Regular ArticleInvolvement of the [uPAR:uPA:PAI-1:LRP] Complex in Human Myogenic Cell Motility
References (51)
- et al.
Serine protease and metalloprotease cascade systems involved in pericellular proteolysis
Cell. Differ. Dev.
(1990) uPA, uPAR, PAI-1: Key intersection of proteolytic, adhesive and chemotactic highways?
Immunol. Today
(1997)- et al.
Focalized proteolysis: Spatial and temporal regulation of extracellular matrix degradation at the cell surface
Curr. Opin. Cell Biol.
(1996) - et al.
Structural requirements for the extracellular interaction of plasminogen activator inhibitor 1 with endothelial cell matrix-associated vitronectin
J. Biol. Chem.
(1990) - et al.
Purified α2-macroglobulin receptor/LDL receptor-related protein binds urokinase plasminogen activator inhibitor type-1 complex
J. Biol. Chem.
(1992) - et al.
Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes
FEBS Lett.
(1994) - et al.
Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator–plasminogen activator inhibitor type-1 complexes
J. Biol. Chem.
(1993) - et al.
The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase–plasminogen activator inhibitor type I complexes
J. Biol. Chem.
(1995) - et al.
Very low density lipoprotein receptor binds and mediates endocytosis of urokinase-type plasminogen activator–type-1 plasminogen activator inhibitor complex
J. Biol. Chem.
(1995) - et al.
Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independent of its function as an inhibitor of plasminogen activation
Exp. Cell Res.
(1997)
Primary human muscle satellite cell culture: Variations of cell yield, proliferation and differentiation according to age and sex of donors, site of muscle biopsy, and delay before processing
Biol. Cell.
Attenuation of thrombolysis by release of plasminogen activator inhibitor type-1 from platelets
Thromb Res.
Modulation of activities and RNA level of the components of the plasminogen activation system during fusion of human myogenic satellite cells in vitro
Dev. Biol.
Cell migration: A physically integrated molecular process
Cell
Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
J. Biol. Chem.
Identification of the urokinase receptor as an adhesion receptor for vitronectin
J. Biol. Chem.
The urokinase receptor is a major vitronectin-binding protein on endothelial cells
Exp. Cell Res.
Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
Curr. Opin. Cell Biol.
Plasminogen activator inhibitor-1 contains a cryptic high affinity binding site for the low density lipoprotein receptor-related protein
J. Biol. Chem.
Actin-based cell motility and cell locomotion
Cell
Extracellular matrix remodeling by metalloproteinases and plasminogen activators
Kidney Int.
The plasminogen activator/plasmin system
J. Clin. Invest.
The cell biology of the plasminogen system
FASEB J.
Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin
J. Biol. Chem.
α2-Macroglobulin receptor/LDL receptor-related protein (Lrp)-dependent internalization of the urokinase receptor
J. Cell Biol.
Cited by (46)
Angiotensin II-induced smooth muscle cell migration is mediated by LDL receptor-related protein 1 via regulation of matrix metalloproteinase 2 expression
2010, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Our finding that LRP1 silencing resulted in a significant decrease in Ang II-induced RAoSMCs migration is consistent with a previous report that LRP1 is essential to human vascular smooth muscle cell migration [10]. Moreover, functional blocking of LRP1 by RAP also led to decreased cell migration, which is also consistent with reports that RAP treatment decreased migration of breast cancer cells, myogenic cells [8,21], as well as smooth muscle cells [9,22], indicating the ligand binding activity of LRP1 is associated with cellular migratory mechanism. In contrast, there are reports that knockdown or deletion of LRP1 increased cell migration, likely by decreasing the catabolic rate of the uPA:PAI-1:uPAR complex [23,24].
The plasminogen activator inhibitor "paradox" in cancer
2008, Immunology LettersThe PAI-1 swing: Microenvironment and cancer cell migration
2006, Comptes Rendus - BiologiesDual role for plasminogen activator inhibitor type 1 as soluble and as matricellular regulator of epithelial alveolar cell wound healing
2006, American Journal of PathologyCitation Excerpt :PAI-1 is found either soluble or matrix-bound,26,49–51 where it plays diverse roles in adhesion depending on the cell type or the experimental conditions. Matrix-bound PAI-1 can either promote cell adhesion21,25,27 and subsequent migration24,28,40,52 or deadhesion.20,22,23,53 The inhibition of healing in the presence of blocking antibodies against PAI-1, dependent on the concentration (up to 40% with 50 μg/ml), together with the dramatic increase in matrix bound PAI-1 (Figure 4D) suggests that a nonproteolytic action of the uPA system is involved in the KGF-induced wound healing.
Interleukin-4 improves the migration of human myogenic precursor cells in vitro and in vivo
2006, Experimental Cell Research
- 1
To whom reprint requests should be addressed. Fax: (33) 1 49 81 36 42. E-mail: [email protected].