메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 159-167

Signal transduction through lipid second messengers

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CARRIER PROTEIN; CERAMIDE; DIACYLGLYCEROL; GLYCEROLIPID; LIPID; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE D; PROTEIN KINASE C; SPHINGOLIPID;

EID: 0029996139     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80061-5     Document Type: Article
Times cited : (479)

References (82)
  • 1
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y: Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992, 258:607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 2
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y: Protein kinase C and lipid signaling for sustained cellular responses. FASEB J 1995, 9:484-496.
    • (1995) FASEB J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 3
    • 0027994349 scopus 로고
    • The sphingomyelin cycles and the second messenger function of ceramide
    • Hannun Y: The sphingomyelin cycles and the second messenger function of ceramide. J Biol Chem 1994, 269:3125-3128.
    • (1994) J Biol Chem , vol.269 , pp. 3125-3128
    • Hannun, Y.1
  • 4
    • 0028297068 scopus 로고
    • The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling
    • Kolesnick R, Golde DW: The sphingomyelin pathway in tumor necrosis factor and interleukin-1 signaling. Cell 1994, 77:325-328.
    • (1994) Cell , vol.77 , pp. 325-328
    • Kolesnick, R.1    Golde, D.W.2
  • 5
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr Opin Cell Biol 1995, 7:183-189.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 183-189
    • Lee, S.B.1    Rhee, S.G.2
  • 6
    • 0027185354 scopus 로고
    • An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling
    • Thomas GMH, Cunningham E, Fensome A, Ball A, Totty NF, Truong O, Hsuan JJ, Cockcroft S: An essential role for phosphatidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling. Cell 1993, 74:919-928.
    • (1993) Cell , vol.74 , pp. 919-928
    • Thomas, G.M.H.1    Cunningham, E.2    Fensome, A.3    Ball, A.4    Totty, N.F.5    Truong, O.6    Hsuan, J.J.7    Cockcroft, S.8
  • 7
    • 0029009762 scopus 로고
    • Requirement for phosphatidylinositol transfer protein in epidermal growth factor signaling
    • Kauffmann-Zeh A, Thomas GMH, Ball A, Prosser S, Cunningham E, Cockcroft S, Hsuan JJ: Requirement for phosphatidylinositol transfer protein in epidermal growth factor signaling. Science 1995, 268:1188-1190. These studies define a critical role for PITP in signaling through the phosphoinositide pathway; PITP ensures the adequacy of quantity of substrate.
    • (1995) Science , vol.268 , pp. 1188-1190
    • Kauffmann-Zeh, A.1    Thomas, G.M.H.2    Ball, A.3    Prosser, S.4    Cunningham, E.5    Cockcroft, S.6    Hsuan, J.J.7
  • 8
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide
    • Liscovitch M, Cantley LC: Signal transduction and membrane traffic: the PITP/phosphoinositide. Cell 1995, 81:659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 9
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton JH: Phosphatidylcholine breakdown and signal transduction. Biochim Biophys Acta 1994, 1212:26-42.
    • (1994) Biochim Biophys Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 10
    • 0027291696 scopus 로고
    • Intracellular signalling mediated by protein-tyrosine kinases: Networking through phospholipid metabolism
    • Foster DA: Intracellular signalling mediated by protein-tyrosine kinases: networking through phospholipid metabolism. Cell Signal 1993, 5:389-399.
    • (1993) Cell Signal , vol.5 , pp. 389-399
    • Foster, D.A.1
  • 11
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar WH: Lysophosphatidic acid, a multifunctional phospholipid messenger. J Biol Chem 1995, 270:12949-12952.
    • (1995) J Biol Chem , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 12
    • 0027142022 scopus 로고
    • ADP ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown HA, Gutowski S, Moomaw CR, Slaughter C, Sternweis PC: ADP ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 1993, 75:1137-1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Sternweis, P.C.5
  • 14
    • 0027138873 scopus 로고
    • ARF signaling: A potential role for phospholipase D in membrane traffic
    • Kahn RA, Yucel JK, Malhotra V: ARF signaling: a potential role for phospholipase D in membrane traffic. Cell 1993, 75:1045-1048.
