메뉴 건너뛰기




Volumn 110, Issue 2, 2006, Pages 153-165

RhoA/Rho-kinase in erectile tissue: Mechanisms of disease and therapeutic insights

Author keywords

Corpus cavernosum; Erectile dysfunction; Penis; Rho kinase; RhoA; Smooth muscle

Indexed keywords

CALCIUM; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN PHOSPHATASE; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 32644449489     PISSN: 01435221     EISSN: None     Source Type: Journal    
DOI: 10.1042/CS20050255     Document Type: Review
Times cited : (77)

References (149)
  • 1
    • 0032810944 scopus 로고    scopus 로고
    • The likely worldwide increase in erectile dysfunction between 1995 and 2025 and some possible policy consequences
    • Ayta, I. A., Mckinlay, J. B. and Krane, R. J. (1999) The likely worldwide increase in erectile dysfunction between 1995 and 2025 and some possible policy consequences. BJU Int. 84, 50-56
    • (1999) BJU Int. , vol.84 , pp. 50-56
    • Ayta, I.A.1    Mckinlay, J.B.2    Krane, R.J.3
  • 2
    • 0028036149 scopus 로고
    • Impotence and its medical and psychosocial correlates: Results of the Massachusetts Male Aging Study
    • Feldman, H. A., Goldstein, I., Hatzichristou, D. G., Krane, R. J. and McKinlay, J. B. (1994) Impotence and its medical and psychosocial correlates: results of the Massachusetts Male Aging Study. J. Urol. 151, 54-61
    • (1994) J. Urol. , vol.151 , pp. 54-61
    • Feldman, H.A.1    Goldstein, I.2    Hatzichristou, D.G.3    Krane, R.J.4    McKinlay, J.B.5
  • 3
    • 0242625953 scopus 로고    scopus 로고
    • Neurophysiology of erectile function: Androgenic effects
    • Burnett, A. L. (2003) Neurophysiology of erectile function: androgenic effects. J. Androl. 24, S2-S5
    • (2003) J. Androl. , vol.24
    • Burnett, A.L.1
  • 4
    • 0028837352 scopus 로고
    • Physiology of penile erection
    • Andersson, K. E. and Wagner, G. (1995) Physiology of penile erection. Physiol. Rev. 75, 191-236
    • (1995) Physiol. Rev. , vol.75 , pp. 191-236
    • Andersson, K.E.1    Wagner, G.2
  • 5
    • 3342887762 scopus 로고    scopus 로고
    • Novel nitric oxide signaling mechanisms regulate the erectile response
    • Burnett, A. L. (2004) Novel nitric oxide signaling mechanisms regulate the erectile response. Int. J. Impot. Res. 16(Suppl. 1), S15-S19
    • (2004) Int. J. Impot. Res. , vol.16 , Issue.SUPPL. 1
    • Burnett, A.L.1
  • 6
    • 0028859180 scopus 로고
    • Role of nitric oxide in the physiology of erection
    • Burnett, A. L. (1995) Role of nitric oxide in the physiology of erection. Biol. Reprod. 52, 485-489
    • (1995) Biol. Reprod. , vol.52 , pp. 485-489
    • Burnett, A.L.1
  • 7
    • 0346502905 scopus 로고    scopus 로고
    • Smooth muscle contraction and relaxation
    • Webb, R. C. (2003) Smooth muscle contraction and relaxation. Adv. Physiol. Edu. 27, 201-206
    • (2003) Adv. Physiol. Edu. , vol.27 , pp. 201-206
    • Webb, R.C.1
  • 8
    • 15144342061 scopus 로고    scopus 로고
    • Calcium movements, distribution, and functions in smooth muscle
    • Karaki, H., Ozaki, H., Hori, M. et al. (1997) Calcium movements, distribution, and functions in smooth muscle. Pharmacol. Rev. 49, 157-230
    • (1997) Pharmacol. Rev. , vol.49 , pp. 157-230
    • Karaki, H.1    Ozaki, H.2    Hori, M.3
  • 9
    • 0036362727 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum: Then and now
    • Somlyo, A. P. and Somlyo, A. V. (2002) The sarcoplasmic reticulum: then and now. Novartis Found. Symp. 246, 258-268
    • (2002) Novartis Found. Symp. , vol.246 , pp. 258-268
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 10
    • 0022272322 scopus 로고
    • Calcium-force relationships as detected with aequorin in two different vascular smooth muscles of the ferret
    • DeFeo, T. T. and Morgan, K. G. (1985) Calcium-force relationships as detected with aequorin in two different vascular smooth muscles of the ferret. J. Physiol. 369, 269-282
    • (1985) J. Physiol. , vol.369 , pp. 269-282
    • DeFeo, T.T.1    Morgan, K.G.2
  • 12
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo, A. P. and Somlyo, A. V. (1994) Signal transduction and regulation in smooth muscle. Nature (London) 372, 231-236
    • (1994) Nature (London) , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 13
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne, D. J., Ito, M. and Erdodi, F. (1998) Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19, 325-341
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 14
    • 0026806476 scopus 로고
    • Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction
    • Hirata, K., Kikuchi, A., Sasaki, T. et al. (1992) Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction. J. Biol. Chem. 267, 8719-8722
    • (1992) J. Biol. Chem. , vol.267 , pp. 8719-8722
    • Hirata, K.1    Kikuchi, A.2    Sasaki, T.3
  • 15
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K. and Wennerberg, K. (2004) Rho and Rac take center stage. Cell 116, 167-179
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 16
    • 0034674417 scopus 로고    scopus 로고
    • Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice
    • Chen, Z., Sun, J., Pradines, A., Favre, G., Adnane, J. and Sebti, S. M. (2000) Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice. J. Biol. Chem. 275, 17974-17978
    • (2000) J. Biol. Chem. , vol.275 , pp. 17974-17978
    • Chen, Z.1    Sun, J.2    Pradines, A.3    Favre, G.4    Adnane, J.5    Sebti, S.M.6
  • 17
    • 0034601487 scopus 로고    scopus 로고
    • Genomic analysis of metastasis reveals an essential role for RhoC
    • Clark, E. A., Golub, T. R., Lander, E. S. and Hynes, R. O. (2000) Genomic analysis of metastasis reveals an essential role for RhoC. Nature (London) 406, 532-535
    • (2000) Nature (London) , vol.406 , pp. 532-535
    • Clark, E.A.1    Golub, T.R.2    Lander, E.S.3    Hynes, R.O.4
  • 18
    • 0026778133 scopus 로고
    • The small GTP-hinding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. and Hall, A. (1992) The small GTP-hinding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 19
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83, 1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 20
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A. L. and Hall, A. (2000) Rho GTPases and their effector proteins. Biochem. J. 348, 241-255
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 21
    • 10944244704 scopus 로고    scopus 로고
    • Rho signalling at a glance
    • Schwartz, M. (2004) Rho signalling at a glance. J. Cell Sci. 117, 5457-5458
    • (2004) J. Cell Sci. , vol.117 , pp. 5457-5458
    • Schwartz, M.1
  • 22
