메뉴 건너뛰기




Volumn 51, Issue 6, 2011, Pages 988-996

Ablation of p21-activated kinase-1 in mice promotes isoproterenol-induced cardiac hypertrophy in association with activation of Erk1/2 and inhibition of protein phosphatase 2A

Author keywords

Mitogen activated protein kinases; Myocardial hypertrophy; P38 MAPK; Pak 1; Troponin I

Indexed keywords

ADENOVIRUS VECTOR; ENZYME INHIBITOR; ISOPRENALINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; P21 ACTIVATED KINASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A;

EID: 80055121231     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2011.09.016     Document Type: Article
Times cited : (49)

References (38)
  • 1
    • 1042279545 scopus 로고    scopus 로고
    • Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes
    • Ke Y., Wang L., Pyle W.G., de Tombe P.P., Solaro R.J. Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes. Circ Res 2004, 94:194-200.
    • (2004) Circ Res , vol.94 , pp. 194-200
    • Ke, Y.1    Wang, L.2    Pyle, W.G.3    de Tombe, P.P.4    Solaro, R.J.5
  • 2
    • 34248364400 scopus 로고    scopus 로고
    • Regulation of L-type calcium channel and delayed rectifier potassium channel activity by p21-activated kinase-1 in guinea pig sinoatrial node pacemaker cells
    • Ke Y., Lei M., Collins T.P., Rakovic S., Mattick P.A., Yamasaki M., et al. Regulation of L-type calcium channel and delayed rectifier potassium channel activity by p21-activated kinase-1 in guinea pig sinoatrial node pacemaker cells. Circ Res 2007, 100:1317-1327.
    • (2007) Circ Res , vol.100 , pp. 1317-1327
    • Ke, Y.1    Lei, M.2    Collins, T.P.3    Rakovic, S.4    Mattick, P.A.5    Yamasaki, M.6
  • 3
    • 58349095764 scopus 로고    scopus 로고
    • Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes
    • Sheehan K.A., Ke Y., Wolska B.M., Solaro R.J. Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes. Am J Physiol Cell Physiol 2009, 296:C47-C58.
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Sheehan, K.A.1    Ke, Y.2    Wolska, B.M.3    Solaro, R.J.4
  • 4
    • 77949669882 scopus 로고    scopus 로고
    • Novel bradykinin signaling in adult rat cardiac myocytes through activation of p21-activated kinase
    • Ke Y., Sheehan K.A., Egom E.E., Lei M., Solaro R.J. Novel bradykinin signaling in adult rat cardiac myocytes through activation of p21-activated kinase. Am J Physiol Heart Circ Physiol 2010, 298:H1283-H1289.
    • (2010) Am J Physiol Heart Circ Physiol , vol.298
    • Ke, Y.1    Sheehan, K.A.2    Egom, E.E.3    Lei, M.4    Solaro, R.J.5
  • 5
    • 34548414482 scopus 로고    scopus 로고
    • P21-Activated kinase-1 and its role in integrated regulation of cardiac contractility
    • Sheehan K.A., Ke Y., Solaro R.J. p21-Activated kinase-1 and its role in integrated regulation of cardiac contractility. Am J Physiol Regul Integr Comp Physiol 2007, 293:R963-R973.
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.293
    • Sheehan, K.A.1    Ke, Y.2    Solaro, R.J.3
  • 6
    • 79251617662 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1 and 2 regulate the balance between eccentric and concentric cardiac growth
    • Kehat I., Davis J., Tiburcy M., Accornero F., Saba-El-Leil M.K., Maillet M., et al. Extracellular signal-regulated kinases 1 and 2 regulate the balance between eccentric and concentric cardiac growth. Circ Res 2011, 108:176-183.
    • (2011) Circ Res , vol.108 , pp. 176-183
    • Kehat, I.1    Davis, J.2    Tiburcy, M.3    Accornero, F.4    Saba-El-Leil, M.K.5    Maillet, M.6
  • 7
    • 0029091356 scopus 로고
    • Ventricular expression of a MLC-2v-ras fusion gene induces cardiac hypertrophy and selective diastolic dysfunction in transgenic mice
    • Hunter J.J., Tanaka N., Rockman H.A., Ross J., Chien K.R. Ventricular expression of a MLC-2v-ras fusion gene induces cardiac hypertrophy and selective diastolic dysfunction in transgenic mice. J Biol Chem 1995, 270:23173-23178.
    • (1995) J Biol Chem , vol.270 , pp. 23173-23178
