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Volumn 1831, Issue 1, 2013, Pages 213-222

Lysophospholipid receptor activation of RhoA and lipid signaling pathways

Author keywords

LPA; Lysophospholipid; RhoA; S1P

Indexed keywords

2 AMINO 2 (3 OCTYLPHENYLCARBAMOYL)ETHYL PHOSPHATE; FINGOLIMOD; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LYSOPHOSPHATIDIC ACID; LYSOPHOSPHOLIPID; LYSOPHOSPHOLIPID RECEPTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOLIPASE C; PHOSPHOLIPASE D; PROTEIN KINASE B; PROTEIN KINASE D; PROTEIN KINASE N; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SPHINGOSINE 1 PHOSPHATE;

EID: 84868576048     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2012.09.004     Document Type: Review
Times cited : (71)

References (182)
  • 1
    • 16644364820 scopus 로고    scopus 로고
    • Lysophospholipids in development: miles apart and edging in
    • J.D. Saba Lysophospholipids in development: miles apart and edging in J. Cell. Biochem. 92 2004 967 992
    • (2004) J. Cell. Biochem. , vol.92 , pp. 967-992
    • Saba, J.D.1
  • 2
    • 35448989224 scopus 로고    scopus 로고
    • Targeting the lipids LPA and S1P and their signalling pathways to inhibit tumour progression
    • M. Murph, and G.B. Mills Targeting the lipids LPA and S1P and their signalling pathways to inhibit tumour progression Expert Rev. Mol. Med. 9 2007 1 18
    • (2007) Expert Rev. Mol. Med. , vol.9 , pp. 1-18
    • Murph, M.1    Mills, G.B.2
  • 3
    • 33845985634 scopus 로고    scopus 로고
    • Effects of LPA and S1P on the nervous system and implications for their involvement in disease
    • D.R. Herr, and J. Chun Effects of LPA and S1P on the nervous system and implications for their involvement in disease Curr. Drug Targets 8 2007 155 167
    • (2007) Curr. Drug Targets , vol.8 , pp. 155-167
    • Herr, D.R.1    Chun, J.2
  • 4
    • 78449244305 scopus 로고    scopus 로고
    • Neurological S1P signaling as an emerging mechanism of action of oral FTY720 (fingolimod) in multiple sclerosis
    • C.W. Lee, J.W. Choi, and J. Chun Neurological S1P signaling as an emerging mechanism of action of oral FTY720 (fingolimod) in multiple sclerosis Arch. Pharm. Res. 33 2010 1567 1574
    • (2010) Arch. Pharm. Res. , vol.33 , pp. 1567-1574
    • Lee, C.W.1    Choi, J.W.2    Chun, J.3
  • 5
    • 78951478960 scopus 로고    scopus 로고
    • Roles for lysophospholipid S1P receptors in multiple sclerosis
    • K. Noguchi, and J. Chun Roles for lysophospholipid S1P receptors in multiple sclerosis Crit. Rev. Biochem. Mol. Biol. 46 2011 2 10
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 2-10
    • Noguchi, K.1    Chun, J.2
  • 6
    • 77949492248 scopus 로고    scopus 로고
    • Lysophosphatidic acid (LPA) receptors: signaling properties and disease relevance
    • M.E. Lin, D.R. Herr, and J. Chun Lysophosphatidic acid (LPA) receptors: signaling properties and disease relevance Prostaglandins Other Lipid Mediat. 91 2010 130 138
    • (2010) Prostaglandins Other Lipid Mediat. , vol.91 , pp. 130-138
    • Lin, M.E.1    Herr, D.R.2    Chun, J.3
  • 8
    • 67449128381 scopus 로고    scopus 로고
    • Lipid signalling in cardiovascular pathophysiology
    • J.S. Karliner, and J.H. Brown Lipid signalling in cardiovascular pathophysiology Cardiovasc. Res. 82 2009 171 174
    • (2009) Cardiovasc. Res. , vol.82 , pp. 171-174
    • Karliner, J.S.1    Brown, J.H.2
  • 9
    • 67449138784 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate receptor signalling in the heart
    • C.K. Means, and J.H. Brown Sphingosine-1-phosphate receptor signalling in the heart Cardiovasc. Res. 82 2009 193 200
    • (2009) Cardiovasc. Res. , vol.82 , pp. 193-200
    • Means, C.K.1    Brown, J.H.2
  • 10
    • 84856265412 scopus 로고    scopus 로고
    • Insights into the pharmacological relevance of lysophospholipid receptors
    • T. Mutoh, R. Rivera, and J. Chun Insights into the pharmacological relevance of lysophospholipid receptors Br. J. Pharmacol. 165 2012 829 844
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 829-844
    • Mutoh, T.1    Rivera, R.2    Chun, J.3
  • 12
    • 14644426000 scopus 로고    scopus 로고
    • Receptors coupled to heterotrimeric G proteins of the G12 family
    • N.A. Riobo, and D.R. Manning Receptors coupled to heterotrimeric G proteins of the G12 family Trends Pharmacol. Sci. 26 2005 146 154
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 146-154
    • Riobo, N.A.1    Manning, D.R.2
  • 13
    • 33947427567 scopus 로고    scopus 로고
    • Lysophospholipid receptors: signalling, pharmacology and regulation by lysophospholipid metabolism
    • D. Meyer zu Heringdorf, and K.H. Jakobs Lysophospholipid receptors: signalling, pharmacology and regulation by lysophospholipid metabolism Biochim. Biophys. Acta 1768 2007 923 940
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 923-940
    • Meyer Zu Heringdorf, D.1    Jakobs, K.H.2
  • 15
    • 74549193568 scopus 로고    scopus 로고
    • Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors
    • M. Aittaleb, C.A. Boguth, and J.J. Tesmer Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors Mol. Pharmacol. 77 2010 111 125
    • (2010) Mol. Pharmacol. , vol.77 , pp. 111-125
    • Aittaleb, M.1    Boguth, C.A.2    Tesmer, J.J.3
  • 16
    • 60149112585 scopus 로고    scopus 로고
    • Regulation and physiological functions of G12/13-mediated signaling pathways
    • N. Suzuki, N. Hajicek, and T. Kozasa Regulation and physiological functions of G12/13-mediated signaling pathways Neurosignals 17 2009 55 70
    • (2009) Neurosignals , vol.17 , pp. 55-70
    • Suzuki, N.1    Hajicek, N.2    Kozasa, T.3
  • 17
    • 69249208550 scopus 로고    scopus 로고
    • Regulation of RhoGEF proteins by G12/13-coupled receptors
    • S. Siehler Regulation of RhoGEF proteins by G12/13-coupled receptors Br. J. Pharmacol. 158 2009 41 49
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 41-49
    • Siehler, S.1
  • 18
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion
    • S. Narumiya, M. Tanji, and T. Ishizaki Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion Cancer Metastasis Rev. 28 2009 65 76
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 20
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • A.B. Jaffe, and A. Hall Rho GTPases: biochemistry and biology Annu. Rev. Cell Dev. Biol. 21 2005 247 269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 22
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • M. Chrzanowska-Wodnicka, and K. Burridge Rho-stimulated contractility drives the formation of stress fibers and focal adhesions J. Cell Biol. 133 1996 1403 1415
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 23
    • 0032485940 scopus 로고    scopus 로고
    • Galpha12 and Galpha13 stimulate Rho-dependent tyrosine phosphorylation of focal adhesion kinase, paxillin, and p130 Crk-associated substrate
