- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Recently Accepted Articles ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Journal of Ophthalmology
Volume 2010 (2010), Article ID 465824, 11 pages
ERK5 Contributes to VEGF Alteration in Diabetic Retinopathy
Department of Pathology, Schulich School of Medicine, University of Western Ontario, London, ON, Canada N6A 5A5
Received 15 December 2009; Revised 15 April 2010; Accepted 19 May 2010
Academic Editor: Susanne Mohr
Copyright © 2010 Yuexiu Wu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- L. P. Aiello, T. W. Gardner, G. L. King et al., “Diabetic retinopathy,” Diabetes Care, vol. 21, no. 1, pp. 143–156, 1998.
- M. Boulton, D. Foreman, G. Williams, and D. McLeod, “VEGF localisation in diabetic retinopathy,” British Journal of Ophthalmology, vol. 82, no. 5, pp. 561–568, 1998.
- G. A. Lutty, D. S. McLeod, C. Merges, A. Diggs, and J. Plouét, “Localization of vascular endothelial growth factor in human retina and choroid,” Archives of Ophthalmology, vol. 114, no. 8, pp. 971–977, 1996.
- F. Malecaze, S. Clamens, V. Simorre-Pinatel et al., “Detection of vascular endothelial growth factor messenger RNA and vascular endothelial growth factor-like activity in proliferative diabetic retinopathy,” Archives of Ophthalmology, vol. 112, no. 11, pp. 1476–1482, 1994.
- M. Cukiernik, D. Hileeto, T. Evans, S. Mukherjee, D. Downey, and S. Chakrabarti, “Vascular endothelial growth factor in diabetes induced early retinal abnormalities,” Diabetes Research and Clinical Practice, vol. 65, no. 3, pp. 197–208, 2004.
- H.-P. Hammes, J. Lin, R. G. Bretzel, M. Brownlee, and G. Breier, “Upregulation of the vascular endothelial growth factor/vascular endothelial growth factor receptor system in experimental background diabetic retinopathy of the rat,” Diabetes, vol. 47, no. 3, pp. 401–406, 1998.
- L. P. Aiello, E. A. Pierce, E. D. Foley et al., “Suppression of retinal neovascularization in vivo by inhibition of vascular endothelial growth factor (VEGF) using soluble VEGF-receptor chimeric proteins,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 23, pp. 10457–10461, 1995.
- S. Chen, M. D. Apostolova, M. G. Cherian, and S. Chakrabarti, “Interaction of endothelin-1 with vasoactive factors in mediating glucose-induced increased permeability in endothelial cells,” Laboratory Investigation, vol. 80, no. 8, pp. 1311–1321, 2000.
- R. Gao, B.-H. Zhu, S.-B. Tang, J.-F. Wang, and J. Ren, “Scutellarein inhibits hypoxia- and moderately-high glucose-induced proliferation and VEGF expression in human retinal endothelial cells,” Acta Pharmacologica Sinica, vol. 29, no. 6, pp. 707–712, 2008.
- H.-X. Wu, X. Xia, K. Liu et al., “Effect of insulin on VEGF expression in bovine retinal microvascular endothelial cells exposed to normal or high glucose,” Zhonghua Yan Ke Za Zhi, vol. 44, no. 7, pp. 640–644, 2008.
- Z. A. Khan and S. Chakrabarti, “Cellular signaling and potential new treatment targets in diabetic retinopathy,” Experimental Diabetes Research, vol. 2007, Article ID 31867, 12 pages, 2007.
- J.-D. Lee, R. J. Ulevitch, and J. Han, “Primary structure of BMK1: a new mammalian MAP kinase,” Biochemical and Biophysical Research Communications, vol. 213, no. 2, pp. 715–724, 1995.
- G. Zhou, Z. Q. Bao, and J. E. Dixon, “Components of a new human protein kinase signal transduction pathway,” Journal of Biological Chemistry, vol. 270, no. 21, pp. 12665–12669, 1995.
- C. Yan, M. Takahashi, M. Okuda, J.-D. Lee, and B. C. Berk, “Fluid shear stress stimulates big mitogen-activated protein kinase 1 (BMK1) activity in endothelial cells: dependence on tyrosine kinases and intracellular calcium,” Journal of Biological Chemistry, vol. 274, no. 1, pp. 143–150, 1999.
- M. Hayashi, S.-W. Kim, K. Imanaka-Yoshida et al., “Targeted deletion of BMK1/ERK5 in adult mice perturbs vascular integrity and leads to endothelial failure,” Journal of Clinical Investigation, vol. 113, no. 8, pp. 1138–1148, 2004.
