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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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Plasminogen kringle 5 is a potent inhibitor of endothelial cell proliferation like an endogenous angiogenesis inhibitor, angiostatin consisting of plasminogen kringles 1-4. In this study, we produced the recombinant protein of plasminogen kringle 5 (PK5) employing an Pichia expression system and examined its effect on endothelial cell migration and its possible inhibitory mechanism. PK5 was expressed in Pichia pastoris GS115 by fusion of the cDNA spanning from Thr456 to Phe546 to the secretion signal sequence of α-factor prepro-peptide. After methanol induction, the secreted PK5 was purified by using S-spin column. SDS-PAGE analysis of the purified protein showed one major band of approximately 10 kDa. In in vitro migration assays, the purified protein inhibited dose-dependently the migration of human umbilical endothelial cells (HUVECs) induced by basic fibroblast growth factor (bFGF) or vascular endothelial growth factor (VEGF) with an IC50 of approximately 500 nM. Accordingly, it inhibited bFGF-stimulated extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylation in HUVECs at 500 nM. In addition, it also potently inhibited bFGF-induced cytoskeletal rearrangement of HUVECs. Thus, these results suggest that Pichia-produced PK5 effectively inhibits endothelial cell migration, in part by suppression of ERK1/2 activation and blocking cytoskeleton rearrangement.
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참고문헌 (30)
참고문헌 신청
Cao, Y., A. Chen, S. S. An, R. W. Ji, D. Davidson and M. Llinas. 1997. Kringle 5 of plasminogen is a novel inhibitor of endothelial cell growth. J. Biol. Chem. 272, 22924-22928.
Cao, Y., R. W. Ji, D. Davidson, J. Schaller, D. Marti, S. Sohndel, S. G. McCance, M. S. O'Reilliy, M. Llinas, J. Folkman. 1996. Kringle domains of human angiostatin. Characterization of the anti-proliferative activity on endothelial cells. J. Biol. Chem.
Davidson, D. J., C. Haskell, S. Majest, A. Kherzai, D. A. Egan, K. A. Walter, A. Schneider, E. F. Gubbins, L. Solomon, Z. Chen, R. Lesniewski, J. Henkin. 2005. Kringle 5 of human plasminogen induces apoptosis of endothelial and tumor cells through surface
Gimbrone, M. A., R. S. Jr. Cotran, S. B. Leapman and J. Folkman. 1974. Tumor growth and neovascularization: an experimental model using the rabbit cornea. J. Natl. Cancer Inst. 52, 413-427.
Gonzalez-Gronow, M., T. Kalfa, C. E. Johnson, G. Gawdi and S. V. Pizzo. 2003. The voltage-dependent anion channel is a receptor for plasminogen kringle 5 on human endothelial cells. J. Biol. Chem. 278, 27312-27318.
Cao, Y., R. W. Ji, D. Davidson, J. Schaller, D. Marti, S. Sohndel, S. G. McCance, M. S. O'Reilliy, M. Llinas, J. Folkman. 1996. Kringle domains of human angiostatin. Characterization of the anti-proliferative activity on endothelial cells. J. Biol. Chem.
Davidson, D. J., C. Haskell, S. Majest, A. Kherzai, D. A. Egan, K. A. Walter, A. Schneider, E. F. Gubbins, L. Solomon, Z. Chen, R. Lesniewski, J. Henkin. 2005. Kringle 5 of human plasminogen induces apoptosis of endothelial and tumor cells through surface
Gimbrone, M. A., R. S. Jr. Cotran, S. B. Leapman and J. Folkman. 1974. Tumor growth and neovascularization: an experimental model using the rabbit cornea. J. Natl. Cancer Inst. 52, 413-427.
Gonzalez-Gronow, M., T. Kalfa, C. E. Johnson, G. Gawdi and S. V. Pizzo. 2003. The voltage-dependent anion channel is a receptor for plasminogen kringle 5 on human endothelial cells. J. Biol. Chem. 278, 27312-27318.
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UCI(KEPA) : I410-ECN-0101-2009-470-017617011