    • L.K. Needham, and E. Rozengurt Galpha12 and Galpha13 stimulate Rho-dependent tyrosine phosphorylation of focal adhesion kinase, paxillin, and p130 Crk-associated substrate J. Biol. Chem. 273 1998 14626 14632
    • (1998) J. Biol. Chem. , vol.273 , pp. 14626-14632
    • Needham, L.K.1    Rozengurt, E.2
  • 24
    • 33645740350 scopus 로고    scopus 로고
    • The G12/13-RhoA signaling pathway contributes to efficient lysophosphatidic acid-stimulated cell migration
    • D. Bian, C. Mahanivong, J. Yu, S.M. Frisch, Z.K. Pan, R.D. Ye, and S. Huang The G12/13-RhoA signaling pathway contributes to efficient lysophosphatidic acid-stimulated cell migration Oncogene 25 2006 2234 2244
    • (2006) Oncogene , vol.25 , pp. 2234-2244
    • Bian, D.1    Mahanivong, C.2    Yu, J.3    Frisch, S.M.4    Pan, Z.K.5    Ye, R.D.6    Huang, S.7
  • 25
    • 0032582343 scopus 로고    scopus 로고
    • Constitutively active Galpha12, Galpha13, and Galphaq induce Rho-dependent neurite retraction through different signaling pathways
    • H. Katoh, J. Aoki, Y. Yamaguchi, Y. Kitano, A. Ichikawa, and M. Negishi Constitutively active Galpha12, Galpha13, and Galphaq induce Rho-dependent neurite retraction through different signaling pathways J. Biol. Chem. 273 1998 28700 28707
    • (1998) J. Biol. Chem. , vol.273 , pp. 28700-28707
    • Katoh, H.1    Aoki, J.2    Yamaguchi, Y.3    Kitano, Y.4    Ichikawa, A.5    Negishi, M.6
  • 26
    • 0033018626 scopus 로고    scopus 로고
    • Activation of RhoA by lysophosphatidic acid and Galpha12/13 subunits in neuronal cells: induction of neurite retraction
    • O. Kranenburg, M. Poland, F.P. van Horck, D. Drechsel, A. Hall, and W.H. Moolenaar Activation of RhoA by lysophosphatidic acid and Galpha12/13 subunits in neuronal cells: induction of neurite retraction Mol. Biol. Cell 10 1999 1851 1857
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1851-1857
    • Kranenburg, O.1    Poland, M.2    Van Horck, F.P.3    Drechsel, D.4    Hall, A.5    Moolenaar, W.H.6
  • 27
    • 13944280988 scopus 로고    scopus 로고
    • G protein mediated signaling pathways in lysophospholipid induced cell proliferation and survival
    • J. Radeff-Huang, T.M. Seasholtz, R.G. Matteo, and J.H. Brown G protein mediated signaling pathways in lysophospholipid induced cell proliferation and survival J. Cell. Biochem. 92 2004 949 966
    • (2004) J. Cell. Biochem. , vol.92 , pp. 949-966
    • Radeff-Huang, J.1    Seasholtz, T.M.2    Matteo, R.G.3    Brown, J.H.4
  • 28
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • C.S. Hill, J. Wynne, and R. Treisman The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF Cell 81 1995 1159 1170
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 31
    • 80053186768 scopus 로고    scopus 로고
    • Plasma membrane association of p63 Rho guanine nucleotide exchange factor (p63RhoGEF) is mediated by palmitoylation and is required for basal activity in cells
    • M. Aittaleb, A. Nishimura, M.E. Linder, and J.J. Tesmer Plasma membrane association of p63 Rho guanine nucleotide exchange factor (p63RhoGEF) is mediated by palmitoylation and is required for basal activity in cells J. Biol. Chem. 286 2011 34448 34456
    • (2011) J. Biol. Chem. , vol.286 , pp. 34448-34456
    • Aittaleb, M.1    Nishimura, A.2    Linder, M.E.3    Tesmer, J.J.4
  • 33
    • 0032493664 scopus 로고    scopus 로고
    • Activation of phospholipase C-beta1 via Galphaq/11 during calcium mobilization by calcitonin gene-related peptide
    • H. Drissi, F. Lasmoles, V. Le Mellay, P.J. Marie, and M. Lieberherr Activation of phospholipase C-beta1 via Galphaq/11 during calcium mobilization by calcitonin gene-related peptide J. Biol. Chem. 273 1998 20168 20174
    • (1998) J. Biol. Chem. , vol.273 , pp. 20168-20174
    • Drissi, H.1    Lasmoles, F.2    Le Mellay, V.3    Marie, P.J.4    Lieberherr, M.5
  • 36
    • 0025793981 scopus 로고
    • Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq
    • A.V. Smrcka, J.R. Hepler, K.O. Brown, and P.C. Sternweis Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq Science 251 1991 804 807
    • (1991) Science , vol.251 , pp. 804-807
    • Smrcka, A.V.1    Hepler, J.R.2    Brown, K.O.3    Sternweis, P.C.4
  • 37
    • 0025860413 scopus 로고
    • Activation of the beta 1 isozyme of phospholipase C by alpha subunits of the Gq class of G proteins
    • S.J. Taylor, H.Z. Chae, S.G. Rhee, and J.H. Exton Activation of the beta 1 isozyme of phospholipase C by alpha subunits of the Gq class of G proteins Nature 350 1991 516 518
    • (1991) Nature , vol.350 , pp. 516-518
    • Taylor, S.J.1    Chae, H.Z.2    Rhee, S.G.3    Exton, J.H.4
  • 38
    • 33645747309 scopus 로고    scopus 로고
    • The Rac and Rho hall of fame: A decade of hypertrophic signaling hits
    • J.H. Brown, D.P. Del Re, and M.A. Sussman The Rac and Rho hall of fame: a decade of hypertrophic signaling hits Circ. Res. 98 2006 730 742
    • (2006) Circ. Res. , vol.98 , pp. 730-742
    • Brown, J.H.1    Del Re, D.P.2    Sussman, M.A.3
  • 39
    • 79953683448 scopus 로고    scopus 로고
    • Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1
    • C.L. Hutchinson, P.N. Lowe, S.H. McLaughlin, H.R. Mott, and D. Owen Mutational analysis reveals a single binding interface between RhoA and its effector, PRK1 Biochemistry 50 2011 2860 2869
    • (2011) Biochemistry , vol.50 , pp. 2860-2869
    • Hutchinson, C.L.1    Lowe, P.N.2    Mclaughlin, S.H.3    Mott, H.R.4    Owen, D.5
  • 40
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • A.L. Bishop, and A. Hall Rho GTPases and their effector proteins Biochem. J. 348 Pt 2 2000 241 255
    • (2000) Biochem. J. , vol.348 , Issue.PART 2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 41
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: multifunctional kinases in cell behaviour
    • K. Riento, and A.J. Ridley Rocks: multifunctional kinases in cell behaviour Nat. Rev. Mol. Cell Biol. 4 2003 446 456
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 42
    • 80053101752 scopus 로고    scopus 로고
    • Rho kinase as a therapeutic target in cardiovascular disease
    • M. Surma, L. Wei, and J. Shi Rho kinase as a therapeutic target in cardiovascular disease Future Cardiol. 7 2011 657 671
    • (2011) Future Cardiol. , vol.7 , pp. 657-671
    • Surma, M.1    Wei, L.2    Shi, J.3
  • 43
    • 83055187108 scopus 로고    scopus 로고
    • Rho kinase proteins - pleiotropic modulators of cell survival and apoptosis
    • C.A. Street, and B.A. Bryan Rho kinase proteins - pleiotropic modulators of cell survival and apoptosis Anticancer Res. 31 2011 3645 3657
    • (2011) Anticancer Res. , vol.31 , pp. 3645-3657
    • Street, C.A.1    Bryan, B.A.2
  • 45
    • 33947591759 scopus 로고    scopus 로고
    • Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis
    • A. Schmidt, J. Durgan, A. Magalhaes, and A. Hall Rho GTPases regulate PRK2/PKN2 to control entry into mitosis and exit from cytokinesis EMBO J. 26 2007 1624 1636
