메뉴 건너뛰기




Volumn 16, Issue , 2010, Pages 3-22

Phospholipase a in plant signal transduction

Author keywords

[No Author keywords available]

Indexed keywords


EID: 74949101590     PISSN: 18611370     EISSN: 18611362     Source Type: Book Series    
DOI: 10.1007/978-3-642-03873-0_1     Document Type: Article
Times cited : (13)

References (139)
  • 2
    • 33645895468 scopus 로고    scopus 로고
    • Citrus abscission and Arabidopsis plant decline in response to 5-chloro-3-methly-4-nitro-1H-pyrazole are mediated by lipid signaling
    • Alferez F, Singh S, Umbach AL, Hockema B, Burns JK (2005) Citrus abscission and Arabidopsis plant decline in response to 5-chloro-3-methly-4-nitro-1H-pyrazole are mediated by lipid signaling. Plant Cell Environ 28:1436-1449
    • (2005) Plant Cell Environ , vol.28 , pp. 1436-1449
    • Alferez, F.1    Singh, S.2    Umbach, A.L.3    Hockema, B.4    Burns, J.K.5
  • 3
    • 23044517301 scopus 로고    scopus 로고
    • Phosphate-limited Oat. The plasma membrane and the tonoplast as major targets for phospholipids to glycolipid replacement and stimulation of phospholipases in the plasma membrane
    • Andersson MX, Larsson KE, Tjellström H, Liljenberg C, Sandelius AS (2005) Phosphate-limited Oat. The plasma membrane and the tonoplast as major targets for phospholipids to glycolipid replacement and stimulation of phospholipases in the plasma membrane. J Biol Chem 280:27578-27586
    • (2005) J Biol Chem , vol.280 , pp. 27578-27586
    • Andersson, M.X.1    Larsson, K.E.2    Tjellström, H.3    Liljenberg, C.4    Sandelius, A.S.5
  • 4
    • 0001039947 scopus 로고
    • Stimulation by auxin of phospholipase A in membrane vesicles from an auxin-sensitive tissue is mediated by an auxin receptor
    • André B, Scherer GFE (1991) Stimulation by auxin of phospholipase A in membrane vesicles from an auxin-sensitive tissue is mediated by an auxin receptor. Planta 185:209-214
    • (1991) Planta , vol.185 , pp. 209-214
    • André, B.1    Scherer, G.F.E.2
  • 5
    • 0024287753 scopus 로고
    • Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning an abundant expression in a baculovirus vector
    • Andrews DL, Beames B, Summers MD, Park WD (1988) Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning an abundant expression in a baculovirus vector. Biochem J 252:199-206
    • (1988) Biochem J , vol.252 , pp. 199-206
    • Andrews, D.L.1    Beames, B.2    Summers, M.D.3    Park, W.D.4
  • 6
    • 33846517635 scopus 로고    scopus 로고
    • Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family
    • Aoki J, Inoue A, Makide K, Saiki N, Arai H (2007) Structure and function of extracellular phospholipase A1 belonging to the pancreatic lipase gene family. Biochimie 89:197-204
    • (2007) Biochimie , vol.89 , pp. 197-204
    • Aoki, J.1    Inoue, A.2    Makide, K.3    Saiki, N.4    Arai, H.5
  • 7
    • 33646384941 scopus 로고    scopus 로고
    • Receptors for auxin: Will it all end in TIRs?
    • Badescu GO, Napier RM (2006) Receptors for auxin: will it all end in TIRs? Trends Plant Sci. 11:217-223
    • (2006) Trends Plant Sci , vol.11 , pp. 217-223
    • Badescu, G.O.1    Napier, R.M.2
  • 8
    • 0141459685 scopus 로고    scopus 로고
    • Characterization of Arabidopsis secretory phospholipase A2-gamma cDNA and its enzymatic properties
    • Bahn SC, Lee HY, Kim HJ, Ryu SB, Shin JS (2003) Characterization of Arabidopsis secretory phospholipase A2-gamma cDNA and its enzymatic properties. FEBS Lett 553:113-118
    • (2003) Febs Lett , vol.553 , pp. 113-118
    • Bahn, S.C.1    Lee, H.Y.2    Kim, H.J.3    Ryu, S.B.4    Shin, J.S.5
  • 11
    • 33747887420 scopus 로고    scopus 로고
    • The role of phospholipase D in plant stress responses
    • Bargmann BOR, Munnik T (2006) The role of phospholipase D in plant stress responses. Curr OpinPlant Biol 9:515-522
    • (2006) Curr Opinplant Biol , vol.9 , pp. 515-522
    • Bargmann, B.O.R.1    Munnik, T.2
  • 12
    • 0032805963 scopus 로고    scopus 로고
    • Unsaturated fatty acids inhibit MP2C, a protein phosphatase 2C involved in the wound-induced MAP kinase pathway regulation
    • Baudouin E, Meskiene I, Hirt H (1999) Unsaturated fatty acids inhibit MP2C, a protein phosphatase 2C involved in the wound-induced MAP kinase pathway regulation. Plant J 20:343-348
    • (1999) Plant J , vol.20 , pp. 343-348
    • Baudouin, E.1    Meskiene, I.2    Hirt, H.3
  • 13
    • 0033827628 scopus 로고    scopus 로고
    • Receptor-mediated increase in cytoplasmic free calcium required for activation of pathogen defense in parsley
    • Blume B, Nürnberger T, Nass N, Scheel D (2000) Receptor-mediated increase in cytoplasmic free calcium required for activation of pathogen defense in parsley. Plant Cell 12:1425-1440
    • (2000) Plant Cell , vol.12 , pp. 1425-1440
    • Blume, B.1    Nürnberger, T.2    Nass, N.3    Scheel, D.4
  • 14
    • 33745453676 scopus 로고    scopus 로고
    • LucTrap vectors are tools to generate luciferase fusions for the quantification of transcript and protein abundance in vivo