    • Hunter, J.J.1    Tanaka, N.2    Rockman, H.A.3    Ross, J.4    Chien, K.R.5
  • 8
    • 49149115868 scopus 로고    scopus 로고
    • The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders
    • Aoki Y., Niihori T., Narumi Y., Kure S., Matsubara Y. The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders. Hum Mutat 2008, 29:992-1006.
    • (2008) Hum Mutat , vol.29 , pp. 992-1006
    • Aoki, Y.1    Niihori, T.2    Narumi, Y.3    Kure, S.4    Matsubara, Y.5
  • 9
    • 4844220471 scopus 로고    scopus 로고
    • Identification and regulation of Sprouty1, a negative inhibitor of the ERK cascade, in the human heart
    • Huebert R.C., Li Q., Adhikari N., Charles N.J., Han X., Ezzat M.K., et al. Identification and regulation of Sprouty1, a negative inhibitor of the ERK cascade, in the human heart. Physiol Genomics 2004, 18:284-289.
    • (2004) Physiol Genomics , vol.18 , pp. 284-289
    • Huebert, R.C.1    Li, Q.2    Adhikari, N.3    Charles, N.J.4    Han, X.5    Ezzat, M.K.6
  • 10
    • 0033840752 scopus 로고    scopus 로고
    • Requirement of activation of the extracellular signal-regulated kinase cascade in myocardial cell hypertrophy
    • Ueyama T., Kawashima S., Sakoda T., Rikitake Y., Ishida T., Kawai M., et al. Requirement of activation of the extracellular signal-regulated kinase cascade in myocardial cell hypertrophy. J Mol Cell Cardiol 2000, 32:947-960.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 947-960
    • Ueyama, T.1    Kawashima, S.2    Sakoda, T.3    Rikitake, Y.4    Ishida, T.5    Kawai, M.6
  • 11
    • 80055115527 scopus 로고    scopus 로고
    • Abstract 1389: PKA constitutes a novel activator of cardiac protective Pak1 signaling
    • Glaser N.D., Ke Y., Zhu W., Zhao A., Solaro R.J., Lakatta E.G., et al. Abstract 1389: PKA constitutes a novel activator of cardiac protective Pak1 signaling. Circulation 2008, 118:S_319-
    • (2008) Circulation , vol.118
    • Glaser, N.D.1    Ke, Y.2    Zhu, W.3    Zhao, A.4    Solaro, R.J.5    Lakatta, E.G.6
  • 12
    • 34848820302 scopus 로고    scopus 로고
    • Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection
    • Noma T., Lemaire A., Naga Prasad S.V., Barki-Harrington L., Tilley D.G., Chen J., et al. Beta-arrestin-mediated beta1-adrenergic receptor transactivation of the EGFR confers cardioprotection. J Clin Invest 2007, 117:2445-2458.
    • (2007) J Clin Invest , vol.117 , pp. 2445-2458
    • Noma, T.1    Lemaire, A.2    Naga Prasad, S.V.3    Barki-Harrington, L.4    Tilley, D.G.5    Chen, J.6
  • 13
    • 59549099037 scopus 로고    scopus 로고
    • PAK1-mediated activation of ERK1/2 regulates lamellipodial dynamics
    • Smith S.D., Jaffer Z.M., Chernoff J., Ridley A.J. PAK1-mediated activation of ERK1/2 regulates lamellipodial dynamics. J Cell Sci 2008, 121:3729-3736.
    • (2008) J Cell Sci , vol.121 , pp. 3729-3736
    • Smith, S.D.1    Jaffer, Z.M.2    Chernoff, J.3    Ridley, A.J.4
  • 15
    • 33750692762 scopus 로고    scopus 로고
    • Method for isolation of adult mouse cardiac myocytes for studies of contraction and microfluorimetry
    • Wolska B.M., Solaro R.J. Method for isolation of adult mouse cardiac myocytes for studies of contraction and microfluorimetry. Am J Physiol 1996, 271:H1250-H1255.
    • (1996) Am J Physiol , vol.271
    • Wolska, B.M.1    Solaro, R.J.2
  • 16
    • 0033574693 scopus 로고    scopus 로고
    • Correlation between myofilament response to Ca2+ and altered dynamics of contraction and relaxation in transgenic cardiac cells that express beta-tropomyosin
    • Wolska B.M., Keller R.S., Evans C.C., Palmiter K.A., Phillips R.M., Muthuchamy M., et al. Correlation between myofilament response to Ca2+ and altered dynamics of contraction and relaxation in transgenic cardiac cells that express beta-tropomyosin. Circ Res 1999, 84:745-751.
    • (1999) Circ Res , vol.84 , pp. 745-751
    • Wolska, B.M.1    Keller, R.S.2    Evans, C.C.3    Palmiter, K.A.4    Phillips, R.M.5    Muthuchamy, M.6
