메뉴 건너뛰기




Volumn 52, Issue 1-2, 1997, Pages 1-8

The oxygen-dependent modification of triacylglycerols and phospholipids, the different way of initiating lipid body mobilization

Author keywords

13 hydroxy octadecanoic acid; lipase; lipid body; lipid hydroperoxide; lipoxygenase; triacylglycerols

Indexed keywords

CUCUMIS SATIVUS;

EID: 0030985149     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1997-1-202     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 0028313568 scopus 로고
    • Synthesis and targeting of Brassica napus oleosin in transgenic tobacco
    • Batchelder C., Ross J. H. E. and Murphy D. J. (1994), Synthesis and targeting of Brassica napus oleosin in transgenic tobacco. Plant Sci. 104, 39-47.
    • (1994) Plant Sci. , vol.104 , pp. 39-47
    • Batchelder, C.1    Ross, J.H.E.2    Murphy, D.J.3
  • 3
    • 0029063167 scopus 로고    scopus 로고
    • A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase
    • Beeor-Tzahar T., Ben-Hayyim G., Holland D., Faltin Z. and Eshdat Y. (1996), A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase. FEBS Lett. 366, 151-155.
    • (1996) FEBS Lett. , vol.366 , pp. 151-155
    • Beeor-Tzahar, T.1    Ben-Hayyim, G.2    Holland, D.3    Faltin, Z.4    Eshdat, Y.5
  • 6
    • 0025856687 scopus 로고
    • Evidence for a peroxisomal fatty acid β-oxidation involving D-3-hydroxyacyl-CoAs
    • Engeland K. and Kindl H. (1991), Evidence for a peroxisomal fatty acid β-oxidation involving D-3-hydroxyacyl-CoAs. Eur. J. Biochem. 200, 1717-1718.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 1717-1718
    • Engeland, K.1    Kindl, H.2
  • 7
    • 0025980871 scopus 로고
    • 3-enoyl-CoA isomerase acting on 3-cis-enoyl-CoA and 3-trans-enoyl-CoA
    • 3-enoyl-CoA isomerase acting on 3-cis-enoyl-CoA and 3-trans-enoyl-CoA. Eur. J. Biochem. 196, 699-705.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 699-705
    • Engeland, K.1    Kindl, H.2
  • 8
    • 0026546973 scopus 로고
    • A lipoxygenase is the main lipid body protein in cucumber and soybean cotyledons during the stage of triglyceride mobilization
    • Feussner I. and Kindl H. (1992), A lipoxygenase is the main lipid body protein in cucumber and soybean cotyledons during the stage of triglyceride mobilization. FEBS Lett. 298, 223-225.
    • (1992) FEBS Lett. , vol.298 , pp. 223-225
    • Feussner, I.1    Kindl, H.2
  • 9
    • 0029055174 scopus 로고
    • The lipid body lipoxygenase from cucumber seedlings exhibits unusual reaction specificity
    • Feussner I. and Kühn H. (1995), The lipid body lipoxygenase from cucumber seedlings exhibits unusual reaction specificity. FEBS Lett. 367, 12-14.
    • (1995) FEBS Lett. , vol.367 , pp. 12-14
    • Feussner, I.1    Kühn, H.2
  • 10
    • 0030043519 scopus 로고    scopus 로고
    • Lipid body lipoxygenase is expressed in cotyledons during germination prior to other lipoxygenase forms
    • Feussner I., Nellen A., Hause B., Wasternack C. and Kindl H. (1996), Lipid body lipoxygenase is expressed in cotyledons during germination prior to other lipoxygenase forms. Planta 198, 288-293.
    • (1996) Planta , vol.198 , pp. 288-293
    • Feussner, I.1    Nellen, A.2    Hause, B.3    Wasternack, C.4    Kindl, H.5
  • 11
    • 0029592021 scopus 로고
    • Lipoxygenase-catalyzed oxygenation of storage lipids is implicated in lipid mobilization during germination
    • Feussner I., Wasternack C., Kindl H. and Kühn H. (1995), Lipoxygenase-catalyzed oxygenation of storage lipids is implicated in lipid mobilization during germination. Proc. Natl. Acad. Sci. USA 92, 11849-11853.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11849-11853
    • Feussner, I.1    Wasternack, C.2    Kindl, H.3    Kühn, H.4
  • 13
    • 0000972548 scopus 로고
    • Calcium stimulated neutral lipase activity in castor bean lipid bodies