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya, S. (1996) The small GTPase Rho: cellular functions and signal transduction. J. Biochem. (Tokyo) 120, 215-228
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 24
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L. and D'Souza-Schorey, C. (1997) Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 25
    • 0027984138 scopus 로고
    • GAPs for Rho-related GTPases
    • Lamarche, N. and Hall, A. (1994) GAPs for Rho-related GTPases. Trends Genet. 10, 436-440
    • (1994) Trends Genet. , vol.10 , pp. 436-440
    • Lamarche, N.1    Hall, A.2
  • 26
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling
    • Olofsson, B. (1999) Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell. Signalling 11, 545-554
    • (1999) Cell. Signalling , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 27
    • 0027437622 scopus 로고
    • Consequences of weak interaction of Rho GDI with the GTP-bound forms of Rho p21 and Rac p21
    • Sasaki, T., Kato, M. and Takai, Y. (1993) Consequences of weak interaction of Rho GDI with the GTP-bound forms of Rho p21 and Rac p21. J. Biol. Chem. 268, 23959-23963
    • (1993) J. Biol. Chem. , vol.268 , pp. 23959-23963
    • Sasaki, T.1    Kato, M.2    Takai, Y.3
  • 28
    • 0036336506 scopus 로고    scopus 로고
    • Inhibition of Rho family GTPases by Rho GDP dissociation inhibitor disrupts cardiac morphogenesis and inhibits cardiomyocyte proliferation
    • Wei, L., Imanaka-Yoshida, K., Wang, L. et al. (2002) Inhibition of Rho family GTPases by Rho GDP dissociation inhibitor disrupts cardiac morphogenesis and inhibits cardiomyocyte proliferation. Development 129, 1705-1714
    • (2002) Development , vol.129 , pp. 1705-1714
    • Wei, L.1    Imanaka-Yoshida, K.2    Wang, L.3
  • 30
    • 0032774587 scopus 로고    scopus 로고
    • Regulation of Rho protein binding to membranes by rhoGDI: Inhibition of releasing activity by physiological ionic conditions
    • Bilodeau, D., Lamy, S., Desrosiers, R. R., Gingras, D. and Beliveau, R. (1999) Regulation of Rho protein binding to membranes by rhoGDI: inhibition of releasing activity by physiological ionic conditions. Biochem. Cell Biol. 77, 59-69
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 59-69
    • Bilodeau, D.1    Lamy, S.2    Desrosiers, R.R.3    Gingras, D.4    Beliveau, R.5
  • 31
    • 0030040750 scopus 로고    scopus 로고
    • Protein kinase a phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes
    • Lang, P., Gesbert, F., Delespine-Carmagnat, M., Stancou, R., Pouchelet, M. and Bertoglio, J. (1996) Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J. 15, 510-519
    • (1996) EMBO J. , vol.15 , pp. 510-519
    • Lang, P.1    Gesbert, F.2    Delespine-Carmagnat, M.3    Stancou, R.4    Pouchelet, M.5    Bertoglio, J.6
  • 32
    • 0037730396 scopus 로고    scopus 로고
    • AMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI
    • Tamma, G., Klussmann, E., Procino, G., Svelto, M., Rosenthal, W. and Valenti, G. (2003) cAMP-induced AQP2 translocation is associated with RhoA inhibition through RhoA phosphorylation and interaction with RhoGDI. J. Cell Sci. 116, 1519-1525
    • (2003) J. Cell Sci. , vol.116 , pp. 1519-1525
    • Tamma, G.1    Klussmann, E.2    Procino, G.3    Svelto, M.4    Rosenthal, W.5    Valenti, G.6
  • 33
    • 0038172667 scopus 로고    scopus 로고
    • PKA inhibits RhoA activation: A protection mechanism against endothelial barrier dysfunction
    • Qiao, J., Huang, F. and Lum, H. (2003) PKA inhibits RhoA activation: a protection mechanism against endothelial barrier dysfunction. Am. J. Physiol. Lung Cell Mol. Physiol. 284, L972-L980
    • (2003) Am. J. Physiol. Lung Cell Mol. Physiol. , vol.284
    • Qiao, J.1    Huang, F.2    Lum, H.3
  • 35
    • 0035668525 scopus 로고    scopus 로고
    • Dbl family guanine nucleotide exchange factors
    • Zheng, Y. (2001) Dbl family guanine nucleotide exchange factors. Trends Biochem. Sci. 26, 724-732
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 724-732
    • Zheng, Y.1
  • 37
    • 0007724488 scopus 로고    scopus 로고
    • The PH superfold: A structural scaffold for multiple functions
    • Blomberg, N., Baraldi, E., Nilges, M. and Saraste, M. (1999) The PH superfold: a structural scaffold for multiple functions. Trends Biochem. Sci. 24, 441-445
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 441-445
    • Blomberg, N.1    Baraldi, E.2    Nilges, M.3    Saraste, M.4
  • 38
    • 8744317101 scopus 로고    scopus 로고
    • Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor
    • Kristelly, R., Gao, G. and Tesmer, J. J. G. (2004) Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor. J. Biol. Chem. 279, 47352-47362
    • (2004) J. Biol. Chem. , vol.279 , pp. 47352-47362
    • Kristelly, R.1    Gao, G.2    Tesmer, J.J.G.3
  • 39
    • 0036733358 scopus 로고    scopus 로고
    • Cellular regulation of RGS proteins: Modulators and integrators of G protein signaling
    • Hollinger, S. and Hepler, J. R. (2002) Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Pharmacol. Rev. 54, 527-559
    • (2002) Pharmacol. Rev. , vol.54 , pp. 527-559
    • Hollinger, S.1    Hepler, J.R.2
  • 40
    • 0242289621 scopus 로고    scopus 로고
    • 13 as key regulatory mediator in signal transduction
    • 13 as key regulatory mediator in signal transduction. Life Sci. 74, 155-161
    • (2003) Life Sci. , vol.74 , pp. 155-161
    • Kurose, H.1
  • 43
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric C proteins to Rho
    • Fukuhara, S., Murga, C., Zohar, M., Igishi, T. and Gutkind, J. S. (1999) A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric C proteins to Rho. J. Biol. Chem. 274, 5868-1879
    • (1999) J. Biol. Chem. , vol.274 , pp. 5868-11879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3    Igishi, T.4    Gutkind, J.S.5
  • 44
    • 16444368009 scopus 로고    scopus 로고
    • 13 mutations that disrupt interaction with p115RhoGEF
    • 13 mutations that disrupt interaction with p115RhoGEF. Oncogene 24, 2155-2165
    • (2005) Oncogene , vol.24 , pp. 2155-2165
    • Grabocka, E.1    Wedegaertner, P.B.2
  • 46
    • 0036261720 scopus 로고    scopus 로고
    • Leukemia-associated Rho guanine nucleotide exchange factor promotes Gaq-coupled activation of RhoA
    • Booden, M. A., Siderovski, D. P. and Der, C. J. (2002) Leukemia-associated Rho guanine nucleotide exchange factor promotes Gaq-coupled activation of RhoA. Mol. Cell. Biol. 22, 4053-4061
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4053-4061
    • Booden, M.A.1    Siderovski, D.P.2    Der, C.J.3
  • 48
    • 0035952680 scopus 로고    scopus 로고
    • RGS-containing RhoGEFs: The missing link between transforming G proteins and Rho?