    • Calderon-Villalobos LI, Kuhnle C, Li H, Rosso M, Weisshaar B, Schwechheimer C (2006) LucTrap vectors are tools to generate luciferase fusions for the quantification of transcript and protein abundance in vivo. Plant Physiol 141:3-14
    • (2006) Plant Physiol , vol.141 , pp. 3-14
    • Calderon-Villalobos, L.I.1    Kuhnle, C.2    Li, H.3    Rosso, M.4    Weisshaar, B.5    Schwechheimer, C.6
  • 16
    • 0030052327 scopus 로고    scopus 로고
    • Activation of phospholipase A by plant defense elicitors
    • Chandra S, Heinstein PF, Low PS (1996) Activation of phospholipase A by plant defense elicitors. Plant Physiol 110:979-986
    • (1996) Plant Physiol , vol.110 , pp. 979-986
    • Chandra, S.1    Heinstein, P.F.2    Low, P.S.3
  • 19
    • 0030614354 scopus 로고    scopus 로고
    • 2 superfamily of signal transduction enzymes
    • 2 superfamily of signal transduction enzymes. Trends Biochem Sci 22:1-2
    • (1997) Trends Biochem Sci , vol.22 , pp. 1-2
    • Dennis, E.A.1
  • 22
    • 2642542593 scopus 로고    scopus 로고
    • Auxin signaling and regulated protein degradation
    • Dharmasiri N, Estelle M (2004) Auxin signaling and regulated protein degradation. Trends Plant Sci 9:302-308
    • (2004) Trends Plant Sci , vol.9 , pp. 302-308
    • Dharmasiri, N.1    Estelle, M.2
  • 23
    • 19544379019 scopus 로고    scopus 로고
    • The F-box protein TIR1 is an auxin receptor
    • Dharmasiri N, Dharmasiri S, Estelle M (2005) The F-box protein TIR1 is an auxin receptor. Nature 435:441-445
    • (2005) Nature , vol.435 , pp. 441-445
    • Dharmasiri, N.1    Dharmasiri, S.2    Estelle, M.3
  • 24
    • 0033624577 scopus 로고    scopus 로고
    • Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes
    • Dhondt S, Geoffroy P, Stelmach BA, Legrand M, Heitz T (2000) Soluble phospholipase A2 activity is induced before oxylipin accumulation in tobacco mosaic virus-infected tobacco leaves and is contributed by patatin-like enzymes. Plant J 23:431-440
    • (2000) Plant J , vol.23 , pp. 431-440
    • Dhondt, S.1    Geoffroy, P.2    Stelmach, B.A.3    Legrand, M.4    Heitz, T.5
  • 25
    • 0036917719 scopus 로고    scopus 로고
    • Spatio-temporal expression of patatin-like lipid acyl hydrolases and accumulation of jasmonates in elicitor-treated tobacco leaves are not affected by endogenous levels of salicylic acid
    • Dhondt S, Gouzerh G, Muller A, Legrand M, Heitz T (2002) Spatio-temporal expression of patatin-like lipid acyl hydrolases and accumulation of jasmonates in elicitor-treated tobacco leaves are not affected by endogenous levels of salicylic acid. Plant J 32:749-762
    • (2002) Plant J , vol.32 , pp. 749-762
    • Dhondt, S.1    Gouzerh, G.2    Muller, A.3    Legrand, M.4    Heitz, T.5
  • 28
    • 84989749022 scopus 로고
    • Use of lysophosphatidylethanolamine, a natural lipid, to retard tomato leaf and fruit senescence
    • Farag KM, Palta JP (1993a) Use of lysophosphatidylethanolamine, a natural lipid, to retard tomato leaf and fruit senescence. Physiol Plant 87:515-524
    • (1993) Physiol Plant , vol.87 , pp. 515-524
    • Farag, K.M.1    Palta, J.P.2
  • 29
    • 0007085145 scopus 로고
    • Use of natural lipids to accelerate ripening and enhance storage life of tomato fruit with and without etephon
    • Farag KM, Palta JP (1993b) Use of natural lipids to accelerate ripening and enhance storage life of tomato fruit with and without etephon. Hortic Tech 3:62-65
    • (1993) Hortic Tech , vol.3 , pp. 62-65
    • Farag, K.M.1    Palta, J.P.2
  • 30
    • 0037310922 scopus 로고    scopus 로고
    • Selective desensitization of jasmonate- and pH-dependent signaling in the induction of benzophenanthridine biosynthesis in cells of Eschscholzia californica
    • Färber K, Schumann B, Miersch O, Roos W (2003) Selective desensitization of jasmonate- and pH-dependent signaling in the induction of benzophenanthridine biosynthesis in cells of Eschscholzia californica. Phytochemistry 62:491-500
    • (2003) Phytochemistry , vol.62 , pp. 491-500
    • Färber, K.1    Schumann, B.2    Miersch, O.3    Roos, W.4
  • 34
    • 0029020361 scopus 로고
    • 2 from the cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen
    • 2 from the cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen. J Biol Chem 270:15359-15367
    • (1995) J Biol Chem , vol.270 , pp. 15359-15367
    • Glover, S.1    Bayburt, T.2    Jonas, M.3    Chi, E.4    Gelb, M.H.5
  • 35
    • 0002647921 scopus 로고
    • Versuche und Hypothese zur Primärwirkung des Auxins beim Streckungswachstum
    • Hager A, Menzel H, Kraus A (1971) Versuche und Hypothese zur Primärwirkung des Auxins beim Streckungswachstum. Planta 100:47-75
    • (1971) Planta , vol.100 , pp. 47-75
    • Hager, A.1    Menzel, H.2    Kraus, A.3
  • 37
    • 0027172870 scopus 로고
    • Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli
    • Harper JF, Binder BM, Sussman MR (1993) Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli. Biochem 32:3282-3290
    • (1993) Biochem , vol.32 , pp. 3282-3290
    • Harper, J.F.1    Binder, B.M.2    Sussman, M.R.3
  • 39
    • 0034787011 scopus 로고    scopus 로고
    • Cloning, expression, purification and characterization of patatin, a novel phospholipase A