    • (1993) Cell , vol.75 , pp. 1045-1048
    • Kahn, R.A.1    Yucel, J.K.2    Malhotra, V.3
  • 15
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase activating protein and acid phospholipids
    • Randazzo PA, Kahn RA: GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase activating protein and acid phospholipids. J Biol Chem 1994, 269:10758-10763.
    • (1994) J Biol Chem , vol.269 , pp. 10758-10763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 16
    • 0029075145 scopus 로고
    • Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain
    • Brown HA, Gutowski S, Kahn RA, Sternweis PC: Partial purification and characterization of Arf-sensitive phospholipase D from porcine brain. J Biol Chem 1995, 270:14935-14943. This paper discusses the purification of the mammalian Arf-dependent PLD and describes the loss of PLD activity at the final stages of purification, suggesting that PLD requires multiple factors for activity.
    • (1995) J Biol Chem , vol.270 , pp. 14935-14943
    • Brown, H.A.1    Gutowski, S.2    Kahn, R.A.3    Sternweis, P.C.4
  • 17
    • 0029020350 scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • Singer WD, Brown AH, Bokach GM, Sternweis PC: Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. J Biol Chem 1995, 270:14944-14950.
    • (1995) J Biol Chem , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, A.H.2    Bokach, G.M.3    Sternweis, P.C.4
  • 18
    • 0027943755 scopus 로고
    • Purification and characterization of phosphatidylcholine phospholipase D from pig lung
    • Okamura S, Yamashita S: Purification and characterization of phosphatidylcholine phospholipase D from pig lung. J Biol Chem 1994, 269:31207-31213.
    • (1994) J Biol Chem , vol.269 , pp. 31207-31213
    • Okamura, S.1    Yamashita, S.2
  • 19
    • 0029584034 scopus 로고    scopus 로고
    • Phospholipase D signaling is essential for meiosis
    • in press. This paper describes the cloning of a yeast PLD by virtue of the requirement of PLD for meiosis
    • Rose K, Rudge S, Frohman MA, Morris A, Engebrecht J: Phospholipase D signaling is essential for meiosis. Proc Natl Acad Sci USA 1996, in press. This paper describes the cloning of a yeast PLD by virtue of the requirement of PLD for meiosis.
    • (1996) Proc Natl Acad Sci USA
    • Rose, K.1    Rudge, S.2    Frohman, M.A.3    Morris, A.4    Engebrecht, J.5
  • 20
    • 0027983786 scopus 로고
    • Cloning and expression of phosphatidylcholine hydrolyzing phospholipase D from Rincus communis L
    • Wang X, Xu L, Zheng L: Cloning and expression of phosphatidylcholine hydrolyzing phospholipase D from Rincus communis L. J Biol Chem 1994, 269:20312-20317.
    • (1994) J Biol Chem , vol.269 , pp. 20312-20317
    • Wang, X.1    Xu, L.2    Zheng, L.3
  • 21
    • 0029564902 scopus 로고
    • Human Art-activated phosphatidylcholine-specific phospholipase D defines a new highly conserved gene family
    • Hammond SM, Altshuller YM, Sung TC, Rudge SA, Ross K, Engebrecht J, Morris AJ, Frohman MA: Human Art-activated phosphatidylcholine-specific phospholipase D defines a new highly conserved gene family. J Biol Chem 1995, 270:29640-29643. This paper describes the cloning of a mammalian PLD by using conserved sequences from a yeast PLD and a plant PLD.
    • (1995) J Biol Chem , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.C.3    Rudge, S.A.4    Ross, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 22
    • 0028921344 scopus 로고
    • Ras mediates the activation of phospholipase D by v-Src
    • Jiang H, Lu Z, Luo J-Q, Wolfman A, Foster DA: Ras mediates the activation of phospholipase D by v-Src. J Biol Chem 1995, 270:6006-6009. This paper implicated a role for Ras in the activation of PLD by the Src oncoprotein.
    • (1995) J Biol Chem , vol.270 , pp. 6006-6009
    • Jiang, H.1    Lu, Z.2    Luo, J.-Q.3    Wolfman, A.4    Foster, D.A.5
  • 23
    • 0028818914 scopus 로고
    • Involvement of Ral GTPase in v-Src-induced phospholipase D activation
    • Jiang H, Luo J-Q, Urano T, Frankel P, Lu Z, Foster DA, Feig LA: Involvement of Ral GTPase in v-Src-induced phospholipase D activation. Nature 1995, 3:409-412. This paper reports that the small GTPase Ral interacts with PLD, and is required for the activation of PLD by Src.