    • Hills M. J. and Beevers H. (1987), Calcium stimulated neutral lipase activity in castor bean lipid bodies. Plant Physiol. 84, 272-276.
    • (1987) Plant Physiol. , vol.84 , pp. 272-276
    • Hills, M.J.1    Beevers, H.2
  • 14
    • 0027352322 scopus 로고
    • Targeting of oleosins to the oil bodies of oilseed rape (Brassica napus L.)
    • Hills M. J., Watson M. D. and Murphy D. J. (1993), Targeting of oleosins to the oil bodies of oilseed rape (Brassica napus L.). Planta 189, 24-29.
    • (1993) Planta , vol.189 , pp. 24-29
    • Hills, M.J.1    Watson, M.D.2    Murphy, D.J.3
  • 15
    • 0029807113 scopus 로고    scopus 로고
    • Lipid body lipoxygenase characterized by protein fragmentation, cDNA sequence and by its very early expression during germination of cucumber seedlings
    • Höhne M., Nellen A., Schwennesen K. and Kindl H. (1996), Lipid body lipoxygenase characterized by protein fragmentation, cDNA sequence and by its very early expression during germination of cucumber seedlings. Eur. J. Biochem. 241, 6-11.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 6-11
    • Höhne, M.1    Nellen, A.2    Schwennesen, K.3    Kindl, H.4
  • 17
    • 0028025663 scopus 로고
    • Structure of plant seed oil bodies
    • Huang A. H. C. (1994), Structure of plant seed oil bodies. Curr. Opinion Struct. Biology 4, 493-498.
    • (1994) Curr. Opinion Struct. Biology , vol.4 , pp. 493-498
    • Huang, A.H.C.1
  • 18
    • 0025016946 scopus 로고
    • The synthesis and molecular dynamics of phospholipids having hydroxylated fatty acids at the sn-2 position
    • Isaacson Y., Sherbourne C. D. and Gross R. (1990), The synthesis and molecular dynamics of phospholipids having hydroxylated fatty acids at the sn-2 position. Chem. Phys. Lipids 52, 217-226.
    • (1990) Chem. Phys. Lipids , vol.52 , pp. 217-226
    • Isaacson, Y.1    Sherbourne, C.D.2    Gross, R.3
  • 19
    • 0029278049 scopus 로고
    • Characterization of cDNA clones for differentially expressed genes in embryos of dormant and nondormant Avena fatua L. caryopses
    • Johnson R., Cranston H. J., Chaverra M. E. and Dyer W. E. (1995), Characterization of cDNA clones for differentially expressed genes in embryos of dormant and nondormant Avena fatua L. caryopses. Plant Mol. Biol. 28, 113-122.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 113-122
    • Johnson, R.1    Cranston, H.J.2    Chaverra, M.E.3    Dyer, W.E.4
  • 20
    • 0001231042 scopus 로고
    • The initiation of membrane lipid peroxidation during bacteria-induced hypersensitive reaction
    • Keppler L. D. and Novacky A. (1987), The initiation of membrane lipid peroxidation during bacteria-induced hypersensitive reaction. Physiol. Mol. Plant Pathol. 30, 233-245.
    • (1987) Physiol. Mol. Plant Pathol. , vol.30 , pp. 233-245
    • Keppler, L.D.1    Novacky, A.2
  • 21
    • 0027159789 scopus 로고
    • Fatty acid degradation in plant peroxisomes: Function and biosynthesis of the enzymes involved
    • Kindl H. (1993), Fatty acid degradation in plant peroxisomes: Function and biosynthesis of the enzymes involved. Biochimie 75, 225-230.
    • (1993) Biochimie , vol.75 , pp. 225-230
    • Kindl, H.1
  • 22
    • 1842396404 scopus 로고
    • Glyoxysome biogenesis via cytosolic pools in cucumber
    • Kindl H. (1982), Glyoxysome biogenesis via cytosolic pools in cucumber. Ann. N. Y. Acad. Sci. 386, 314-328.
    • (1982) Ann. N. Y. Acad. Sci. , vol.386 , pp. 314-328
    • Kindl, H.1
  • 23
  • 24
    • 0025912868 scopus 로고
    • Maize oleosin is correctly targeted to seed oil bodies in Brassica napus transformed with the maize oleosin gene
    • Lee W. S., Tzen J. T. C., Kridl J. C., Radke S. E. and Huang A. H. C. (1991), Maize oleosin is correctly targeted to seed oil bodies in Brassica napus transformed with the maize oleosin gene. Proc. Natl. Acad. Sci. USA 88, 6181-6185.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6181-6185