    • Hirschberg HJ, Simons JW, Dekker N, Egmond MR (2001) Cloning, expression, purification and characterization of patatin, a novel phospholipase A. Eur J Biochem 268:5037-5044
    • (2001) Eur J Biochem , vol.268 , pp. 5037-5044
    • Hirschberg, H.J.1    Simons, J.W.2    Dekker, N.3    Egmond, M.R.4
  • 40
    • 0036738078 scopus 로고    scopus 로고
    • Molecular identification of cytosolic, patatin-related phospholipases A from Arabidopsis with potential functions in plant signal transduction
    • Holk A, Rietz S, Zahn M, Paul RU, Quader H, Scherer GFE (2002) Molecular identification of cytosolic, patatin-related phospholipases A from Arabidopsis with potential functions in plant signal transduction. Plant Physiol 130:90-101
    • (2002) Plant Physiol , vol.130 , pp. 90-101
    • Holk, A.1    Rietz, S.2    Zahn, M.3    Paul, R.U.4    Quader, H.5    Scherer, G.F.E.6
  • 41
    • 0035115051 scopus 로고    scopus 로고
    • Cloning of an Arabidopsis patatin-like gene, STURDY, by activation tagging
    • Huang S, Cerny RE, Bhat DS, Brown SM (2001) Cloning of an Arabidopsis patatin-like gene, STURDY, by activation tagging. Plant Physiol 125:573-584
    • (2001) Plant Physiol , vol.125 , pp. 573-584
    • Huang, S.1    Cerny, R.E.2    Bhat, D.S.3    Brown, S.M.4
  • 43
    • 0034740304 scopus 로고    scopus 로고
    • The defective in anther dehiscience gene encodes a novel phospholipase A1 catalyzing the initial step of jasmonic acid biosynthesis, which synchronizes pollen maturation, anther dehiscence, and flower opening in Arabidopsis
    • Ishiguro S, Kawai-Oda A, Ueda J, Nishida I, Okada K (2001) The DEFECTIVE IN ANTHER DEHISCIENCE gene encodes a novel phospholipase A1 catalyzing the initial step of jasmonic acid biosynthesis, which synchronizes pollen maturation, anther dehiscence, and flower opening in Arabidopsis. Plant Cell 13:2191-2209
    • (2001) Plant Cell , vol.13 , pp. 2191-2209
    • Ishiguro, S.1    Kawai-Oda, A.2    Ueda, J.3    Nishida, I.4    Okada, K.5
  • 44
    • 0037665246 scopus 로고    scopus 로고
    • The patatin-like protein from the latex of Hevea brasiliensis (Hev b 7) is not a vacuolar protein
    • Jekel PA, Hofsteenge J, Beintema JJ (2003) The patatin-like protein from the latex of Hevea brasiliensis (Hev b 7) is not a vacuolar protein. Phytochem 63:517-522
    • (2003) Phytochem , vol.63 , pp. 517-522
    • Jekel, P.A.1    Hofsteenge, J.2    Beintema, J.J.3
  • 47
    • 0036007912 scopus 로고    scopus 로고
    • SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are involved in the shoot gravitropism of Arabidopsis
    • Kato T, Morita MT, Fukaki H, Yamauchi Y, Uehara M, Niihama M, Tasaka M (2002) SGR2, a phospholipase-like protein, and ZIG/SGR4, a SNARE, are involved in the shoot gravitropism of Arabidopsis. Plant Cell 14:33-46
    • (2002) Plant Cell , vol.14 , pp. 33-46
    • Kato, T.1    Morita, M.T.2    Fukaki, H.3    Yamauchi, Y.4    Uehara, M.5    Niihama, M.6    Tasaka, M.7
  • 48
    • 0030759299 scopus 로고    scopus 로고
    • Postharvest dip in lysophosphatidylethanolamine, a natural phospholipid, may prolong vase-life of snapdragon flowers
    • Kaur N, Palta JP (1997) Postharvest dip in lysophosphatidylethanolamine, a natural phospholipid, may prolong vase-life of snapdragon flowers. HortScience 32:888-890
    • (1997) Hortscience , vol.32 , pp. 888-890
    • Kaur, N.1    Palta, J.P.2
  • 49
    • 19544386804 scopus 로고    scopus 로고
    • The Arabidopsis F-box protein TIR1 is an auxin receptor
    • Kepinski S, Leyser O (2005) The Arabidopsis F-box protein TIR1 is an auxin receptor. Nature 435:446-451
    • (2005) Nature , vol.435 , pp. 446-451
    • Kepinski, S.1    Leyser, O.2
  • 51
    • 0028181660 scopus 로고
    • 2's
    • 2 (PLA2) activities in leaves of higher plants Vicia faba and comparison with mammalian PLA2's. FEBS Lett 343:213-218
    • (1994) Febs Lett , vol.343 , pp. 213-218
    • Kim, D.K.1    Lee, H.J.2    Lee, Y.3
  • 52
    • 0032753426 scopus 로고    scopus 로고
    • Characterization of the full-length sequences of phospholipase A2 induced during flower development
    • Kim JY, Chung YS, Ok SH, Lee SG, Chung WI, Kim IY, Shin JS (1999) Characterization of the full-length sequences of phospholipase A2 induced during flower development. Biochim Biophys Acta 1489:389-392
    • (1999) Biochim Biophys Acta , vol.1489 , pp. 389-392
    • Kim, J.Y.1    Chung, Y.S.2    Ok, S.H.3    Lee, S.G.4    Chung, W.I.5    Kim, I.Y.6    Shin, J.S.7
  • 53
    • 0033570171 scopus 로고    scopus 로고
    • Blue light activates the plasma membrane H+-ATPase by phosphorylation of the C-terminus in stomatal guard cells
    • +-ATPase by phosphorylation of the C-terminus in stomatal guard cells. EMBO J 18:5548-5558
    • (1999) Embo J , vol.18 , pp. 5548-5558
    • Kinoshita, T.1    Shimazaki, K.2
  • 54
    • 0023668516 scopus 로고
    • Calcium-independent activation of two plant leaf calcium-regulated protein kinases by fatty acids
    • Klucis E, Polya GM (1987) Calcium-independent activation of two plant leaf calcium-regulated protein kinases by fatty acids. Biochem Biophys Res Commun 147:1041-1047
    • (1987) Biochem Biophys Res Commun , vol.147 , pp. 1041-1047