    • (2007) EMBO J. , vol.26 , pp. 1624-1636
    • Schmidt, A.1    Durgan, J.2    Magalhaes, A.3    Hall, A.4
  • 48
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • H. Mukai The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC J. Biochem. 133 2003 17 27
    • (2003) J. Biochem. , vol.133 , pp. 17-27
    • Mukai, H.1
  • 50
    • 0034771776 scopus 로고    scopus 로고
    • Signalling roles of mammalian phospholipase D1 and D2
    • S. Cockcroft Signalling roles of mammalian phospholipase D1 and D2 Cell. Mol. Life Sci. 58 2001 1674 1687
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1674-1687
    • Cockcroft, S.1
  • 51
    • 0037201951 scopus 로고    scopus 로고
    • Regulation of phospholipase D
    • J.H. Exton Regulation of phospholipase D FEBS Lett. 531 2002 58 61
    • (2002) FEBS Lett. , vol.531 , pp. 58-61
    • Exton, J.H.1
  • 52
    • 23644455714 scopus 로고    scopus 로고
    • Phospholipase D: A lipid centric review
    • G.M. Jenkins, and M.A. Frohman Phospholipase D: a lipid centric review Cell. Mol. Life Sci. 62 2005 2305 2316
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2305-2316
    • Jenkins, G.M.1    Frohman, M.A.2
  • 54
    • 0037023746 scopus 로고    scopus 로고
    • Mechanisms of regulation of phospholipase D1 and D2 by the heterotrimeric G proteins G13 and Gq
    • Z. Xie, W.T. Ho, R. Spellman, S. Cai, and J.H. Exton Mechanisms of regulation of phospholipase D1 and D2 by the heterotrimeric G proteins G13 and Gq J. Biol. Chem. 277 2002 11979 11986
    • (2002) J. Biol. Chem. , vol.277 , pp. 11979-11986
    • Xie, Z.1    Ho, W.T.2    Spellman, R.3    Cai, S.4    Exton, J.H.5
  • 57
    • 0037135598 scopus 로고    scopus 로고
    • Specificity of Rho insert-mediated activation of phospholipase D1
    • S.J. Walker, and H.A. Brown Specificity of Rho insert-mediated activation of phospholipase D1 J. Biol. Chem. 277 2002 26260 26267
    • (2002) J. Biol. Chem. , vol.277 , pp. 26260-26267
    • Walker, S.J.1    Brown, H.A.2
  • 59
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • L.D. Chong, A. Traynor-Kaplan, G.M. Bokoch, and M.A. Schwartz The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells Cell 79 1994 507 513
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 60
    • 0036845015 scopus 로고    scopus 로고
    • Involvement of phospholipases D1 and D2 in sphingosine 1-phosphate-induced ERK (extracellular-signal-regulated kinase) activation and interleukin-8 secretion in human bronchial epithelial cells
    • L. Wang, R. Cummings, P. Usatyuk, A. Morris, K. Irani, and V. Natarajan Involvement of phospholipases D1 and D2 in sphingosine 1-phosphate-induced ERK (extracellular-signal-regulated kinase) activation and interleukin-8 secretion in human bronchial epithelial cells Biochem. J. 367 2002 751 760
    • (2002) Biochem. J. , vol.367 , pp. 751-760
    • Wang, L.1    Cummings, R.2    Usatyuk, P.3    Morris, A.4    Irani, K.5    Natarajan, V.6
  • 61
    • 0037119432 scopus 로고    scopus 로고
    • Phospholipase D activation by sphingosine 1-phosphate regulates interleukin-8 secretion in human bronchial epithelial cells
    • R.J. Cummings, N.L. Parinandi, A. Zaiman, L. Wang, P.V. Usatyuk, J.G. Garcia, and V. Natarajan Phospholipase D activation by sphingosine 1-phosphate regulates interleukin-8 secretion in human bronchial epithelial cells J. Biol. Chem. 277 2002 30227 30235
    • (2002) J. Biol. Chem. , vol.277 , pp. 30227-30235
    • Cummings, R.J.1    Parinandi, N.L.2    Zaiman, A.3    Wang, L.4    Usatyuk, P.V.5    Garcia, J.G.6    Natarajan, V.7
  • 62
    • 0037457818 scopus 로고    scopus 로고
    • Activation of phospholipase D by bradykinin and sphingosine 1-phosphate in A549 human lung adenocarcinoma cells via different GTP-binding proteins and protein kinase C delta signaling pathways
    • E. Meacci, F. Nuti, S. Catarzi, V. Vasta, C. Donati, S. Bourgoin, P. Bruni, J. Moss, and M. Vaughan Activation of phospholipase D by bradykinin and sphingosine 1-phosphate in A549 human lung adenocarcinoma cells via different GTP-binding proteins and protein kinase C delta signaling pathways Biochemistry 42 2003 284 292
    • (2003) Biochemistry , vol.42 , pp. 284-292
    • Meacci, E.1    Nuti, F.2    Catarzi, S.3    Vasta, V.4    Donati, C.5    Bourgoin, S.6    Bruni, P.7    Moss, J.8    Vaughan, M.9
  • 63
    • 0031938954 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates phospholipase D activity and cell proliferation in PC-3 human prostate cancer cells
    • C. Qi, J.H. Park, T.C. Gibbs, D.W. Shirley, C.D. Bradshaw, K.M. Ella, and K.E. Meier Lysophosphatidic acid stimulates phospholipase D activity and cell proliferation in PC-3 human prostate cancer cells J. Cell. Physiol. 174 1998 261 272
    • (1998) J. Cell. Physiol. , vol.174 , pp. 261-272
    • Qi, C.1    Park, J.H.2    Gibbs, T.C.3    Shirley, D.W.4    Bradshaw, C.D.5    Ella, K.M.6    Meier, K.E.7
  • 64
    • 0026740688 scopus 로고
    • The biologically active phospholipid, lysophosphatidic acid, induces phosphatidylcholine breakdown in fibroblasts via activation of phospholipase D. Comparison with the response to endothelin
    • R.L. van der Bend, J. de Widt, E.J. van Corven, W.H. Moolenaar, and W.J. van Blitterswijk The biologically active phospholipid, lysophosphatidic acid, induces phosphatidylcholine breakdown in fibroblasts via activation of phospholipase D. Comparison with the response to endothelin Biochem. J. 285 Pt 1 1992 235 240
    • (1992) Biochem. J. , vol.285 , Issue.PART 1 , pp. 235-240
    • Van Der Bend, R.L.1    De Widt, J.2    Van Corven, E.J.3    Moolenaar, W.H.4    Van Blitterswijk, W.J.5
  • 65
    • 33745964754 scopus 로고    scopus 로고
    • Oxidative stress and redox regulation of phospholipase D in myocardial disease
    • P.S. Tappia, M.R. Dent, and N.S. Dhalla Oxidative stress and redox regulation of phospholipase D in myocardial disease Free Radic. Biol. Med. 41 2006 349 361
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 349-361
    • Tappia, P.S.1    Dent, M.R.2    Dhalla, N.S.3
  • 67
    • 77951209408 scopus 로고    scopus 로고
    • Direct activation of RhoA by reactive oxygen species requires a redox-sensitive motif
    • A. Aghajanian, E.S. Wittchen, S.L. Campbell, and K. Burridge Direct activation of RhoA by reactive oxygen species requires a redox-sensitive motif PLoS One 4 2009 e8045
    • (2009) PLoS One , vol.4 , pp. 8045
    • Aghajanian, A.1    Wittchen, E.S.2    Campbell, S.L.3    Burridge, K.4
  • 70
    • 1442314696 scopus 로고    scopus 로고
    • Role of direct RhoA-phospholipase D1 interaction in mediating adenosine-induced protection from cardiac ischemia
    • S. Mozzicato, B.V. Joshi, K.A. Jacobson, and B.T. Liang Role of direct RhoA-phospholipase D1 interaction in mediating adenosine-induced protection from cardiac ischemia FASEB J. 18 2004 406 408
    • (2004) FASEB J. , vol.18 , pp. 406-408
