Regulation of cell adhesion by PAI-1
- Resource Type
- Authors
- David J. Loskutoff; Scott A. Curriden; Gang Deng; Geng Hu
- Source
- APMIS : acta pathologica, microbiologica, et immunologica Scandinavica. 107(1)
- Subject
- Microbiology (medical)
Receptors, Cell Surface
Pathology and Forensic Medicine
Receptors, Urokinase Plasminogen Activator
chemistry.chemical_compound
Somatomedin B
Plasminogen Activator Inhibitor 1
Cell Adhesion
Immunology and Allergy
Animals
Humans
Vitronectin
Cell adhesion
neoplasms
Integrin binding
Binding Sites
biology
Cell adhesion molecule
General Medicine
Cell biology
Urokinase receptor
chemistry
Plasminogen activator inhibitor-1
biology.protein
biological phenomena, cell phenomena, and immunity
Plasminogen activator
- Language
- ISSN
- 0903-4641
Type I plasminogen activator inhibitor (PAI-1) is the primary inhibitor of tissue- and urokinase-type plasminogen activators. It circulates in plasma complexed with vitronectin (VN), the primary PAI-1 binding protein. The somatomedin B (SMB) domain of VN contains both the high affinity PAI-1 binding site and the specific site for urokinase plasminogen activator receptor (uPAR). PAI-1 is able to regulate uPAR-mediated cell adhesion by competing with uPAR for VN binding. Binding of PAI-1 to SMD may also affect integrin-mediated cell adhesion to VN by hindering integrin binding to the RGD sequence adjacent to the uPAR binding site.