    • Klucis, E.1    Polya, G.M.2
  • 56
    • 33644843050 scopus 로고    scopus 로고
    • A pathogeninducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis
    • La Camera S, Geoffroy P, Samaha H, Ndiaye A, Rahim G, Legrand M, Heitz S (2005) A pathogeninducible patatin-like lipid acyl hydrolase facilitates fungal and bacterial host colonization in Arabidopsis. Plant J 44:810-825
    • (2005) Plant J , vol.44 , pp. 810-825
    • la Camera, S.1    Geoffroy, P.2    Samaha, H.3    Ndiaye, A.4    Rahim, G.5    Legrand, M.6    Heitz, S.7
  • 57
    • 0036017860 scopus 로고    scopus 로고
    • Phospholipid signaling in plant defence
    • Laxalt AM, Munnik T (2002) Phospholipid signaling in plant defence. Curr Opin Plant Biol 5:332-338
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 332-338
    • Laxalt, A.M.1    Munnik, T.2
  • 58
    • 0000962839 scopus 로고
    • Stimulation of phospholipase A2 in strawberry cells treated with AF-toxin 1 produced by Alternaria alternata strawberry phenotype
    • Lee S-S, Kawakita K, Tsuge T, Doke N (1992) Stimulation of phospholipase A2 in strawberry cells treated with AF-toxin 1 produced by Alternaria alternata strawberry phenotype. Physiol Mol Plant Pathol 41:283-294
    • (1992) Physiol Mol Plant Pathol , vol.41 , pp. 283-294
    • Lee, S.-S.1    Kawakita, K.2    Tsuge, T.3    Doke, N.4
  • 60
    • 0030847575 scopus 로고    scopus 로고
    • Systemic elevation of phosphatidic acid and lysophospholipid levels in wounded plants
    • Lee S, Suh S, Kim S, Crain RC, Kwak JM, Nam H-G, Lee Y (1997) Systemic elevation of phosphatidic acid and lysophospholipid levels in wounded plants. Plant J 12:547-556
    • (1997) Plant J , vol.12 , pp. 547-556
    • Lee, S.1    Suh, S.2    Kim, S.3    Crain, R.C.4    Kwak, J.M.5    Nam, H.-G.6    Lee, Y.7
  • 61
    • 0141746126 scopus 로고    scopus 로고
    • Secretory low molecular weight phospholipase A2 plays important roles in cell elongation and shoot gravitropism in Arabidopsis
    • Lee HY, Bahn SC, Kang Y-M, Lee KH, Kim HJ, Noh EK, Palta JP, Shin JS, Ryu SB (2003) Secretory low molecular weight phospholipase A2 plays important roles in cell elongation and shoot gravitropism in Arabidopsis. Plant Cell 15:1990-2002
    • (2003) Plant Cell , vol.15 , pp. 1990-2002
    • Lee, H.Y.1    Bahn, S.C.2    Kang, Y.-M.3    Lee, K.H.4    Kim, H.J.5    Noh, E.K.6    Palta, J.P.7    Shin, J.S.8    Ryu, S.B.9
  • 65
    • 0002556558 scopus 로고
    • 2+-regulated protein kinase by unsaturated fatty acids in the presence and absence of calcium
    • 2+-regulated protein kinase by unsaturated fatty acids in the presence and absence of calcium. FEBS Lett 221:33-36
    • (1987) Febs Lett , vol.221 , pp. 33-36
    • Lucantoni, A.1    Polya, G.M.2
  • 66
    • 35148886196 scopus 로고    scopus 로고
    • 2-alpha from Arabidopsis thaliana: Functional parameters and substrate preference
    • 2-alpha from Arabidopsis thaliana: functional parameters and substrate preference. Chem Phys Lipids 150:156-166
    • (2007) Chem Phys Lipids , vol.150 , pp. 156-166
    • Mansfeld, J.1    Ulbrich-Hofmann, R.2
  • 67
    • 33646480037 scopus 로고    scopus 로고
    • 2 from Arabidopsis thaliana: Insights into the three-dimensional structure and the amino acids involved in catalysis
    • 2 from Arabidopsis thaliana: insights into the three-dimensional structure and the amino acids involved in catalysis. Biochemistry 45:5687-5694
    • (2006) Biochemistry , vol.45 , pp. 5687-5694
    • Mansfeld, J.1    Gebauer, S.2    Dathe, K.3    Ulbrich-Hofmann, R.4
  • 68
    • 0010607247 scopus 로고
    • A plant protein kinase and plant microsomal H+ transport are stimulated by the ether lipid platelet-activating factor
    • Martiny-Baron G, Scherer GFE (1988) A plant protein kinase and plant microsomal H+ transport are stimulated by the ether lipid platelet-activating factor. Plant Cell Rep 7:579-582
    • (1988) Plant Cell Rep , vol.7 , pp. 579-582
    • Martiny-Baron, G.1    Scherer, G.F.E.2
  • 69
    • 0024978628 scopus 로고
    • Phospholipid-stimulated protein kinase in plants
    • Martiny-Baron G, Scherer GFE (1989) Phospholipid-stimulated protein kinase in plants. J Biol Chem 264:18052-18059
    • (1989) J Biol Chem , vol.264 , pp. 18052-18059
    • Martiny-Baron, G.1    Scherer, G.F.E.2
  • 70
    • 0000260152 scopus 로고
    • Proton transport and phosphorylation of tonoplast polypeptides from zucchini are stimulated by the phospholipids platelet-activating factor
    • Martiny-Baron G, Hecker D, Manolson MF, Poole RJ, Scherer GFE (1992) Proton transport and phosphorylation of tonoplast polypeptides from zucchini are stimulated by the phospholipids platelet-activating factor. Plant Physiol 99:1635-1641
    • (1992) Plant Physiol , vol.99 , pp. 1635-1641
    • Martiny-Baron, G.1    Hecker, D.2    Manolson, M.F.3    Poole, R.J.4    Scherer, G.F.E.5
  • 72
    • 0037040284 scopus 로고    scopus 로고
    • 2 activity in macrophages stimulated with receptor-recognized forms of alpha 2-macroglobulin: Role in mitogenesis and cell proliferation