    • Mozzicato, S.1    Joshi, B.V.2    Jacobson, K.A.3    Liang, B.T.4
  • 73
    • 70349629000 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate is an important endogenous cardioprotectant released by ischemic pre- and postconditioning
    • D.A. Vessey, L. Li, N. Honbo, and J.S. Karliner Sphingosine 1-phosphate is an important endogenous cardioprotectant released by ischemic pre- and postconditioning Am. J. Physiol. Heart Circ. Physiol. 297 2009 H1429 H1435
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Vessey, D.A.1    Li, L.2    Honbo, N.3    Karliner, J.S.4
  • 74
    • 43249109652 scopus 로고    scopus 로고
    • Sphingosine can pre- and post-condition heart and utilizes a different mechanism from sphingosine 1-phosphate
    • D.A. Vessey, L. Li, M. Kelley, J. Zhang, and J.S. Karliner Sphingosine can pre- and post-condition heart and utilizes a different mechanism from sphingosine 1-phosphate J. Biochem. Mol. Toxicol. 22 2008 113 118
    • (2008) J. Biochem. Mol. Toxicol. , vol.22 , pp. 113-118
    • Vessey, D.A.1    Li, L.2    Kelley, M.3    Zhang, J.4    Karliner, J.S.5
  • 75
    • 33747184318 scopus 로고    scopus 로고
    • Supervised membrane swimming: small G-protein lifeguards regulate PIPK signalling and monitor intracellular PtdIns(4,5)P2 pools
    • M. Santarius, C.H. Lee, and R.A. Anderson Supervised membrane swimming: small G-protein lifeguards regulate PIPK signalling and monitor intracellular PtdIns(4,5)P2 pools Biochem. J. 398 2006 1 13
    • (2006) Biochem. J. , vol.398 , pp. 1-13
    • Santarius, M.1    Lee, C.H.2    Anderson, R.A.3
  • 77
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • X.D. Ren, G.M. Bokoch, A. Traynor-Kaplan, G.H. Jenkins, R.A. Anderson, and M.A. Schwartz Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells Mol. Biol. Cell 7 1996 435 442
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 79
    • 33745143631 scopus 로고    scopus 로고
    • Galpha12/13- and rho-dependent activation of phospholipase C-epsilon by lysophosphatidic acid and thrombin receptors
    • M.D. Hains, M.R. Wing, S. Maddileti, D.P. Siderovski, and T.K. Harden Galpha12/13- and rho-dependent activation of phospholipase C-epsilon by lysophosphatidic acid and thrombin receptors Mol. Pharmacol. 69 2006 2068 2075
    • (2006) Mol. Pharmacol. , vol.69 , pp. 2068-2075
    • Hains, M.D.1    Wing, M.R.2    Maddileti, S.3    Siderovski, D.P.4    Harden, T.K.5
  • 80
  • 81
    • 9144254020 scopus 로고    scopus 로고
    • RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism
    • J.P. Seifert, M.R. Wing, J.T. Snyder, S. Gershburg, J. Sondek, and T.K. Harden RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism J. Biol. Chem. 279 2004 47992 47997
    • (2004) J. Biol. Chem. , vol.279 , pp. 47992-47997
    • Seifert, J.P.1    Wing, M.R.2    Snyder, J.T.3    Gershburg, S.4    Sondek, J.5    Harden, T.K.6
  • 82
    • 0142135070 scopus 로고    scopus 로고
    • Direct activation of phospholipase C-epsilon by Rho
    • M.R. Wing, J.T. Snyder, J. Sondek, and T.K. Harden Direct activation of phospholipase C-epsilon by Rho J. Biol. Chem. 278 2003 41253 41258
    • (2003) J. Biol. Chem. , vol.278 , pp. 41253-41258
    • Wing, M.R.1    Snyder, J.T.2    Sondek, J.3    Harden, T.K.4
  • 83
    • 33751315308 scopus 로고    scopus 로고
    • Phospholipase C epsilon: linking second messengers and small GTPases
    • T.D. Bunney, and M. Katan Phospholipase C epsilon: linking second messengers and small GTPases Trends Cell Biol. 16 2006 640 648
    • (2006) Trends Cell Biol. , vol.16 , pp. 640-648
    • Bunney, T.D.1    Katan, M.2
  • 84
    • 84862778234 scopus 로고    scopus 로고
    • Role of phospholipase Cepsilon in physiological phosphoinositide signaling networks
    • A.V. Smrcka, J.H. Brown, and G.G. Holz Role of phospholipase Cepsilon in physiological phosphoinositide signaling networks Cell. Signal. 24 2012 1333 1343
    • (2012) Cell. Signal. , vol.24 , pp. 1333-1343
    • Smrcka, A.V.1    Brown, J.H.2    Holz, G.G.3
  • 85
    • 2342514426 scopus 로고    scopus 로고
    • PLC-epsilon: A shared effector protein in Ras-, Rho-, and G alpha beta gamma-mediated signaling
    • M.R. Wing, D.M. Bourdon, and T.K. Harden PLC-epsilon: a shared effector protein in Ras-, Rho-, and G alpha beta gamma-mediated signaling Mol. Interv. 3 2003 273 280
    • (2003) Mol. Interv. , vol.3 , pp. 273-280
    • Wing, M.R.1    Bourdon, D.M.2    Harden, T.K.3
  • 86
    • 33744533321 scopus 로고    scopus 로고
    • Phospholipase Cepsilon guanine nucleotide exchange factor activity and activation of Rap1
    • T. Satoh, H. Edamatsu, and T. Kataoka Phospholipase Cepsilon guanine nucleotide exchange factor activity and activation of Rap1 Methods Enzymol. 407 2006 281 290
    • (2006) Methods Enzymol. , vol.407 , pp. 281-290
    • Satoh, T.1    Edamatsu, H.2    Kataoka, T.3
  • 87
    • 33744511065 scopus 로고    scopus 로고
    • Ras and Rap1 activation of PLCepsilon lipase activity
    • H. Edamatsu, T. Satoh, and T. Kataoka Ras and Rap1 activation of PLCepsilon lipase activity Methods Enzymol. 407 2006 99 107
    • (2006) Methods Enzymol. , vol.407 , pp. 99-107
    • Edamatsu, H.1    Satoh, T.2    Kataoka, T.3
  • 89
    • 0035951882 scopus 로고    scopus 로고
    • A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway
    • I. Lopez, E.C. Mak, J. Ding, H.E. Hamm, and J.W. Lomasney A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway J. Biol. Chem. 276 2001 2758 2765
    • (2001) J. Biol. Chem. , vol.276 , pp. 2758-2765
    • Lopez, I.1    Mak, E.C.2    Ding, J.3    Hamm, H.E.4    Lomasney, J.W.5
  • 90
    • 1542344841 scopus 로고    scopus 로고
    • Hormonal regulation of phospholipase Cepsilon through distinct and overlapping pathways involving G12 and Ras family G-proteins
    • G.G. Kelley, S.E. Reks, and A.V. Smrcka Hormonal regulation of phospholipase Cepsilon through distinct and overlapping pathways involving G12 and Ras family G-proteins Biochem. J. 378 2004 129 139
    • (2004) Biochem. J. , vol.378 , pp. 129-139
    • Kelley, G.G.1    Reks, S.E.2    Smrcka, A.V.3
  • 93
    • 69449092270 scopus 로고    scopus 로고
    • Phospholipase Cepsilon promotes intestinal tumorigenesis of Apc(Min/+) mice through augmentation of inflammation and angiogenesis
    • M. Li, H. Edamatsu, R. Kitazawa, S. Kitazawa, and T. Kataoka Phospholipase Cepsilon promotes intestinal tumorigenesis of Apc(Min/+) mice through augmentation of inflammation and angiogenesis Carcinogenesis 30 2009 1424 1432
    • (2009) Carcinogenesis , vol.30 , pp. 1424-1432
    • Li, M.1    Edamatsu, H.2    Kitazawa, R.3    Kitazawa, S.4    Kataoka, T.5
  • 94
    • 79955535554 scopus 로고    scopus 로고
    • Phospholipase Cvarepsilon has a crucial role in ultraviolet B-induced neutrophil-associated skin inflammation by regulating the expression of CXCL1/KC