    • (1995) Nature , vol.3 , pp. 409-412
    • Jiang, H.1    Luo, J.-Q.2    Urano, T.3    Frankel, P.4    Lu, Z.5    Foster, D.A.6    Feig, L.A.7
  • 24
    • 0027372389 scopus 로고
    • Neutrophil phospholipase D is activated by a membrane associated Rho family small molecular weight GTP-binding protein
    • Bowman EP, Uhlinger DJ, Lambeth JD: Neutrophil phospholipase D is activated by a membrane associated Rho family small molecular weight GTP-binding protein. J Biol Chem 1993, 268:21509-21512.
    • (1993) J Biol Chem , vol.268 , pp. 21509-21512
    • Bowman, E.P.1    Uhlinger, D.J.2    Lambeth, J.D.3
  • 25
    • 0027999909 scopus 로고
    • Activation of rat liver phospholipase D by the small GTP-binding protein RhoA
    • Malcolm KC, Ross AH, Qiu R-G, Symons M, Exton JH: Activation of rat liver phospholipase D by the small GTP-binding protein RhoA. J Biol Chem 1994, 269:25951-25954.
    • (1994) J Biol Chem , vol.269 , pp. 25951-25954
    • Malcolm, K.C.1    Ross, A.H.2    Qiu, R.-G.3    Symons, M.4    Exton, J.H.5
  • 27
    • 0029364428 scopus 로고
    • Seeing two domains
    • Newton AC: Seeing two domains. Curr Biol 1995, 5:973-976.
    • (1995) Curr Biol , vol.5 , pp. 973-976
    • Newton, A.C.1
  • 28
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator binding domain of protein kinase Cγ in complex with phorbol ester
    • Zhang G, Kazanictz MG, Blumberg PM, Hurley JH: Crystal structure of the Cys2 activator binding domain of protein kinase Cγ in complex with phorbol ester. Cell 1995, 81:917-924. The crystallization of the Cys2 region of the C1 domain of PKCγ in complex with phorbol ester allows for direct evaluation of lipid-protein signaling interactions at the atomic level.
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanictz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 29
    • 0028986240 scopus 로고
    • 2+/phospholipid-binding fold
    • 2+/phospholipid-binding fold. Cell 1995, 80:929-938. Crystallization of the C2 domain of synaptotagmin provides information concerning the role of calcium and acidic phospholipids in PKC translocation and activation.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuls, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 30
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D: Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 1995, 268:247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 31
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: A homolog of the beta subunit of G proteins
    • Ron D, Chen CH, Caldwell J, Jamieson L, Orr E, Mochly-Rosen D: Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins. Proc Natl Acad Sci USA 1994, 91:839-843. Cloning of the intracellular PKC receptor, which is detailed in this paper, should provide important information concerning the mechanisms of PKC activation and translocation.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 839-843
    • Ron, D.1    Chen, C.H.2    Caldwell, J.3    Jamieson, L.4    Orr, E.5    Mochly-Rosen, D.6
  • 32
    • 0028255915 scopus 로고
    • Lysophosphatidic acid possesses dual action in cell proliferation
    • Tigyi G, Dyer DL, Miledi R: Lysophosphatidic acid possesses dual action in cell proliferation. Proc Natl Acad Sci USA 1994, 91:1908-1912.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1908-1912
    • Tigyi, G.1    Dyer, D.L.2    Miledi, R.3
  • 33
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink K, Van Corven EJ, Hengeveld T, Morii N, Narumiya S, Moolenaar WH: Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J Cell Biol 1994, 126:801-810.
    • (1994) J Cell Biol , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 34
    • 0028091046 scopus 로고
    • Protein tyrosine phosphorylation induced by lysophosphatidic acid in Rat-1 fibroblasts. Evidence that phosphorylation of MAP kinase is mediated by the Gi-p21 ras pathway
    • Hordijk PL, Verlaan I, Van Corven EJ, Moolenaar WH: Protein tyrosine phosphorylation induced by lysophosphatidic acid in Rat-1 fibroblasts. Evidence that phosphorylation of MAP kinase is mediated by the Gi-p21 ras pathway. J Biol Chem 1994, 269:645-651. This study suggests an interesting model in which LPA-induced phosphorylation of MAPK is mediated by p21Ras, and tyrosine phosphorylation of other substrates, including focal adhesion kinase, is mediated by PLC activation.
