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Volumn 82, Issue 1, 2014, Pages 49-56

ROCK inhibitor Y-27632 prevents porcine oocyte maturation

Author keywords

Actin; Oocyte maturation; Rho associated protein kinase; Spindle migration; Y 27632

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ACTIN; AMIDE; ENZYME INHIBITOR; PYRIDINE DERIVATIVE;

EID: 84901424718     PISSN: 0093691X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.theriogenology.2014.02.020     Document Type: Article
Times cited : (26)

References (43)
  • 1
    • 0037000624 scopus 로고    scopus 로고
    • Synchronization of porcine oocyte meiosis using cycloheximide and its application to the study of regulation by cumulus cells
    • Ye J., Flint A., Campbell K., Luck M. Synchronization of porcine oocyte meiosis using cycloheximide and its application to the study of regulation by cumulus cells. Reprod Fertil Dev 2003, 14:433-442.
    • (2003) Reprod Fertil Dev , vol.14 , pp. 433-442
    • Ye, J.1    Flint, A.2    Campbell, K.3    Luck, M.4
  • 2
    • 0347358003 scopus 로고    scopus 로고
    • Actin reorganization and morphological changes in human neutrophils stimulated by TNF, GM-CSF, and G-CSF: the role of MAP kinases
    • Kutsuna H., Suzuki K., Kamata N., Kato T., Hato F., Mizuno K., et al. Actin reorganization and morphological changes in human neutrophils stimulated by TNF, GM-CSF, and G-CSF: the role of MAP kinases. Am J Physiol Cell Physiol 2004, 286:C55-C64.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Kutsuna, H.1    Suzuki, K.2    Kamata, N.3    Kato, T.4    Hato, F.5    Mizuno, K.6
  • 3
    • 78650393385 scopus 로고    scopus 로고
    • Positioning to get out of meiosis: the asymmetry of division
    • Brunet S., Verlhac M.H. Positioning to get out of meiosis: the asymmetry of division. Hum reprod update 2011, 17:68-75.
    • (2011) Hum reprod update , vol.17 , pp. 68-75
    • Brunet, S.1    Verlhac, M.H.2
  • 4
    • 33244481055 scopus 로고    scopus 로고
    • Regulation of dynamic events by microfilaments during oocyte maturation and fertilization
    • Sun Q.Y., Schatten H. Regulation of dynamic events by microfilaments during oocyte maturation and fertilization. Reproduction 2006, 131:193-205.
    • (2006) Reproduction , vol.131 , pp. 193-205
    • Sun, Q.Y.1    Schatten, H.2
  • 5
    • 0021922975 scopus 로고
    • Development of cortical polarity in mouse eggs: involvement of the meiotic apparatus
    • Longo F.J., Chen D.Y. Development of cortical polarity in mouse eggs: involvement of the meiotic apparatus. Dev Biol 1985, 107:382-394.
    • (1985) Dev Biol , vol.107 , pp. 382-394
    • Longo, F.J.1    Chen, D.Y.2
  • 6
    • 0022556508 scopus 로고
    • Regulation of development in the fully grown mouse oocyte: chromosome-mediated temporal and spatial differentiation of the cytoplasm and plasma membrane
    • Van Blerkom J., Bell H. Regulation of development in the fully grown mouse oocyte: chromosome-mediated temporal and spatial differentiation of the cytoplasm and plasma membrane. J Embryol Exp Morphol 1986, 93:213-238.
    • (1986) J Embryol Exp Morphol , vol.93 , pp. 213-238
    • Van Blerkom, J.1    Bell, H.2
  • 7
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung T., Chen X.Q., Manser E., Lim L. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol Cell Biol 1996, 16:5313-5327.
    • (1996) Mol Cell Biol , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 8
    • 9244257348 scopus 로고    scopus 로고
    • Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho
    • Matsui T., Amano M., Yamamoto T., Chihara K., Nakafuku M., Ito M., et al. Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J 1996, 15:2208.
    • (1996) EMBO J , vol.15 , pp. 2208
    • Matsui, T.1    Amano, M.2    Yamamoto, T.3    Chihara, K.4    Nakafuku, M.5    Ito, M.6
  • 9
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: cellular functions and signal transduction
    • Narumiya S. The small GTPase Rho: cellular functions and signal transduction. J Biochem 1996, 120:215-228.
