Hostname: page-component-77c89778f8-vpsfw Total loading time: 0 Render date: 2024-07-19T07:32:02.131Z Has data issue: false hasContentIssue false
  • English
  • Français

RHO PROTEINS, PREGNANCY AND LABOUR

Part of: Bespoke shallow archive Weizmann

Published online by Cambridge University Press:  13 November 2009

J LARTEY  and
A LÓPEZ BERNAL
J LARTEY*
Affiliation:
University of Newcastle, Institute of Cellular Medicine, Medical School, Newcastle upon Tyne, NE2 4HH, United Kingdom.
A LÓPEZ BERNAL
Affiliation:
University of Bristol, Clinical Sciences South Bristol, Division of Obstetrics and Gynaecology, Henry Wellcome Laboratories for Integrative Neuroscience and Endocrinology, Dorothy Hodgkin Building, Whitson St, Bristol, BS1 3NY, United Kingdom.
*
J Lartey, Newcastle University, Institute of Cellular Medicine, 3rd Floor, William Leech Building, Medical School, Framlington Place, Newcastle upon Tyne, NE2 4HH, United Kingdom.
Get access Rights & Permissions [Opens in a new window]

Extract

Premature birth is the most important cause of perinatal death and long term morbidity in the world today. Although an increasing proportion of premature births are induced secondary to pre-existing fetal and maternal conditions, over half of these deliveries are due to spontaneous onset of uterine contractions (spontaneous preterm labour). So far, our ability to successfully treat women whose pregnancies are complicated by preterm labour is hampered by a lack of knowledge of the endocrine and biochemical factors that initiate human parturition.

Type
Research Article
Information
Fetal and Maternal Medicine Review , Volume 20 , Issue 4 , November 2009 , pp. 283 - 299
Copyright
Copyright © Cambridge University Press 2009

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1Somlyo, AP, Somlyo, AV. Signal transduction and regulation in smooth muscle. Nature 1994; 372: 231–36.CrossRefGoogle ScholarPubMed
2Van Aelst, L, D'Souza-Schorey, C. Rho GTPases and signaling networks. Genes Dev 1997; 11: 2295–322.CrossRefGoogle ScholarPubMed
3Moon, SY, Zheng, Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol 2003; 13: 13–22.CrossRefGoogle ScholarPubMed
4Michaelson, D, Silletti, J, Murphy, G, D'Eustachio, P, Rush, M, Philips, MR. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J Cell Biol 2001; 152: 111–26.CrossRefGoogle ScholarPubMed
5Riento, K, Guasch, RM, Garg, R, Jin, B, Ridley, AJ. RhoE Binds to ROCK I and Inhibits Downstream Signaling. Mol Cell Biol. 2003; 23: 4219–229.CrossRefGoogle Scholar
6Ishizaki, T, Maekawa, M, Fujisawa, K, Okawa, K, Iwamatsu, A, Fujita, A, et al. The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. Embo J 1996; 15: 1885–893.CrossRefGoogle ScholarPubMed
7Rikitake, Y, Oyama, N, Wang, C-YC, Noma, K, Satoh, M, Kim, H-H, et al. Decreased Perivascular Fibrosis but Not Cardiac Hypertrophy in ROCK1+/- Haploinsufficient Mice. Circulation 2005; 112: 2959–965.CrossRefGoogle ScholarPubMed
8Thumkeo, D, Keel, J, Ishizaki, T, Hirose, M, Nonomura, K, Oshima, H, et al. Targeted Disruption of the Mouse Rho-Associated Kinase 2 Gene Results in Intrauterine Growth Retardation and Fetal Death. Mol Cell Biol 2003; 23: 5043–5055.CrossRefGoogle ScholarPubMed
9Kim, BK, Ozaki, H, Hori, M, Takahashi, K, Karaki, H. Increased contractility of rat uterine smooth muscle at the end of pregnancy. Comp Biochem Physiol A Mol Integr Physiol 1998; 121: 165–73.CrossRefGoogle ScholarPubMed
10Riley, M, Baker, PN, Tribe, RM, Taggart, MJ. Expression of scaffolding, signalling and contractile-filament proteins in human myometria: effects of pregnancy and labour. J Cell Mol Med 2005; 9: 122–34.CrossRefGoogle ScholarPubMed