    • Fukuhara, S., Chikumi, H. and Gutkind, J. S. (2001) RGS-containing RhoGEFs: the missing link between transforming G proteins and Rho? Oncogene 20, 1661-1668
    • (2001) Oncogene , vol.20 , pp. 1661-1668
    • Fukuhara, S.1    Chikumi, H.2    Gutkind, J.S.3
  • 49
    • 0043237427 scopus 로고    scopus 로고
    • Protein kinase Co-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement
    • Holinstat, M., Mehta, D., Kozasa, T., Minshall, R. D. and Malik, A. B. (2003) Protein kinase Co-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement. J. Biol. Chem. 278, 28793-28798
    • (2003) J. Biol. Chem. , vol.278 , pp. 28793-28798
    • Holinstat, M.1    Mehta, D.2    Kozasa, T.3    Minshall, R.D.4    Malik, A.B.5
  • 50
    • 0030759770 scopus 로고    scopus 로고
    • Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
    • Rittinger, K., Walker, P. A., Eccleston, J. F. et al. (1997) Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature (London) 388, 693-697
    • (1997) Nature (London) , vol.388 , pp. 693-697
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3
  • 51
    • 0035018025 scopus 로고    scopus 로고
    • Phosphorylation of p190 on Tyr1105 by c-Src is necessary but not sufficient for EGF-induced actin disassembly in C3H10T1/2 fibroblasts
    • Haskell, M., Nickles, A., Agati, J., Su, L., Dukes, B. and Parsons, S. (2001) Phosphorylation of p190 on Tyr1105 by c-Src is necessary but not sufficient for EGF-induced actin disassembly in C3H10T1/2 fibroblasts. J. Cell Sci. 114, 1699-1708
    • (2001) J. Cell Sci. , vol.114 , pp. 1699-1708
    • Haskell, M.1    Nickles, A.2    Agati, J.3    Su, L.4    Dukes, B.5    Parsons, S.6
  • 52
    • 0028853289 scopus 로고
    • A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities
    • Homma, Y. and Emori, Y. (1995) A dual functional signal mediator showing RhoGAP and phospholipase C-δ stimulating activities. EMBO J. 14, 286-291
    • (1995) EMBO J. , vol.14 , pp. 286-291
    • Homma, Y.1    Emori, Y.2
  • 53
    • 0032478821 scopus 로고    scopus 로고
    • Characterization of graf, the GTPase-activating protein for rho associated with focal adhesion kinase. Phosphorylation and possible regulation by mitogen-activated protein kinase
    • Taylor, J. M., Hildebrand, J. D., Mack, C. P., Cox, M. E. and Parsons, J. T. (1998) Characterization of graf, the GTPase-activating protein for rho associated with focal adhesion kinase. Phosphorylation and possible regulation by mitogen-activated protein kinase. J. Biol. Chem. 273, 8063-8070
    • (1998) J. Biol. Chem. , vol.273 , pp. 8063-8070
    • Taylor, J.M.1    Hildebrand, J.D.2    Mack, C.P.3    Cox, M.E.4    Parsons, J.T.5
  • 54
    • 0035913909 scopus 로고    scopus 로고
    • Regulating axon branch stability: The role of p190 RhoGAP in repressing a retraction signaling pathway
    • Billuart, P., Winter, C. G., Maresh, A., Zhao, X. and Luo, L. (2001) Regulating axon branch stability: the role of p190 RhoGAP in repressing a retraction signaling pathway. Cell 107, 195-207
    • (2001) Cell , vol.107 , pp. 195-207
    • Billuart, P.1    Winter, C.G.2    Maresh, A.3    Zhao, X.4    Luo, L.5
  • 55
    • 0034715885 scopus 로고    scopus 로고
    • Regulation and functions of Rho-associated kinase
    • Amano, M., Fukata, Y. and Kaibuchi, K. (2000) Regulation and functions of Rho-associated kinase. Exp. Cell Res. 261, 44-51
    • (2000) Exp. Cell Res. , vol.261 , pp. 44-51
    • Amano, M.1    Fukata, Y.2    Kaibuchi, K.3
  • 56
    • 0037066777 scopus 로고    scopus 로고
    • Characterization of RhoA-binding kinase ROKα: 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. and Leung, T. (2002) Characterization of RhoA-binding kinase ROKα: implication of the pleckstrin homology domain in ROKα function using region-specific antibodies. J. Biol. Chem. 277, 12680-12688
    • (2002) J. Biol. Chem. , vol.277 , pp. 12680-12688
    • Chen, X.-Q.1    Tan, I.2    Ng, C.H.3    Hall, C.4    Lim, L.5    Leung, T.6
  • 57
    • 1942538405 scopus 로고    scopus 로고
    • Myosin phosphatase: Structure, regulation and function
    • Ito, M., Nakano, T., Erdodi, F. and Hartshorne, D. J. (2004) Myosin phosphatase: structure, regulation and function. Mol. Cell. Biochem. 259, 197-209
    • (2004) Mol. Cell. Biochem. , vol.259 , pp. 197-209
    • Ito, M.1    Nakano, T.2    Erdodi, F.3    Hartshorne, D.J.4
  • 58
    • 0032564320 scopus 로고    scopus 로고
    • Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase
    • Tanaka, J., Ito, M., Feng, J. et al. (1998) Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase. Biochemistry 37, 16697-16703
    • (1998) Biochemistry , vol.37 , pp. 16697-16703
    • Tanaka, J.1    Ito, M.2    Feng, J.3
  • 59
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83, 1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 60
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo, A. P. and Somlyo, A. V. (2000) Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522, 177-185
    • (2000) J. Physiol. , vol.522 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 61
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng, J., Ito, M., Ichikawa, K. et al. (1999) Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274, 37385-37390
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3
  • 62
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura, K., Ito, M., Amano, M. et al. (1996) Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 273, 245-248
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3
  • 64
    • 23744492968 scopus 로고    scopus 로고
    • 2+ sensitization: Rho-associated kinase-mediated phosphorylation of MYPT1 at Thr-855, but not Thr-697
    • 2+ sensitization: Rho-associated kinase-mediated phosphorylation of MYPT1 at Thr-855, but not Thr-697. Biochem. J. 389, 763-774
    • (2005) Biochem. J. , vol.389 , pp. 763-774
    • Wilson, D.P.1    Susnjar, M.2    Kiss, E.3    Sutherland, C.4    Walsh, M.P.5
  • 66
    • 0037063362 scopus 로고    scopus 로고
    • Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
    • Velasco, G., Armstrong, C., Morrice, N., Frame, S. and Cohen, P. (2002) Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin. FEBS Lett. 527, 101-104