- X. Pi, C. Yan, and B. C. Berk, “Big mitogen-activated protein kinase (BMK1)/ERK5 protects endothelial cells from apoptosis,” Circulation Research, vol. 94, no. 3, pp. 362–369, 2004.
- D. Spiering, M. Schmolke, N. Ohnesorge et al., “MEK5/ERK5 signaling modulates endothelial cell migration and focal contact turnover,” Journal of Biological Chemistry, vol. 284, no. 37, pp. 24972–24980, 2009.
- X. Pi, G. Garin, L. Xie et al., “BMK1/ERK5 is a novel regulator of angiogenesis by destabilizing hypoxia inducible factor 1α,” Circulation Research, vol. 96, no. 11, pp. 1145–1151, 2005.
- S. J. Sohn, B. K. Sarvis, D. Cado, and A. Winoto, “ERK5 MAPK regulates embryonic angiogenesis and acts as a hypoxia-sensitive repressor of vascular endothelial growth factor expression,” Journal of Biological Chemistry, vol. 277, no. 45, pp. 43344–43351, 2002.
- S. J. Sohn, D. Li, L. K. Lee, and A. Winoto, “Transcriptional regulation of tissue-specific genes by the ERK5 mitogen-activated protein kinase,” Molecular and Cellular Biology, vol. 25, no. 19, pp. 8553–8566, 2005.
- R. Bhattacharya, S. Senbanerjee, Z. Lin et al., “Inhibition of vascular permeability factor/vascular endothelial growth factor-mediated angiogenesis by the Kruppel-like factor KLF2,” Journal of Biological Chemistry, vol. 280, no. 32, pp. 28848–28851, 2005.
- K. Sako, S. Fukuhara, T. Minami et al., “Angiopoietin-1 induces Krüppel-like factor 2 expression through a phosphoinositide 3-kinase/AKT-dependent activation of myocyte enhancer factor 2,” Journal of Biological Chemistry, vol. 284, no. 9, pp. 5592–5601, 2009.
- R. A. Boon, J. O. Fledderus, O. L. Volger et al., “KLF2 suppresses TGF-β signaling in endothelium through induction of Smad7 and inhibition of AP-1,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 3, pp. 532–539, 2007.
- R. J. Dekker, R. A. Boon, M. G. Rondaij et al., “KLF2 provokes a gene expression pattern that establishes functional quiescent differentiation of the endothelium,” Blood, vol. 107, no. 11, pp. 4354–4363, 2006.
- Y. Zuo, S.-K. Shields, and C. Chakraborty, “Enhanced intrinsic migration of aggressive breast cancer cells by inhibition of Rac1 GTPase,” Biochemical and Biophysical Research Communications, vol. 351, no. 2, pp. 361–367, 2006.
- S. Chen, Z. A. Khan, M. Cukiernik, and S. Chakrabarti, “Differential activation of NF-κB and AP-1 in increased fibronectin synthesis in target organs of diabetic complications,” American Journal of Physiology, vol. 284, no. 6, pp. E1089–E1097, 2003.
- Z. A. Khan, M. Cukiernik, J. R. Gonder, and S. Chakrabarti, “Oncofetal fibronectin in diabetic retinopathy,” Investigative Ophthalmology and Visual Science, vol. 45, no. 1, pp. 287–295, 2004.
- H. Kaur, S. Chen, X. Xin, J. Chiu, Z. A. Khan, and S. Chakrabarti, “Diabetes-induced extracellular matrix protein expression is mediated by transcription coactivator p300,” Diabetes, vol. 55, no. 11, pp. 3104–3111, 2006.
- B. Xu, J. Chiu, B. Feng, S. Chen, and S. Chakrabarti, “PARP activation and the alteration of vasoactive factors and extracellular matrix protein in retina and kidney in diabetes,” Diabetes/Metabolism Research and Reviews, vol. 24, no. 5, pp. 404–412, 2008.
- H. Morimoto, K. Kondoh, S. Nishimoto, K. Terasawa, and E. Nishida, “Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation,” Journal of Biological Chemistry, vol. 282, no. 49, pp. 35449–35456, 2007.
- X. Wang and C. Tournier, “Regulation of cellular functions by the ERK5 signalling pathway,” Cellular Signalling, vol. 18, no. 6, pp. 753–760, 2006.
- J. Pe'er, D. Shweiki, A. Itin, I. Hemo, H. Gnessin, and E. Keshet, “Hypoxia-induced expression of vascular endothelial growth factor by retinal cells is a common factor in neovascularizing ocular diseases,” Laboratory Investigation, vol. 72, no. 6, pp. 638–645, 1995.