  • 17
    • 73349091252 scopus 로고    scopus 로고
    • Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I
    • Kirk J.A., MacGowan G.A., Evans C., Smith S.H., Warren C.M., Mamidi R., et al. Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I. Circ Res 2009, 105:1232-1239.
    • (2009) Circ Res , vol.105 , pp. 1232-1239
    • Kirk, J.A.1    MacGowan, G.A.2    Evans, C.3    Smith, S.H.4    Warren, C.M.5    Mamidi, R.6
  • 20
    • 0026016543 scopus 로고
    • Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban
    • MacDougall L.K., Jones L.R., Cohen P. Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban. Eur J Biochem 1991, 196:725-734.
    • (1991) Eur J Biochem , vol.196 , pp. 725-734
    • MacDougall, L.K.1    Jones, L.R.2    Cohen, P.3
  • 21
    • 0027731172 scopus 로고
    • Protein phosphatase 2A reverses inhibition of inward rectifying K+ currents by thyrotropin-releasing hormone in GH3 pituitary cells
    • Barros F., Mieskes G., del Camino D., de la Pena P. Protein phosphatase 2A reverses inhibition of inward rectifying K+ currents by thyrotropin-releasing hormone in GH3 pituitary cells. FEBS Lett 1993, 336:433-439.
    • (1993) FEBS Lett , vol.336 , pp. 433-439
    • Barros, F.1    Mieskes, G.2    del Camino, D.3    de la Pena, P.4
  • 22
    • 0034671738 scopus 로고    scopus 로고
    • Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase
    • Davare M.A., Horne M.C., Hell J.W. Protein phosphatase 2A is associated with class C L-type calcium channels (Cav1.2) and antagonizes channel phosphorylation by cAMP-dependent protein kinase. J Biol Chem 2000, 275:39710-39717.
    • (2000) J Biol Chem , vol.275 , pp. 39710-39717
    • Davare, M.A.1    Horne, M.C.2    Hell, J.W.3
  • 23
    • 0035800083 scopus 로고    scopus 로고
    • Isoproterenol activates extracellular signal-regulated protein kinases in cardiomyocytes through calcineurin
    • Zou Y., Yao A., Zhu W., Kudoh S., Hiroi Y., Shimoyama M., et al. Isoproterenol activates extracellular signal-regulated protein kinases in cardiomyocytes through calcineurin. Circulation 2001, 104:102-108.
    • (2001) Circulation , vol.104 , pp. 102-108
    • Zou, Y.1    Yao, A.2    Zhu, W.3    Kudoh, S.4    Hiroi, Y.5    Shimoyama, M.6
  • 24
    • 0034682836 scopus 로고    scopus 로고
    • Beta 2-adrenergic receptor activates extracellular signal-regulated kinases (ERKs) via the small G protein rap1 and the serine/threonine kinase B-Raf
    • Schmitt J.M., Stork P.J. beta 2-adrenergic receptor activates extracellular signal-regulated kinases (ERKs) via the small G protein rap1 and the serine/threonine kinase B-Raf. J Biol Chem 2000, 275:25342-25350.
    • (2000) J Biol Chem , vol.275 , pp. 25342-25350
    • Schmitt, J.M.1    Stork, P.J.2
  • 25
    • 0028973270 scopus 로고
    • Dual effect of beta-adrenergic receptors on mitogen-activated protein kinase. Evidence for a beta gamma-dependent activation and a G alpha s-cAMP-mediated inhibition
    • Crespo P., Cachero T.G., Xu N., Gutkind J.S. Dual effect of beta-adrenergic receptors on mitogen-activated protein kinase. Evidence for a beta gamma-dependent activation and a G alpha s-cAMP-mediated inhibition. J Biol Chem 1995, 270:25259-25265.
    • (1995) J Biol Chem , vol.270 , pp. 25259-25265
    • Crespo, P.1    Cachero, T.G.2    Xu, N.3    Gutkind, J.S.4
  • 26
    • 0037163048 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation of the beta 2-adrenergic receptor regulates its coupling to Gs and Gi. Demonstration in a reconstituted system
    • Zamah A.M., Delahunty M., Luttrell L.M., Lefkowitz R.J. Protein kinase A-mediated phosphorylation of the beta 2-adrenergic receptor regulates its coupling to Gs and Gi. Demonstration in a reconstituted system. J Biol Chem 2002, 277:31249-31256.
    • (2002) J Biol Chem , vol.277 , pp. 31249-31256
    • Zamah, A.M.1    Delahunty, M.2    Luttrell, L.M.3    Lefkowitz, R.J.4
  • 28
    • 0027772552 scopus 로고