    • M. Oka, H. Edamatsu, M. Kunisada, L. Hu, N. Takenaka, M. Sakaguchi, T. Kataoka, and C. Nishigori Phospholipase Cvarepsilon has a crucial role in ultraviolet B-induced neutrophil-associated skin inflammation by regulating the expression of CXCL1/KC Lab. Invest. 91 2011 711 718
    • (2011) Lab. Invest. , vol.91 , pp. 711-718
    • Oka, M.1    Edamatsu, H.2    Kunisada, M.3    Hu, L.4    Takenaka, N.5    Sakaguchi, M.6    Kataoka, T.7    Nishigori, C.8
  • 95
    • 79961026124 scopus 로고    scopus 로고
    • Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology
    • Y. Fu, and C.S. Rubin Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology EMBO Rep. 12 2011 785 796
    • (2011) EMBO Rep. , vol.12 , pp. 785-796
    • Fu, Y.1    Rubin, C.S.2
  • 96
    • 33744926666 scopus 로고    scopus 로고
    • PKD at the crossroads of DAG and PKC signaling
    • Q.J. Wang PKD at the crossroads of DAG and PKC signaling Trends Pharmacol. Sci. 27 2006 317 323
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 317-323
    • Wang, Q.J.1
  • 98
    • 0035914392 scopus 로고    scopus 로고
    • Activation of protein kinase D by signaling through Rho and the alpha subunit of the heterotrimeric G protein G13
    • J. Yuan, L.W. Slice, and E. Rozengurt Activation of protein kinase D by signaling through Rho and the alpha subunit of the heterotrimeric G protein G13 J. Biol. Chem. 276 2001 38619 38627
    • (2001) J. Biol. Chem. , vol.276 , pp. 38619-38627
    • Yuan, J.1    Slice, L.W.2    Rozengurt, E.3
  • 99
    • 62649104179 scopus 로고    scopus 로고
    • Loss of cell-cell contacts induces NF-kappaB via RhoA-mediated activation of protein kinase D1
    • C.F. Cowell, I.K. Yan, T. Eiseler, A.C. Leightner, H. Doppler, and P. Storz Loss of cell-cell contacts induces NF-kappaB via RhoA-mediated activation of protein kinase D1 J. Cell. Biochem. 106 2009 714 728
    • (2009) J. Cell. Biochem. , vol.106 , pp. 714-728
    • Cowell, C.F.1    Yan, I.K.2    Eiseler, T.3    Leightner, A.C.4    Doppler, H.5    Storz, P.6
  • 101
    • 69949177413 scopus 로고    scopus 로고
    • The protein scaffold NHERF-1 controls the amplitude and duration of localized protein kinase D activity
    • M.T. Kunkel, E.L. Garcia, T. Kajimoto, R.A. Hall, and A.C. Newton The protein scaffold NHERF-1 controls the amplitude and duration of localized protein kinase D activity J. Biol. Chem. 284 2009 24653 24661
    • (2009) J. Biol. Chem. , vol.284 , pp. 24653-24661
    • Kunkel, M.T.1    Garcia, E.L.2    Kajimoto, T.3    Hall, R.A.4    Newton, A.C.5
  • 102
    • 34250338923 scopus 로고    scopus 로고
    • Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter
    • M.T. Kunkel, A. Toker, R.Y. Tsien, and A.C. Newton Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter J. Biol. Chem. 282 2007 6733 6742
    • (2007) J. Biol. Chem. , vol.282 , pp. 6733-6742
    • Kunkel, M.T.1    Toker, A.2    Tsien, R.Y.3    Newton, A.C.4
  • 103
    • 0035839496 scopus 로고    scopus 로고
    • Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling
    • T.G. Jin, T. Satoh, Y. Liao, C. Song, X. Gao, K. Kariya, C.D. Hu, and T. Kataoka Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling J. Biol. Chem. 276 2001 30301 30307
    • (2001) J. Biol. Chem. , vol.276 , pp. 30301-30307
    • Jin, T.G.1    Satoh, T.2    Liao, Y.3    Song, C.4    Gao, X.5    Kariya, K.6    Hu, C.D.7    Kataoka, T.8
  • 104
    • 41149153993 scopus 로고    scopus 로고
    • Protein kinase d in the cardiovascular system: emerging roles in health and disease
    • M. Avkiran, A.J. Rowland, F. Cuello, and R.S. Haworth Protein kinase d in the cardiovascular system: emerging roles in health and disease Circ. Res. 102 2008 157 163
    • (2008) Circ. Res. , vol.102 , pp. 157-163
    • Avkiran, M.1    Rowland, A.J.2    Cuello, F.3    Haworth, R.S.4
  • 106
    • 45749116898 scopus 로고    scopus 로고
    • Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis
    • C.H. Ha, W. Wang, B.S. Jhun, C. Wong, A. Hausser, K. Pfizenmaier, T.A. McKinsey, E.N. Olson, and Z.G. Jin Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis J. Biol. Chem. 283 2008 14590 14599
    • (2008) J. Biol. Chem. , vol.283 , pp. 14590-14599
    • Ha, C.H.1    Wang, W.2    Jhun, B.S.3    Wong, C.4    Hausser, A.5    Pfizenmaier, K.6    Mckinsey, T.A.7    Olson, E.N.8    Jin, Z.G.9
  • 107
    • 4544315655 scopus 로고    scopus 로고
    • Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5
    • R.B. Vega, B.C. Harrison, E. Meadows, C.R. Roberts, P.J. Papst, E.N. Olson, and T.A. McKinsey Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5 Mol. Cell. Biol. 24 2004 8374 8385
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8374-8385
    • Vega, R.B.1    Harrison, B.C.2    Meadows, E.3    Roberts, C.R.4    Papst, P.J.5    Olson, E.N.6    Mckinsey, T.A.7
  • 108
    • 36148962891 scopus 로고    scopus 로고
    • A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation
    • H. Doppler, and P. Storz A novel tyrosine phosphorylation site in protein kinase D contributes to oxidative stress-mediated activation J. Biol. Chem. 282 2007 31873 31881
    • (2007) J. Biol. Chem. , vol.282 , pp. 31873-31881
    • Doppler, H.1    Storz, P.2
  • 109
    • 66849099601 scopus 로고    scopus 로고
    • Mitochondrial diacylglycerol initiates protein-kinase D1-mediated ROS signaling
    • C.F. Cowell, H. Doppler, I.K. Yan, A. Hausser, Y. Umezawa, and P. Storz Mitochondrial diacylglycerol initiates protein-kinase D1-mediated ROS signaling J. Cell Sci. 122 2009 919 928
    • (2009) J. Cell Sci. , vol.122 , pp. 919-928
    • Cowell, C.F.1    Doppler, H.2    Yan, I.K.3    Hausser, A.4    Umezawa, Y.5    Storz, P.6
  • 110
    • 25444449225 scopus 로고    scopus 로고
    • Protein kinase D mediates mitochondrion-to-nucleus signaling and detoxification from mitochondrial reactive oxygen species
    • P. Storz, H. Doppler, and A. Toker Protein kinase D mediates mitochondrion-to-nucleus signaling and detoxification from mitochondrial reactive oxygen species Mol. Cell. Biol. 25 2005 8520 8530
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8520-8530
    • Storz, P.1    Doppler, H.2    Toker, A.3
  • 111
    • 0038043212 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation
    • P. Storz, H. Doppler, F.J. Johannes, and A. Toker Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation J. Biol. Chem. 278 2003 17969 17976
    • (2003) J. Biol. Chem. , vol.278 , pp. 17969-17976
    • Storz, P.1    Doppler, H.2    Johannes, F.J.3    Toker, A.4
  • 112
    • 0037413711 scopus 로고    scopus 로고
    • Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway
    • P. Storz, and A. Toker Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway EMBO J. 22 2003 109 120
    • (2003) EMBO J. , vol.22 , pp. 109-120
    • Storz, P.1    Toker, A.2
  • 113
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • B.D. Manning, and L.C. Cantley AKT/PKB signaling: navigating downstream Cell 129 2007 1261 1274
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 115