    • (1996) J Biochem , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 10
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science 1998, 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 11
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • Amano M., Chihara K., Kimura K., Fukata Y., Nakamura N., Matsuura Y., et al. Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 1997, 275:1308-1311.
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3    Fukata, Y.4    Nakamura, N.5    Matsuura, Y.6
  • 12
    • 0030615004 scopus 로고    scopus 로고
    • P160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki T., Naito M., Fujisawa K., Maekawa M., Watanabe N., Saito Y., et al. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett 1997, 404:118-124.
    • (1997) FEBS Lett , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6
  • 13
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura 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, 273:245-248.
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3    Chihara, K.4    Fukata, Y.5    Nakafuku, M.6
  • 15
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • Ohashi K., Nagata K., Maekawa M., Ishizaki T., Narumiya S., Mizuno K. Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J Biol Chem 2000, 275:3577-3582.
    • (2000) J Biol Chem , vol.275 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 16
    • 0035808419 scopus 로고    scopus 로고
    • Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase
    • Sumi T., Matsumoto K., Nakamura T. Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem 2001, 276:670-676.
    • (2001) J Biol Chem , vol.276 , pp. 670-676
    • Sumi, T.1    Matsumoto, K.2    Nakamura, T.3
  • 17
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A., et al. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 1999, 285:895-898.
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1    Ishizaki, T.2    Boku, S.3    Watanabe, N.4    Fujita, A.5    Iwamatsu, A.6
  • 18
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata 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, 389:990-994.
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3    Ono, T.4    Kawahara, T.5    Morishita, T.6
  • 19
    • 0034017744 scopus 로고    scopus 로고
    • Pharmacological properties of Y-27632, a specific inhibitor of rho-associated kinases
    • Ishizaki T., Uehata M., Tamechika I., Keel J., Nonomura K., Maekawa M., et al. Pharmacological properties of Y-27632, a specific inhibitor of rho-associated kinases. Mol Pharmacol 2000, 57:976-983.
    • (2000) Mol Pharmacol , vol.57 , pp. 976-983
    • Ishizaki, T.1    Uehata, M.2    Tamechika, I.3    Keel, J.4    Nonomura, K.5    Maekawa, M.6
  • 20
    • 0037298073 scopus 로고    scopus 로고
    • Reduction of hepatic ischemia/reperfusion-induced injury by a specific ROCK/Rho kinase inhibitor Y-27632
    • Ikeda F., Terajima H., Shimahara Y., Kondo T., Yamaoka Y. Reduction of hepatic ischemia/reperfusion-induced injury by a specific ROCK/Rho kinase inhibitor Y-27632. J Surg Res 2003, 109:155-160.
    • (2003) J Surg Res , vol.109 , pp. 155-160
    • Ikeda, F.1    Terajima, H.2    Shimahara, Y.3    Kondo, T.4    Yamaoka, Y.5
  • 21
    • 0034842254 scopus 로고    scopus 로고
    • A highly selective inhibitor of Rho-associated coiled-coil forming protein kinase, Y-27632, prolongs cardiac allograft survival of the BALB/c-to-C3H/He mouse model
    • Ohki S., Iizuka K., Ishikawa S., Kano M., Dobashi K., Yoshii A., et al. A highly selective inhibitor of Rho-associated coiled-coil forming protein kinase, Y-27632, prolongs cardiac allograft survival of the BALB/c-to-C3H/He mouse model. J Heart Lung Transplant 2001, 20:956-963.
    • (2001) J Heart Lung Transplant , vol.20 , pp. 956-963
    • Ohki, S.1    Iizuka, K.2    Ishikawa, S.3    Kano, M.4    Dobashi, K.5    Yoshii, A.6
  • 22
    • 0034955193 scopus 로고    scopus 로고
    • Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: dissociation from tyrosine phosphorylation of p130(CAS)
    • Sinnett-Smith J., Lunn J.A., Leopoldt D., Rozengurt E. Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: dissociation from tyrosine phosphorylation of p130(CAS). Exp Cell Res 2001, 266:292-302.
    • (2001) Exp Cell Res , vol.266 , pp. 292-302
    • Sinnett-Smith, J.1    Lunn, J.A.2    Leopoldt, D.3    Rozengurt, E.4
  • 23
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung T., Manser E., Tan L., Lim L. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem 1995, 270:29051-29054.
    • (1995) J Biol Chem , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 24
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase
    • Kimura 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, 273:5542-5548.
    • (1998) J Biol Chem , vol.273 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3    Bennett, V.4    Matsuura, Y.5    Okawa, K.6
  • 25
    • 59249101080 scopus 로고    scopus 로고
    • Identification of the Rock-dependent transcriptome in rodent fibroblasts
    • Berenjeno I.M., Bustelo X.R. Identification of the Rock-dependent transcriptome in rodent fibroblasts. Clin Transl Oncol 2008, 10:726-738.
    • (2008) Clin Transl Oncol , vol.10 , pp. 726-738
    • Berenjeno, I.M.1    Bustelo, X.R.2
  • 26
    • 60349086029 scopus 로고    scopus 로고
    • Spindle positioning: actin mediates pushing and pulling
    • Bezanilla M., Wadsworth P. Spindle positioning: actin mediates pushing and pulling. Curr Biol 2009, 19:R168-R169.
    • (2009) Curr Biol , vol.19
    • Bezanilla, M.1    Wadsworth, P.2
  • 27
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi K., Sasaki T., Kuroda S., Itoh T., Takai Y. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J Cell Biol 1993, 120:1187-1195.
    • (1993) J Cell Biol , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 28
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi I., Hamaguchi Y., Fujimoto H., Morii N., Mishima M., Narumiya S. A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote 1993, 1:325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 29
    • 0033601744 scopus 로고    scopus 로고
    • The small GTP-binding protein rho regulates cortical activities in cultured cells during division
    • O'Connell C.B., Wheatley S.P., Ahmed S., Wang Y.L. The small GTP-binding protein rho regulates cortical activities in cultured cells during division. J Cell Biol 1999, 144:305-313.
    • (1999) J Cell Biol , vol.144 , pp. 305-313
    • O'Connell, C.B.1    Wheatley, S.P.2    Ahmed, S.3    Wang, Y.L.4
  • 30
    • 0034619765 scopus 로고    scopus 로고
    • Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow
    • Kosako H., Yoshida T., Matsumura F., Ishizaki T., Narumiya S., Inagaki M. Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene 2000, 19:6059-6064.
    • (2000) Oncogene , vol.19 , pp. 6059-6064
    • Kosako, H.1    Yoshida, T.2    Matsumura, F.3    Ishizaki, T.4    Narumiya, S.5    Inagaki, M.6
  • 31
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui Y., Amano M., Nagata K.-i., Inagaki N., Nakamura H., Saya H., et al. Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J Cell Biol 1998, 143:1249-1258.
    • (1998) J Cell Biol , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Nagata, K.-I.3    Inagaki, N.4    Nakamura, H.5    Saya, H.6
  • 32
    • 0035184138 scopus 로고    scopus 로고
    • Animal cell cytokinesis
    • Glotzer M. Animal cell cytokinesis. Ann Rev Cell Dev Biol 2001, 17:351-386.
    • (2001) Ann Rev Cell Dev Biol , vol.17 , pp. 351-386
    • Glotzer, M.1
  • 33
    • 0034212988 scopus 로고    scopus 로고
    • Towards a molecular understanding of cytokinesis
    • Robinson D.N., Spudich J.A. Towards a molecular understanding of cytokinesis. Trends Cell Biol 2000, 10:228-237.
    • (2000) Trends Cell Biol , vol.10 , pp. 228-237
    • Robinson, D.N.1    Spudich, J.A.2
  • 35
    • 0037066777 scopus 로고    scopus 로고
