Our present findings of the specific ubiquitin ligase for topo IIα could provide Epoxomicin means of elucidating the mechanisms of topo IIα degradation to better attack the resistance of microenvironmentally stressed solid tumors either with proteasome inhibitors used currently in the clinic or by targeting specific components of the ubiquitin system.
Acknowledgments
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea Government (MEST) through the Research Center for Resistant Cells (R13-2003-009).
Keywords
Snake venom VEGF; VEGFR-2; Interaction; Neuropilins; Capillary permeability
Introduction
Snake venoms represent an extraordinary source of biologically active molecules. For instance, it has been shown that several venom proteins are able to induce endothelial cell growth and angiogenesis [1]. These proteins are closely related to the human vascular endothelial growth factor (VEGF), and are capable of strongly increasing capillary permeability, thereby presumably facilitating the access of neurotoxic venom components to their target cells. These snake venom VEGFs (svVEGFs) may be very useful and attractive tools for the study of angiogenesis and the treatment of cardiovascular diseases.
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Expression pattern analysis of the putative
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