    • 0036765743 scopus 로고    scopus 로고
    • Akt activation induced by lysophosphatidic acid and sphingosine-1- phosphate requires both mitogen-activated protein kinase kinase and p38 mitogen-activated protein kinase and is cell-line specific
    • L.M. Baudhuin, K.L. Cristina, J. Lu, and Y. Xu Akt activation induced by lysophosphatidic acid and sphingosine-1-phosphate requires both mitogen-activated protein kinase kinase and p38 mitogen-activated protein kinase and is cell-line specific Mol. Pharmacol. 62 2002 660 671
    • (2002) Mol. Pharmacol. , vol.62 , pp. 660-671
    • Baudhuin, L.M.1    Cristina, K.L.2    Lu, J.3    Xu, Y.4
  • 116
    • 34250809874 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate S1P2 and S1P3 receptor-mediated Akt activation protects against in vivo myocardial ischemia-reperfusion injury
    • C.K. Means, C.Y. Xiao, Z. Li, T. Zhang, J.H. Omens, I. Ishii, J. Chun, and J.H. Brown Sphingosine 1-phosphate S1P2 and S1P3 receptor-mediated Akt activation protects against in vivo myocardial ischemia-reperfusion injury Am. J. Physiol. Heart Circ. Physiol. 292 2007 H2944 H2951
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Means, C.K.1    Xiao, C.Y.2    Li, Z.3    Zhang, T.4    Omens, J.H.5    Ishii, I.6    Chun, J.7    Brown, J.H.8
  • 117
    • 45449115620 scopus 로고    scopus 로고
    • S1P1 receptor localization confers selectivity for Gi-mediated cAMP and contractile responses
    • C.K. Means, S. Miyamoto, J. Chun, and J.H. Brown S1P1 receptor localization confers selectivity for Gi-mediated cAMP and contractile responses J. Biol. Chem. 283 2008 11954 11963
    • (2008) J. Biol. Chem. , vol.283 , pp. 11954-11963
    • Means, C.K.1    Miyamoto, S.2    Chun, J.3    Brown, J.H.4
  • 119
    • 0035853775 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and activation of endothelial nitric-oxide synthase. differential regulation of Akt and MAP kinase pathways by EDG and bradykinin receptors in vascular endothelial cells
    • J. Igarashi, S.G. Bernier, and T. Michel Sphingosine 1-phosphate and activation of endothelial nitric-oxide synthase. differential regulation of Akt and MAP kinase pathways by EDG and bradykinin receptors in vascular endothelial cells J. Biol. Chem. 276 2001 12420 12426
    • (2001) J. Biol. Chem. , vol.276 , pp. 12420-12426
    • Igarashi, J.1    Bernier, S.G.2    Michel, T.3
  • 120
    • 58149092317 scopus 로고    scopus 로고
    • Focal adhesion kinase as a RhoA-activable signaling scaffold mediating Akt activation and cardiomyocyte protection
    • D.P. Del Re, S. Miyamoto, and J.H. Brown Focal adhesion kinase as a RhoA-activable signaling scaffold mediating Akt activation and cardiomyocyte protection J. Biol. Chem. 283 2008 35622 35629
    • (2008) J. Biol. Chem. , vol.283 , pp. 35622-35629
    • Del Re, D.P.1    Miyamoto, S.2    Brown, J.H.3
  • 121
    • 0034637556 scopus 로고    scopus 로고
    • Activation of NF-kappa B by bradykinin through a Galpha(q)- and Gbeta gamma-dependent pathway that involves phosphoinositide 3-kinase and Akt
    • P. Xie, D.D. Browning, N. Hay, N. Mackman, and R.D. Ye Activation of NF-kappa B by bradykinin through a Galpha(q)- and Gbeta gamma-dependent pathway that involves phosphoinositide 3-kinase and Akt J. Biol. Chem. 275 2000 24907 24914
    • (2000) J. Biol. Chem. , vol.275 , pp. 24907-24914
    • Xie, P.1    Browning, D.D.2    Hay, N.3    Mackman, N.4    Ye, R.D.5
  • 122
    • 0037047463 scopus 로고    scopus 로고
    • Adenosine-mediated activation of Akt/protein kinase B in the rat hippocampus in vitro and in vivo
    • L.M. Gervitz, D. Nalbant, S.C. Williams, and J.C. Fowler Adenosine-mediated activation of Akt/protein kinase B in the rat hippocampus in vitro and in vivo Neurosci. Lett. 328 2002 175 179
    • (2002) Neurosci. Lett. , vol.328 , pp. 175-179
    • Gervitz, L.M.1    Nalbant, D.2    Williams, S.C.3    Fowler, J.C.4
  • 123
    • 67650673258 scopus 로고    scopus 로고
    • Akt mediated mitochondrial protection in the heart: metabolic and survival pathways to the rescue
    • S. Miyamoto, A.N. Murphy, and J.H. Brown Akt mediated mitochondrial protection in the heart: metabolic and survival pathways to the rescue J. Bioenerg. Biomembr. 41 2009 169 180
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 169-180
    • Miyamoto, S.1    Murphy, A.N.2    Brown, J.H.3
  • 124
    • 33747384625 scopus 로고    scopus 로고
    • Akt promotes increased cardiomyocyte cycling and expansion of the cardiac progenitor cell population
    • N. Gude, J. Muraski, M. Rubio, J. Kajstura, E. Schaefer, P. Anversa, and M.A. Sussman Akt promotes increased cardiomyocyte cycling and expansion of the cardiac progenitor cell population Circ. Res. 99 2006 381 388
    • (2006) Circ. Res. , vol.99 , pp. 381-388
    • Gude, N.1    Muraski, J.2    Rubio, M.3    Kajstura, J.4    Schaefer, E.5    Anversa, P.6    Sussman, M.A.7
  • 125
    • 33845711358 scopus 로고    scopus 로고
    • Regulation of cardiac growth and coronary angiogenesis by the Akt/PKB signaling pathway
    • I. Shiojima, and K. Walsh Regulation of cardiac growth and coronary angiogenesis by the Akt/PKB signaling pathway Genes Dev. 20 2006 3347 3365
    • (2006) Genes Dev. , vol.20 , pp. 3347-3365
    • Shiojima, I.1    Walsh, K.2
  • 127
    • 0036237137 scopus 로고    scopus 로고
    • Akt phosphorylation and neuronal survival after traumatic brain injury in mice
    • N. Noshita, A. Lewen, T. Sugawara, and P.H. Chan Akt phosphorylation and neuronal survival after traumatic brain injury in mice Neurobiol. Dis. 9 2002 294 304
    • (2002) Neurobiol. Dis. , vol.9 , pp. 294-304
    • Noshita, N.1    Lewen, A.2    Sugawara, T.3    Chan, P.H.4
  • 128
    • 33747183699 scopus 로고    scopus 로고
    • Akt/GSK3beta survival signaling is involved in acute brain injury after subarachnoid hemorrhage in rats
    • H. Endo, C. Nito, H. Kamada, F. Yu, and P.H. Chan Akt/GSK3beta survival signaling is involved in acute brain injury after subarachnoid hemorrhage in rats Stroke 37 2006 2140 2146
    • (2006) Stroke , vol.37 , pp. 2140-2146
    • Endo, H.1    Nito, C.2    Kamada, H.3    Yu, F.4    Chan, P.H.5
  • 130
    • 13044305289 scopus 로고    scopus 로고
    • PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway
    • H. Sun, R. Lesche, D.M. Li, J. Liliental, H. Zhang, J. Gao, N. Gavrilova, B. Mueller, X. Liu, and H. Wu PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway Proc. Natl. Acad. Sci. U. S. A. 96 1999 6199 6204
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6199-6204
    • Sun, H.1    Lesche, R.2    Li, D.M.3    Liliental, J.4    Zhang, H.5    Gao, J.6    Gavrilova, N.7    Mueller, B.8    Liu, X.9    Wu, H.10
  • 134
    • 35848933939 scopus 로고    scopus 로고
    • HDL and its sphingosine-1-phosphate content in cardioprotection
    • P. Keul, K. Sattler, and B. Levkau HDL and its sphingosine-1-phosphate content in cardioprotection Heart Fail. Rev. 12 2007 301 306
