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Journal articles on the topic 'Rho-kinase'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Liao, James K. "Rho-Kinase." Circulation Research 99, no. 3 (2006): 238–39. http://dx.doi.org/10.1161/01.res.0000236798.01988.5d.

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2

Kimura, K., M. Ito, M. Amano, et al. "Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)." Science 273, no. 5272 (1996): 245–48. http://dx.doi.org/10.1126/science.273.5272.245.

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3

Kaikita, Koichi, and Hisao Ogawa. "Rho-Kinase Pathway." Circulation Journal 76, no. 11 (2012): 2536–37. http://dx.doi.org/10.1253/circj.cj-12-1179.

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4

Seto, Minoru, and Toshio Asano. "Rho-kinase inhibitors." Folia Pharmacologica Japonica 138, no. 3 (2011): 112–16. http://dx.doi.org/10.1254/fpj.138.112.

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5

WANG, JING, XIAOHONG LIU, and YISHENG ZHONG. "Rho/Rho-associated kinase pathway in glaucoma." International Journal of Oncology 43, no. 5 (2013): 1357–67. http://dx.doi.org/10.3892/ijo.2013.2100.

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6

Yamagishi, Satoru, Masashi Fujitani, Katsuhiko Hata, et al. "Wallerian Degeneration Involves Rho/Rho-kinase Signaling." Journal of Biological Chemistry 280, no. 21 (2005): 20384–88. http://dx.doi.org/10.1074/jbc.m501945200.

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7

Amano, Mutsuki, Kazuyasu Chihara, Nao Nakamura, Takako Kaneko, Yoshiharu Matsuura, and Kozo Kaibuchi. "The COOH Terminus of Rho-kinase Negatively Regulates Rho-kinase Activity." Journal of Biological Chemistry 274, no. 45 (1999): 32418–24. http://dx.doi.org/10.1074/jbc.274.45.32418.

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8

Amano, Mutsuki, Masaaki Ito, Kazushi Kimura, et al. "Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)." Journal of Biological Chemistry 271, no. 34 (1996): 20246–49. http://dx.doi.org/10.1074/jbc.271.34.20246.

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9

Kang, Jeong-Hun, Daisuke Asai, Akira Tsuchiya, Takeshi Mori, Takuro Niidome, and Yoshiki Katayama. "Peptide Substrates for Rho-Associated Kinase 2 (Rho-Kinase 2/ROCK2)." PLoS ONE 6, no. 7 (2011): e22699. http://dx.doi.org/10.1371/journal.pone.0022699.

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10

Yu Mei and James K. Liao. "Rho Kinase and Angiogenesis." Immunology, Endocrine & Metabolic Agents in Medicinal Chemistry 12, no. 1 (2012): 14–28. http://dx.doi.org/10.2174/187152212799857682.

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11

Watanabe, Hiroyuki, Kenji Iino, and Hiroshi Ito. "Rho-Kinase in Leukocytes." Circulation Journal 77, no. 10 (2013): 2471–72. http://dx.doi.org/10.1253/circj.cj-13-0935.

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12

Liao, James K., Minoru Seto, and Kensuke Noma. "Rho Kinase (ROCK) Inhibitors." Journal of Cardiovascular Pharmacology 50, no. 1 (2007): 17–24. http://dx.doi.org/10.1097/fjc.0b013e318070d1bd.

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13

Wirth, Angela. "Rho kinase and hypertension." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1802, no. 12 (2010): 1276–84. http://dx.doi.org/10.1016/j.bbadis.2010.05.002.

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14

Christ, George J., and Karl-Erik Andersson. "Rho-kinase and effects of Rho-kinase inhibition on the lower urinary tract." Neurourology and Urodynamics 26, S6 (2007): 948–54. http://dx.doi.org/10.1002/nau.20475.

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15

KUBAT, Havva, Ahmet Sencer YURTSEVER, and Kansu BÜYÜKAFŞAR. "Rho/rho-kinase signalling in chronically alcohol-fed mice." TURKISH JOURNAL OF MEDICAL SCIENCES 47 (2017): 668–74. http://dx.doi.org/10.3906/sag-1512-161.

