메뉴 건너뛰기




Volumn 396, Issue 1, 2010, Pages 105-110

Regulation of the activity of 5-lipoxygenase, a key enzyme in leukotriene biosynthesis

Author keywords

Arachidonic acid; Eicosanoid; Inflammation; Leukotriene

Indexed keywords

ARACHIDONATE 5 LIPOXYGENASE; ARACHIDONATE 5 LIPOXYGENASE ACTIVATING PROTEIN; LEUKOTRIENE; LEUKOTRIENE A4; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHATIDYLCHOLINE;

EID: 77952312969     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.02.173     Document Type: Article
Times cited : (110)

References (44)
  • 1
    • 0020597565 scopus 로고
    • Leukotrienes: mediators of immediate hypersensitivity reactions and inflammation
    • Samuelsson B. Leukotrienes: mediators of immediate hypersensitivity reactions and inflammation. Science 220 (1983) 568-575
    • (1983) Science , vol.220 , pp. 568-575
    • Samuelsson, B.1
  • 2
    • 33644815175 scopus 로고    scopus 로고
    • Treatment of asthma with antileukotrienes: first line or last resort therapy?
    • Dahlen S.E. Treatment of asthma with antileukotrienes: first line or last resort therapy?. Eur. J. Pharmacol. 533 (2006) 40-56
    • (2006) Eur. J. Pharmacol. , vol.533 , pp. 40-56
    • Dahlen, S.E.1
  • 4
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • (Published erratum appears in Nat. Struct. Biol. 5(3) (1998) 242)
    • Gillmor S.A., Villasenor A., Fletterick R., et al. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat. Struct. Biol. 4 (1997) 1003-1009 (Published erratum appears in Nat. Struct. Biol. 5(3) (1998) 242)
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1003-1009
    • Gillmor, S.A.1    Villasenor, A.2    Fletterick, R.3
  • 5
    • 0037066761 scopus 로고    scopus 로고
    • Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase
    • Kulkarni S., Das S., Funk C.D., et al. Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase. J. Biol. Chem. 277 (2002) 13167-13174
    • (2002) J. Biol. Chem. , vol.277 , pp. 13167-13174
    • Kulkarni, S.1    Das, S.2    Funk, C.D.3
  • 6
    • 18144399317 scopus 로고    scopus 로고
    • Structural organization of the regulatory domain of human 5-lipoxygenase
    • Allard J.B., and Brock T.G. Structural organization of the regulatory domain of human 5-lipoxygenase. Curr. Protein Pept. Sci. 6 (2005) 125-131
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 125-131
    • Allard, J.B.1    Brock, T.G.2
  • 7
    • 58149487199 scopus 로고    scopus 로고
    • Human Dicer C-terminus functions as a 5-lipoxygenase binding domain
    • Dincbas-Renqvist V., Pepin G., Rakonjac M., et al. Human Dicer C-terminus functions as a 5-lipoxygenase binding domain. Biochim. Biophys. Acta 1789 (2009) 99-108
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 99-108
    • Dincbas-Renqvist, V.1    Pepin, G.2    Rakonjac, M.3
  • 8
    • 34347397335 scopus 로고    scopus 로고
    • 5-Lipoxygenase: regulation of expression and enzyme activity
    • Rådmark O., Werz O., Steinhilber D., et al. 5-Lipoxygenase: regulation of expression and enzyme activity. Trends Biochem. Sci. 32 (2007) 332-341
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 332-341
    • Rådmark, O.1    Werz, O.2    Steinhilber, D.3
  • 9
    • 0345008359 scopus 로고
    • On the nature of the 5-lipoxygenase reaction in human leukocytes: enzyme purification and requirement for multiple stimulatory factors