    • (2007) Heart Fail. Rev. , vol.12 , pp. 301-306
    • Keul, P.1    Sattler, K.2    Levkau, B.3
  • 137
    • 50849090922 scopus 로고    scopus 로고
    • Combined sphingosine, S1P and ischemic postconditioning rescue the heart after protracted ischemia
    • D.A. Vessey, L. Li, M. Kelley, and J.S. Karliner Combined sphingosine, S1P and ischemic postconditioning rescue the heart after protracted ischemia Biochem. Biophys. Res. Commun. 375 2008 425 429
    • (2008) Biochem. Biophys. Res. Commun. , vol.375 , pp. 425-429
    • Vessey, D.A.1    Li, L.2    Kelley, M.3    Karliner, J.S.4
  • 139
    • 0036773971 scopus 로고    scopus 로고
    • FTY720: targeting G-protein-coupled receptors for sphingosine 1-phosphate in transplantation and autoimmunity
    • V. Brinkmann, and K.R. Lynch FTY720: targeting G-protein-coupled receptors for sphingosine 1-phosphate in transplantation and autoimmunity Curr. Opin. Immunol. 14 2002 569 575
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 569-575
    • Brinkmann, V.1    Lynch, K.R.2
  • 140
    • 77953200332 scopus 로고    scopus 로고
    • Pharmacological pre- and post-conditioning with the sphingosine-1- phosphate receptor modulator FTY720 after myocardial ischaemia-reperfusion
    • U. Hofmann, K. Hu, F. Walter, N. Burkard, G. Ertl, J. Bauersachs, O. Ritter, S. Frantz, and A. Bonz Pharmacological pre- and post-conditioning with the sphingosine-1-phosphate receptor modulator FTY720 after myocardial ischaemia-reperfusion Br. J. Pharmacol. 160 2010 1243 1251
    • (2010) Br. J. Pharmacol. , vol.160 , pp. 1243-1251
    • Hofmann, U.1    Hu, K.2    Walter, F.3    Burkard, N.4    Ertl, G.5    Bauersachs, J.6    Ritter, O.7    Frantz, S.8    Bonz, A.9
  • 141
    • 67650263679 scopus 로고    scopus 로고
    • Protective effects of sphingosine-1-phosphate receptor agonist treatment after myocardial ischaemia-reperfusion
    • U. Hofmann, N. Burkard, C. Vogt, A. Thoma, S. Frantz, G. Ertl, O. Ritter, and A. Bonz Protective effects of sphingosine-1-phosphate receptor agonist treatment after myocardial ischaemia-reperfusion Cardiovasc. Res. 83 2009 285 293
    • (2009) Cardiovasc. Res. , vol.83 , pp. 285-293
    • Hofmann, U.1    Burkard, N.2    Vogt, C.3    Thoma, A.4    Frantz, S.5    Ertl, G.6    Ritter, O.7    Bonz, A.8
  • 146
    • 14644408845 scopus 로고    scopus 로고
    • The heart rate decrease caused by acute FTY720 administration is mediated by the G protein-gated potassium channel I
    • L. Koyrakh, M.I. Roman, V. Brinkmann, and K. Wickman The heart rate decrease caused by acute FTY720 administration is mediated by the G protein-gated potassium channel I Am. J. Transplant. 5 2005 529 536
    • (2005) Am. J. Transplant. , vol.5 , pp. 529-536
    • Koyrakh, L.1    Roman, M.I.2    Brinkmann, V.3    Wickman, K.4
  • 147
    • 77953503635 scopus 로고    scopus 로고
    • S1P2 receptor-dependent Rho-kinase activation mediates vasoconstriction in the murine pulmonary circulation induced by sphingosine 1-phosphate
    • W.S. Szczepaniak, B.R. Pitt, and B.J. McVerry S1P2 receptor-dependent Rho-kinase activation mediates vasoconstriction in the murine pulmonary circulation induced by sphingosine 1-phosphate Am. J. Physiol. Lung Cell. Mol. Physiol. 299 2010 L137 L145
    • (2010) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.299
    • Szczepaniak, W.S.1    Pitt, B.R.2    Mcverry, B.J.3
  • 149
    • 0037162064 scopus 로고    scopus 로고
    • Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors
    • Y. Takuwa Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors Biochim. Biophys. Acta 1582 2002 112 120
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 112-120
    • Takuwa, Y.1
  • 150
    • 0037067769 scopus 로고    scopus 로고
    • Marked perinatal lethality and cellular signaling deficits in mice null for the two sphingosine 1-phosphate (S1P) receptors, S1P(2)/LP(B2)/EDG-5 and S1P(3)/LP(B3)/EDG-3
    • I. Ishii, X. Ye, B. Friedman, S. Kawamura, J.J. Contos, M.A. Kingsbury, A.H. Yang, G. Zhang, J.H. Brown, and J. Chun Marked perinatal lethality and cellular signaling deficits in mice null for the two sphingosine 1-phosphate (S1P) receptors, S1P(2)/LP(B2)/EDG-5 and S1P(3)/LP(B3)/EDG-3 J. Biol. Chem. 277 2002 25152 25159
    • (2002) J. Biol. Chem. , vol.277 , pp. 25152-25159
    • Ishii, I.1    Ye, X.2    Friedman, B.3    Kawamura, S.4    Contos, J.J.5    Kingsbury, M.A.6    Yang, A.H.7    Zhang, G.8    Brown, J.H.9    Chun, J.10
  • 151
    • 0035970539 scopus 로고    scopus 로고
    • Reperfusion-activated Akt kinase prevents apoptosis in transgenic mouse hearts overexpressing insulin-like growth factor-1
    • K. Yamashita, J. Kajstura, D.J. Discher, B.J. Wasserlauf, N.H. Bishopric, P. Anversa, and K.A. Webster Reperfusion-activated Akt kinase prevents apoptosis in transgenic mouse hearts overexpressing insulin-like growth factor-1 Circ. Res. 88 2001 609 614
    • (2001) Circ. Res. , vol.88 , pp. 609-614
    • Yamashita, K.1    Kajstura, J.2    Discher, D.J.3    Wasserlauf, B.J.4    Bishopric, N.H.5    Anversa, P.6    Webster, K.A.7
  • 153
    • 33748177384 scopus 로고    scopus 로고
    • Ischemic postconditioning protects remodeled myocardium via the PI3K-PKB/Akt reperfusion injury salvage kinase pathway
    • M. Zhu, J. Feng, E. Lucchinetti, G. Fischer, L. Xu, T. Pedrazzini, M.C. Schaub, and M. Zaugg Ischemic postconditioning protects remodeled myocardium via the PI3K-PKB/Akt reperfusion injury salvage kinase pathway Cardiovasc. Res. 72 2006 152 162
    • (2006) Cardiovasc. Res. , vol.72 , pp. 152-162
    • Zhu, M.1    Feng, J.2    Lucchinetti, E.3    Fischer, G.4    Xu, L.5    Pedrazzini, T.6    Schaub, M.C.7    Zaugg, M.8
  • 154
    • 33744918504 scopus 로고    scopus 로고
    • Cardiac protection by mitoKATP channels is dependent on Akt translocation from cytosol to mitochondria during late preconditioning
    • N. Ahmad, Y. Wang, K.H. Haider, B. Wang, Z. Pasha, O. Uzun, and M. Ashraf Cardiac protection by mitoKATP channels is dependent on Akt translocation from cytosol to mitochondria during late preconditioning Am. J. Physiol. Heart Circ. Physiol. 290 2006 H2402 H2408
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.290
    • Ahmad, N.1    Wang, Y.2    Haider, K.H.3    Wang, B.4    Pasha, Z.5    Uzun, O.6    Ashraf, M.7
  • 155
    • 0034683064 scopus 로고    scopus 로고
    • Ischemic preconditioning activates phosphatidylinositol-3-kinase upstream of protein kinase C
    • H. Tong, W. Chen, C. Steenbergen, and E. Murphy Ischemic preconditioning activates phosphatidylinositol-3-kinase upstream of protein kinase C Circ. Res. 87 2000 309 315
    • (2000) Circ. Res. , vol.87 , pp. 309-315
    • Tong, H.1    Chen, W.2    Steenbergen, C.3    Murphy, E.4
  • 156
    • 0036623989 scopus 로고    scopus 로고
    • PI3 kinase and not p42/p44 appears to be implicated in the protection conferred by ischemic preconditioning