    • (2002) FEBS Lett. , vol.527 , pp. 101-104
    • Velasco, G.1    Armstrong, C.2    Morrice, N.3    Frame, S.4    Cohen, P.5
  • 67
    • 0012322071 scopus 로고    scopus 로고
    • 2+ sensitization of smooth muscle contraction through activation of Rho-kinase
    • 2+ sensitization of smooth muscle contraction through activation of Rho-kinase. Pflugers Arch. 441, 596-603
    • (2001) Pflugers Arch. , vol.441 , pp. 596-603
    • Araki, S.1    Ito, M.2    Kureishi, Y.3
  • 69
    • 0141615707 scopus 로고    scopus 로고
    • GTPase regulation getting aRnd Rock and Rho inhibition
    • Chardin, P. (2003) GTPase regulation getting aRnd Rock and Rho inhibition. Curr. Biol. 13, R702-R704
    • (2003) Curr. Biol. , vol.13
    • Chardin, P.1
  • 71
  • 73
    • 0031920581 scopus 로고    scopus 로고
    • Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle
    • Li, L., Eto, M., Lee, M. R., Morita, F., Yazawa, M. and Kitazawa, T. (1998) Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. J. Physiol. 508, 871-881
    • (1998) J. Physiol. , vol.508 , pp. 871-881
    • Li, L.1    Eto, M.2    Lee, M.R.3    Morita, F.4    Yazawa, M.5    Kitazawa, T.6
  • 74
    • 0035955681 scopus 로고    scopus 로고
    • Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17 kDa
    • Hayashi, Y., Senba, S., Yazawa, M., Brautigan, D. L. and Eto, M. (2001) Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17 kDa. J. Biol. Chem. 276, 39858-39863
    • (2001) J. Biol. Chem. , vol.276 , pp. 39858-39863
    • Hayashi, Y.1    Senba, S.2    Yazawa, M.3    Brautigan, D.L.4    Eto, M.5
  • 75
    • 0030795828 scopus 로고    scopus 로고
    • Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: Its specific localization in smooth muscle
    • Eto, M., Senba, S., Morita, F. and Yazawa, M. (1997) Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: its specific localization in smooth muscle. FEBS Lett. 410, 356-360
    • (1997) FEBS Lett. , vol.410 , pp. 356-360
    • Eto, M.1    Senba, S.2    Morita, F.3    Yazawa, M.4
  • 76
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto, M., Ohmori, T., Suzuki, M., Furuya, K. and Morita, F. (1995) A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J. Biochem. (Tokyo) 118, 1104-1107
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 77
    • 21044445509 scopus 로고    scopus 로고
    • Phospho-pivot modeling predicts specific interactions of protein phosphatase-1 with a phospho-inhibitor protein CPI-17
    • Matsuzawa, F., Aikawa, S.-i., Ohki, S.-y. and Eto, M. (2005) Phospho-pivot modeling predicts specific interactions of protein phosphatase-1 with a phospho-inhibitor protein CPI-17. J. Biochem. (Tokyo) 137, 633-641
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 633-641
    • Matsuzawa, F.1    Aikawa, S.-I.2    Ohki, S.-Y.3    Eto, M.4
  • 78
    • 0035800812 scopus 로고    scopus 로고
    • Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase Cα and δ isoforms
    • Eto, M., Kitazawa, T., Yazawa, M., Mukai, H., Ono, Y. and Brautigan, D. L. (2001) Histamine-induced vasoconstriction involves phosphorylation of a specific inhibitor protein for myosin phosphatase by protein kinase Cα and δ isoforms. J. Biol. Chem. 276, 29072-29078
    • (2001) J. Biol. Chem. , vol.276 , pp. 29072-29078
    • Eto, M.1    Kitazawa, T.2    Yazawa, M.3    Mukai, H.4    Ono, Y.5    Brautigan, D.L.6
  • 79
    • 0034705765 scopus 로고    scopus 로고
    • Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase
    • Koyama, M., Ito, M., Feng, J., Seko, T., Shiraki, K., Takase, K., Hartshorne, D. J. and Nakano, T. (2000) Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 475, 197-200
    • (2000) FEBS Lett. , vol.475 , pp. 197-200
    • Koyama, M.1    Ito, M.2    Feng, J.3    Seko, T.4    Shiraki, K.5    Takase, K.6    Hartshorne, D.J.7    Nakano, T.8
  • 80
    • 21044460169 scopus 로고    scopus 로고
    • RhoA/Rho kinase mediates thrombin- and U-46619-induced phosphorylation of a myosin phosphatase inhibitor, CPI-17, in vascular smooth muscle cells
    • Pang, H., Guo, Z., Su, W., Xie, Z., Eto, M. and Gong, M. C. (2005) RhoA/Rho kinase mediates thrombin- and U-46619-induced phosphorylation of a myosin phosphatase inhibitor, CPI-17, in vascular smooth muscle cells. Am. J. Physiol. Cell Physiol. 289, C352-C360
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Pang, H.1    Guo, Z.2    Su, W.3    Xie, Z.4    Eto, M.5    Gong, M.C.6
  • 81
    • 0036181829 scopus 로고    scopus 로고
    • Nitric oxide induces dilation of rat aorta via inhibition of rho-kinase signaling
    • Chitaley, K. and Webb, R. C. (2002) Nitric oxide induces dilation of rat aorta via inhibition of rho-kinase signaling. Hypertension 39, 438-442
    • (2002) Hypertension , vol.39 , pp. 438-442
    • Chitaley, K.1    Webb, R.C.2
  • 82
    • 0036784012 scopus 로고    scopus 로고
    • Acute and chronic NOS inhibition enhances α2-adrenoreceptor- stimulated RhoA and Rho kinase in rat aorta
    • Carter, R. W., Begaye, M. and Kanagy, N. L. (2002) Acute and chronic NOS inhibition enhances α2-adrenoreceptor-stimulated RhoA and Rho kinase in rat aorta. Am. J. Physiol. Heart Circ. Physiol. 283, H1361-H1369
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.283
    • Carter, R.W.1    Begaye, M.2    Kanagy, N.L.3
  • 84
    • 0034810237 scopus 로고    scopus 로고
    • cGMP-dependent protein kinase phosphorylates and inactivates RhoA
    • Sawada, N., Itoh, H., Yamashita, J. et al. (2001) cGMP-dependent protein kinase phosphorylates and inactivates RhoA. Biochem. Biophys. Res. Commun. 280, 798-805
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 798-805
    • Sawada, N.1    Itoh, H.2    Yamashita, J.3
  • 85
    • 0038660670 scopus 로고    scopus 로고
    • RhoA expression is controlled by nitric oxide through cGMP-dependent protein kinase activation
    • Sauzeau, V., Rolli-Derkinderen, M., Marionneau, C., Loirand, G. and Pacaud, P. (2003) RhoA expression is controlled by nitric oxide through cGMP-dependent protein kinase activation. J. Biol. Chem. 278, 9472-9480
    • (2003) J. Biol. Chem. , vol.278 , pp. 9472-9480
    • Sauzeau, V.1    Rolli-Derkinderen, M.2    Marionneau, C.3    Loirand, G.4    Pacaud, P.5