    • 2 activity in macrophages stimulated with receptor-recognized forms of alpha 2-macroglobulin: role in mitogenesis and cell proliferation. J Biol Chem 277:4069-4078
    • (2002) J Biol Chem , vol.277 , pp. 4069-4078
    • Misra, U.K.1    Pizzo, S.V.2
  • 73
    • 0032486481 scopus 로고    scopus 로고
    • The functions of five distinct mammalian phospholipase A2s in regulating arachidonic acid release. Type IIA and Type V secretory phospholipase A2s are functionally redundant and act in concert with cytosolic phospholipase A2
    • Murakami M, Shimbara S, Kambe T, Kuwata H, Winstead MV, Tischfield JA, Kudo I (1998) The functions of five distinct mammalian phospholipase A2s in regulating arachidonic acid release. Type IIA and Type V secretory phospholipase A2s are functionally redundant and act in concert with cytosolic phospholipase A2. J Biol Chem 273:14411-14423
    • (1998) J Biol Chem , vol.273 , pp. 14411-14423
    • Murakami, M.1    Shimbara, S.2    Kambe, T.3    Kuwata, H.4    Winstead, M.V.5    Tischfield, J.A.6    Kudo, I.7
  • 74
    • 0027535742 scopus 로고
    • Activation of the zeta-isoform of protein kinase C by phosphatidylinositol 3, 4, 5-trisphosphate
    • Nakanishi H, Brewer KA, Exton JH (1993) Activation of the zeta-isoform of protein kinase C by phosphatidylinositol 3, 4, 5-trisphosphate. J Biol Chem 268:13-16
    • (1993) J Biol Chem , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 77
    • 0032728644 scopus 로고    scopus 로고
    • Positional specificity of a phospholipase A activity induced by wounding, systemin, and oligosaccharide elicitors in tomato leaves
    • Narvaez-Vasquez J, Florin-Christensen J, Ryan CA (1999) Positional specificity of a phospholipase A activity induced by wounding, systemin, and oligosaccharide elicitors in tomato leaves. Plant Cell 11:2249-2260
    • (1999) Plant Cell , vol.11 , pp. 2249-2260
    • Narvaez-Vasquez, J.1    Florin-Christensen, J.2    Ryan, C.A.3
  • 78
    • 0000929167 scopus 로고
    • The phospholipid platelet-activating factor stimulates proton extrusion in cultured soybean cells and protein phosphorylation and ATPase activity in plasma membranes
    • Nickel R, Schütte M, Hecker D, Scherer GFE (1991) The phospholipid platelet-activating factor stimulates proton extrusion in cultured soybean cells and protein phosphorylation and ATPase activity in plasma membranes. J Plant Physiol 139:205-211
    • (1991) J Plant Physiol , vol.139 , pp. 205-211
    • Nickel, R.1    Schütte, M.2    Hecker, D.3    Scherer, G.F.E.4
  • 79
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y (1992) Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258:607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 80
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y (1995) Protein kinase C and lipid signaling for sustained cellular responses. FASEB J 9:484-496
    • (1995) Faseb J , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 81
    • 4544277312 scopus 로고    scopus 로고
    • Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana
    • Noiriel A, Benveniste P, Banas A, Stymne S, Bouvier-Navé P (2004) Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana. Eur J Biochem 271:3752-3764
    • (2004) Eur J Biochem , vol.271 , pp. 3752-3764
    • Noiriel, A.1    Benveniste, P.2    Banas, A.3    Stymne, S.4    Bouvier-Navé, P.5
  • 82
    • 0023919129 scopus 로고
    • Regulation of protein kinase C by lysophospholipids. Potential role in signal transduction
    • Oishi K, Raynor RL, Charp PA, Kou JF (1988) Regulation of protein kinase C by lysophospholipids. Potential role in signal transduction. J Biol Chem 263:6865-6871
    • (1988) J Biol Chem , vol.263 , pp. 6865-6871
    • Oishi, K.1    Raynor, R.L.2    Charp, P.A.3    Kou, J.F.4
  • 83
    • 84969785201 scopus 로고
    • Lysophosphatidylcholine stimulates ATP-dependent proton accumulation in isolated oat root plasma membrane vesicles
    • Palmgren MG, Sommarin M (1989) Lysophosphatidylcholine stimulates ATP-dependent proton accumulation in isolated oat root plasma membrane vesicles. Plant Physiol 90:1009-1014
    • (1989) Plant Physiol , vol.90 , pp. 1009-1014
    • Palmgren, M.G.1    Sommarin, M.2
  • 85
    • 0032409077 scopus 로고    scopus 로고
    • 2 activity by auxin in suspension-cultured parsley and soybean cells
    • 2 activity by auxin in suspension-cultured parsley and soybean cells. Plant J 16:601-611
    • (1998) Plant J , vol.16 , pp. 601-611
    • Paul, R.1    Holk, A.2    Scherer, G.F.E.3
  • 86
    • 0010570703 scopus 로고
    • Differential inhibition of plant calciumdependent protein kinases by long-chain fatty acids and other amphiphiles
    • Polya GM, Minichiello J, Nott R, Klucis E, Keane PJ (1990) Differential inhibition of plant calciumdependent protein kinases by long-chain fatty acids and other amphiphiles. Plant Sci 71:45-54
    • (1990) Plant Sci , vol.71 , pp. 45-54
    • Polya, G.M.1    Minichiello, J.2    Nott, R.3    Klucis, E.4    Keane, P.J.5
  • 87
    • 0027340390 scopus 로고
    • 2 activation by phosphorylation in mouse peritoneal macrophages
    • 2 activation by phosphorylation in mouse peritoneal macrophages. J Biol Chem 268:24506-24513
    • (1993) J Biol Chem , vol.268 , pp. 24506-24513
