Proteases and Glioma Angiogenesis
Year: 2005
Type: review
Abstract: Angiogenesis, the process by which new branches sprout from existing vessels, requires the degradation of the vascular basement membrane and remodeling of the ECM in order to allow endothelial cells to migrate and invade into the surrounding tissues. Serine, metallo, and cysteine proteinases are 3 types of a family of enzymes that proteolytically degrade various components of extracellular matrix. These proteases release various growth factors and also increase adhesive molecules and signaling pathway molecules upon their activation, which plays a significant role in angiogenesis. Downregulation of these molecules by antisense/siRNA or synthetic inhibitors decreases the levels of these molecules, inhibits the release of growth factors, and decreases the levels of various signaling pathway molecules, thereby leading to the inhibition of angiogenesis. Furthermore, MMPs degrade specific substrates and release angiogenic inhibitors which inhibit angiogenesis. Downregulation of 2 molecules, such as uPA and uPAR, uPAR and MMP-9, or Cathepsin B and MMP-9, are more effective to inhibit angiogenesis rather than downregulation of single molecules. However, careful testing of these combinations are most important because multiple effects of these combinations play a significant role in angiogenesis.
Source: Brain Pathology
Institution: Peoria campus of the University of Illinois System
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: green
Awards: G1320390427, Suppression of glioma invasion by a bicistronic constuct, G3760626908, G4091456469, G4366939855, Role of TFPI-2 in human gliomas invasiveness, Role of uPA and uPAR in Human Glioma Invasiveness, G4770781718, Inhibition of glioma tumor growth by antisense MMP-9, Cath B and uPAR si RNA constructs regressed glioma growth, G7746031331, EFFECT OF SERINE PROTEASES BY RADIATION IN CNS INJURY
OpenAlex ID: W1995570995