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16

Wettschureck, Nina, and Stefan Offermanns. "Rho/Rho-kinase mediated signaling in physiology and pathophysiology." Journal of Molecular Medicine 80, no. 10 (2002): 629–38. http://dx.doi.org/10.1007/s00109-002-0370-2.

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17

Kishida, Shosei, Hideki Yamamoto, and Akira Kikuchi. "Wnt-3a and Dvl Induce Neurite Retraction by Activating Rho-Associated Kinase." Molecular and Cellular Biology 24, no. 10 (2004): 4487–501. http://dx.doi.org/10.1128/mcb.24.10.4487-4501.2004.

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ABSTRACT Dvl is a key protein that transmits the Wnt signal to the canonical β-catenin pathway and the noncanonical planar cell polarity (PCP) pathway. We studied the roles of Rho-associated kinase (Rho-kinase), which is activated by Dvl in the PCP pathway of mammalian cells. The expression of Dvl-1, Wnt-1, or Wnt-3a activated Rho-kinase in COS cells, and this activation was inhibited by the Rho-binding domain of Rho-kinase. The expression of Dvl-1 in PC12 cells activated Rho and inhibited nerve growth factor (NGF)-induced neurite outgrowth. This inhibition was reversed by a Rho-kinase inhibit

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18

Kim, Young-Bum. "Rho-kinase and Insulin Signaling." Journal of Korean Diabetes Association 30, no. 4 (2006): 237. http://dx.doi.org/10.4093/jkda.2006.30.4.237.

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19

Okumura, Naoki, Shintaro Nakao, Toshihiro Inoue, and Padmanabhan Pattabiraman. "Rho Kinase in Eye Disease." Journal of Ophthalmology 2017 (2017): 1–2. http://dx.doi.org/10.1155/2017/9281745.

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20

Labandeira-Garcia, Jose L., Ana I. Rodríguez-Perez, Begoña Villar-Cheda, Ana Borrajo, Antonio Dominguez-Meijide, and Maria J. Guerra. "Rho Kinase and Dopaminergic Degeneration." Neuroscientist 21, no. 6 (2014): 616–29. http://dx.doi.org/10.1177/1073858414554954.

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21

Sádaba, Justo Rafael. "Rho-kinase, the forgotten link?" European Journal of Cardio-Thoracic Surgery 35, no. 6 (2009): 1115. http://dx.doi.org/10.1016/j.ejcts.2009.02.025.

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22

Kavitha, Srinivasan, and Megha Gopalakrishna. "Rho-kinase inhibitors in ophthalmology." TNOA Journal of Ophthalmic Science and Research 59, no. 1 (2021): 56. http://dx.doi.org/10.4103/tjosr.tjosr_146_20.

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23

Simões, Sérgio de Matos, Avantika Mainieri, and Jennifer A. Zallen. "Rho GTPase and Shroom direct planar polarized actomyosin contractility during convergent extension." Journal of Cell Biology 204, no. 4 (2014): 575–89. http://dx.doi.org/10.1083/jcb.201307070.

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Actomyosin contraction generates mechanical forces that influence cell and tissue structure. During convergent extension in Drosophila melanogaster, the spatially regulated activity of the myosin activator Rho-kinase promotes actomyosin contraction at specific planar cell boundaries to produce polarized cell rearrangement. The mechanisms that direct localized Rho-kinase activity are not well understood. We show that Rho GTPase recruits Rho-kinase to adherens junctions and is required for Rho-kinase planar polarity. Shroom, an asymmetrically localized actin- and Rho-kinase–binding protein, ampl

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24

Harrod, Jeremy S., Cara C. Rada, Stephanie L. Pierce, Sarah K. England, and Kathryn G. Lamping. "Altered contribution of RhoA/Rho kinase signaling in contractile activity of myometrium in leptin receptor-deficient mice." American Journal of Physiology-Endocrinology and Metabolism 301, no. 2 (2011): E362—E369. http://dx.doi.org/10.1152/ajpendo.00696.2010.