    • Qin, Z.-H.1    de Carvalho, M.S.2    Leslie, C.C.3
  • 89
    • 0000236933 scopus 로고
    • Lipid acyl hydrolase of patatin
    • Racusen D (1984) Lipid acyl hydrolase of patatin. Can J Bot 62:1640-1644
    • (1984) Can J Bot , vol.62 , pp. 1640-1644
    • Racusen, D.1
  • 90
    • 4644251290 scopus 로고    scopus 로고
    • Expression of the patatin-related phospholipase A-gene AtPLA IIA in Arabidopsis thaliana is up-regulated by salicylic acid, wounding, ethylene, and by deficiency of iron and phosphate
    • Rietz S, Holk A, Scherer GFE (2004) Expression of the patatin-related phospholipase A-gene AtPLA IIA in Arabidopsis thaliana is up-regulated by salicylic acid, wounding, ethylene, and by deficiency of iron and phosphate. Planta 219:743-753
    • (2004) Planta , vol.219 , pp. 743-753
    • Rietz, S.1    Holk, A.2    Scherer, G.F.E.3
  • 91
    • 0347760574 scopus 로고
    • Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein of potato tubers
    • Rosahl S, Schmidt R, Schell J, Willmitzer L (1986) Isolation and characterization of a gene from Solanum tuberosum encoding patatin, the major storage protein of potato tubers. Mol Gen Genet 203:214-220
    • (1986) Mol Gen Genet , vol.203 , pp. 214-220
    • Rosahl, S.1    Schmidt, R.2    Schell, J.3    Willmitzer, L.4
  • 94
    • 2442541250 scopus 로고    scopus 로고
    • Phospholipid-derived signaling mediated by phospholipase A in plants
    • Ryu SB (2004) Phospholipid-derived signaling mediated by phospholipase A in plants. Trends Plant Sci 9:229-235
    • (2004) Trends Plant Sci , vol.9 , pp. 229-235
    • Ryu, S.B.1
  • 95
    • 0030812596 scopus 로고    scopus 로고
    • Inhibition of phospholipase D by lysophosphatidylethanolamine, a lipid-derived senescence retardant
    • Ryu SB, Karlsson BH, O ̈ zgen M, Palta JP (1997) Inhibition of phospholipase D by lysophosphatidylethanolamine, a lipid-derived senescence retardant. Proc Natl Acad Sci USA 94:12717-12721
    • (1997) Proc Natl Acad Sci Usa , vol.94 , pp. 12717-12721
  • 96
    • 24344453295 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding Arabidopsis secretory phospholipase A2-alpha, an enzyme that generates bioactive lysophospholipids and free fatty acids
    • 2-alpha, an enzyme that generates bioactive lysophospholipids and free fatty acids. Biochim Biophys Acta 1736:144-151
    • (2005) Biochim Biophys Acta , vol.1736 , pp. 144-151
    • Ryu, S.B.1    Lee, H.Y.2    Doelling, J.H.3    Palta, J.P.4
  • 98
    • 0000276916 scopus 로고
    • Stimulation of growth and phospholipase A2 by the peptides mastoparan and melittin and by the auxin 2, 4-dichlorophenoxyacetic acid
    • Scherer GFE (1992) Stimulation of growth and phospholipase A2 by the peptides mastoparan and melittin and by the auxin 2, 4-dichlorophenoxyacetic acid. Plant Growth Regul 11:153-157
    • (1992) Plant Growth Regul , vol.11 , pp. 153-157
    • Scherer, G.F.E.1
  • 99
    • 0029106029 scopus 로고
    • Activation of phospholipase A by auxin and mastoparan in hypocotyls segments from zucchini and sunflower
    • Scherer GFE (1995) Activation of phospholipase A by auxin and mastoparan in hypocotyls segments from zucchini and sunflower. J Plant Physiol 145:483-490
    • (1995) J Plant Physiol , vol.145 , pp. 483-490
    • Scherer, G.F.E.1
  • 100
    • 0000440880 scopus 로고    scopus 로고
    • Phospholipid signaling and lipid-derived second messengers in plants
    • Scherer GFE (1996) Phospholipid signaling and lipid-derived second messengers in plants. Plant Growth Regul 18:125-133
    • (1996) Plant Growth Regul , vol.18 , pp. 125-133
    • Scherer, G.F.E.1
  • 101
    • 0035999458 scopus 로고    scopus 로고
    • Secondary messengers and phospholipase A2 in auxin signal transduction
    • 2 in auxin signal transduction. Plant Mol Biol 49:357-372
    • (2002) Plant Mol Biol , vol.49 , pp. 357-372
    • Scherer, G.F.E.1
  • 102
    • 0024981347 scopus 로고
    • A rapid response to a plant hormone: Auxin stimulates phospholipase A2 in vivo and in vitro
    • Scherer GFE, André B (1989) A rapid response to a plant hormone: auxin stimulates phospholipase A2 in vivo and in vitro. Biochem Biophys Res Commun 163:111-117
    • (1989) Biochem Biophys Res Commun , vol.163 , pp. 111-117
    • Scherer, G.F.E.1    André, B.2
  • 103
    • 0000816261 scopus 로고
    • 2 by auxin in microsomes from suspension-cultured soybean cells is receptor-mediated and influenced by nucleotides
    • 2 by auxin in microsomes from suspension-cultured soybean cells is receptor-mediated and influenced by nucleotides. Planta 191:515-523
    • (1993) Planta , vol.191 , pp. 515-523
    • Scherer, G.F.E.1    André, B.2
  • 104
    • 0030873342 scopus 로고    scopus 로고
    • Auxin-induced growth is inhibited by phospholipase A2 inhibitors. Implications for auxin-induced signal transduction
    • Scherer GFE, Arnold B (1997) Auxin-induced growth is inhibited by phospholipase A2 inhibitors. Implications for auxin-induced signal transduction. Planta 202:462-469
    • (1997) Planta , vol.202 , pp. 462-469
    • Scherer, G.F.E.1    Arnold, B.2
  • 105
    • 0001406086 scopus 로고