11Word, RA, Stull, JT, Casey, ML, Kamm, KE. Contractile elements and myosin light chain phosphorylation in myometrial tissue from nonpregnant and pregnant women. J Clin Invest 1993; 92: 29–37.CrossRefGoogle ScholarPubMed
12Loirand, G, Cario-Toumaniantz, C, Chardin, P, Pacaud, P. The Rho-related protein Rnd1 inhibits Ca2+ sensitization of rat smooth muscle. J Physiol 1999; 516: 825–34.CrossRefGoogle ScholarPubMed
13Kim, Y-S, Kim, B, Karaki, H, Hori, M, Ozaki, H. Up-regulation of Rnd1 during pregnancy serves as a negative-feedback control for Ca2+ sensitization of contractile elements in rat myometrium. Biochem Biophys Res Commun 2003; 311: 972–78.CrossRefGoogle ScholarPubMed
14Cario-Toumaniantz, C, Reillaudoux, G, Sauzeau, V, Heutte, F, Vaillant, N, Finet, M, et al. Modulation of RhoA-Rho kinase-mediated Ca2+ sensitization of rabbit myometrium during pregnancy – role of Rnd3. J Physiol 2003; 552: 403–13.CrossRefGoogle ScholarPubMed
15Niiro, N, Nishimura, J, Sakihara, C, Nakano, H, Kanaide, H. Up-Regulation of rho A and rho-Kinase mRNAs in the Rat Myometrium during Pregnancy. Biochem Biophys Res Commun 1997; 230: 356–59.CrossRefGoogle Scholar
16Lartey, J, Gampel, A, Pawade, J, Mellor, H, Lopez Bernal, A. Expression of RND Proteins in human myometrium. Biol Reprod 2006; 75: 452–61.CrossRefGoogle ScholarPubMed
17Bishop, AL, Hall, A. Rho GTPases and their effector proteins. Biochem J 2000; 348: 241–55.CrossRefGoogle ScholarPubMed
18Moore, F, Da Silva, C, Wilde, JI, Smarason, A, Watson, SP, Lopez Bernal, A. Up-Regulation of p21- and RhoA-Activated Protein Kinases in Human Pregnant Myometrium. Biochem Biophys Res Commun 2000; 269: 322–26.CrossRefGoogle ScholarPubMed
19Moran, CJ, Friel, AM, Smith, TJ, Cairns, M, Morrison, JJ. Expression and modulation of Rho kinase in human pregnant myometrium. Mol Hum Reprod 2002; 8: 196–200.CrossRefGoogle ScholarPubMed
20Tahara, M, Morishige, K-i, Sawada, K, Ikebuchi, Y, Kawagishi, R, Tasaka, K, et al. RhoA/Rho-Kinase Cascade Is Involved in Oxytocin-Induced Rat Uterine Contraction. Endocrinology 2002; 143: 920–29.CrossRefGoogle ScholarPubMed
21Lartey, J, Smith, M, Pawade, J, Strachan, B, Mellor, H, Lopez Bernal, A. Up-regulation of myometrial RHO effector proteins (PKN1 and DIAPH1) and CPI-17 (PPP1R14A) phosphorylation in human pregnancy is associated with increased GTP-RHOA in spontaneous preterm labor. Biol Reprod 2007; 76: 971–82.CrossRefGoogle ScholarPubMed
22Moore, F, Asboth, G, Lopez, BA. Thromboxane receptor signalling in human myometrial cells. Prostaglandins Other Lipid Mediat 2002; 67: 31–47.CrossRefGoogle ScholarPubMed
23Moore, F, Lopez Bernal, A. Chronic exposure to TXA2 increases expression of ROCKI in human myometrial cells. Prostaglandins Other Lipid Mediat 2003; 71: 23–32.CrossRefGoogle ScholarPubMed
24Kupittayanant, S, Burdyga, T, Wray, S. The effects of inhibiting Rho-associated kinase with Y-27632 on force and intracellular calcium in human myometrium. Pflugers Arch 2001; 443: 112–14.CrossRefGoogle ScholarPubMed
25Murthy, KS, Zhou, H, Grider, JR, Brautigan, DL, Eto, M, Makhlouf, GM. Differential signalling by muscarinic receptors in smooth muscle: m2-mediated inactivation of myosin light chain kinase via Gi3, Cdc42/Rac1 and p21-activated kinase 1 pathway, and m3-mediated MLC20 (20 kDa regulatory light chain of myosin II) phosphorylation via Rho-associated kinase/myosin phosphatase targeting subunit 1 and protein kinase C/CPI-17 pathway. Biochem J 2003; 374: 145–55.CrossRefGoogle ScholarPubMed
