δ2−89 t-PA weie puiified; form II displayed higher fibrinolytic activity than form I. When foini I was partially deglycosylated or treated to remove sialic acid, fibrinolytic activity was increased. Production of Δ2−89 in the presence of timicamycin led to secielion of a glyean-free activator with higher activity. These findings suggest that certain oligusacchaiide side chains, particularly (hose containing sialic acid, can interfere with the interaction between the kringle region of t-PA and fibrin.


Author(s):  
Kimberly J. Riehle ◽  
Melissa M. Johnson ◽  
Fredrik Johansson ◽  
Renay L. Bauer ◽  
Brian J. Hayes ◽  
...  

2003 ◽  
Vol 270 (8) ◽  
pp. 1850-1854 ◽  
Author(s):  
Uffe B. Westergaard ◽  
Mikkel H. Andersen ◽  
Christian W. Heegaard ◽  
Sergey N. Fedosov ◽  
Torben E. Petersen

Sign in / Sign up

Export Citation Format

Share Document