    • A new set of regulatory molecules in plants: A plant phospholipid similar to platelet-activating factor stimulates protein kinase and protontranslocating ATPase in membrane vesicles
    • Scherer GFE, Martiny-Baron G, Stoffel B (1988) A new set of regulatory molecules in plants: a plant phospholipid similar to platelet-activating factor stimulates protein kinase and protontranslocating ATPase in membrane vesicles. Planta 175:241-253
    • (1988) Planta , vol.175 , pp. 241-253
    • Scherer, G.F.E.1    Martiny-Baron, G.2    Stoffel, B.3
  • 106
    • 74949125464 scopus 로고
    • Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction
    • In Battey NH, Dickinson HG, HetheringtonAM(eds), Cambridge University Press, Cambridge, UK
    • Scherer GFE, Führ A, Schütte M (1993a) Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction. In Battey NH, Dickinson HG, HetheringtonAM(eds) Society for Experimental Biology Seminar Series 53: Post-translational modifications in plants, vol 53. Cambridge University Press, Cambridge, UK, pp. 109-121
    • (1993) Society For Experimental Biology Seminar Series 53: Post-translational Modifications In Plants , vol.53 , pp. 109-121
    • Scherer, G.F.E.1    Führ, A.2    Schütte, M.3
  • 107
    • 0027137268 scopus 로고
    • Ca2+ ions and lysophospholipids activate phosphorylation of different proteins in plasma membranes and tonoplast purified by free-flow electrophoresis
    • 2+ ions and lysophospholipids activate phosphorylation of different proteins in plasma membranes and tonoplast purified by free-flow electrophoresis. J Plant Physiol 142:432-437
    • (1993) J Plant Physiol , vol.142 , pp. 432-437
  • 108
    • 34548127886 scopus 로고    scopus 로고
    • A role for phospholipase A in auxin-regulated gene expression
    • Scherer GF, Zahn M, Callis J, Jones AM (2007) A role for phospholipase A in auxin-regulated gene expression. FEBS Lett 581:4205-4211
    • (2007) Febs Lett , vol.581 , pp. 4205-4211
    • Scherer, G.F.1    Zahn, M.2    Callis, J.3    Jones, A.M.4
  • 112
    • 0031794674 scopus 로고    scopus 로고
    • 2 activity in potato tubers treated with fungal elicitor
    • 2 activity in potato tubers treated with fungal elicitor. Plant Cell Physiol 39:1080-1086
    • (1998) Plant Cell Physiol , vol.39 , pp. 1080-1086
    • Senda, K.1    Doke, N.2    Kawakita, K.3
  • 116
    • 0034739463 scopus 로고    scopus 로고
    • The expanding superfamily of phospholipase A2 enzymes: Classification and characterization
    • Six DA, Dennis EA (2000) The expanding superfamily of phospholipase A2 enzymes: classification and characterization. Biochim Biophys Acta 1488:1-19
    • (2000) Biochim Biophys Acta , vol.1488 , pp. 1-19
    • Six, D.A.1    Dennis, E.A.2
  • 117
    • 0034739438 scopus 로고    scopus 로고
    • Bacterial phospholipase A: Structure and function of an integral membrane phospholipase
    • Snijder HJ, Dijkstra BW (2000) Bacterial phospholipase A: Structure and function of an integral membrane phospholipase. Biochim Biophys Acta 1488:91-101
    • (2000) Biochim Biophys Acta , vol.1488 , pp. 91-101
    • Snijder, H.J.1    Dijkstra, B.W.2
  • 121
    • 0032409169 scopus 로고    scopus 로고
    • 2 in light signal transduction of guard cells of Commelina communis
    • 2 in light signal transduction of guard cells of Commelina communis. Physiol Plant 104:306-310
    • (1998) Physiol Plant , vol.104 , pp. 306-310
    • Suh, S.1    Park, J.2    Lee, Y.3
  • 124
    • 0028852494 scopus 로고
    • Phospholipase activities associated with the tonoplast from Acer pseudoplatanus cells: Identification of a phospholipase A1 activity
    • Tavernier E, Pugin A (1995) Phospholipase activities associated with the tonoplast from Acer pseudoplatanus cells: identification of a phospholipase A1 activity. Biochim Biophys Acta 1233:118-122
    • (1995) Biochim Biophys Acta , vol.1233 , pp. 118-122
    • Tavernier, E.1    Pugin, A.2
  • 125
    • 24644492447 scopus 로고    scopus 로고
    • Biochemical characterization of plasma membrane H + -ATPase activation in guard cell protoplasts of Arabidopsis thaliana in response to blue light
    • Ueno K, Kinoshita T, Inoue S, Emi T, Shimazaki K (2005) Biochemical characterization of plasma membrane H + -ATPase activation in guard cell protoplasts of Arabidopsis thaliana in response to blue light. Plant Cell Physiol 46:955-963
    • (2005) Plant Cell Physiol , vol.46 , pp. 955-963
    • Ueno, K.1    Kinoshita, T.2    Inoue, S.3    Emi, T.4    Shimazaki, K.5
  • 126
    • 0030195294 scopus 로고    scopus 로고
    • A calcium and free fatty acid-modulated protein kinase as putative effector of the fusicoccin 14-3-3 receptor
    • van der Hoeven PC, Siderius M, Korthout HA, Drabkin AV, de Boer AH (1996) A calcium and free fatty acid-modulated protein kinase as putative effector of the fusicoccin 14-3-3 receptor. Plant Physiol 111:857-865
    • (1996) Plant Physiol , vol.111 , pp. 857-865
    • van der Hoeven, P.C.1    Siderius, M.2    Korthout, H.A.3    Drabkin, A.V.4    de Boer, A.H.5
  • 127
    • 4344592436 scopus 로고    scopus 로고
    • Learning the lipid language of plant signaling