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In late gestation, enhanced myometrial contractility is mediated in part through increased Rho/Rho kinase. Since leptin, which is elevated in pregnancy and obesity, can directly depress myometrial function, we hypothesized that in leptin receptor-deficient mice, myometrial contractility would be greater in late pregnancy due to increased Rho/Rho kinase activity. To test this, we correlated RhoA and Rho kinase expression to contractility in myometrium from nonpregnant (NP) and late-pregnant (P18) heterozygous leptin receptor-deficient mice ( db/+) vs. wild-type (WT) mice. In NP mice, KCl-induce

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25

Zhao, Yidan D., Lei Cai, Muhammad K. Mirza, et al. "Protein Kinase G-I Deficiency Induces Pulmonary Hypertension through Rho A/Rho Kinase Activation." American Journal of Pathology 180, no. 6 (2012): 2268–75. http://dx.doi.org/10.1016/j.ajpath.2012.02.016.

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26

Roovers, Kristin, Eric A. Klein, Paola Castagnino, and Richard K. Assoian. "Nuclear Translocation of LIM Kinase Mediates Rho-Rho Kinase Regulation of Cyclin D1 Expression." Developmental Cell 10, no. 5 (2006): 681. http://dx.doi.org/10.1016/j.devcel.2006.04.016.

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27

Nishikimi, Toshio. "Role of the Rho/Rho-kinase pathway in the development of hypertensive glomerulosclerosis: renoprotective effect of Rho-kinase inhibitor in hypertensive glomerulosclerosis and its molecular mechanism." Folia Pharmacologica Japonica 128, no. 3 (2006): 153–59. http://dx.doi.org/10.1254/fpj.128.153.

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28

Zhang, Juan, Fei Xu, Xiao-Bo Liu, Shao-jie Bi, and Qing-Hua Lu. "Increased Rho kinase activity in patients with heart ischemia/reperfusion." Perfusion 34, no. 1 (2018): 15–21. http://dx.doi.org/10.1177/0267659118787432.

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Background/Aim: Rho kinase is a downstream effector of Rho GTPase that is known to regulate various pathological processes. The aim of this study was to evaluate the regulation of Rho kinase activity in leukocytes in patients with ischemia/reperfusion (I/R) injury. Patients and Methods: We investigated 38 patients with acute ST-segment elevation myocardial infarction (STEMI), 26 patients with atherosclerosis (AS) and 22 normal subjects. All patients underwent coronary angiography (CAG) and all STEMI patients received primary percutaneous coronary intervention (PPCI) of the left anterior descen

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29

Ikeda, Hitoshi, Kayo Nagashima, Mikio Yanase, et al. "Involvement of Rho/Rho kinase pathway in regulation of apoptosis in rat hepatic stellate cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 285, no. 5 (2003): G880—G886. http://dx.doi.org/10.1152/ajpgi.00039.2003.

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Hepatic stellate cells (HSCs) play a central role in the development of hepatic fibrosis. Recent evidence has revealed that HSCs also play a role in its resolution, where HSC apoptosis was determined. Moreover, induction of HSC apoptosis caused a reduction of experimental hepatic fibrosis in rats. Thus knowing the mechanism of HSC apoptosis might be important to clarify the pathophysiology and establish the therapeutic strategy for hepatic fibrosis. In HSCs, Rho and Rho kinase are known to regulate contraction, migration, and proliferation with modulation of cell morphology. Controversy exists

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30

Vincent, S., and J. Settleman. "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization." Molecular and Cellular Biology 17, no. 4 (1997): 2247–56. http://dx.doi.org/10.1128/mcb.17.4.2247.

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The Ras-related Rho family GTPases mediate signal transduction pathways that regulate a variety of cellular processes. Like Ras, the Rho proteins (which include Rho, Rac, and CDC42) interact directly with protein kinases, which are likely to serve as downstream effector targets of the activated GTPase. Activated RhoA has recently been reported to interact directly with several protein kinases, p120 PKN, p150 ROK alpha and -beta, p160 ROCK, and p164 Rho kinase. Here, we describe the purification of a novel Rho-associated kinase, p140, which appears to be the major Rho-associated kinase activity

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31

Matoba, Keiichiro, Daiji Kawanami, Masami Tsukamoto та ін. "Rho-kinase regulation of TNF-α-induced nuclear translocation of NF-κB RelA/p65 and M-CSF expression via p38 MAPK in mesangial cells". American Journal of Physiology-Renal Physiology 307, № 5 (2014): F571—F580. http://dx.doi.org/10.1152/ajprenal.00113.2014.