    • (1994) J Biol Chem , vol.269 , pp. 645-651
    • Hordijk, P.L.1    Verlaan, I.2    Van Corven, E.J.3    Moolenaar, W.H.4
  • 35
    • 0025283928 scopus 로고
    • An update of the enzymology and regulation of sphingomyelin metabolism
    • Merrill AH Jr, Jones DD: An update of the enzymology and regulation of sphingomyelin metabolism. Biochim Biophys Acta 1990, 1044:1-12.
    • (1990) Biochim Biophys Acta , vol.1044 , pp. 1-12
    • Merrill A.H., Jr.1    Jones, D.D.2
  • 36
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann K, Schutze S, Machleidt T, Witte O, Kronke M: Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling. Cell 1994, 78:1005-1015. This paper proposes that different domains of the 55kDa TNF receptor activate distinct sphingomyelinases to signal specific biological effects.
    • (1994) Cell , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    Machleidt, T.3    Witte, O.4    Kronke, M.5
  • 37
    • 0027984782 scopus 로고
    • Processing of human acid sphingomyelinase in normal and I-cell fibroblasts
    • Hurwitz R, Ferlinz K, Vielhaber G, Moczall H, Sandhoff K: Processing of human acid sphingomyelinase in normal and I-cell fibroblasts. J Biol Chem 1994, 269:5440-5445.
    • (1994) J Biol Chem , vol.269 , pp. 5440-5445
    • Hurwitz, R.1    Ferlinz, K.2    Vielhaber, G.3    Moczall, H.4    Sandhoff, K.5
  • 38
    • 0027978352 scopus 로고
    • Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle
    • Linardic LA, Hannun YA: Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle. J Biol Chem 1994, 269:23530-23537. These studies show that the cytokine-responsive sphingomyelin pool is located on the inner surface of the plasma membrane.
    • (1994) J Biol Chem , vol.269 , pp. 23530-23537
    • Linardic, L.A.1    Hannun, Y.A.2
  • 39
    • 0029014350 scopus 로고
    • Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease)
    • Otterbach B, Stoeffel W: Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease). Cell 1995, 81:1053-1061.
    • (1995) Cell , vol.81 , pp. 1053-1061
    • Otterbach, B.1    Stoeffel, W.2
  • 41
    • 0027968517 scopus 로고
    • Renaturation and TNFα stimulation of a 97 kDa ceramide-activated protein kinase
    • Liu J, Mathias S, Yang Z, Kolesnick RN: Renaturation and TNFα stimulation of a 97 kDa ceramide-activated protein kinase. J Biol Chem 1994, 269:3047-3052.
    • (1994) J Biol Chem , vol.269 , pp. 3047-3052
    • Liu, J.1    Mathias, S.2    Yang, Z.3    Kolesnick, R.N.4
  • 42
    • 0026723048 scopus 로고
    • Ceramide stimulates a cytosolic protein phosphatase
    • Dobrowsky RT, Hannun YA: Ceramide stimulates a cytosolic protein phosphatase. J Biol Chem 1992, 267:5048-5051.
    • (1992) J Biol Chem , vol.267 , pp. 5048-5051
    • Dobrowsky, R.T.1    Hannun, Y.A.2
  • 44
    • 0027965006 scopus 로고
    • Protein kinase C isoform is critical for kappa B-dependent promoter activation by sphingomyelinase
    • Lozano J, Berra E, Municio MM, Diaz-Meco MT, Dominguez I, Sanz L, Moscat J: Protein kinase C isoform is critical for kappa B-dependent promoter activation by sphingomyelinase. J Biol Chem 1994, 269:19200-19202. This paper defines PKCζ as a target for ceramide.
    • (1994) J Biol Chem , vol.269 , pp. 19200-19202
    • Lozano, J.1    Berra, E.2    Municio, M.M.3    Diaz-Meco, M.T.4    Dominguez, I.5    Sanz, L.6    Moscat, J.7
  • 45
    • 0029003788 scopus 로고
    • PKC ζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Muller G, Ayoub M, Storz P, Rennecke J, Fabbro D, Pfizenmaier K: PKC ζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO J 1995,14:1961-1969.