    • Rouzer C.A., and Samuelsson B. On the nature of the 5-lipoxygenase reaction in human leukocytes: enzyme purification and requirement for multiple stimulatory factors. Proc. Natl. Acad. Sci. USA 82 (1985) 6040-6044
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6040-6044
    • Rouzer, C.A.1    Samuelsson, B.2
  • 10
    • 0034624019 scopus 로고    scopus 로고
    • The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity
    • Hammarberg T., Provost P., Persson B., et al. The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity. J. Biol. Chem. 275 (2000) 38787-38793
    • (2000) J. Biol. Chem. , vol.275 , pp. 38787-38793
    • Hammarberg, T.1    Provost, P.2    Persson, B.3
  • 11
    • 72449124354 scopus 로고    scopus 로고
    • Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102
    • Esser J., Rakonjac M., Hofmann B., et al. Coactosin-like protein functions as a stabilizing chaperone for 5-lipoxygenase: role of tryptophan 102. Biochem. J. 425 (2010) 265-274
    • (2010) Biochem. J. , vol.425 , pp. 265-274
    • Esser, J.1    Rakonjac, M.2    Hofmann, B.3
  • 12
    • 0035808471 scopus 로고    scopus 로고
    • The N-terminal "beta-barrel" domain of 5-lipoxygenase is essential for nuclear membrane translocation
    • Chen X.S., and Funk C.D. The N-terminal "beta-barrel" domain of 5-lipoxygenase is essential for nuclear membrane translocation. J. Biol. Chem. 276 (2001) 811-818
    • (2001) J. Biol. Chem. , vol.276 , pp. 811-818
    • Chen, X.S.1    Funk, C.D.2
  • 13
    • 0942276361 scopus 로고    scopus 로고
    • Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium
    • Walther M., Wiesner R., and Kuhn H. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic roles of surface-exposed hydrophobic amino acids and calcium. J. Biol. Chem. 279 (2004) 3717-3725
    • (2004) J. Biol. Chem. , vol.279 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kuhn, H.3
  • 14
    • 8744267513 scopus 로고    scopus 로고
    • Modulation of human 5-lipoxygenase activity by membrane lipids
    • Pande A.H., Moe D., Nemec K.N., et al. Modulation of human 5-lipoxygenase activity by membrane lipids. Biochemistry 43 (2004) 14653-14666
    • (2004) Biochemistry , vol.43 , pp. 14653-14666
    • Pande, A.H.1    Moe, D.2    Nemec, K.N.3
  • 15
    • 22244452942 scopus 로고    scopus 로고
    • Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase
    • Pande A.H., Qin S., and Tatulian S.A. Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase. Biophys. J. 88 (2005) 4084-4094
    • (2005) Biophys. J. , vol.88 , pp. 4084-4094
    • Pande, A.H.1    Qin, S.2    Tatulian, S.A.3
  • 16
    • 0035844240 scopus 로고    scopus 로고
    • 5-Lipoxygenase Interacts with Coactosin-like protein
    • Provost P., Doucet J., Hanmmarberg T., et al. 5-Lipoxygenase Interacts with Coactosin-like protein. J. Biol. Chem. 276 (2001) 16520-16527
    • (2001) J. Biol. Chem. , vol.276 , pp. 16520-16527
    • Provost, P.1    Doucet, J.2    Hanmmarberg, T.3
  • 17
    • 33748348405 scopus 로고    scopus 로고
    • Coactosin-like protein supports 5-lipoxygenase enzyme activity and up-regulates leukotriene A4 production
    • Rakonjac M., Fischer L., Provost P., et al. Coactosin-like protein supports 5-lipoxygenase enzyme activity and up-regulates leukotriene A4 production. Proc. Natl. Acad. Sci. USA 103 (2006) 13150-13155
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13150-13155
    • Rakonjac, M.1    Fischer, L.2    Provost, P.3