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The small GTPase Rho and its downstream effector, Rho-associated coiled-coil containing protein kinase (Rho-kinase), regulate a number of cellular processes, including organization of the actin cytoskeleton, cell adhesion, and migration. While pharmacological inhibitors of Rho-kinase signaling are known to block renal inflammation, the molecular basis for this effect is unclear. Here, we provide evidence that proinflammatory TNF-α promotes mesangial expression of macrophage colony-stimulating factor (M-CSF), a key regulator for the growth and differentiation of mononuclear phagocytes, in a Rho

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32

Kobayashi, Kenta, Hiromi Sano, Shigeki Kato, et al. "Survival of corticostriatal neurons by Rho/Rho-kinase signaling pathway." Neuroscience Letters 630 (September 2016): 45–52. http://dx.doi.org/10.1016/j.neulet.2016.07.020.

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33

Yagita, Yoshiki, Kazuo Kitagawa, Tsutomu Sasaki, et al. "Activation of Rho/Rho kinase system after focal cerebral ischemia." Journal of Cerebral Blood Flow & Metabolism 25, no. 1_suppl (2005): S264. http://dx.doi.org/10.1038/sj.jcbfm.9591524.0264.

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34

Meyer-Schwesinger, Catherine, Silke Dehde, Marlies Sachs, et al. "Rho-kinase inhibition prevents proteinuria in immune-complex-mediated antipodocyte nephritis." American Journal of Physiology-Renal Physiology 303, no. 7 (2012): F1015—F1025. http://dx.doi.org/10.1152/ajprenal.00380.2011.

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Podocyte foot process retraction is a hallmark of proteinuric glomerulonephritis. Cytoskeletal rearrangement causes a redistribution of slit membrane proteins from the glomerular filtration barrier towards the cell body. However, the underlying signaling mechanisms are presently unknown. Recently, we have developed a new experimental model of immune-mediated podocyte injury in mice, the antipodocyte nephritis (APN). Podocytes were targeted with a polyclonal antipodocyte antibody causing massive proteinuria around day 10. Rho-kinases play a central role in the organization of the actin cytoskel

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35

Meyer-Schwesinger, Catherine, Silke Dehde, Claudia von Ruffer та ін. "Rho kinase inhibition attenuates LPS-induced renal failure in mice in part by attenuation of NF-κB p65 signaling". American Journal of Physiology-Renal Physiology 296, № 5 (2009): F1088—F1099. http://dx.doi.org/10.1152/ajprenal.90746.2008.

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Rho kinase signaling regulates inflammatory cell migration and chemokine production. We therefore investigated the mechanisms of Rho-kinase-dependent inflammation in lipopolysaccharide (LPS)-induced renal failure. C57/BL6 mice received intraperitoneal LPS with or without daily treatment with specific Rho kinase inhibitors (Y-27632 or HA-1077; 5 mg/kg). Rho kinase inhibitors were applied in a preventive (12 or 1 h before LPS) or a therapeutic (6 h after LPS) scheme. Both protected renal function and decreased tubular injury in LPS-treated mice. Enhanced Rho kinase activity was inhibited by HA-1

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36

Zong, Hui, Kozo Kaibuchi, and Lawrence A. Quilliam. "The Insert Region of RhoA Is Essential for Rho Kinase Activation and Cellular Transformation." Molecular and Cellular Biology 21, no. 16 (2001): 5287–98. http://dx.doi.org/10.1128/mcb.21.16.5287-5298.2001.

