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Journal of Ophthalmology
Volume 2010 (2010), Article ID 175163, 9 pages
ROCK as a Therapeutic Target of Diabetic Retinopathy
Department of Ophthalmology, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-Ku, Fukuoka 812-8582, Japan
Received 2 December 2009; Accepted 9 April 2010
Academic Editor: Kavita Hegde
Copyright © 2010 Ryoichi Arita 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.
- J. H. Kempen, B. J. O'Colmain, M. C. Leske, et al., “The prevalence of diabetic retinopathy among adults in the United States,” Archives of Ophthalmology, vol. 122, no. 4, pp. 552–563, 2004.
- H. King, R. E. Aubert, and W. H. Herman, “Global burden of diabetes, 1995–2025: prevalence, numerical estimates, and projections,” Diabetes Care, vol. 21, no. 9, pp. 1414–1431, 1998.
- “Early photocoagulation for diabetic retinopathy. ETDRS report number 9. Early Treatment Diabetic Retinopathy Study Research Group,” Ophthalmology, vol. 98, pp. 766–785, 1991.
- L. P. Aiello, “Angiogenic pathways in diabetic retinopathy,” The New England Journal of Medicine, vol. 353, no. 8, pp. 839–841, 2005.
- D. S. Fong, L. Aiello, T. W. Gardner, et al., “Diabetic retinopathy,” Diabetes Care, vol. 26, no. 1, pp. S99–S102, 2003.
- A. M. Joussen, T. Murata, A. Tsujikawa, B. Kirchhof, S.-E. Bursell, and A. P. Adamis, “Leukocyte-mediated endothelial cell injury and death in the diabetic retina,” American Journal of Pathology, vol. 158, no. 1, pp. 147–152, 2001.
- C. W. Smith, S. D. Marlin, R. Rothlein, C. Toman, and D. C. Anderson, “Cooperative interactions of LFA-1 and Mac-1 with intracellular adhesion molecule-1 in facilitating adherence and transendothelial migration of human neutrophils in vitro,” Journal of Clinical Investigation, vol. 83, no. 6, pp. 2008–2017, 1989.
- F. C. Barouch, K. Miyamoto, J. R. Allport, et al., “Integrin-mediated neutrophil adhesion and retinal leukostasis in diabetes,” Investigative Ophthalmology and Visual Science, vol. 41, no. 5, pp. 1153–1158, 2000.
- A. M. Joussen, V. Poulaki, N. Mitsiades, et al., “Suppression of Fas-FasL-induced endothelial cell apoptosis prevents diabetic blood-retinal barrier breakdown in a model of streptozotocin-induced diabetes,” The FASEB Journal, vol. 17, no. 1, pp. 76–78, 2003.
- R. Arita, Y. Hata, S. Nakao, et al., “Rho kinase inhibition by fasudil ameliorates diabetes-induced microvascular damage,” Diabetes, vol. 58, no. 1, pp. 215–226, 2009.
- N. Ferrara, “Vascular endothelial growth factor: basic science and clinical progress,” Endocrine Reviews, vol. 25, no. 4, pp. 581–611, 2004.
- A. P. Adamis and D. T. Shima, “The role of vascular endothelial growth factor in ocular health and disease,” Retina, vol. 25, no. 2, pp. 111–118, 2005.
- S. Moradian, H. Ahmadieh, M. Malihi, M. Soheilian, M. H. Dehghan, and M. Azarmina, “Intravitreal bevacizumab in active progressive proliferative diabetic retinopathy,” Graefe's Archive for Clinical and Experimental Ophthalmology, vol. 246, no. 12, pp. 1699–1705, 2008.
- C. Shima, H. Sakaguchi, F. Gomi, et al., “Complications in patients after intravitreal injection of bevacizumab,” Acta Ophthalmologica, vol. 86, no. 4, pp. 372–376, 2008.
- B. P. Eliceiri, R. Klemke, S. Stromblad, and D. A. Cheresh, “Integrin v3 requirement for sustained mitogen-activated protein kinase activity during angiogenesis,” Journal of Cell Biology, vol. 140, no. 5, pp. 1255–1263, 1998.
- G. Mavria, Y. Vercoulen, M. Yeo, et al., “ERK-MAPK signaling opposes Rho-kinase to promote endothelial cell survival and sprouting during angiogenesis,” Cancer Cell, vol. 9, no. 1, pp. 33–44, 2006.
- G. P. van Nieuw Amerongen, P. Koolwijk, A. Versteilen, and V. W. M. Van Hinsbergh, “Involvement of RhoA/Rho kinase signaling in VEGF-induced endothelial cell migration and angiogenesis in vitro,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 23, no. 2, pp. 211–217, 2003.
- Y. Noda, Y. Hata, T. Hisatomi, et al., “Functional properties of hyalocytes under PDGF-rich conditions,” Investigative Ophthalmology and Visual Science, vol. 45, no. 7, pp. 2107–2114, 2004.
- K. Hirayama, Y. Hata, Y. Noda, et al., “The involvement of the Rho-kinase pathway and its regulation in cytokine-induced collagen gel contraction by hyalocytes,” Investigative Ophthalmology and Visual Science, vol. 45, no. 11, pp. 3896–3903, 2004.