    • van Leeuwen W, Okre ́sz L, Bögre L, Munnik T (2004) Learning the lipid language of plant signaling. Trends Plant Sci 9:378-384
    • (2004) Trends Plant Sci , vol.9 , pp. 378-384
  • 128
    • 0035984052 scopus 로고    scopus 로고
    • 2 generates lysophosphatidylcholines that mobilize the vacuolar H+ pool for pH signaling via the activation of Na+-dependent proton fluxes
    • 2 generates lysophosphatidylcholines that mobilize the vacuolar H+ pool for pH signaling via the activation of Na+-dependent proton fluxes. Plant Cell 14:1509-1525
    • (2002) Plant Cell , vol.14 , pp. 1509-1525
    • Viehweger, K.1    Dordschbal, B.2    Roos, W.3
  • 129
    • 30944456817 scopus 로고    scopus 로고
    • The Galpha protein controls a pH-dependent signal path to the induction of phytoalexin biosynthesis in Eschscholzia californica
    • Viehweger K, Schwartze W, Schumann B, Lein W, Roos W (2006) The Galpha protein controls a pH-dependent signal path to the induction of phytoalexin biosynthesis in Eschscholzia californica. Plant Cell 18:1510-1523
    • (2006) Plant Cell , vol.18 , pp. 1510-1523
    • Viehweger, K.1    Schwartze, W.2    Schumann, B.3    Lein, W.4    Roos, W.5
  • 130
    • 31844454590 scopus 로고    scopus 로고
    • Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses
    • Wang X (2005) Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses. Plant Physiol 139:566-573
    • (2005) Plant Physiol , vol.139 , pp. 566-573
    • Wang, X.1
  • 131
    • 0035202094 scopus 로고    scopus 로고
    • A novel phospholipase D of Arabidopsis that is activated by oleic acid and associated with the plasma membrane
    • Wang C, Wang X (2001) A novel phospholipase D of Arabidopsis that is activated by oleic acid and associated with the plasma membrane. Plant Physiol 127:1102-1112
    • (2001) Plant Physiol , vol.127 , pp. 1102-1112
    • Wang, C.1    Wang, X.2
  • 132
    • 34848897179 scopus 로고    scopus 로고
    • Jasmonates: An update on biosynthesis, signal transduction and action in plant stress response, growth and development
    • Wasternack C (2007) Jasmonates: an update on biosynthesis, signal transduction and action in plant stress response, growth and development. Ann Bot 100:681-697
    • (2007) Ann Bot , vol.100 , pp. 681-697
    • Wasternack, C.1
  • 133
    • 0035209452 scopus 로고    scopus 로고
    • Nitric oxide: Comparative synthesis and signaling in animal and plant cells
    • Wendehenne D, Pugin A, Klessig DF, Durne J (2001) Nitric oxide: comparative synthesis and signaling in animal and plant cells. Trends Plant Sci 4:177-183
    • (2001) Trends Plant Sci , vol.4 , pp. 177-183
    • Wendehenne, D.1    Pugin, A.2    Klessig, D.F.3    Durne, J.4
  • 136
    • 34547119951 scopus 로고    scopus 로고
    • AtPLAI is an acyl hydrolase involved in basal jasmonic acid production and Arabidopsis resistance to Botrytis cinerea
    • Yang W, Devaiah SP, Pan X, Isaac G, Welti R, Wang X (2007) AtPLAI is an acyl hydrolase involved in basal jasmonic acid production and Arabidopsis resistance to Botrytis cinerea. J Biol Chem 282:18116-18128
    • (2007) J Biol Chem , vol.282 , pp. 18116-18128
    • Yang, W.1    Devaiah, S.P.2    Pan, X.3    Isaac, G.4    Welti, R.5    Wang, X.6
  • 137
    • 0000846345 scopus 로고    scopus 로고
    • In vivo evidence for the involvement of phospholipase A and protein kinase in the signal transduction pathway for auxin-induced corn coleoptile elongation
    • Yi H, Park D, Lee Y (1996) In vivo evidence for the involvement of phospholipase A and protein kinase in the signal transduction pathway for auxin-induced corn coleoptile elongation. Physiol Plant 96:359-368
    • (1996) Physiol Plant , vol.96 , pp. 359-368
    • Yi, H.1    Park, D.2    Lee, Y.3
  • 138
    • 30944449966 scopus 로고    scopus 로고
    • Expression of Arabidopis phospholipase A genes in Petunia x hybrida. Increased hypersensitive-like response after infection with Botrytis cinerea and Pseudomonas syringae pv. Tomato DC3000 demonstrates a function for phospholipase A in pathogen defence
    • Zahn M, Wymalasekara R, Göbel C, Feußner I, Holk A, Scherer GFE (2005) Expression of Arabidopis phospholipase A genes in Petunia x hybrida. Increased hypersensitive-like response after infection with Botrytis cinerea and Pseudomonas syringae pv. Tomato DC3000 demonstrates a function for phospholipase A in pathogen defence. Physiol Mol Plant Pathol 67:2-14
    • (2005) Physiol Mol Plant Pathol , vol.67 , pp. 2-14
    • Zahn, M.1    Wymalasekara, R.2    Göbel, C.3    Feußner, I.4    Holk, A.5    Scherer, G.F.E.6
  • 139
    • 0142124100 scopus 로고    scopus 로고
    • The oleate-stimulated phospholipase D, PLDg and phosphatidic acid decrease H2O2-induced cell death in Arabidopsis
    • Zhang W, Eang C, Qin C, Wood T, Olafsdottir G, Welti R, Wang X (2003) The oleate-stimulated phospholipase D, PLDg and phosphatidic acid decrease H2O2-induced cell death in Arabidopsis. Plant Cell 15:2285-2295
    • (2003) Plant Cell , vol.15 , pp. 2285-2295
    • Zhang, W.1    Eang, C.2    Qin, C.3    Wood, T.4    Olafsdottir, G.5    Welti, R.6    Wang, X.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.