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ABSTRACT RhoA is involved in multiple cellular processes, including cytoskeletal organization, gene expression, and transformation. These processes are mediated by a variety of downstream effector proteins. However, which effectors are involved in cellular transformation and how these proteins are activated following interaction with Rho remains to be established. A unique feature that distinguishes the Rho family from other Ras-related GTPases is the insert region, which may confer Rho-specific signaling events. Here we report that deletion of the insert region does not result in impaired eff

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37

Calautti, Enzo, Maddalena Grossi, Cristina Mammucari, et al. "Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell–cell adhesion." Journal of Cell Biology 156, no. 1 (2002): 137–48. http://dx.doi.org/10.1083/jcb.200105140.

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The Rho GTPase and Fyn tyrosine kinase have been implicated previously in positive control of keratinocyte cell–cell adhesion. Here, we show that Rho and Fyn operate along the same signaling pathway. Endogenous Rho activity increases in differentiating keratinocytes and is required for both Fyn kinase activation and increased tyrosine phosphorylation of β- and γ-catenin, which is associated with the establishment of keratinocyte cell–cell adhesion. Conversely, expression of constitutive active Rho is sufficient to promote cell–cell adhesion through a tyrosine kinase- and Fyn-dependent mechanis

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38

Roovers, Kristin, Eric A. Klein, Paola Castagnino, and Richard K. Assoian. "RETRACTED: Nuclear Translocation of LIM Kinase Mediates Rho-Rho Kinase Regulation of Cyclin D1 Expression." Developmental Cell 5, no. 2 (2003): 273–84. http://dx.doi.org/10.1016/s1534-5807(03)00206-5.

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39

Yang, Seun-Ah, Christopher L. Carpenter, and Charles S. Abrams. "Rho and Rho-kinase Mediate Thrombin-induced Phosphatidylinositol 4-Phosphate 5-Kinase Trafficking in Platelets." Journal of Biological Chemistry 279, no. 40 (2004): 42331–36. http://dx.doi.org/10.1074/jbc.m404335200.

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40

Nagumo, Hiromitsu, Yasuharu Sasaki, Yoshitaka Ono, Hiroyuki Okamoto, Minoru Seto, and Yoh Takuwa. "Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells." American Journal of Physiology-Cell Physiology 278, no. 1 (2000): C57—C65. http://dx.doi.org/10.1152/ajpcell.2000.278.1.c57.

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In smooth muscle, a Rho-regulated system of myosin phosphatase exists; however, it has yet to be established whether Rho kinase, one of the downstream effectors of Rho, mediates the regulation of myosin phosphatase activity in vivo. In the present study, we demonstrate in permeabilized vascular smooth muscle cells (SMCs) that the vasodilator 1-(5-isoquinolinesulfonyl)-homopiperazine (HA-1077), which we show to be a potent inhibitor of Rho kinase, dose dependently inhibits Rho-mediated enhancement of Ca2+-induced 20-kDa myosin light chain (MLC20) phosphorylation due to abrogating Rho-mediated i

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41

Yasuda, Tadashi, Yuji Tada, Nobuhiro Tanabe, Koichiro Tatsumi, and James West. "Rho-kinase inhibition alleviates pulmonary hypertension in transgenic mice expressing a dominant-negative type II bone morphogenetic protein receptor gene." American Journal of Physiology-Lung Cellular and Molecular Physiology 301, no. 5 (2011): L667—L674. http://dx.doi.org/10.1152/ajplung.00423.2010.

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Pulmonary arterial hypertension (PAH) is a life-threatening disease characterized by a sustained elevation in the pulmonary artery pressure and subsequent right heart failure. The activation of Rho/Rho-kinase activity and the beneficial effect of Rho-kinase inhibition have been demonstrated in several experimental models of pulmonary hypertension. However, it remains unclear whether Rho-kinase inhibitors can also be used against pulmonary hypertension associated with mutations in the type II bone morphogenetic protein receptor (BMPRII) gene. Transgenic mice expressing a dominant-negative BMPRI

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42

Nagaoka, Tetsutaro, Yoshiteru Morio, Nina Casanova, et al. "Rho/Rho kinase signaling mediates increased basal pulmonary vascular tone in chronically hypoxic rats." American Journal of Physiology-Lung Cellular and Molecular Physiology 287, no. 4 (2004): L665—L672. http://dx.doi.org/10.1152/ajplung.00050.2003.

