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The recombinant kringle domain of urokinase plasminogen activator inhibits VEGF165-induced angiogenesis of HUVECs by suppressing VEGFR2 dimerization and subsequent signal transduction

Authors
 Byeong Mo Kim  ;  Dong-Heon Lee  ;  Hyun Jin Choi  ;  Kee-Ho Lee  ;  Su Jin Kang  ;  Young Ae Joe  ;  Yong-Kil Hong  ;  Sung Hee Hong 
Citation
 IUBMB LIFE, Vol.64(3) : 259-265, 2012 
Journal Title
 IUBMB LIFE 
ISSN
 1521-6543 
Issue Date
2012
MeSH
Angiogenesis Inducing Agents ; Blotting, Western ; Cell Movement ; Cell Proliferation ; Cells, Cultured ; Dimerization ; Enzyme-Linked Immunosorbent Assay ; Human Umbilical Vein Endothelial Cells/cytology ; Human Umbilical Vein Endothelial Cells/metabolism* ; Humans ; Kringles ; Matrix Metalloproteinase 2/metabolism ; Neovascularization, Physiologic* ; Phosphorylation ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism* ; Signal Transduction* ; Urokinase-Type Plasminogen Activator/pharmacology* ; Vascular Endothelial Growth Factor A/metabolism* ; Vascular Endothelial Growth Factor Receptor-2/antagonists & inhibitors*
Abstract
The recombinant kringle domain (UK1) of urokinase plasminogen activator was previously reported to exert antiangiogenic activity against Vascular Endothelial Growth Factor (VEGF)-induced angiogenesis in both in vitro and in vivo models. In this study, we explored the molecular signaling mechanisms involved in the antiangiogenic activity of UK1 by examining VEGF signaling proteins. VEGF165 stimulates the phosphorylation of VEGF signaling molecules, and pretreatment with UK1 blocked VEGF-induced signal transduction associated with proliferation, survival, and migration. UK1 also suppressed VEGF165-induced activation of MMP-2. Moreover, UK1 suppressed the phosphorylation and activation of VEGFR2 in VEGF-stimulated human umbilical cord vein endothelial cells (HUVECs) by blocking the dimerization of VEGFR2. Overall, our findings suggest that UK1 inhibits VEGF-induced proliferation, migration, and matrix metalloproteinase activity of HUVECs by suppressing VEGFR2 dimerization and subsequent angiogenic signals.
Full Text
http://onlinelibrary.wiley.com/doi/10.1002/iub.604/abstract
DOI
10.1002/iub.604
Appears in Collections:
5. Research Institutes (연구소) > Yonsei Integrative Research Institute for Cerebral & Cardiovascular Disease (뇌심혈관질환융합연구사업단) > 1. Journal Papers
Yonsei Authors
Kim, Byeong Mo(김병모) ORCID logo https://orcid.org/0000-0002-0582-3132
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/158297
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