26Taggart, MJ, Lee, Y-H, Morgan, KG. Cellular Redistribution of PKC[alpha], rhoA, and ROK[alpha] Following Smooth Muscle Agonist Stimulation. Exp Cell Res 1999; 251: 92–101.CrossRefGoogle Scholar
27Oh, JH, You, SK, Hwang, MK, Ahn, DS, Kwon, SC, Taggart, MJ, et al. Inhibition of rho-associated kinase reduces MLC20 phosphorylation and contractility of intact myometrium and attenuates agonist-induced Ca2 +sensitization of force of permeabilized rat myometrium. J Vet Med Sci 2003; 65: 43–50.CrossRefGoogle ScholarPubMed
28Lartey, J, Gampel, A, Mellor, H, Pawade, J, Lopez Bernal, A. Localisation and function of new RHO family member RHOB GTPase in pregnant human myometrium. J Obstet Gynaecol 2006; 26: S25–S31.Google Scholar
29Lartey, J, López Bernal, A. Oxytocin and Carbachol Induced Membrane Translocation of RHO GTP Binding Proteins in Human Myometrial Tissue Strips. Reprod Sci 2008; 15: 61A–319A.Google Scholar
30Karteris, E, Hillhouse, EW, Grammatopoulos, D. Urocortin II is expressed in human pregnant myometrial cells and regulates myosin light chain phosphorylation: potential role of the type-2 corticotropin-releasing hormone receptor in the control of myometrial contractility. Endocrinology 2004; 145: 890–900.CrossRefGoogle ScholarPubMed
31Woodcock, NA, Taylor, CW, Thornton, S. Effect of an oxytocin receptor antagonist and rho kinase inhibitor on the [Ca++]i sensitivity of human myometrium. Am J Obstet Gynecol 2004; 190: 222–28.CrossRefGoogle ScholarPubMed
32Woodcock, NA, Taylor, CW, Thornton, S. Prostaglandin F2alpha increases the sensitivity of the contractile proteins to Ca2+ in human myometrium. Am J Obstet Gynecol 2006; 195: 1404–406.CrossRefGoogle ScholarPubMed
33Lartey, J, Lopez-Bernal, A. Oxytocin Mediates ROCK Dependent Phosphorylation of the Regulatory Subunit (PPP1R12A) of Myosin Phosphatase To Increase Myosin Phosphorylation in Human Myometrium. Reprod Sci 2008; 15: 61A–319A.Google Scholar
34Ozaki, H, Yasuda, K, Kim, YS, Egawa, M, Kanzaki, H, Nakazawa, H, et al. Possible role of the protein kinase C/CPI-17 pathway in the augmented contraction of human myometrium after gestation. Br J Pharmacol 2003; 140: 1303–312.CrossRefGoogle ScholarPubMed
35Lartey, J, Gampel, A, Mellor, H, Pawade, J, Lopez Bernal, A. Down regulation of RHOD GTPase in spontaneous labour may be associated with increased RHOA mediated calcium sensitisation during pregnancy. J Obstet Gynaecol 2006; 26: Supplement 1. S22–S31.Google Scholar
36Mukherjee, S, Gurevich, VV, Jones, JC, Casanova, JE, Frank, SR, Maizels, ET, et al. The ADP ribosylation factor nucleotide exchange factor ARNO promotes beta-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization. Proc Natl Acad Sci 2000; 97: 5901–906.CrossRefGoogle ScholarPubMed
37Salvador, LM, Mukherjee, S, Kahn, RA, Lamm, ML, Fazleabas, AT, Maizels, ET et al. Activation of the luteinizing hormone/choriogonadotropin hormone receptor promotes ADP ribosylation factor 6 activation in porcine ovarian follicular membranes. J Biol Chem 2001; 276: 33773–781.CrossRefGoogle ScholarPubMed
38Lartey, J, Lopez Bernal, A. Up Regulation of ARFGEF PSCD3 Expression in Labour Represents a Mechanism for Receptor Desensitisation in Human Myometrium. Reprod Sci 2008; 15: 61A.Google Scholar
39Lartey, J, Smith, M, Pawade, J, Strachan, B, Mellor, H, Lopez Bernal, A. Up-Regulation of Myometrial RHO Effector Proteins (PKN1 and DIAPH1) and CPI-17 (PPP1R14A) Phosphorylation in Human Pregnancy Is Associated with Increased GTP-RHOA in Spontaneous Preterm Labor. Biol Reprod 2007; 76: 971–82.CrossRefGoogle ScholarPubMed