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Recent evidence suggests that Rho/Rho kinase signaling plays an important role in the sustained vasoconstriction induced by many agonists and is involved in the pathogenesis of systemic vascular diseases. However, little is known about its role in increased vascular tone in hypoxic pulmonary hypertension (PH). The purpose of this study was to examine whether Rho/Rho kinase-mediated Ca2+ sensitization contributed to sustained vasoconstriction and increased vasoreactivity in hypoxic PH in rats. Acute intravenous administration of Y-27632, a Rho kinase inhibitor, nearly normalized the high pulmon

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43

Yasui, Yoshihiro, Mutsuki Amano, Koh-ichi Nagata, et al. "Roles of Rho-associated Kinase in Cytokinesis; Mutations in Rho-associated Kinase Phosphorylation Sites Impair Cytokinetic Segregation of Glial Filaments." Journal of Cell Biology 143, no. 5 (1998): 1249–58. http://dx.doi.org/10.1083/jcb.143.5.1249.

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Rho-associated kinase (Rho-kinase), which is activated by the small GTPase Rho, regulates formation of stress fibers and focal adhesions, myosin fiber organization, and neurite retraction through the phosphorylation of cytoskeletal proteins, including myosin light chain, the ERM family proteins (ezrin, radixin, and moesin) and adducin. Rho-kinase was found to phosphorylate a type III intermediate filament (IF) protein, glial fibrillary acidic protein (GFAP), exclusively at the cleavage furrow during cytokinesis. In the present study, we examined the roles of Rho-kinase in cytokinesis, in parti

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44

Fukata, Yuko, Noriko Oshiro, Nagatoki Kinoshita, et al. "Phosphorylation of Adducin by Rho-Kinase Plays a Crucial Role in Cell Motility." Journal of Cell Biology 145, no. 2 (1999): 347–61. http://dx.doi.org/10.1083/jcb.145.2.347.

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Adducin is a membrane skeletal protein that binds to actin filaments (F-actin) and thereby promotes the association of spectrin with F-actin to form a spectrin-actin meshwork beneath plasma membranes such as ruffling membranes. Rho-associated kinase (Rho- kinase), which is activated by the small guanosine triphosphatase Rho, phosphorylates α-adducin and thereby enhances the F-actin–binding activity of α-adducin in vitro. Here we identified the sites of phosphorylation of α-adducin by Rho-kinase as Thr445 and Thr480. We prepared antibody that specifically recognized α-adducin phosphorylated at

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45

Ocaranza, Maria P., Camila Fierro, Jorge E. Jalil, et al. "Rho kinase activation in circulating leukocytes is related to hypertensive myocardial remodeling." Clinical Science 132, no. 16 (2018): 1837–53. http://dx.doi.org/10.1042/cs20180312.

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Rho-kinase has relevant functions in blood pressure modulation and cardiovascular remodeling. Rho-kinase activity is determined in circulating leukocytes measuring phosphorylation of its target myosin phosphatase target subunit 1 (MYPT1), but its relationship with Rho-kinase activity in the myocardium and in vasculature in hypertension has not been evaluated. The aim was to determine the degree of association between Rho-kinase cascade activation in circulating leukocytes with cardiac and aortic Rho-kinase pathway activation in a model of hypertension and to analyze it with a cause–effect pers

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46

Parker, Thomas A., Gates Roe, Theresa R. Grover, and Steven H. Abman. "Rho kinase activation maintains high pulmonary vascular resistance in the ovine fetal lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 291, no. 5 (2006): L976—L982. http://dx.doi.org/10.1152/ajplung.00512.2005.