  • 86
    • 0036892061 scopus 로고    scopus 로고
    • Rho GTPase/Rho kinase negatively regulates endothelial nitric oxide synthase phosphorylation through the inhibition of protein kinase B/Akt in human endothelial cells
    • Ming, X. F., Viswambharan, H., Barandier, C. et al. (2002) Rho GTPase/Rho kinase negatively regulates endothelial nitric oxide synthase phosphorylation through the inhibition of protein kinase B/Akt in human endothelial cells. Mol. Cell. Biol. 22, 8467-8477
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8467-8477
    • Ming, X.F.1    Viswambharan, H.2    Barandier, C.3
  • 87
    • 12344323503 scopus 로고    scopus 로고
    • Cardioprotective mechanisms of Rho-kinase inhibition associated with eNOS and oxidative stress-LOX-1 pathway in Dahl salt-sensitive hypertensive rats
    • Mita, S., Kobayashi, N., Yoshida, K., Nakano, S. and Matsuoka, H. (2005) Cardioprotective mechanisms of Rho-kinase inhibition associated with eNOS and oxidative stress-LOX-1 pathway in Dahl salt-sensitive hypertensive rats. J. Hypertens. 23, 87-96
    • (2005) J. Hypertens. , vol.23 , pp. 87-96
    • Mita, S.1    Kobayashi, N.2    Yoshida, K.3    Nakano, S.4    Matsuoka, H.5
  • 88
    • 0041707712 scopus 로고    scopus 로고
    • Entrapment of Rho ADP-ribosylated by clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex
    • Genth, H., Gerhard, R., Maeda, A. et al. (2003) Entrapment of Rho ADP-ribosylated by clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor-1 complex. J. Biol. Chem. 278, 28523-28527
    • (2003) J. Biol. Chem. , vol.278 , pp. 28523-28527
    • Genth, H.1    Gerhard, R.2    Maeda, A.3
  • 89
    • 0032515914 scopus 로고    scopus 로고
    • Glucosylation and ADP ribosylation of rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • Sehr, P., Joseph, G., Genth, H., Just, I., Pick, F., and Aktories, K. (1998) Glucosylation and ADP ribosylation of rho proteins: effects on nucleotide binding, GTPase activity, and effector coupling. Biochemistry 37, 5296-5304
    • (1998) Biochemistry , vol.37 , pp. 5296-5304
    • Sehr, P.1    Joseph, G.2    Genth, H.3    Just, I.4    Pick, F.5    Aktories, K.6
  • 91
    • 0030721443 scopus 로고    scopus 로고
    • Inhibition of RhoA translocation and calcium sensitization by in vivo ADP-ribosylation with the chimeric toxin DC3B
    • Fujihara, H., Walker, L. A., Gong, M. C. et al. (1997) Inhibition of RhoA translocation and calcium sensitization by in vivo ADP-ribosylation with the chimeric toxin DC3B. Mol. Biol. Cell 8, 2437-2447
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2437-2447
    • Fujihara, H.1    Walker, L.A.2    Gong, M.C.3
  • 92
    • 0033924259 scopus 로고    scopus 로고
    • Rho GTPases as targets of bacterial protein toxins
    • Aktories, K., Schmidt, G. and Just, I. (2000) Rho GTPases as targets of bacterial protein toxins. Biol. Chem. 381, 421-426
    • (2000) Biol. Chem. , vol.381 , pp. 421-426
    • Aktories, K.1    Schmidt, G.2    Just, I.3
  • 93
    • 0033427140 scopus 로고    scopus 로고
    • Bacterial toxins inhibiting or activating small GTP-binding proteins
    • Boquet, P. (1999) Bacterial toxins inhibiting or activating small GTP-binding proteins. Ann. NY Acad. Sci. 886, 83-90
    • (1999) Ann. NY Acad. Sci. , vol.886 , pp. 83-90
    • Boquet, P.1
  • 94
    • 0037386736 scopus 로고    scopus 로고
    • A new turn in Rho GTPase activation by Escherichia coli cytotoxic necrotizing factors
    • Aktories, K. and Schmidt, G. (2003) A new turn in Rho GTPase activation by Escherichia coli cytotoxic necrotizing factors. Trends Microbiol. 11, 152-155
    • (2003) Trends Microbiol. , vol.11 , pp. 152-155
    • Aktories, K.1    Schmidt, G.2
  • 95
    • 1942469488 scopus 로고    scopus 로고
    • The Yersinia pseudotuberculosis cytotoxic necrotizing factor (CNFY) selectively activates RhoA
    • Hoffmann, C., Pop, M., Leemhuis, J., Schirmer, J., Aktories, K. and Schmidt, G. (2004) The Yersinia pseudotuberculosis cytotoxic necrotizing factor (CNFY) selectively activates RhoA. J. Biol. Chem. 279, 16026-16032
    • (2004) J. Biol. Chem. , vol.279 , pp. 16026-16032
    • Hoffmann, C.1    Pop, M.2    Leemhuis, J.3    Schirmer, J.4    Aktories, K.5    Schmidt, G.6
  • 96
    • 0034017744 scopus 로고    scopus 로고
    • Pharmacological properties of Y-27632, a specific inhibitor of Rho-associated kinases
    • Ishizaki, T., Uehata, M., Tamechika, I. et al. (2000) Pharmacological properties of Y-27632, a specific inhibitor of Rho-associated kinases. Mol. Pharmacol. 57, 976-983
    • (2000) Mol. Pharmacol. , vol.57 , pp. 976-983
    • Ishizaki, T.1    Uehata, M.2    Tamechika, I.3
  • 97
    • 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. et al. (1997) Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature (London) 389, 990-994
    • (1997) Nature (London) , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3
  • 99
    • 0037704150 scopus 로고    scopus 로고
    • Inhibition of high K+-induced contraction by the ROCKs inhibitor Y-27632 in vascular smooth muscle: Possible involvement of ROCKs in a signal transduction pathway
    • Sakamoto, K., Hori, M., Izumi, M. et al. (2003) Inhibition of high K+-induced contraction by the ROCKs inhibitor Y-27632 in vascular smooth muscle: possible involvement of ROCKs in a signal transduction pathway. J. Pharmacol. Sci. 92, 56-69
    • (2003) J. Pharmacol. Sci. , vol.92 , pp. 56-69
    • Sakamoto, K.1    Hori, M.2    Izumi, M.3
  • 100
    • 0033955903 scopus 로고    scopus 로고
    • Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells
    • Nagumo, H., Sasaki, Y., Ono, Y., Okamoto, H., Seto, M. and Takuwa, Y. (2000) Rho kinase inhibitor HA-1077 prevents Rho-mediated myosin phosphatase inhibition in smooth muscle cells. Am. J. Physiol. Cell Physiol. 278, C57-C65
    • (2000) Am. J. Physiol. Cell Physiol. , vol.278
    • Nagumo, H.1    Sasaki, Y.2    Ono, Y.3    Okamoto, H.4    Seto, M.5    Takuwa, Y.6
  • 101
    • 0035990918 scopus 로고    scopus 로고
    • The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4- methyl-5-isoquinoline)sulfonyl]-homopiperazine as a probing molecule for Rho-kinase-involved pathway