    • Lee, W.S.1    Tzen, J.T.C.2    Kridl, J.C.3    Radke, S.E.4    Huang, A.H.C.5
  • 25
    • 0027267496 scopus 로고
    • Expression and characterization of the N-terminal domain of an oleosin protein from sunflower
    • Li M., Keddie J. S., Smith L. J., Clark D. C. and Murphy D. J. (1993), Expression and characterization of the N-terminal domain of an oleosin protein from sunflower J. Biol. Chem. 268, 17504-17512.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17504-17512
    • Li, M.1    Keddie, J.S.2    Smith, L.J.3    Clark, D.C.4    Murphy, D.J.5
  • 26
    • 0001753239 scopus 로고
    • Involvement of glyoxysomal lipase in the hydrolysis of storage triacylglycerols in the cotyledons of soybean seedlings
    • Lin Y. H., Moreau R. A. and Huang A. H. C. (1982), Involvement of glyoxysomal lipase in the hydrolysis of storage triacylglycerols in the cotyledons of soybean seedlings. Plant Physiol. 70, 108-112.
    • (1982) Plant Physiol. , vol.70 , pp. 108-112
    • Lin, Y.H.1    Moreau, R.A.2    Huang, A.H.C.3
  • 27
    • 0001137013 scopus 로고
    • Lipase in the lipid bodies of corn scutella during seedling growth
    • Lin Y. H., Wimer L. T. and Huang A. H. C. (1983), Lipase in the lipid bodies of corn scutella during seedling growth. Plant Physiol. 73, 460-463.
    • (1983) Plant Physiol. , vol.73 , pp. 460-463
    • Lin, Y.H.1    Wimer, L.T.2    Huang, A.H.C.3
  • 28
    • 0001655813 scopus 로고
    • Cotranslational integration of soybean (Glycine max) oil body membrane protein oleosin into microsomal membranes
    • Loer D. S. and Herman E. M. (1993), Cotranslational integration of soybean (Glycine max) oil body membrane protein oleosin into microsomal membranes. Plant Physiol. 101, 993-998.
    • (1993) Plant Physiol. , vol.101 , pp. 993-998
    • Loer, D.S.1    Herman, E.M.2
  • 29
    • 0029068580 scopus 로고
    • Cucumber cotyledon lipoxygenase oxygenizes trilinolein at the lipid/water interface
    • Matsui K. and Kajiwara T. (1995), Cucumber cotyledon lipoxygenase oxygenizes trilinolein at the lipid/water interface. Lipids 30, 733-738.
    • (1995) Lipids , vol.30 , pp. 733-738
    • Matsui, K.1    Kajiwara, T.2
  • 30
    • 0028795705 scopus 로고
    • The lipid composition of cytosolic particles isolated from senescing bean cotyledons
    • McKegney G., Yao K., Ghosh S., Huff A., Mayak S. and Thompson J. E. (1995), The lipid composition of cytosolic particles isolated from senescing bean cotyledons. Phytochemistry 39, 1335-1345.
    • (1995) Phytochemistry , vol.39 , pp. 1335-1345
    • McKegney, G.1    Yao, K.2    Ghosh, S.3    Huff, A.4    Mayak, S.5    Thompson, J.E.6
  • 31
    • 0025543191 scopus 로고
    • Storage lipid bodies in plants and other organisms
    • Murphy D. J. (1990), Storage lipid bodies in plants and other organisms. Prog. Lipid Res. 29, 299-324.
    • (1990) Prog. Lipid Res. , vol.29 , pp. 299-324
    • Murphy, D.J.1
  • 32
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation - Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity
    • Preisig-Müller R., Gühnemann-Schäfer K. and Kindl H. (1994), Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation - demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity. J. Biol. Chem. 269, 20475-20481.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20475-20481
    • Preisig-Müller, R.1    Gühnemann-Schäfer, K.2    Kindl, H.3
  • 33
    • 0028158043 scopus 로고
    • Heat shock enhances the amount of prenylated DNAJ protein at membranes of glyoxysomes
    • Preisig-Müller R., Muster G. and Kindl H. (1994), Heat shock enhances the amount of prenylated DNAJ protein at membranes of glyoxysomes. Eur. J. Biochem. 219, 57-63.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 57-63
    • Preisig-Müller, R.1    Muster, G.2    Kindl, H.3
  • 34
    • 0001554273 scopus 로고
    • Transient occurrence of lipoxygenase and glycoprotein gp49 in lipid bodies during fat mobilization in anise seedlings
