Translocation of plasminogen activator inhibitor type 2 in vivo: High expression levels result in intracellular polymerisation

1994 ◽  
Vol 8 ◽  
pp. 28
Author(s):  
P. Mikus ◽  
T. Ny
Keyword(s):  
Plasminogen Activator ◽  
Plasminogen Activator Inhibitor ◽  
High Expression ◽  
Expression Levels ◽  
Plasminogen Activator Inhibitor Type ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor

scholarly journals Interaction between Plasminogen Activator Inhibitor Type-2 and Pre-mRNA Processing Factor 8

2004 ◽  
Vol 36 (9) ◽  
pp. 623-628 ◽  
Author(s):  
Jing Fan ◽  
Yu-Qing Zhang ◽  
Ping Li ◽  
Chang Tong ◽  
Li Tan ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Plasminogen Activator Inhibitor ◽  
Mrna Processing ◽  
Processing Factor ◽  
Plasminogen Activator Inhibitor Type ◽  
Inhibitor Type ◽  
Activator Inhibitor Type ◽  
Activator Inhibitor

Abstract The plasminogen activator inhibitor type-2 (PAI-2) dependent apoptosis protection is due to the 33 amino acids fragment located between helix C and D of PAI-2, this fragment may interact with some unknown intracellular proteins. In this study we used the fragment between helix C and D of PAI-2 as a bait to perform a yeast two-hybrid screen using a cDNA library constructed with HeLa cells during apoptosis, and retrieved a clone encoding 94 amino acid residues of C-terminus of pre-mRNA processing factor 8 (PRPF8). Co-immunoprecipitation experiments confirmed that PAI-2 could interact with PRPF8 in vivo. PAI-2 could bind PRPF8 C-terminal in both the inside and outside of nuclear. These results suggested that the interaction between these two proteins might not be involved in the apoptosis process.

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