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 46
    • 0027197994 scopus 로고
    • Substrate recognition by ceramide-activated protein kinase: Evidence that kinase activity is proline-directed
    • Joseph CK, Byun HS, Bittman R, Kolesnick RN: Substrate recognition by ceramide-activated protein kinase: evidence that kinase activity is proline-directed. J Biol Chem 1993, 268:20002-20006.
    • (1993) J Biol Chem , vol.268 , pp. 20002-20006
    • Joseph, C.K.1    Byun, H.S.2    Bittman, R.3    Kolesnick, R.N.4
  • 47
    • 0028122397 scopus 로고
    • Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction
    • Wolff RA, Dobrowsky TR, Bielawska, A, Hannun YA: Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction. J Biol Chem 1994, 269:19605-19609.
    • (1994) J Biol Chem , vol.269 , pp. 19605-19609
    • Wolff, R.A.1    Dobrowsky, T.R.2    Bielawska, A.3    Hannun, Y.A.4
  • 48
    • 0028838235 scopus 로고
    • Ceramide-activated protein kinase is a Raf kinase
    • Yao B, Zhang Y, Delikat S, Mathias S, Basu S, Kolesnick R: Ceramide-activated protein kinase is a Raf kinase. Nature 1995, 378:307-310. These investigations define a mechanism which links ceramide signaling to the MAPK pathway.
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3    Mathias, S.4    Basu, S.5    Kolesnick, R.6
  • 49
    • 0028246298 scopus 로고
    • Bacterial lipopolysaccharide has structural similarity to ceramide and stimulates ceramide-activated protein kinase in myeloid cells
    • Joseph CK, Wright SD, Bornmann WG, Randolph JT, Kumar ER, Bittman R, Liu J, Kolesnick RN: Bacterial lipopolysaccharide has structural similarity to ceramide and stimulates ceramide-activated protein kinase in myeloid cells. J Biol Chem 1994, 269:17606-17610. These investigations show that the lipid A moiety of LPS contains a ceramide-like structure, and suggest that LPS mimics TNF and IL-1 action by taking on the second messenger function of ceramide.
    • (1994) J Biol Chem , vol.269 , pp. 17606-17610
    • Joseph, C.K.1    Wright, S.D.2    Bornmann, W.G.3    Randolph, J.T.4    Kumar, E.R.5    Bittman, R.6    Liu, J.7    Kolesnick, R.N.8
  • 52
    • 0028287960 scopus 로고
    • Ionizing radiation acts on cellular membranes to generate ceramide and initiate apoptosis
    • Haimovitz-Friedman A, Kan C-C, Ehleiter D, Persaud RS, McLoughlin M, Fuks Z, Kolesnick RN: Ionizing radiation acts on cellular membranes to generate ceramide and initiate apoptosis. J Exp Med 1994, 180:525-535. These investigations propose that ionizing radiation may initiate a form of apoptosis by direct activation of membrane sphingomyelinase.
    • (1994) J Exp Med , vol.180 , pp. 525-535
    • Haimovitz-Friedman, A.1    Kan, C.-C.2    Ehleiter, D.3    Persaud, R.S.4    McLoughlin, M.5    Fuks, Z.6    Kolesnick, R.N.7
  • 53
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • Bose R, Verheij M, Haimovitz-Friedman A, Scotto K, Fuks Z, Kolesnick R: Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals. Cell 1995, 82:405-414. These studies propose that ceramide synthesis mediates daunorubicin-induced apoptosis.
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 54
    • 0028229012 scopus 로고
    • The stress-activated protein kinase subfamily of c-Jun kinases
    • Kyriakis JM, Banerjee P, Nikolakaki E, Dai T, Rubie EA, Ahmad MF, Avruch J, Woodgett JR: The stress-activated protein kinase subfamily of c-Jun kinases. Nature 1994, 369:156-160. This paper proposes that the sphingomyelin pathway might, in part, mediate the effect of stresses on c-Jun activation.