    • Sasaki, Y., Suzuki, M. and Hidaka, H. (2002) The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]- homopiperazine as a probing molecule for Rho-kinase-involved pathway. Pharmacol. Ther. 93, 225-232
    • (2002) Pharmacol. Ther. , vol.93 , pp. 225-232
    • Sasaki, Y.1    Suzuki, M.2    Hidaka, H.3
  • 102
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases
    • Feig, L. A. (1999) Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat. Cell Biol. 1, E25-E27
    • (1999) Nat. Cell Biol. , vol.1
    • Feig, L.A.1
  • 103
    • 0036156469 scopus 로고    scopus 로고
    • Post-transcriptional down-regulation of ROCK1/Rho-kinase through an MEK-dependent pathway leads to cytoskeleton disruption in Ras-transformed fibroblasts
    • Pawlak, G. and Helfman, D. M. (2002) Post-transcriptional down-regulation of ROCK1/Rho-kinase through an MEK-dependent pathway leads to cytoskeleton disruption in Ras-transformed fibroblasts. Mol. Biol. Cell 13, 336-347
    • (2002) Mol. Biol. Cell , vol.13 , pp. 336-347
    • Pawlak, G.1    Helfman, D.M.2
  • 104
    • 0035049575 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of dominant-negative Rho-kinase induces a regression of coronary arteriosclerosis in pigs in vivo
    • Morishige, K., Shimokawa, H., Eto, Y. et al. (2001) Adenovirus-mediated transfer of dominant-negative Rho-kinase induces a regression of coronary arteriosclerosis in pigs in vivo. Arterioscler., Thromb., Vasc. Biol. 21, 548-554
    • (2001) Arterioscler., Thromb., Vasc. Biol. , vol.21 , pp. 548-554
    • Morishige, K.1    Shimokawa, H.2    Eto, Y.3
  • 105
    • 19944432271 scopus 로고    scopus 로고
    • Anti-RhoA and Anti-RhoC siRNAs inhibit the proliferation and invasiveness of MDA-MB-231 breast cancer cells in vitro and in vivo
    • Pille, J.-Y., Denoyelle, C., Varet, J. et al. (2005) Anti-RhoA and Anti-RhoC siRNAs inhibit the proliferation and invasiveness of MDA-MB-231 breast cancer cells in vitro and in vivo. Mol. Ther. 11, 267-274
    • (2005) Mol. Ther. , vol.11 , pp. 267-274
    • Pille, J.-Y.1    Denoyelle, C.2    Varet, J.3
  • 106
    • 0037384873 scopus 로고    scopus 로고
    • EphrinA1 inactivates integrin-mediated vascular smooth muscle cell spreading via the Rac/PAK pathway
    • Deroanne, C., Vouret-Craviari, V., Wang, B. and Pouyssegur, J. (2003) EphrinA1 inactivates integrin-mediated vascular smooth muscle cell spreading via the Rac/PAK pathway. J. Cell Sci. 116, 1367-1376
    • (2003) J. Cell Sci. , vol.116 , pp. 1367-1376
    • Deroanne, C.1    Vouret-Craviari, V.2    Wang, B.3    Pouyssegur, J.4
  • 107
    • 0035134310 scopus 로고    scopus 로고
    • Antagonism of Rho-kinase stimulates rat penile erection via a nitric oxide-independent pathway
    • Chitaley, K., Wingard, C. J., Webb, R. C. et al. (2001) Antagonism of Rho-kinase stimulates rat penile erection via a nitric oxide-independent pathway. Nat. Med. 7, 119-122
    • (2001) Nat. Med. , vol.7 , pp. 119-122
    • Chitaley, K.1    Wingard, C.J.2    Webb, R.C.3
  • 110
    • 0036430608 scopus 로고    scopus 로고
    • Adeno-associated viral gene transfer of dominant negative RhoA enhances erectile function in rats
    • Chitaley, K., Bivalacqua, T. J., Champion, H. C. et al. (2002) Adeno-associated viral gene transfer of dominant negative RhoA enhances erectile function in rats. Biochem. Biophys. Res. Commun. 298, 427-432
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 427-432
    • Chitaley, K.1    Bivalacqua, T.J.2    Champion, H.C.3
  • 111
    • 0034849563 scopus 로고    scopus 로고
    • Pharmacology of penile erection
    • Andersson, K.-E. (2001) Pharmacology of penile erection. Pharmacol. Rev. 53, 417-450
    • (2001) Pharmacol. Rev. , vol.53 , pp. 417-450
    • Andersson, K.-E.1
  • 112
    • 0037397573 scopus 로고    scopus 로고
    • Inhibition of the tonic contraction in the treatment of erectile dysfunction
    • Jin, L., Under, A. E., Mills, T. M. and Webb, R. C. (2003) Inhibition of the tonic contraction in the treatment of erectile dysfunction. Fxpert Opin. Then Targets 7, 265-276
    • (2003) Fxpert Opin. Then Targets , vol.7 , pp. 265-276
    • Jin, L.1    Under, A.E.2    Mills, T.M.3    Webb, R.C.4
  • 113
    • 0034955766 scopus 로고    scopus 로고
    • Y-27632, an inhibitor of Rho-kinase, antagonizes noradrenergic contractions in the rabbit and human penile corpus cavernosum
    • Rees, R. W., Ralph, D. J., Royle, M., Moncada, S. and Cellek, S. (2001) Y-27632, an inhibitor of Rho-kinase, antagonizes noradrenergic contractions in the rabbit and human penile corpus cavernosum. Br. J. Pharmacol. 133, 455-458
    • (2001) Br. J. Pharmacol. , vol.133 , pp. 455-458
    • Rees, R.W.1    Ralph, D.J.2    Royle, M.3    Moncada, S.4    Cellek, S.5
  • 115
    • 0034863248 scopus 로고    scopus 로고
    • Effect of Rho-kinase inhibition on vasoconstriction in the penile circulation
    • Mills, T. M., Chitaley, K., Wingard, C. J., Lewis, R. W. and Webb, R. C. (2001) Effect of Rho-kinase inhibition on vasoconstriction in the penile circulation. J. Appl. Physiol. 91, 1269-1273
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1269-1273
    • Mills, T.M.1    Chitaley, K.2    Wingard, C.J.3    Lewis, R.W.4    Webb, R.C.5
  • 117
    • 4644253670 scopus 로고    scopus 로고
    • Role of PKCα and PKCι in phenylephrine-induced contraction of rat corpora cavernosa
    • Husain, S., Young, D. and Wingard, C. J. (2004) Role of PKCα and PKCι in phenylephrine-induced contraction of rat corpora cavernosa. Int. J. Impot. Res. 16, 325-333
    • (2004) Int. J. Impot. Res. , vol.16 , pp. 325-333
    • Husain, S.1    Young, D.2    Wingard, C.J.3
  • 118
    • 0037192607 scopus 로고    scopus 로고
    • Nitric oxide inhibits RhoA/Rho-kinase signaling to cause penile erection
    • Mills, T. M., Chitaley, K., Lewis, R. W. and Webb, R. C. (2002) Nitric oxide inhibits RhoA/Rho-kinase signaling to cause penile erection. Eur. J. Pharmacol. 439, 173-174
    • (2002) Eur. J. Pharmacol. , vol.439 , pp. 173-174
    • Mills, T.M.1    Chitaley, K.2    Lewis, R.W.3    Webb, R.C.4
  • 119
    • 25644450347 scopus 로고    scopus 로고