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Mechanisms that maintain high pulmonary vascular resistance (PVR) in the fetal lung are poorly understood. Activation of the Rho kinase signal transduction pathway, which promotes actin-myosin interaction in vascular smooth muscle cells, is increased in the pulmonary circulation of adult animals with experimental pulmonary hypertension. However, the role of Rho kinase has not been studied in the fetal lung. We hypothesized that activation of Rho kinase contributes to elevated PVR in the fetus. To address this hypothesis, we studied the pulmonary hemodynamic effects of brief (10 min) intrapulmo

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47

Satoh, Kimio, Yoshihiro Fukumoto, and Hiroaki Shimokawa. "Rho-kinase: important new therapeutic target in cardiovascular diseases." American Journal of Physiology-Heart and Circulatory Physiology 301, no. 2 (2011): H287—H296. http://dx.doi.org/10.1152/ajpheart.00327.2011.

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Rho-kinase (ROCKs) belongs to the family of serine/threonine kinases and is an important downstream effector of the small GTP-binding protein RhoA. There are two isoforms of Rho-kinase, ROCK1 and ROCK2, and they have different functions with ROCK1 for circulating inflammatory cells and ROCK2 for vascular smooth muscle cells. It has been demonstrated that the RhoA/Rho-kinase pathway plays an important role in various fundamental cellular functions, including contraction, motility, proliferation, and apoptosis, leading to the development of cardiovascular disease. The important role of Rho-kinas

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48

Flavahan, Sheila, and Nicholas A. Flavahan. "The atypical structure and function of newborn arterial endothelium is mediated by Rho/Rho kinase signaling." American Journal of Physiology-Heart and Circulatory Physiology 307, no. 4 (2014): H628—H632. http://dx.doi.org/10.1152/ajpheart.00327.2014.

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Endothelium of fetal or newborn arteries is atypical, displaying actin stress fibers and reduced nitric oxide (NO)-mediated dilatation. This study tested the hypothesis that Rho/Rho kinase signaling, which promotes endothelial stress fibers and inhibits endothelial dilatation, contributed to this phenotype. Carotid arteries were isolated from newborn [ postnatal day 1 (P1)], P7, and P21 mice. Endothelial dilatation to acetylcholine (pressure myograph) was minimal at P1, increased at P7, and further increased at P21. Inhibition of Rho (C3 transferase) or Rho kinase (Y27632, fasudil) significant

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49

Nuno, Daniel W., Jeremy S. Harrod, and Kathryn G. Lamping. "Sex-dependent differences in Rho activation contribute to contractile dysfunction in type 2 diabetic mice." American Journal of Physiology-Heart and Circulatory Physiology 297, no. 4 (2009): H1469—H1477. http://dx.doi.org/10.1152/ajpheart.00407.2009.

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The objective of this study was to determine if mechanisms involved in vascular dysfunction in type 2 diabetes differ with sex. Vascular reactivity, expression, and activation of rhoA and rho kinase were measured in aorta from male and female nondiabetic C57BLKS/J and diabetic BKS.Cg- m+/+ Leprdb/J (db/db) mice, a model of type 2 diabetes. Relaxation to acetylcholine and nitroprusside was similar in aorta from nondiabetic male and female mice. Relaxation to acetylcholine was reduced ∼50% in both male and female diabetic mice. Although inhibition of rho kinase with H-1152 increased relaxation t

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Fukata, Yuko, Kazushi Kimura, Noriko Oshiro, Hideyuki Saya, Yoshiharu Matsuura, and Kozo Kaibuchi. "Association of the Myosin-binding Subunit of Myosin Phosphatase and Moesin: Dual Regulation of Moesin Phosphorylation by Rho-associated Kinase and Myosin Phosphatase." Journal of Cell Biology 141, no. 2 (1998): 409–18. http://dx.doi.org/10.1083/jcb.141.2.409.

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Abstract:

The small GTPase Rho is believed to regulate the actin cytoskeleton and cell adhesion through its specific targets. We previously identified the Rho targets: protein kinase N, Rho-associated kinase (Rho- kinase), and the myosin-binding subunit (MBS) of myosin phosphatase. We found that in MDCK epithelial cells, MBS accumulated at the tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling area, where moesin, a member of the ERM (ezrin, radixin, and moesin) family, was localized. Neither membrane ruffling nor an accumulation of moesin and MBS at the free-end plasma membrane was induced

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