- D. Ray, M. Mishra, S. Ralph, I. Read, R. Davies, and P. Brenchley, “Association of the VEGF gene with proliferative diabetic retinopathy but not proteinuria in diabetes,” Diabetes, vol. 53, no. 3, pp. 861–864, 2004.
- P. E. Depeille, Y. Ding, J. L. Bromberg-White, and N. S. Duesbery, “MKK signaling and vascularization,” Oncogene, vol. 26, no. 9, pp. 1290–1296, 2007.
- J. Milanini, F. Viñals, J. Pouysségur, and G. Pagès, “p42/p44 MAP kinase module plays a key role in the transcriptional regulation of the vascular endothelial growth factor gene in fibroblasts,” Journal of Biological Chemistry, vol. 273, no. 29, pp. 18165–18172, 1998.
- G. Pagès, E. Berra, J. Milanini, A. P. Levy, and J. Pouysségur, “Stress-activated protein kinases (JNK and p38/HOG) are essential for vascular endothelial growth factor mRNA stability,” Journal of Biological Chemistry, vol. 275, no. 34, pp. 26484–26491, 2000.
- M. Guma, J. Rius, K. X. Duong-Polk, G. G. Haddad, J. D. Lindsey, and M. Karin, “Genetic and pharmacological inhibition of JNK ameliorates hypoxia-induced retinopathy through interference with VEGF expression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 21, pp. 8760–8765, 2009.
- Y. Chen, Y. Hu, T. Zhou et al., “Activation of the wnt pathway plays a pathogenic role in diabetic retinopathy in humans and animal models,” American Journal of Pathology, vol. 175, no. 6, pp. 2676–2685, 2009.
- H. G. Kasler, J. Victoria, O. Duramad, and A. Winoto, “ERK5 is a novel type of mitogen-activated protein kinase containing a transcriptional activation domain,” Molecular and Cellular Biology, vol. 20, no. 22, pp. 8382–8389, 2000.
- T. Shishido, C.-H. Woo, B. Ding et al., “Effects of MEK5/ERK5 association on small ubiquitin-related modification of ERK5: implications for diabetic ventricular dysfunction after myocardial infarction,” Circulation Research, vol. 102, no. 11, pp. 1416–1425, 2008.
- Y. Kato, M. Zhao, A. Morikawa et al., “Big mitogen-activated kinase regulates multiple members of the MEF2 protein family,” Journal of Biological Chemistry, vol. 275, no. 24, pp. 18534–18540, 2000.
- D. Kawanami, G. H. Mahabeleshwar, Z. Lin et al., “Kruppel-like factor 2 inhibits hypoxia-inducible factor 1α expression and function in the endothelium,” Journal of Biological Chemistry, vol. 284, no. 31, pp. 20522–20530, 2009.
- M. K. Van den Enden, J. R. Nyengaard, E. Ostrow, J. H. Burgan, and J. R. Williamson, “Elevated glucose levels increase retinal glycolysis and sorbitol pathway metabolism: implications for diabetic retinopathy,” Investigative Ophthalmology and Visual Science, vol. 36, no. 8, pp. 1675–1685, 1995.
- J. R. Williamson, K. Chang, M. Frangos et al., “Hyperglycemic pseudohypoxia and diabetic complications,” Diabetes, vol. 42, no. 6, pp. 801–813, 1993.
- W. Lui, A. Schoenkerman, and W. L. Lowe Jr., “Activation of members of the mitogen-activated protein kinase family by glucose in endothelial cells,” American Journal of Physiology, vol. 279, no. 4, pp. E782–E790, 2000.
- H. Wu, X. Xia, C. Jiang et al., “High glucose attenuates insulin-induced VEGF expression in bovine retinal microvascular endothelial cells,” Eye, vol. 24, no. 1, pp. 145–151, 2010.
- S. Hoshi, K.-I. Nomoto, J. Kuromitsu, S. Tomari, and M. Nagata, “High glucose induced VEGF expression via PKC and ERK in glomerular podocytes,” Biochemical and Biophysical Research Communications, vol. 290, no. 1, pp. 177–184, 2002.
- S. Kamakura, T. Moriguchi, and E. Nishida, “Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. Identification and characterization of a signaling pathway to the nucleus,” Journal of Biological Chemistry, vol. 274, no. 37, pp. 26563–26571, 1999.
- Y. Kato, R. I. Tapping, S. Huang, M. H. Watson, R. J. Ulevitch, and J.-D. Lee, “Bmk1/Erk5 is required for cell proliferation induced by epidermal growth factor,” Nature, vol. 395, no. 6703, pp. 713–716, 1998.