    • Characterization of RhoA-binding kinase ROKalpha implication of the pleckstrin homology domain in ROKα function using region-specific antibodies
    • Chen X.q., Tan I., Ng C.H., Hall C., Lim L., Leung T. Characterization of RhoA-binding kinase ROKalpha implication of the pleckstrin homology domain in ROKα function using region-specific antibodies. J Biol Chem 2002, 277:12680-12688.
    • (2002) J Biol Chem , vol.277 , pp. 12680-12688
    • Chen, X.1    Tan, I.2    Ng, C.H.3    Hall, C.4    Lim, L.5    Leung, T.6
  • 36
    • 55549144707 scopus 로고    scopus 로고
    • Actin-driven chromosomal motility leads to symmetry breaking in mammalian meiotic oocytes
    • Li H., Guo F., Rubinstein B., Li R. Actin-driven chromosomal motility leads to symmetry breaking in mammalian meiotic oocytes. Nat Cell Biol 2008, 10:1301-1308.
    • (2008) Nat Cell Biol , vol.10 , pp. 1301-1308
    • Li, H.1    Guo, F.2    Rubinstein, B.3    Li, R.4
  • 37
    • 0036904735 scopus 로고    scopus 로고
    • Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes
    • Leader B., Lim H., Carabatsos M.J., Harrington A., Ecsedy J., Pellman D., et al. Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes. Nat Cell Biol 2002, 4:921-928.
    • (2002) Nat Cell Biol , vol.4 , pp. 921-928
    • Leader, B.1    Lim, H.2    Carabatsos, M.J.3    Harrington, A.4    Ecsedy, J.5    Pellman, D.6
  • 38
    • 79954499485 scopus 로고    scopus 로고
    • Arp2/3 complex regulates asymmetric division and cytokinesis in mouse oocytes
    • Sun S.C., Wang Z.B., Xu Y.N., Lee S.E., Cui X.S., Kim N.H. Arp2/3 complex regulates asymmetric division and cytokinesis in mouse oocytes. PLoS One 2011, 6:e18392.
    • (2011) PLoS One , vol.6
    • Sun, S.C.1    Wang, Z.B.2    Xu, Y.N.3    Lee, S.E.4    Cui, X.S.5    Kim, N.H.6
  • 39
    • 80053488949 scopus 로고    scopus 로고
    • Dynamic maintenance of asymmetric meiotic spindle position through Arp2/3-complex-driven cytoplasmic streaming in mouse oocytes
    • Yi K., Unruh J.R., Deng M., Slaughter B.D., Rubinstein B., Li R. Dynamic maintenance of asymmetric meiotic spindle position through Arp2/3-complex-driven cytoplasmic streaming in mouse oocytes. Nat Cell Biol 2011, 13:1252-1258.
    • (2011) Nat Cell Biol , vol.13 , pp. 1252-1258
    • Yi, K.1    Unruh, J.R.2    Deng, M.3    Slaughter, B.D.4    Rubinstein, B.5    Li, R.6
  • 40
    • 33744997166 scopus 로고    scopus 로고
    • Asymmetric positioning and organization of the meiotic spindle of mouse oocytes requires CDC42 function
    • Na J., Zernicka-Goetz M. Asymmetric positioning and organization of the meiotic spindle of mouse oocytes requires CDC42 function. Curr Biol 2006, 16:1249-1254.
    • (2006) Curr Biol , vol.16 , pp. 1249-1254
    • Na, J.1    Zernicka-Goetz, M.2
  • 41
    • 84876314142 scopus 로고    scopus 로고
    • Polarized Cdc42 activation promotes polar body protrusion and asymmetric division in mouse oocytes
    • Dehapiot B., Carrière V., Carrollc J., Halet G. Polarized Cdc42 activation promotes polar body protrusion and asymmetric division in mouse oocytes. Dev Biol 2013, 377:201-212.
    • (2013) Dev Biol , vol.377 , pp. 201-212
    • Dehapiot, B.1    Carrière, V.2    Carrollc, J.3    Halet, G.4
  • 42
    • 33846646483 scopus 로고    scopus 로고
    • Rac activity is polarized and regulates meiotic spindle stability and anchoring in mammalian oocytes
    • Halet G., Carroll J. Rac activity is polarized and regulates meiotic spindle stability and anchoring in mammalian oocytes. Dev Cell 2007, 12:309-317.
    • (2007) Dev Cell , vol.12 , pp. 309-317
    • Halet, G.1    Carroll, J.2
  • 43
    • 84878540835 scopus 로고    scopus 로고
    • Ran GTPase promotes oocyte polarization by regulating ERM (Ezrin/Radixin/Moesin) activation
    • Dehapiot B., Halet G. Ran GTPase promotes oocyte polarization by regulating ERM (Ezrin/Radixin/Moesin) activation. Cell Cycle 2013, 12:1672-1678.
    • (2013) Cell Cycle , vol.12 , pp. 1672-1678
    • Dehapiot, B.1    Halet, G.2


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