    • Pro-erectile effects of the Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4- methyl-5-isoquinolinyl)sulfonyl] homopiperazine (H-1152) in the rat penis
    • Teixeira, C. E., Ying, Z. and Webb, R. C. (2005) Pro-erectile effects of the Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinolinyl)sulfonyl] homopiperazine (H-1152) in the rat penis. J. Pharmacol. Exp. Ther. 315, 155-162
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 155-162
    • Teixeira, C.E.1    Ying, Z.2    Webb, R.C.3
  • 120
    • 2942678702 scopus 로고    scopus 로고
    • RhoA/Rho-kinase suppresses endothelial nitric oxide synthase in the penis: A mechanism for diabetes-associated erectile dysfunction
    • Bivalacqua, T. J., Champion, H. C., Usta, M. F. et al. (2004) RhoA/Rho-kinase suppresses endothelial nitric oxide synthase in the penis: a mechanism for diabetes-associated erectile dysfunction. Proc. Natl. Acad. Sci. U.S.A. 101, 9121-9126
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9121-9126
    • Bivalacqua, T.J.1    Champion, H.C.2    Usta, M.F.3
  • 122
    • 0033822704 scopus 로고    scopus 로고
    • Hypertension is associated with severe erectile dysfunction
    • Burchardt, M., Burchardt, T., Baer, L. et al. (2000) Hypertension is associated with severe erectile dysfunction. J. Urol. 164, 1188-1191
    • (2000) J. Urol. , vol.164 , pp. 1188-1191
    • Burchardt, M.1    Burchardt, T.2    Baer, L.3
  • 123
    • 2542438558 scopus 로고    scopus 로고
    • The multinational Men's Attitudes to Life Events and Sexuality (MALES) study: I. Prevalence of erectile dysfunction and related health concerns in the general population
    • Rosen, R. C., Fisher, W. A., Eardley, I., Niederberger, C., Nadel, A. and Sand, M. (2004) The multinational Men's Attitudes to Life Events and Sexuality (MALES) study: I. Prevalence of erectile dysfunction and related health concerns in the general population. Curr. Med. Res. Opin. 20, 607-617
    • (2004) Curr. Med. Res. Opin. , vol.20 , pp. 607-617
    • Rosen, R.C.1    Fisher, W.A.2    Eardley, I.3    Niederberger, C.4    Nadel, A.5    Sand, M.6
  • 126
    • 0033063676 scopus 로고    scopus 로고
    • The penis is not protected: In hypertension there are vascular changes in the penis which are similar to those in other vascular beds
    • Okabe, H., Hale, T. M., Kumon, H., Heaton, J. P. and Adams, M. A. (1999) The penis is not protected: in hypertension there are vascular changes in the penis which are similar to those in other vascular beds. Int. J. Impot. Res. 11, 133-140
    • (1999) Int. J. Impot. Res. , vol.11 , pp. 133-140
    • Okabe, H.1    Hale, T.M.2    Kumon, H.3    Heaton, J.P.4    Adams, M.A.5
  • 127
    • 0035674453 scopus 로고    scopus 로고
    • Decreased penile erection in DOCA-salt and stroke prone-spontaneously hypertensive rats
    • Chitaley, K., Webb, R. C., Dorrance, A. M. and Mills, T. M. (2001) Decreased penile erection in DOCA-salt and stroke prone-spontaneously hypertensive rats. Int. J. Impot. Res. 13 (Suppl. 5), S16-S20
    • (2001) Int. J. Impot. Res. , vol.13 , Issue.SUPPL. 5
    • Chitaley, K.1    Webb, R.C.2    Dorrance, A.M.3    Mills, T.M.4
  • 128
    • 2342621539 scopus 로고    scopus 로고
    • Phosphodiesterase-5 inhibition synergizes rho-kinase antagonism and enhances erectile response in male hypertensive rats
    • Wilkes, N., White, S., Stein, P., Bernie, J. and Rajasekaran, M. (2004) Phosphodiesterase-5 inhibition synergizes rho-kinase antagonism and enhances erectile response in male hypertensive rats. Int. J. Impot. Res. 16, 187-194
    • (2004) Int. J. Impot. Res. , vol.16 , pp. 187-194
    • Wilkes, N.1    White, S.2    Stein, P.3    Bernie, J.4    Rajasekaran, M.5
  • 129
    • 0037301102 scopus 로고    scopus 로고
    • Increased contractility of diabetic rabbit corpora smooth muscle in response to endothelin is mediated via Rho-kinase β
    • Chang, S., Hypolite, J. A., Changolkar, A., Wein, A. J., Chacko, S. and DiSanto, M. E. (2003) Increased contractility of diabetic rabbit corpora smooth muscle in response to endothelin is mediated via Rho-kinase β. Int. J. Impot. Res. 15, 53-62
    • (2003) Int. J. Impot. Res. , vol.15 , pp. 53-62
    • Chang, S.1    Hypolite, J.A.2    Changolkar, A.3    Wein, A.J.4    Chacko, S.5    DiSanto, M.E.6
  • 130
    • 0029005253 scopus 로고
    • Endothelin-1 as a putative modulator of erectile dysfunction: I. Characteristics of contraction of isolated corporal tissue strips
    • Christ, G. J., Lerner, S. E., Kim, D. C. and Melman, A. (1995) Endothelin-1 as a putative modulator of erectile dysfunction: I. Characteristics of contraction of isolated corporal tissue strips. J. Urol. 153, 1998-2003
    • (1995) J. Urol. , vol.153 , pp. 1998-2003
    • Christ, G.J.1    Lerner, S.E.2    Kim, D.C.3    Melman, A.4
  • 131
    • 0142122880 scopus 로고    scopus 로고
    • Effects of the Rho-kinase inhibitors, Y-27632 and fasudil, on the corpus cavernosum from diabetic mice
    • Buyukafsar, K. and Un, I. (2003) Effects of the Rho-kinase inhibitors, Y-27632 and fasudil, on the corpus cavernosum from diabetic mice. Eur. J. Pharmacol. 472, 235-238
    • (2003) Eur. J. Pharmacol. , vol.472 , pp. 235-238
    • Buyukafsar, K.1    Un, I.2
  • 132
    • 0033765780 scopus 로고    scopus 로고
    • Regulation of myosin-bound protein phosphatase by insulin in vascular smooth muscle cells: Evaluation of the role of Rho kinase and phosphatidylinositol-3-kinase-dependent signaling pathways
    • Begum, N., Duddy, N., Sandu, O., Reinzie, J. and Ragolia, L. (2000) Regulation of myosin-bound protein phosphatase by insulin in vascular smooth muscle cells: evaluation of the role of Rho kinase and phosphatidylinositol-3- kinase-dependent signaling pathways. Mol. Endocrinol. 14, 1365-1376
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1365-1376
    • Begum, N.1    Duddy, N.2    Sandu, O.3    Reinzie, J.4    Ragolia, L.5
  • 133
    • 0033661262 scopus 로고    scopus 로고
    • Diabetes in the Goto-Kakizaki rat is accompanied by impaired insulin-mediated myosin-bound phosphatase activation and vascular smooth muscle cell relaxation