    • Radetzky R., Feussner I., Theimer R. R. and Kindl H. (1993), Transient occurrence of lipoxygenase and glycoprotein gp49 in lipid bodies during fat mobilization in anise seedlings. Planta 191, 166-172.
    • (1993) Planta , vol.191 , pp. 166-172
    • Radetzky, R.1    Feussner, I.2    Theimer, R.R.3    Kindl, H.4
  • 35
    • 0030098004 scopus 로고    scopus 로고
    • Lipoxygenases in plants - Their role in development and stress response
    • Rosahl S. (1996), Lipoxygenases in plants - their role in development and stress response. Z. Naturforsch. 51c, 123-138.
    • (1996) Z. Naturforsch. , vol.51 C , pp. 123-138
    • Rosahl, S.1
  • 36
    • 0029915115 scopus 로고    scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products
    • Schnurr K., Belkner J., Ursini F., Schewe T. and Kühn H. (1996), The selenoenzyme phospholipid hydroperoxide glutathione peroxidase controls the activity of the 15-lipoxygenase with complex substrates and preserves the specificity of the oxygenation products. J. Biol. Chem. 271, 4653-4658.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4653-4658
    • Schnurr, K.1    Belkner, J.2    Ursini, F.3    Schewe, T.4    Kühn, H.5
  • 37
    • 0001596943 scopus 로고
    • The biochemistry and the physiological and molecular actions of jasmonates
    • Sembdner G. and Parthier B. (1993), The biochemistry and the physiological and molecular actions of jasmonates. Annu. Rev. Plant. Physiol. Plant. Mol. Biol. 44, 569-589.
    • (1993) Annu. Rev. Plant. Physiol. Plant. Mol. Biol. , vol.44 , pp. 569-589
    • Sembdner, G.1    Parthier, B.2
  • 38
    • 0022113589 scopus 로고
    • Isolation of proteins assembled in lipid body membranes during fat mobilization in cucumber cotyledons
    • Sturm A., Schwennesen K. and Kindl H. (1985), Isolation of proteins assembled in lipid body membranes during fat mobilization in cucumber cotyledons. Eur. J. Biochem. 150, 461-468.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 461-468
    • Sturm, A.1    Schwennesen, K.2    Kindl, H.3
  • 39
    • 0001621254 scopus 로고
    • Development and intracellular localization of lipase activity in rape seed (Brassica napus L.) cotyledons
    • Theimer R. R. and Rosnitschek I. (1978), Development and intracellular localization of lipase activity in rape seed (Brassica napus L.) cotyledons. Planta 139, 249-256.
    • (1978) Planta , vol.139 , pp. 249-256
    • Theimer, R.R.1    Rosnitschek, I.2
  • 40
    • 0023654019 scopus 로고
    • Biosynthesis of lipase in the scutellum of maize kernel
    • Wang S. and Huang A. H. C. (1987), Biosynthesis of lipase in the scutellum of maize kernel. J. Biol. Chem. 262, 2270-2274.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2270-2274
    • Wang, S.1    Huang, A.H.C.2
  • 41
    • 0001039144 scopus 로고
    • Membranous appendices of spherosomes (oleosomes)
    • Wanner G. and Theimer R. R. (1978), Membranous appendices of spherosomes (oleosomes). Planta 140, 163-169.
    • (1978) Planta , vol.140 , pp. 163-169
    • Wanner, G.1    Theimer, R.R.2
  • 42
    • 0028587157 scopus 로고
    • Lipid bodies: Intracellular sites for eicosanoid formation
    • Weller P. F. and Dvorak A. M. (1994), Lipid bodies: intracellular sites for eicosanoid formation. J. Allerg. Clin. Immunol. 94, 1151-1156.
    • (1994) J. Allerg. Clin. Immunol. , vol.94 , pp. 1151-1156
    • Weller, P.F.1    Dvorak, A.M.2
  • 43
    • 0030026422 scopus 로고    scopus 로고
    • Lipoxygenase-mediated formation of hydrocarbons and unsaturated aldehydes in freshwater diatoms
    • Wendel T. and Juttner F. (1996), Lipoxygenase-mediated formation of hydrocarbons and unsaturated aldehydes in freshwater diatoms. Phytochemistry 41, 1445-1449.
    • (1996) Phytochemistry , vol.41 , pp. 1445-1449
    • Wendel, T.1    Juttner, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.