Document Detail


Acute phase protein alpha 1-acid glycoprotein interacts with plasminogen activator inhibitor type 1 and stabilizes its inhibitory activity.
MedLine Citation:
PMID:  11418606     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
alpha(1)-Acid glycoprotein, one of the major acute phase proteins, was found to interact with plasminogen activator inhibitor type 1 (PAI-1) and to stabilize its inhibitory activity toward plasminogen activators. This conclusion is based on the following observations: (a) alpha(1)-acid glycoprotein was identified to bind PAI-1 by a yeast two-hybrid system. Three of 10 positive clones identified by this method to interact with PAI-1 contained almost the entire sequence of alpha(1)-acid glycoprotein; (b) this protein formed complexes with PAI-1 that could be immunoprecipitated from both the incubation mixtures and blood plasma by specific antibodies to either PAI-1 or alpha(1)-acid glycoprotein. Such complexes could be also detected by a solid phase binding assay; and (c) the real-time bimolecular interactions monitored by surface plasmon resonance indicated that the complex of alpha(1)-acid glycoprotein with PAI-1 is less stable than that formed by vitronectin with PAI-1, but in both cases, the apparent K(D) values were in the range of strong interactions (4.51 + 1.33 and 0.58 + 0.07 nm, respectively). The on rate for binding of PAI-1 to alpha(1)-glycoprotein or vitronectin differed by 2-fold, indicating much faster complex formation by vitronectin than by alpha(1)-acid glycoprotein. On the other hand, dissociation of PAI-1 bound to vitronectin was much slower than that from the alpha(1)-acid glycoprotein, as indicated by 4-fold lower k(off) values. Furthermore, the PAI-1 activity toward urokinase-type plasminogen activator and tissue-type plasminogen activator was significantly prolonged in the presence of alpha(1)-acid glycoprotein. These observations suggest that the complex of PAI-1 with alpha(1)-acid glycoprotein can play a role as an alternative reservoir of the physiologically active form of the inhibitor, particularly during inflammation or other acute phase reactions.
Authors:
J Boncela; I Papiewska; I Fijalkowska; B Walkowiak; C S Cierniewski
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2001-06-19
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  276     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2001 Sep 
Date Detail:
Created Date:  2001-09-17     Completed Date:  2001-10-25     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  35305-11     Citation Subset:  IM    
Affiliation:
Center for Microbiology and Virology, Polish Academy of Sciences 93-232 Lodz, Poland.
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MeSH Terms
Descriptor/Qualifier:
Humans
Orosomucoid / metabolism*
Plasminogen Activator Inhibitor 1 / metabolism*
Precipitin Tests
Protein Binding
Surface Plasmon Resonance
Tissue Plasminogen Activator / antagonists & inhibitors
Two-Hybrid System Techniques
Urokinase-Type Plasminogen Activator / antagonists & inhibitors
Vitronectin / metabolism
Chemical
Reg. No./Substance:
0/Orosomucoid; 0/Plasminogen Activator Inhibitor 1; 0/Vitronectin; EC 3.4.21.68/Tissue Plasminogen Activator; EC 3.4.21.73/Urokinase-Type Plasminogen Activator

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