    • Sandu, O., Ragolia, L. and Begum, N. (2000) Diabetes in the Goto-Kakizaki rat is accompanied by impaired insulin-mediated myosin-bound phosphatase activation and vascular smooth muscle cell relaxation. Diabetes 49, 2178-2189
    • (2000) Diabetes , vol.49 , pp. 2178-2189
    • Sandu, O.1    Ragolia, L.2    Begum, N.3
  • 134
    • 11244337568 scopus 로고    scopus 로고
    • Testosterone therapy in erectile dysfunction
    • Shabsigh, R. (2004) Testosterone therapy in erectile dysfunction. Aging Male 7, 312-318
    • (2004) Aging Male , vol.7 , pp. 312-318
    • Shabsigh, R.1
  • 135
    • 4243091823 scopus 로고    scopus 로고
    • Androgen replacement in men with hypogonadism and erectile dysfunction
    • Albrecht-Betancourt, M., Hijazi, R. A. and Cunningham, G. R. (2004) Androgen replacement in men with hypogonadism and erectile dysfunction. Endocrine 23, 143-148
    • (2004) Endocrine , vol.23 , pp. 143-148
    • Albrecht-Betancourt, M.1    Hijazi, R.A.2    Cunningham, G.R.3
  • 136
    • 0032880551 scopus 로고    scopus 로고
    • Androgenic maintenance of the erectile response in the rat
    • Mills, T. M., Dai, Y., Stopper, V. S. and Lewis, R. W. (1999) Androgenic maintenance of the erectile response in the rat. Steroids 64, 605-609
    • (1999) Steroids , vol.64 , pp. 605-609
    • Mills, T.M.1    Dai, Y.2    Stopper, V.S.3    Lewis, R.W.4
  • 138
    • 3042702873 scopus 로고    scopus 로고
    • Topical application of a Rho-kinase inhibitor in rats causes penile erection
    • Dai, Y., Chitaley, K., Webb, R. C., Lewis, R. W. and Mills, T. M. (2004) Topical application of a Rho-kinase inhibitor in rats causes penile erection. Int. J. Impot. Res. 16, 294-298
    • (2004) Int. J. Impot. Res. , vol.16 , pp. 294-298
    • Dai, Y.1    Chitaley, K.2    Webb, R.C.3    Lewis, R.W.4    Mills, T.M.5
  • 139
    • 0028880076 scopus 로고
    • Restoration of normal adult penile erectile response in aged rats by long-term treatment with androgens
    • Garban, H., Marquez, D., Cai, L., Rajfer, J. and Gonzalez-Cadavid, N. (1995) Restoration of normal adult penile erectile response in aged rats by long-term treatment with androgens. Biol. Reprod. 53, 1365-1372
    • (1995) Biol. Reprod. , vol.53 , pp. 1365-1372
    • Garban, H.1    Marquez, D.2    Cai, L.3    Rajfer, J.4    Gonzalez-Cadavid, N.5
  • 140
    • 0031013228 scopus 로고    scopus 로고
    • Age decreases nitric oxide synthase-containing nerve fibers in the rat penis
    • Carrier, S., Nagaraju, P., Morgan, D. M., Baba, K., Nunes, L. and Lue, T. F. (1997) Age decreases nitric oxide synthase-containing nerve fibers in the rat penis. J. Urol. 157, 1088-1092
    • (1997) J. Urol. , vol.157 , pp. 1088-1092
    • Carrier, S.1    Nagaraju, P.2    Morgan, D.M.3    Baba, K.4    Nunes, L.5    Lue, T.F.6
  • 141
    • 0036221668 scopus 로고    scopus 로고
    • Altered growth factor expression in the aging penis: The Brown-Norway rat model
    • Rajasekaran, M., Kasyan, A., Jain, A., Kim, S.-W. and Monga, M. (2002) Altered growth factor expression in the aging penis: the Brown-Norway rat model. J. Androl. 23, 393-399
    • (2002) J. Androl. , vol.23 , pp. 393-399
    • Rajasekaran, M.1    Kasyan, A.2    Jain, A.3    Kim, S.-W.4    Monga, M.5
  • 144
    • 14344255882 scopus 로고    scopus 로고
    • Rho-kinase inhibition improves erectile function in aging male Brown-Norway rats
    • Rajasekaran, M., White, S., Baquir, A. and Wilkes, N. (2005) Rho-kinase inhibition improves erectile function in aging male Brown-Norway rats. J. Androl. 26, 182-188
    • (2005) J. Androl. , vol.26 , pp. 182-188
    • Rajasekaran, M.1    White, S.2    Baquir, A.3    Wilkes, N.4
  • 145
    • 32644433302 scopus 로고    scopus 로고
    • Elevated RhoA/Rho-kinase activity in the aged rat penis: Mechanism for age-associated erectile dysfunction
    • in the press
    • Jin, L., Liu, T., Lagoda, G. A., Champion, H. C., Bivalacqua, T. J. and Burnett, A. L. (2005) Elevated RhoA/Rho-kinase activity in the aged rat penis: mechanism for age-associated erectile dysfunction. FASEB J., in the press
    • (2005) FASEB J.
    • Jin, L.1    Liu, T.2    Lagoda, G.A.3    Champion, H.C.4    Bivalacqua, T.J.5    Burnett, A.L.6
  • 146
    • 0037275707 scopus 로고    scopus 로고
    • The Rho-kinase inhibitor Y-27632 and the soluble guanylyl cyclase activator BAY41-B2272 relax rabbit vaginal wall and clitoral corpus cavernosum
    • Cellek, S. (2003) The Rho-kinase inhibitor Y-27632 and the soluble guanylyl cyclase activator BAY41-B2272 relax rabbit vaginal wall and clitoral corpus cavernosum. Br. J. Pharmacol. 138, 287-290
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 287-290
    • Cellek, S.1
  • 147
    • 0036937881 scopus 로고    scopus 로고
    • Role of rho-kinase activity in angiotensin II-mduced contraction of rabbit clitoral cavernosum smooth muscle
    • Park, J. K., Lee, S. O., Kim, Y. G., Kim, S. H., Koh, G. Y. and Cho, K. W. (2002) Role of rho-kinase activity in angiotensin II-mduced contraction of rabbit clitoral cavernosum smooth muscle. Int. J. Impot. Res. 14, 472-477
    • (2002) Int. J. Impot. Res. , vol.14 , pp. 472-477
    • Park, J.K.1    Lee, S.O.2    Kim, Y.G.3    Kim, S.H.4    Koh, G.Y.5    Cho, K.W.6
  • 148
    • 18044396920 scopus 로고    scopus 로고
    • Contractile properties of the cultured vascular smooth muscle cells: The crucial role played by RhoA in the regulation of contractility
    • Bi, D., Nishimura, J., Niiro, N., Hirano, K. and Kanaide, H. (2005) Contractile properties of the cultured vascular smooth muscle cells: the crucial role played by RhoA in the regulation of contractility. Circ. Res. 96, 890-897
    • (2005) Circ. Res. , vol.96 , pp. 890-897
    • Bi, D.1    Nishimura, J.2    Niiro, N.3    Hirano, K.4    Kanaide, H.5
  • 149
    • 18044366013 scopus 로고    scopus 로고
    • 2+ sensitization and the regulation of contractility in rat anococcygeus and retractor penis muscle
    • 2+ sensitization and the regulation of contractility in rat anococcygeus and retractor penis muscle. Biochem. Pharmacol. 69, 1483-1492
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1483-1492
    • Teixeira, C.E.1    Jin, L.2    Ying, Z.3    Palmer, T.4    Webb, R.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.