    • (1994) Nature , vol.369 , pp. 156-160
    • Kyriakis, J.M.1    Banerjee, P.2    Nikolakaki, E.3    Dai, T.4    Rubie, E.A.5    Ahmad, M.F.6    Avruch, J.7    Woodgett, J.R.8
  • 56
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
    • Hannun YA, Bell RM: Functions of sphingolipids and sphingolipid breakdown products in cellular regulation. Science 1989, 243:500-507.
    • (1989) Science , vol.243 , pp. 500-507
    • Hannun, Y.A.1    Bell, R.M.2
  • 57
    • 0025021423 scopus 로고
    • Sphingosine stimulates cellular proliferation via a protein kinase C-independent pathway
    • Zhang H, Buckley NE, Gibson K, Spiegel S: Sphingosine stimulates cellular proliferation via a protein kinase C-independent pathway. J Biol Chem 1990, 365:76-81.
    • (1990) J Biol Chem , vol.365 , pp. 76-81
    • Zhang, H.1    Buckley, N.E.2    Gibson, K.3    Spiegel, S.4
  • 58
    • 0028234366 scopus 로고
    • Stereospecificity of sphingosine-induced intracellular calcium mobilization and cellular proliferation
    • Olivera A, Zhang H, Carlson RO, Mattie ME, Schmidt RR, Spiegel S: Stereospecificity of sphingosine-induced intracellular calcium mobilization and cellular proliferation. J Biol Chem 1994, 289:17924-17930.
    • (1994) J Biol Chem , vol.289 , pp. 17924-17930
    • Olivera, A.1    Zhang, H.2    Carlson, R.O.3    Mattie, M.E.4    Schmidt, R.R.5    Spiegel, S.6
  • 59
    • 0028107081 scopus 로고
    • Disruption of sphingolipid metabolism and stimulation of DNa synthesis by fumonisin B1. a molecular mechanism for carcinogenesis associated with Fusarium moniliforme
    • Schroeder JJ, Crane HM, Xia J, Liotta DC, Merrill AH: Disruption of sphingolipid metabolism and stimulation of DNA synthesis by fumonisin B1. A molecular mechanism for carcinogenesis associated with Fusarium moniliforme. J Biol Chem 1994, 269:3475-3481.
    • (1994) J Biol Chem , vol.269 , pp. 3475-3481
    • Schroeder, J.J.1    Crane, H.M.2    Xia, J.3    Liotta, D.C.4    Merrill, A.H.5
  • 60
    • 0029075192 scopus 로고
    • Serine palmitoyltransferase is the primary target of a sphingosine-like immunosuppressant, ISP-1/myriocin
    • Miyake Y, Kozutsumi Y, Nakamura S, Fujita T, Kawasaki T: Serine palmitoyltransferase is the primary target of a sphingosine-like immunosuppressant, ISP-1/myriocin. Biochem Biophys Res Commun 1995, 211:396-403.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 396-403
    • Miyake, Y.1    Kozutsumi, Y.2    Nakamura, S.3    Fujita, T.4    Kawasaki, T.5
  • 61
    • 0027371722 scopus 로고
    • Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens
    • Olivera A, Spiegel S: Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens. Nature 1993, 365:557-560.
    • (1993) Nature , vol.365 , pp. 557-560
    • Olivera, A.1    Spiegel, S.2
  • 63
    • 0028848344 scopus 로고
    • Differential regulation of sphingomyelinase and ceramidase activity by growth factor and cytokines: Implication for cellular proliferation and differentiation
    • Coroneos E, Martinez M, McKenna S, Kester M: Differential regulation of sphingomyelinase and ceramidase activity by growth factor and cytokines: implication for cellular proliferation and differentiation J Biol Chem 1995, 270:23305-23309. These investigations suggest that the pleiotropic responses induced by growth factors, and by cytokines involved in cell growth and survival, might be a consequence of regulation of the levels of distinct sphingolipid-derived second messengers.
    • (1995) J Biol Chem , vol.270 , pp. 23305-23309
    • Coroneos, E.1    Martinez, M.2    McKenna, S.3    Kester, M.4
  • 64
    • 0028900748 scopus 로고
    • Induction of apoptosis by sphingosine in human leukemic HL-60 cells: A possible endogenous modulator of apoptotic DNa fragmentation occurring during phorbol ester-induced differentiation
    • Ohta H, Sweeney EA, Masamune A, Yatomi Y, Hakomori S, Igarashi Y: Induction of apoptosis by sphingosine in human leukemic HL-60 cells: a possible endogenous modulator of apoptotic DNA fragmentation occurring during phorbol ester-induced differentiation. Cancer Res 1995, 55:691-697.