- T. Kita, Y. Hata, K. Kano, et al., “Transforming growth factor-2 and connective tissue growth factor in proliferative vitreoretinal diseases: possible involvement of hyalocytes and therapeutic potential of rho kinase inhibitor,” Diabetes, vol. 56, no. 1, pp. 231–238, 2007.
- K. E. Kamm and J. T. Stull, “The function of myosin and myosin light chain kinase phosphorylation in smooth muscle,” Annual Review of Pharmacology and Toxicology, vol. 25, pp. 593–620, 1985.
- Y. Fukata, K. Kaibuchi, M. Amano, and K. Kaibuchi, “Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells,” Trends in Pharmacological Sciences, vol. 22, no. 1, pp. 32–39, 2001.
- T. Kita, Y. Hata, R. Arita, et al., “Role of TGF- in proliferative vitreoretinal diseases and ROCK as a therapeutic target,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 45, pp. 17504–17509, 2008.
- K. Kaibuchi, S. Kuroda, and M. Amano, “Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells,” Annual Review of Biochemistry, vol. 68, pp. 459–486, 1999.
- H. Iwasaki, R. Okamoto, S. Kato, et al., “High glucose induces plasminogen activator inhibitor-1 expression through Rho/Rho-kinase-mediated NF-B activation in bovine aortic endothelial cells,” Atherosclerosis, vol. 196, no. 1, pp. 22–28, 2008.
- V. Kolavennu, L. Zeng, H. Peng, Y. Wang, and F. R. Danesh, “Targeting of RhoA/ROCK signaling ameliorates progression of diabetic nephropathy independent of glucose control,” Diabetes, vol. 57, no. 3, pp. 714–723, 2008.
- J. Tang, I. Kusaka, A. R. Massey, S. Rollins, and J. H. Zhang, “Increased RhoA translocation in aorta of diabetic rats,” Acta Pharmacologica Sinica, vol. 27, no. 5, pp. 543–548, 2006.
- H. Lee, I. L. Chi, J.-J. Liao, et al., “Lysophospholipids increase ICAM-1 expression in HUVEC through a G i- and NF-B-dependent mechanism,” American Journal of Physiology, vol. 287, no. 6, pp. C1657–C1666, 2004.
- B. Wojciak-Stothard, L. Williams, and A. J. Ridley, “Monocyte adhesion and spreading on human endothelial cells is dependent on Rho-regulated receptor clustering,” Journal of Cell Biology, vol. 145, no. 6, pp. 1293–1307, 1999.
- C. Giagulli, E. Scarpini, L. Ottoboni, et al., “RhoA and PKC control distinct modalities of LFA-1 activation by chemokines: critical role of LFA-1 affinity triggering in lymphocyte in vivo homing,” Immunity, vol. 20, no. 1, pp. 25–35, 2004.
- O. Barreiro, M. Yanez-Mo, J. M. Serrador, et al., “Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes,” Journal of Cell Biology, vol. 157, no. 7, pp. 1233–1245, 2002.
- D. J. G. Mackay, F. Esch, H. Furthmayr, and A. Hall, “Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins,” Journal of Cell Biology, vol. 138, no. 4, pp. 927–938, 1997.
- L. Zeng, H. Xu, T.-L. Chew, et al., “HMG CoA reductase inhibition modulates VEGF-induced endothelial cell hyperpermeability by preventing RhoA activation and myosin regulatory light chain phosphorylation,” FASEB Journal, vol. 19, no. 13, pp. 1845–1847, 2005.
- M. V. Hoang, M. C. Whelan, and D. R. Senger, “Rho activity critically and selectively regulates endothelial cell organization during angiogenesis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 7, pp. 1874–1879, 2004.
- J.-M. Hyvelin, K. Howell, A. Nichol, C. M. Costello, R. J. Preston, and P. McLoughlin, “Inhibition of Rho-kinase attenuates hypoxia-induced angiogenesis in the pulmonary circulation,” Circulation Research, vol. 97, no. 2, pp. 185–191, 2005.
- H. Shimokawa and M. Rashid, “Development of Rho-kinase inhibitors for cardiovascular medicine,” Trends in Pharmacological Sciences, vol. 28, no. 6, pp. 296–302, 2007.
- M. Shibuya, Y. Suzuki, K. Sugita, et al., “Dose escalation trial of a novel calcium antagonist, AT877, in patients with aneurysmal subarachnoid haemorrhage,” Acta Neurochirurgica, vol. 107, no. 1-2, pp. 11–15, 1990.
- M. Shibuya, S. Hirai, M. Seto, S.-I. Satoh, and E. Ohtomo, “Effects of fasudil in acute ischemic stroke: results of a prospective placebo-controlled double-blind trial,” Journal of the Neurological Sciences, vol. 238, no. 1-2, pp. 31–39, 2005.