  • 18
    • 68549132365 scopus 로고    scopus 로고
    • Hyperforin is a novel type of 5-lipoxygenase inhibitor with high efficacy in vivo
    • Feisst C., Pergola C., Rakonjac M., et al. Hyperforin is a novel type of 5-lipoxygenase inhibitor with high efficacy in vivo. Cell. Mol. Life Sci. 66 (2009) 2759-2771
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2759-2771
    • Feisst, C.1    Pergola, C.2    Rakonjac, M.3
  • 19
    • 5144223918 scopus 로고    scopus 로고
    • Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding
    • Hammel M., Walther M., Prassl R., et al. Structural flexibility of the N-terminal beta-barrel domain of 15-lipoxygenase-1 probed by small angle X-ray scattering. Functional consequences for activity regulation and membrane binding. J. Mol. Biol. 343 (2004) 917-929
    • (2004) J. Mol. Biol. , vol.343 , pp. 917-929
    • Hammel, M.1    Walther, M.2    Prassl, R.3
  • 20
    • 0032751682 scopus 로고    scopus 로고
    • Colipase: structure and interaction with pancreatic lipase
    • van Tilbeurgh H., Bezzine S., Cambillau C., et al. Colipase: structure and interaction with pancreatic lipase. Biochim. Biophys. Acta 1441 (1999) 173-184
    • (1999) Biochim. Biophys. Acta , vol.1441 , pp. 173-184
    • van Tilbeurgh, H.1    Bezzine, S.2    Cambillau, C.3
  • 22
    • 33750102847 scopus 로고    scopus 로고
    • Therapeutic options for 5-lipoxygenase inhibitors
    • Werz O., and Steinhilber D. Therapeutic options for 5-lipoxygenase inhibitors. Pharmacol. Ther. 112 (2006) 701-718
    • (2006) Pharmacol. Ther. , vol.112 , pp. 701-718
    • Werz, O.1    Steinhilber, D.2
  • 23
    • 38749113897 scopus 로고    scopus 로고
    • What's all the FLAP about?: 5-lipoxygenase-activating protein inhibitors for inflammatory diseases
    • Evans J.F., Ferguson A.D., Mosley R.T., et al. What's all the FLAP about?: 5-lipoxygenase-activating protein inhibitors for inflammatory diseases. Trends Pharmacol. Sci. 29 (2008) 72-78
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 72-78
    • Evans, J.F.1    Ferguson, A.D.2    Mosley, R.T.3
  • 24
    • 7244239214 scopus 로고    scopus 로고
    • Multiple nuclear localization sequences allow modulation of 5-lipoxygenase nuclear import
    • Luo M., Pang C.W., Gerken A.E., et al. Multiple nuclear localization sequences allow modulation of 5-lipoxygenase nuclear import. Traffic 5 (2004) 847-854
    • (2004) Traffic , vol.5 , pp. 847-854
    • Luo, M.1    Pang, C.W.2    Gerken, A.E.3
  • 25
    • 0030972551 scopus 로고    scopus 로고
    • Rapid import of cytosolic 5-lipoxygenase into the nucleus of neutrophils after in vivo recruitment and in vitro adherence
    • Brock T.G., McNish R.W., Bailie M.B., et al. Rapid import of cytosolic 5-lipoxygenase into the nucleus of neutrophils after in vivo recruitment and in vitro adherence. J. Biol. Chem. 272 (1997) 8276-8280
    • (1997) J. Biol. Chem. , vol.272 , pp. 8276-8280
    • Brock, T.G.1    McNish, R.W.2    Bailie, M.B.3
  • 26
    • 58649091333 scopus 로고    scopus 로고
    • Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export
    • Flamand N., Luo M., Peters-Golden M., et al. Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export. J. Biol. Chem. 284 (2009) 306-313
    • (2009) J. Biol. Chem. , vol.284 , pp. 306-313
    • Flamand, N.1    Luo, M.2    Peters-Golden, M.3
  • 28
    • 0036464591 scopus 로고    scopus 로고