    • (1995) Cancer Res , vol.55 , pp. 691-697
    • Ohta, H.1    Sweeney, E.A.2    Masamune, A.3    Yatomi, Y.4    Hakomori, S.5    Igarashi, Y.6
  • 65
    • 0028339322 scopus 로고
    • Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts
    • Gomez MA, Martin A, O'Brien L, Brindley DN: Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts. J Biol Chem 1994, 269:8937-8943.
    • (1994) J Biol Chem , vol.269 , pp. 8937-8943
    • Gomez, M.A.1    Martin, A.2    O'Brien, L.3    Brindley, D.N.4
  • 66
    • 0028109996 scopus 로고
    • Identification of a defect in the phospholipase D/diacylglycerol pathway in cellular senescence
    • Venable ME, Blobe GC, Obeid LM: Identification of a defect in the phospholipase D/diacylglycerol pathway in cellular senescence. J Biol Chem 1994, 269:26040-26044.
    • (1994) J Biol Chem , vol.269 , pp. 26040-26044
    • Venable, M.E.1    Blobe, G.C.2    Obeid, L.M.3
  • 67
    • 0027991078 scopus 로고
    • Sphingosine-1-phosphate, a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway
    • Mattie ME, Brooker G, Spiegel S: Sphingosine-1-phosphate, a putative second messenger, mobilizes calcium from internal stores via an inositol trisphosphate-independent pathway. J Biol Chem 1994, 269:3181-3188.
    • (1994) J Biol Chem , vol.269 , pp. 3181-3188
    • Mattie, M.E.1    Brooker, G.2    Spiegel, S.3
  • 68
    • 0028128763 scopus 로고
    • Sphingosine 1-phosphate generated in the endoplasmic reticulum membrane activates release of stored calcium
    • Ghosh TK, Bian J, Gill DL: Sphingosine 1-phosphate generated in the endoplasmic reticulum membrane activates release of stored calcium. J Biol Chem 1994, 269:22628-22635. Sphingosine is present in the endoplasmic reticulum, where it may be converted to SPP and release stored calcium.
    • (1994) J Biol Chem , vol.269 , pp. 22628-22635
    • Ghosh, T.K.1    Bian, J.2    Gill, D.L.3
  • 70
    • 0029079324 scopus 로고
    • Sphingosine-1-phosphate rapidly activates the MAP kinase pathway by a G-protein dependent mechanism
    • Wu J, Spiegel S, Sturgill TW: Sphingosine-1-phosphate rapidly activates the MAP kinase pathway by a G-protein dependent mechanism. J Biol Chem 1995, 270:11484-11488. This study shows that MAPK is a downstream effector for the mitogenic action of SPP.
    • (1995) J Biol Chem , vol.270 , pp. 11484-11488
    • Wu, J.1    Spiegel, S.2    Sturgill, T.W.3
  • 71
    • 0028322142 scopus 로고
    • Sphingosine 1-phosphate, a novel signaling molecule, stimulates DNA binding activity of AP-1 in quiescent 3T3 fibroblasts
    • Su Y, Rosenthal D, Smulson M, Spiegel S: Sphingosine 1-phosphate, a novel signaling molecule, stimulates DNA binding activity of AP-1 in quiescent 3T3 fibroblasts. J Biol Chem 1994, 269:16512-16517. This report suggests that SPP-induced DNA synthesis and cell division result from activation of the transcription factor AP-1, linking signal transduction by SPP to gene expression.
    • (1994) J Biol Chem , vol.269 , pp. 16512-16517
    • Su, Y.1    Rosenthal, D.2    Smulson, M.3    Spiegel, S.4
  • 72
    • 0028172435 scopus 로고
    • Sphingosine induces p125FAK and paxillin tyrosine phosphorylation, actin stress fiber formation, and focal contact assembly in Swiss 3T3 cells
    • Seufferlein T, Rozengurt E: Sphingosine induces p125FAK and paxillin tyrosine phosphorylation, actin stress fiber formation, and focal contact assembly in Swiss 3T3 cells. J Biol Chem 1994, 269:27610-27617.