- X.-F. Ming, H. Viswambharan, C. Barandier, et al., “Rho GTPase/Rho kinase negatively regulates endothelial nitric oxide synthase phosphorylation through the inhibition of protein kinase B/Akt in human endothelial cells,” Molecular and Cellular Biology, vol. 22, no. 24, pp. 8467–8477, 2002.
- J. Marin and M. A. Rodriguez-Martinez, “Role of vascular nitric oxide in physiological and pathological conditions,” Pharmacology and Therapeutics, vol. 75, no. 2, pp. 111–134, 1997.
- L. Rossig, B. Fichtlscherer, K. Breitschopf, et al., “Nitric oxide inhibits caspase-3 by S-nitrosation in vivo,” The Journal of Biological Chemistry, vol. 274, no. 11, pp. 6823–6826, 1999.
- L. Rossig, J. Haendeler, C. Hermann, et al., “Nitric oxide down-regulates MKP-3 mRNA levels: involvement in endothelial cell protection from apoptosis,” The Journal of Biological Chemistry, vol. 275, no. 33, pp. 25502–25507, 2000.
- Y. Hata, M. Miura, S. Nakao, S. Kawahara, T. Kita, and T. Ishibashi, “Antiangiogenic properties of fasudil, a potent Rho-kinase inhibitor,” Japanese Journal of Ophthalmology, vol. 52, no. 1, pp. 16–23, 2008.
- J. Molgaard, H. von Schenck, and A. G. Olsson, “Effects of simvastatin on plasma lipid, lipoprotein and apolipoprotein concentrations in hypercholesterolaemia,” European Heart Journal, vol. 9, no. 5, pp. 541–551, 1988.
- L. Van Aelst and C. D'Souza-Schorey, “Rho GTPases and signaling networks,” Genes and Development, vol. 11, no. 18, pp. 2295–2322, 1997.
- S. Kawahara, Y. Hata, T. Kita, et al., “Potent inhibition of cicatricial contraction in proliferative vitreoretinal diseases by statins,” Diabetes, vol. 57, no. 10, pp. 2784–2793, 2008.
- A. Masumoto, M. Mohri, H. Shimokawa, L. Urakami, M. Usui, and A. Takeshita, “Suppression of coronary artery spasm by the Rho-kinase inhibitor fasudil in patients with vasospastic angina,” Circulation, vol. 105, no. 13, pp. 1545–1547, 2002.
- N. Okamura, M. Saito, A. Mori, et al., “Vasodilator effects of fasudil, a Rho-kinase inhibitor, on retinal arterioles in stroke-prone spontaneously hypertensive rats,” Journal of Ocular Pharmacology and Therapeutics, vol. 23, no. 3, pp. 207–212, 2007.
- A. Masumoto, Y. Hirooka, H. Shimokawa, K. Hironaga, S. Setoguchi, and A. Takeshita, “Possible involvement of Rho-kinase in the pathogenesis of hypertension in humans,” Hypertension, vol. 38, no. 6, pp. 1307–1310, 2001.
- A. J. Barber, “A new view of diabetic retinopathy: a neurodegenerative disease of the eye,” Progress in Neuro-Psychopharmacology and Biological Psychiatry, vol. 27, no. 2, pp. 283–290, 2003.
- V. Parisi and L. Uccioli, “Visual electrophysiological responses in persons with type 1 diabetes,” Diabetes/Metabolism Research and Reviews, vol. 17, no. 1, pp. 12–18, 2001.
- E. Lieth, T. W. Gardner, A. J. Barber, and D. A. Antonetti, “Retinal neurodegeneration: early pathology in diabetes,” Clinical and Experimental Ophthalmology, vol. 28, no. 1, pp. 3–8, 2000.
- B. K. Mueller, H. Mack, and N. Teusch, “Rho kinase, a promising drug target for neurological disorders,” Nature Reviews Drug Discovery, vol. 4, no. 5, pp. 387–398, 2005.
- Y. Kitaoka, Y. Kitaoka, T. Kumai, et al., “Involvement of RhoA and possible neuroprotective effect of fasudil, a Rho kinase inhibitor, in NMDA-induced neurotoxicity in the rat retina,” Brain Research, vol. 1018, no. 1, pp. 111–118, 2004.
- P. Lingor, N. Teusch, K. Schwarz, et al., “Inhibition of Rho kinase (ROCK) increases neurite outgrowth on chondroitin sulphate proteoglycan in vitro and axonal regeneration in the adult optic nerve in vivo,” Journal of Neurochemistry, vol. 103, no. 1, pp. 181–189, 2007.
- A. Hirata, M. Inatani, Y. Inomata, et al., “Y-27632, a Rho-associated protein kinase inhibitor, attenuates neuronal cell death after transient retinal ischemia,” Graefe's Archive for Clinical and Experimental Ophthalmology, vol. 246, no. 1, pp. 51–59, 2008.
- A. Tura, F. Schuettauf, P. P. Monnier, K. U. Bartz-Schmidt, and S. Henke-Fahle, “Efficacy of Rho-kinase inhibition in promoting cell survival and reducing reactive gliosis in the rodent retina,” Investigative Ophthalmology & Visual Science, vol. 50, no. 1, pp. 452–461, 2009.