    • M.M. Mocanu, R.M. Bell, and D.M. Yellon PI3 kinase and not p42/p44 appears to be implicated in the protection conferred by ischemic preconditioning J. Mol. Cell. Cardiol. 34 2002 661 668
    • (2002) J. Mol. Cell. Cardiol. , vol.34 , pp. 661-668
    • Mocanu, M.M.1    Bell, R.M.2    Yellon, D.M.3
  • 159
    • 0037134431 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria
    • F. Tsuruta, N. Masuyama, and Y. Gotoh The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria J. Biol. Chem. 277 2002 14040 14047
    • (2002) J. Biol. Chem. , vol.277 , pp. 14040-14047
    • Tsuruta, F.1    Masuyama, N.2    Gotoh, Y.3
  • 161
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • S.R. Datta, H. Dudek, X. Tao, S. Masters, H. Fu, Y. Gotoh, and M.E. Greenberg Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery Cell 91 1997 231 241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7
  • 162
    • 84860134497 scopus 로고    scopus 로고
    • The mPTP and its regulatory proteins: final common targets of signalling pathways for protection against necrosis
    • T. Miura, and M. Tanno The mPTP and its regulatory proteins: final common targets of signalling pathways for protection against necrosis Cardiovasc. Res. 94 2012 181 189
    • (2012) Cardiovasc. Res. , vol.94 , pp. 181-189
    • Miura, T.1    Tanno, M.2
  • 163
    • 39449114808 scopus 로고    scopus 로고
    • Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II
    • S. Miyamoto, A.N. Murphy, and J.H. Brown Akt mediates mitochondrial protection in cardiomyocytes through phosphorylation of mitochondrial hexokinase-II Cell Death Differ. 15 2008 521 529
    • (2008) Cell Death Differ. , vol.15 , pp. 521-529
    • Miyamoto, S.1    Murphy, A.N.2    Brown, J.H.3
  • 164
    • 0034848312 scopus 로고    scopus 로고
    • A novel cardioprotective role of RhoA: new signaling mechanism for adenosine
    • J.E. Lee, G. Bokoch, and B.T. Liang A novel cardioprotective role of RhoA: new signaling mechanism for adenosine FASEB J. 15 2001 1886 1894
    • (2001) FASEB J. , vol.15 , pp. 1886-1894
    • Lee, J.E.1    Bokoch, G.2    Liang, B.T.3
  • 168
    • 74449093467 scopus 로고    scopus 로고
    • Sphingosine kinase 1 regulates the expression of proinflammatory cytokines and nitric oxide in activated microglia
    • D. Nayak, Y. Huo, W.X. Kwang, P.N. Pushparaj, S.D. Kumar, E.A. Ling, and S.T. Dheen Sphingosine kinase 1 regulates the expression of proinflammatory cytokines and nitric oxide in activated microglia Neuroscience 166 2010 132 144
    • (2010) Neuroscience , vol.166 , pp. 132-144
    • Nayak, D.1    Huo, Y.2    Kwang, W.X.3    Pushparaj, P.N.4    Kumar, S.D.5    Ling, E.A.6    Dheen, S.T.7
  • 170
    • 3042743990 scopus 로고    scopus 로고
    • FTY720: Sphingosine 1-phosphate receptor-1 in the control of lymphocyte egress and endothelial barrier function
    • V. Brinkmann, J.G. Cyster, and T. Hla FTY720: sphingosine 1-phosphate receptor-1 in the control of lymphocyte egress and endothelial barrier function Am. J. Transplant. 4 2004 1019 1025
    • (2004) Am. J. Transplant. , vol.4 , pp. 1019-1025
    • Brinkmann, V.1    Cyster, J.G.2    Hla, T.3
  • 173
    • 35348970884 scopus 로고    scopus 로고
    • Brain penetration of the oral immunomodulatory drug FTY720 and its phosphorylation in the central nervous system during experimental autoimmune encephalomyelitis: Consequences for mode of action in multiple sclerosis
    • C.A. Foster, L.M. Howard, A. Schweitzer, E. Persohn, P.C. Hiestand, B. Balatoni, R. Reuschel, C. Beerli, M. Schwartz, and A. Billich Brain penetration of the oral immunomodulatory drug FTY720 and its phosphorylation in the central nervous system during experimental autoimmune encephalomyelitis: consequences for mode of action in multiple sclerosis J. Pharmacol. Exp. Ther. 323 2007 469 475
    • (2007) J. Pharmacol. Exp. Ther. , vol.323 , pp. 469-475
    • Foster, C.A.1    Howard, L.M.2    Schweitzer, A.3    Persohn, E.4    Hiestand, P.C.5    Balatoni, B.6    Reuschel, R.7    Beerli, C.8    Schwartz, M.9    Billich, A.10
  • 175
    • 39049125218 scopus 로고    scopus 로고
    • FTY720 modulates human oligodendrocyte progenitor process extension and survival
    • V.E. Miron, C.G. Jung, H.J. Kim, T.E. Kennedy, B. Soliven, and J.P. Antel FTY720 modulates human oligodendrocyte progenitor process extension and survival Ann. Neurol. 63 2008 61 71
    • (2008) Ann. Neurol. , vol.63 , pp. 61-71
    • Miron, V.E.1    Jung, C.G.2    Kim, H.J.3    Kennedy, T.E.4    Soliven, B.5    Antel, J.P.6
  • 176
    • 34047253376 scopus 로고    scopus 로고
    • Phosphorylated FTY720 stimulates ERK phosphorylation in astrocytes via S1P receptors
    • M. Osinde, F. Mullershausen, and K.K. Dev Phosphorylated FTY720 stimulates ERK phosphorylation in astrocytes via S1P receptors Neuropharmacology 52 2007 1210 1218
    • (2007) Neuropharmacology , vol.52 , pp. 1210-1218
    • Osinde, M.1    Mullershausen, F.2    Dev, K.K.3
  • 179
    • 33745700262 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates PC-3 prostate cancer cell Matrigel invasion through activation of RhoA and NF-kappaB activity
    • Y.S. Hwang, J.C. Hodge, N. Sivapurapu, and P.F. Lindholm Lysophosphatidic acid stimulates PC-3 prostate cancer cell Matrigel invasion through activation of RhoA and NF-kappaB activity Mol. Carcinog. 45 2006 518 529
    • (2006) Mol. Carcinog. , vol.45 , pp. 518-529
    • Hwang, Y.S.1    Hodge, J.C.2    Sivapurapu, N.3    Lindholm, P.F.4
  • 180
    • 80054078065 scopus 로고    scopus 로고
    • PLCepsilon cooperates with the NF-kappaB pathway to augment TNFalpha-stimulated CCL2/MCP1 expression in human keratinocyte
    • Y. Harada, H. Edamatsu, and T. Kataoka PLCepsilon cooperates with the NF-kappaB pathway to augment TNFalpha-stimulated CCL2/MCP1 expression in human keratinocyte Biochem. Biophys. Res. Commun. 414 2011 106 111
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 106-111
    • Harada, Y.1    Edamatsu, H.2    Kataoka, T.3
  • 181
    • 33847012148 scopus 로고    scopus 로고
    • Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB
    • T.T. Chiu, W.Y. Leung, M.P. Moyer, R.M. Strieter, and E. Rozengurt Protein kinase D2 mediates lysophosphatidic acid-induced interleukin 8 production in nontransformed human colonic epithelial cells through NF-kappaB Am. J. Physiol. Cell Physiol. 292 2007 C767 C777
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Chiu, T.T.1    Leung, W.Y.2    Moyer, M.P.3    Strieter, R.M.4    Rozengurt, E.5
  • 182
    • 79955061032 scopus 로고    scopus 로고
    • Protein kinase D signaling: multiple biological functions in health and disease
    • E. Rozengurt Protein kinase D signaling: multiple biological functions in health and disease Physiology (Bethesda) 26 2011 23 33
    • (2011) Physiology (Bethesda) , vol.26 , pp. 23-33
    • Rozengurt, E.1


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