    • (1994) J Biol Chem , vol.269 , pp. 27610-27617
    • Seufferlein, T.1    Rozengurt, E.2
  • 73
    • 0029052921 scopus 로고
    • Sphingosine-1-phosphate: A platelet-activating sphingolipid released from agonist-stimulated human platelets
    • Yatomi Y, Ruan F, Hakomori S, Igarashi Y: Sphingosine-1-phosphate: a platelet-activating sphingolipid released from agonist-stimulated human platelets. Blood 1995, 86:193-202. This is the first demonstration that SPP can be released from activated cells, suggesting that it may play a physiological role in thrombosis, hemostasis and natural wound healing.
    • (1995) Blood , vol.86 , pp. 193-202
    • Yatomi, Y.1    Ruan, F.2    Hakomori, S.3    Igarashi, Y.4
  • 74
    • 0028956049 scopus 로고
    • Involvement of a pertussis toxin sensitive G protein in the mitogenic signaling pathways of sphingosine-1-phosphate
    • Goodemote KA, Mattie ME, Berger A, Spiegel S: Involvement of a pertussis toxin sensitive G protein in the mitogenic signaling pathways of sphingosine-1-phosphate. J Biol Chem 1995, 270:10272-10277.
    • (1995) J Biol Chem , vol.270 , pp. 10272-10277
    • Goodemote, K.A.1    Mattie, M.E.2    Berger, A.3    Spiegel, S.4
  • 76
    • 0028046589 scopus 로고
    • Attenuation of ceramide-induced apoptosis by diglyceride and pharmacological activators of protein kinase C in human myeloid leukemia cells
    • Jarvis WD, Fornari FA Jr, Browning JL, Gewirtz DA, Kolesnick RN, Grant S: Attenuation of ceramide-induced apoptosis by diglyceride and pharmacological activators of protein kinase C in human myeloid leukemia cells. J Biol Chem 1994, 268:31685-31692. This paper details regulation of apoptosis via the sphingomyelin and phosphoinositide signaling systems; these two systems appear to coordinately regulate apoptosis in an opposing manner.
    • (1994) J Biol Chem , vol.268 , pp. 31685-31692
    • Jarvis, W.D.1    Fornari F.A., Jr.2    Browning, J.L.3    Gewirtz, D.A.4    Kolesnick, R.N.5    Grant, S.6
  • 78
    • 0029000942 scopus 로고
    • Ceramide: A signal for apoptosis or mitogenesis?
    • Kolesnick R, Fuks Z: Ceramide: a signal for apoptosis or mitogenesis? J Exp Med 1995, 181:1949-1952.
    • (1995) J Exp Med , vol.181 , pp. 1949-1952
    • Kolesnick, R.1    Fuks, Z.2
  • 79
    • 0027430787 scopus 로고
    • Ceramide 1-phosphate phosphatase activity in brain
    • Shinghal R, Scheller RH, Bajjalieh SM: Ceramide 1-phosphate phosphatase activity in brain. J Neurochem 1993, 61:2279-2285.
    • (1993) J Neurochem , vol.61 , pp. 2279-2285
    • Shinghal, R.1    Scheller, R.H.2    Bajjalieh, S.M.3
  • 80
    • 0027377618 scopus 로고
    • Detection and characterization of ceramide-1-phosphate phosphatase activity in rat liver plasma membrane
    • Boudker O, Futerman AH: Detection and characterization of ceramide-1-phosphate phosphatase activity in rat liver plasma membrane. J Biol Chem 1993, 268:22150-22155.
    • (1993) J Biol Chem , vol.268 , pp. 22150-22155
    • Boudker, O.1    Futerman, A.H.2
  • 81
    • 0028198427 scopus 로고
    • Sphingosine 1-phosphate metabolism in cultured skin fibroblasts: Evidence for the existence of a sphingosine phosphatase
    • Van Veldhoven PP, Mannaerts GP: Sphingosine 1-phosphate metabolism in cultured skin fibroblasts: evidence for the existence of a sphingosine phosphatase. Biochem J 1994, 299:567-601.
    • (1994) Biochem J , vol.299 , pp. 567-601
    • Van Veldhoven, P.P.1    Mannaerts, G.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.