40Lartey, J, Lopez Bernal, A. Nuclear localisation of RHO associated kinases ROCK1 and ROCK2 in human myometrial and interstitial cells represents a pathway of nuclear activation during pregnancy and in labour. Reprod Sci 2009; 16: 292–94.Google Scholar
41Tong, W, Pollard, JW. Progesterone inhibits estrogen-induced cyclin D1 and cdk4 nuclear translocation, cyclin E- and cyclin A-cdk2 kinase activation, and cell proliferation in uterine epithelial cells in mice. Mol Cell Biol 1999; 19: 2251–64.CrossRefGoogle ScholarPubMed
42Nautiyal, J, Kumar, PG, Laloraya, M. 17Beta-estradiol induces nuclear translocation of CrkL at the window of embryo implantation. Biochem Biophys Res Commun 2004; 318: 103–12.CrossRefGoogle ScholarPubMed
43Liu, Y, Suzuki, YJ, Day, RM, Fanburg, BL. Rho kinase-induced nuclear translocation of ERK1/ERK2 in smooth muscle cell mitogenesis caused by serotonin. Circ Res 2004; 95: 579–86.CrossRefGoogle ScholarPubMed
44Bhowmick, NA, Ghiassi, M, Aakre, M, Brown, K, Singh, V, Moses, HL. TGF-beta-induced RhoA and p160ROCK activation is involved in the inhibition of Cdc25A with resultant cell-cycle arrest. Proc Natl Acad Sci 2003; 100: 15548–553.CrossRefGoogle ScholarPubMed
45Ozaki, H, Yasuda, K, Kim, Y-S, Egawa, M, Kanzaki, H, Nakazawa, H, et al. Possible role of the protein kinase C//CPI-17 pathway in the augmented contraction of human myometrium after gestation. Br J Pharmacol 2003; 140: 1303–12.CrossRefGoogle ScholarPubMed
46Watanabe, N, Madaule, P, Reid, T, Ishizaki, T, Watanabe, G, Kakizuka, A, et al. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J 1997; 16: 3044–56.CrossRefGoogle ScholarPubMed
47Watanabe, N KT, Fujita, A, Ishizaki, T, Narumiya, S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1999; 1: 136–43.CrossRefGoogle ScholarPubMed
48Takizawa, N, Koga, Y, Ikebe, M. Phosphorylation of CPI17 and myosin binding subunit of type 1 protein phosphatase by p21-activated kinase. Biochem Biophys Res Commun 2002; 297: 773–78.CrossRefGoogle ScholarPubMed
49Muranyi, A, Zhang, R, Liu, F, Hirano, K, Ito, M, Epstein, HF, et al. Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity. FEBS Lett 2001; 493: 80–84.CrossRefGoogle ScholarPubMed
50Muranyi, A, MacDonald, JA, Deng, JT, Wilson, DP, Haystead, TA, Walsh, MP, et al. Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase. Biochem J 2002; 366: 211–16.CrossRefGoogle ScholarPubMed
51MacDonald, JA, Borman, MA, Muranyi, A, Somlyo, AV, Hartshorne, DJ, Haystead, TA. Identification of the endogenous smooth muscle myosin phosphatase-associated kinase. Proc Natl Acad Sci 2001; 98: 2419–424.CrossRefGoogle ScholarPubMed
52Lartey, J, Lopez Bernal, A. Dimerization of death associated protein kinase 3 (DAPK3) is associated with an increase in RHOA activity in human myometrium during spontaneous labour. Reprod Sci 2009; 16: 219–20.Google Scholar
53Uehata, M, Ishizaki, T, Satoh, H, Ono, T, Kawahara, T, Morishita, T, et al. Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 1997; 389: 990–94.CrossRefGoogle ScholarPubMed
54Davies, SP, Reddy, H, Caivano, M, Cohen, P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 2000; 351: 95–105.CrossRefGoogle ScholarPubMed
55Amano, M, Chihara, K, Nakamura, N, Kaneko, T, Matsuura, Y, Kaibuchi, K. The COOH terminus of Rho-kinase negatively regulates rho-kinase activity. J Biol Chem 1999; 274: 32418–424.CrossRefGoogle ScholarPubMed
56Niggli, V. Rho-kinase in human neutrophils: a role in signalling for myosin light chain phosphorylation and cell migration. FEBS Lett 1999; 445: 69–72.CrossRefGoogle ScholarPubMed
