Document Detail


Protease nexin-1 inhibits plasminogen activation-induced apoptosis of adherent cells.
MedLine Citation:
PMID:  14699093     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Degradation of adhesive glycoproteins by plasmin is implicated in cell migration. In this study, we further explored the role of plasminogen activation in cell adhesion and survival and show that uncontrolled plasminogen activation at the cell surface may induce cell detachment and apoptosis. We hypothesized that this process could be prevented in adherent cells by expression of protease nexin-1, a potent serpin able to inhibit thrombin, plasmin, and plasminogen activators. Using two- and three-dimensional culture systems, we demonstrate that Chinese hamster ovary fibroblasts constitutively express tissue-type plasminogen activator and efficiently activate exogenously added plasminogen in a specific and saturable manner (K(m) = 46 nm). The formation of plasmin results in proteolysis of fibronectin and laminin, which is followed by cell detachment and apoptosis. Protease nexin-1 expressed by transfected cells significantly inhibited the activity of plasmin and tissue-type plasminogen activator via the formation of inhibitory complexes and prevented cell detachment and apoptosis. In conclusion, protease nexin-1 may be an important anti-apoptotic factor for adherent cells. This cell model could be a useful tool to evaluate therapeutic agents such as serpins in vascular pathologies involving pericellular protease-protease inhibitor imbalance.
Authors:
Patrick Rossignol; Benoît Ho-Tin-Noé; Roger Vranckx; Marie-Christine Bouton; Olivier Meilhac; H Roger Lijnen; Marie-Claude Guillin; Jean-Baptiste Michel; Eduardo Anglés-Cano
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2003-12-29
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  279     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-08     Completed Date:  2004-05-19     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:  10346-56     Citation Subset:  IM    
Affiliation:
INSERM U460, Centre Hospitalier Universitaire Bichat-Claude Bernard, Paris 18, France.
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MeSH Terms
Descriptor/Qualifier:
Amyloid beta-Protein Precursor
Animals
Anoikis*
Apoptosis*
CHO Cells
Carrier Proteins / physiology*
Caspases / metabolism
Cell Adhesion
Cell Culture Techniques
Cell Division
Cell Survival
Cell-Free System
Cricetinae
DNA / chemistry
DNA Fragmentation
Dose-Response Relationship, Drug
Fibronectins / chemistry
Humans
Immunoblotting
In Situ Nick-End Labeling
Kinetics
Laminin / chemistry
Matrix Metalloproteinase 9 / metabolism
Plasminogen / chemistry,  metabolism*
Plasminogen Activator Inhibitor 1 / metabolism
Receptors, Cell Surface
Time Factors
Transfection
Urokinase-Type Plasminogen Activator / metabolism
Chemical
Reg. No./Substance:
0/Amyloid beta-Protein Precursor; 0/Carrier Proteins; 0/Fibronectins; 0/Laminin; 0/Plasminogen Activator Inhibitor 1; 0/Receptors, Cell Surface; 0/protease nexins; 9001-91-6/Plasminogen; 9007-49-2/DNA; EC 3.4.21.73/Urokinase-Type Plasminogen Activator; EC 3.4.22.-/Caspases; EC 3.4.24.35/Matrix Metalloproteinase 9

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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