    • Activation of 5-lipoxygenase by cell stress is calcium independent in human polymorphonuclear leukocytes
    • Werz O., Bürkert E., Samuelsson B., et al. Activation of 5-lipoxygenase by cell stress is calcium independent in human polymorphonuclear leukocytes. Blood 99 (2002) 1044-1052
    • (2002) Blood , vol.99 , pp. 1044-1052
    • Werz, O.1    Bürkert, E.2    Samuelsson, B.3
  • 29
    • 0036719157 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases phosphorylate 5-lipoxygenase and stimulate 5-lipoxygenase product formation in leukocytes
    • Werz O., Burkert E., Fischer L., et al. Extracellular signal-regulated kinases phosphorylate 5-lipoxygenase and stimulate 5-lipoxygenase product formation in leukocytes. FASEB J. 16 (2002) 1441-1443
    • (2002) FASEB J. , vol.16 , pp. 1441-1443
    • Werz, O.1    Burkert, E.2    Fischer, L.3
  • 30
    • 0035871688 scopus 로고    scopus 로고
    • Phorbol ester up-regulates capacities for nuclear translocation and phosphorylation of 5-lipoxygenase in Mono Mac 6 cells and human polymorphonuclear leukocytes
    • Werz O., Klemm J., Samuelsson B., et al. Phorbol ester up-regulates capacities for nuclear translocation and phosphorylation of 5-lipoxygenase in Mono Mac 6 cells and human polymorphonuclear leukocytes. Blood 97 (2001) 2487-2495
    • (2001) Blood , vol.97 , pp. 2487-2495
    • Werz, O.1    Klemm, J.2    Samuelsson, B.3
  • 31
    • 24344468621 scopus 로고    scopus 로고
    • 2+ mobilisation in polymorphonuclear leukocytes involving Src family kinases
    • 2+ mobilisation in polymorphonuclear leukocytes involving Src family kinases. Biochim. Biophys. Acta 1736 (2005) 109-119
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 109-119
    • Fischer, L.1    Poeckel, D.2    Buerkert, E.3
  • 32
    • 28844492469 scopus 로고    scopus 로고
    • Phosphorylation by protein kinase a inhibits nuclear import of 5-lipoxygenase
    • Luo M., Jones S.M., Flamand N., et al. Phosphorylation by protein kinase a inhibits nuclear import of 5-lipoxygenase. J. Biol. Chem. 280 (2005) 40609-40616
    • (2005) J. Biol. Chem. , vol.280 , pp. 40609-40616
    • Luo, M.1    Jones, S.M.2    Flamand, N.3
  • 33
    • 0036076153 scopus 로고    scopus 로고
    • Cyclic AMP-mediated inhibition of 5-lipoxygenase translocation and leukotriene biosynthesis in human neutrophils
    • Flamand N., Surette M.E., Picard S., et al. Cyclic AMP-mediated inhibition of 5-lipoxygenase translocation and leukotriene biosynthesis in human neutrophils. Mol. Pharmacol. 62 (2002) 250-256
    • (2002) Mol. Pharmacol. , vol.62 , pp. 250-256
    • Flamand, N.1    Surette, M.E.2    Picard, S.3
  • 34
    • 33644857422 scopus 로고    scopus 로고
    • Arachidonic acid regulates the translocation of 5-lipoxygenase to the nuclear membranes in human neutrophils
    • Flamand N., Lefebvre J., Surette M.E., et al. Arachidonic acid regulates the translocation of 5-lipoxygenase to the nuclear membranes in human neutrophils. J. Biol. Chem. 281 (2006) 129-136
    • (2006) J. Biol. Chem. , vol.281 , pp. 129-136
    • Flamand, N.1    Lefebvre, J.2    Surette, M.E.3
  • 35
    • 42549138031 scopus 로고    scopus 로고
    • Capturing proteins that bind polyunsaturated fatty acids: demonstration using arachidonic acid and eicosanoids
    • Brock T.G. Capturing proteins that bind polyunsaturated fatty acids: demonstration using arachidonic acid and eicosanoids. Lipids 43 (2008) 161-169