57Sebti, SM, Hamilton, AD. Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies. Oncogene 2000; 19: 6584–593.CrossRefGoogle ScholarPubMed
58Goldberg, L, Kloog, Y. A Ras inhibitor tilts the balance between Rac and Rho and blocks phosphatidylinositol 3-kinase-dependent glioblastoma cell migration. Cancer Res 2006; 66: 11709–717.CrossRefGoogle ScholarPubMed
59Smalley, KS, Eisen, TG. Farnesyl transferase inhibitor SCH66336 is cytostatic, pro-apoptotic and enhances chemosensitivity to cisplatin in melanoma cells. Int J Cancer 2003; 105: 165–75.CrossRefGoogle ScholarPubMed
60Wareing, M, O'Hara, M, Seghier, F, Baker, PN, Taggart, MJ. The involvement of Rho-associated kinases in agonist-dependent contractions of human maternal and placental arteries at term gestation. Am J Obstet Gynecol 2005; 193: 815–24.CrossRefGoogle ScholarPubMed
61Lartey, J, Gampel, A, Mellor, H, Bernal, AL. Expression of RND2 and RND3 mRNA in human myometrial and placental tissues. Proc Physiol Soc 3, PC104 2006; 138–39.Google Scholar
62Kimura, K, Ito, M, Amano, M, Chihara, K, Fukata, Y, Nakafuku, M, et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 1996; 273: 245–48.CrossRefGoogle ScholarPubMed
63Feng, J, Ito, M, Ichikawa, K, Isaka, N, Nishikawa, M, Hartshorne, DJ, et al. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J Biol Chem 1999; 274: 37385–390.CrossRefGoogle ScholarPubMed
64Kawano, Y, Fukata, Y, Oshiro, N, Amano, M, Nakamura, T, Ito, M, et al. Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J Cell Biol 1999; 147: 1023–1038.CrossRefGoogle ScholarPubMed
65Kitazawa, T, Eto, M, Woodsome, TP, Khalequzzaman, M. Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle. J Physiol 2003; 546: 879–89.CrossRefGoogle ScholarPubMed
66Eto, M, Kitazawa, T, Yazawa, M, Mukai, H, Ono, Y, Brautigan, DL. Histamine-induced Vasoconstriction Involves Phosphorylation of a Specific Inhibitor Protein for Myosin Phosphatase by Protein Kinase C alpha and delta Isoforms. J Biol Chem 2001; 276: 29072–9078.CrossRefGoogle ScholarPubMed
67Kitazawa, T, Eto, M, Woodsome, TP, Brautigan, DL. Agonists Trigger G Protein-mediated Activation of the CPI-17 Inhibitor Phosphoprotein of Myosin Light Chain Phosphatase to Enhance Vascular Smooth Muscle Contractility. J Biol Chem 2000; 275: 9897–900.CrossRefGoogle ScholarPubMed
68Kureishi, Y, Kobayashi, S, Amano, M, Kimura, K, Kanaide, H, Nakano, T, et al. Rho-associated Kinase Directly Induces Smooth Muscle Contraction through Myosin Light Chain Phosphorylation. J Biol Chem 1997; 272: 12257–260.CrossRefGoogle ScholarPubMed
69Hagerty, L, Weitzel, DH, Chambers, J, Fortner, CN, Brush, MH, Loiselle, D, et al. ROCK1 phosphorylates and activates ZIP kinase. J Biol Chem 2006: M609990200.Google Scholar
70Kiss, E, Muranyi, A, Csortos, C, Gergely, P, Ito, M, Hartshorne, DJ, et al. Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton. Biochem J 2002; 365: 79–87.CrossRefGoogle ScholarPubMed
71Haystead, TAJ. ZIP kinase, a key regulator of myosin protein phosphatase 1. Cell Signal 2005; 17: 1313–322.CrossRefGoogle ScholarPubMed
72Matsui, T, Maeda, M, Doi, Y, Yonemura, S, Amano, M, Kaibuchi, K, et al. Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association. J Cell Biol 1998; 140: 647–57.CrossRefGoogle ScholarPubMed
73Kimura, K, Fukata, Y, Matsuoka, Y, Bennett, V, Matsuura, Y, Okawa, K, et al. Regulation of the Association of Adducin with Actin Filaments by Rho-associated Kinase (Rho-kinase) and Myosin Phosphatase. J Biol Chem 1998; 273: 5542–548.CrossRefGoogle ScholarPubMed