    • The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation
    • Sontag E., Fedorov S., Kamibayashi C., Robbins D., Cobb M., Mumby M. The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation. Cell 1993, 75:887-897.
    • (1993) Cell , vol.75 , pp. 887-897
    • Sontag, E.1    Fedorov, S.2    Kamibayashi, C.3    Robbins, D.4    Cobb, M.5    Mumby, M.6
  • 30
    • 67649958065 scopus 로고    scopus 로고
    • The role of PAK-1 in activation of MAP kinase cascade and oncogenic transformation by Akt
    • Somanath P.R., Vijai J., Kichina J.V., Byzova T., Kandel E.S. The role of PAK-1 in activation of MAP kinase cascade and oncogenic transformation by Akt. Oncogene 2009, 28:2365-2369.
    • (2009) Oncogene , vol.28 , pp. 2365-2369
    • Somanath, P.R.1    Vijai, J.2    Kichina, J.V.3    Byzova, T.4    Kandel, E.S.5
  • 31
    • 0242664130 scopus 로고    scopus 로고
    • Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration
    • Zhou G.L., Zhuo Y., King C.C., Fryer B.H., Bokoch G.M., Field J. Akt phosphorylation of serine 21 on Pak1 modulates Nck binding and cell migration. Mol Cell Biol 2003, 23:8058-8069.
    • (2003) Mol Cell Biol , vol.23 , pp. 8058-8069
    • Zhou, G.L.1    Zhuo, Y.2    King, C.C.3    Fryer, B.H.4    Bokoch, G.M.5    Field, J.6
  • 32
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang S., Han J., Sells M.A., Chernoff J., Knaus U.G., Ulevitch R.J., et al. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem 1995, 270:23934-23936.
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6
  • 33
    • 0030134625 scopus 로고    scopus 로고
    • Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway
    • Brown J.L., Stowers L., Baer M., Trejo J., Coughlin S., Chant J. Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. Curr Biol 1996, 6:598-605.
    • (1996) Curr Biol , vol.6 , pp. 598-605
    • Brown, J.L.1    Stowers, L.2    Baer, M.3    Trejo, J.4    Coughlin, S.5    Chant, J.6
  • 34
    • 0029950672 scopus 로고    scopus 로고
    • Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members
    • Frost J.A., Xu S., Hutchison M.R., Marcus S., Cobb M.H. Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members. Mol Cell Biol 1996, 16:3707-3713.
    • (1996) Mol Cell Biol , vol.16 , pp. 3707-3713
    • Frost, J.A.1    Xu, S.2    Hutchison, M.R.3    Marcus, S.4    Cobb, M.H.5
  • 35
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia S., Derijard B., Davis R.J., Cerione R.A. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J Biol Chem 1995, 270:27995-27998.
    • (1995) J Biol Chem , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 36
    • 0037144667 scopus 로고    scopus 로고
    • P21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I
    • Buscemi N., Foster D.B., Neverova I., Van Eyk J.E. p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I. Circ Res 2002, 91:509-516.
    • (2002) Circ Res , vol.91 , pp. 509-516
    • Buscemi, N.1    Foster, D.B.2    Neverova, I.3    Van Eyk, J.E.4
  • 37
    • 79954485456 scopus 로고    scopus 로고
    • A preferred AMPK phosphorylation site adjacent to the inhibitory loop of cardiac and skeletal troponin I
    • Sancho Solis R., Ge Y., Walker J.W. A preferred AMPK phosphorylation site adjacent to the inhibitory loop of cardiac and skeletal troponin I. Protein Sci 2011, 20:894-907.
    • (2011) Protein Sci , vol.20 , pp. 894-907
    • Sancho Solis, R.1    Ge, Y.2    Walker, J.W.3
  • 38
    • 0020069347 scopus 로고
    • The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin
    • Robertson S.P., Johnson J.D., Holroyde M.J., Kranias E.G., Potter J.D., Solaro R.J. The effect of troponin I phosphorylation on the Ca2+-binding properties of the Ca2+-regulatory site of bovine cardiac troponin. J Biol Chem 1982, 257:260-263.
    • (1982) J Biol Chem , vol.257 , pp. 260-263
    • Robertson, S.P.1    Johnson, J.D.2    Holroyde, M.J.3    Kranias, E.G.4    Potter, J.D.5    Solaro, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.