    • (2008) Lipids , vol.43 , pp. 161-169
    • Brock, T.G.1
  • 36
    • 2342503757 scopus 로고    scopus 로고
    • The membrane organization of leukotriene synthesis
    • (Epub 2004 Apr 14)
    • Mandal A.K., Skoch J., Bacskai B.J., et al. The membrane organization of leukotriene synthesis. Proc. Natl. Acad. Sci. USA 101 (2004) 6587-6592 (Epub 2004 Apr 14)
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6587-6592
    • Mandal, A.K.1    Skoch, J.2    Bacskai, B.J.3
  • 37
    • 30044446862 scopus 로고    scopus 로고
    • 5-Lipoxygenase activating protein homodimer in human neutrophils. Evidence for a role in leukotriene synthesis
    • Plante H., Picard S., Mancini J., et al. 5-Lipoxygenase activating protein homodimer in human neutrophils. Evidence for a role in leukotriene synthesis. Biochem. J. 393 (2006) 211-218
    • (2006) Biochem. J. , vol.393 , pp. 211-218
    • Plante, H.1    Picard, S.2    Mancini, J.3
  • 38
    • 34547560098 scopus 로고    scopus 로고
    • Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein
    • Ferguson A.D., McKeever B.M., Xu S., et al. Crystal structure of inhibitor-bound human 5-lipoxygenase-activating protein. Science 317 (2007) 510-512
    • (2007) Science , vol.317 , pp. 510-512
    • Ferguson, A.D.1    McKeever, B.M.2    Xu, S.3
  • 39
    • 58149511977 scopus 로고    scopus 로고
    • The nuclear membrane organization of leukotriene synthesis
    • Mandal A.K., Jones P.B., Bair A.M., et al. The nuclear membrane organization of leukotriene synthesis. Proc. Natl. Acad. Sci. USA 105 (2008) 20434-20439
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20434-20439
    • Mandal, A.K.1    Jones, P.B.2    Bair, A.M.3
  • 40
    • 33947365144 scopus 로고    scopus 로고
    • Leukotriene synthesis in response to A23187 is inhibited by methyl-beta-cyclodextrin in RBL-2H3 cells
    • You H.J., Seo J.M., Moon J.Y., et al. Leukotriene synthesis in response to A23187 is inhibited by methyl-beta-cyclodextrin in RBL-2H3 cells. Mol. Cell 23 (2007) 57-63
    • (2007) Mol. Cell , vol.23 , pp. 57-63
    • You, H.J.1    Seo, J.M.2    Moon, J.Y.3
  • 41
    • 71049123949 scopus 로고    scopus 로고
    • Protein profiling of plasma membranes defines aberrant signaling pathways in mantle cell lymphoma
    • Boyd R.S., Jukes-Jones R., Walewska R., et al. Protein profiling of plasma membranes defines aberrant signaling pathways in mantle cell lymphoma. Mol. Cell. Proteomics 8 (2009) 1501-1515
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1501-1515
    • Boyd, R.S.1    Jukes-Jones, R.2    Walewska, R.3
  • 42
    • 58149398605 scopus 로고    scopus 로고
    • ERK-mediated regulation of leukotriene biosynthesis by androgens: a molecular basis for gender differences in inflammation and asthma
    • Pergola C., Dodt G., Rossi A., et al. ERK-mediated regulation of leukotriene biosynthesis by androgens: a molecular basis for gender differences in inflammation and asthma. Proc. Natl. Acad. Sci. USA 105 (2008) 19881-19886
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19881-19886
    • Pergola, C.1    Dodt, G.2    Rossi, A.3
  • 43
    • 67349265997 scopus 로고    scopus 로고
    • Leukocyte lipid bodies - biogenesis and functions in inflammation
    • Bozza P.T., Magalhaes K.G., and Weller P.F. Leukocyte lipid bodies - biogenesis and functions in inflammation. Biochim. Biophys. Acta 1791 (2009) 540-551
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 540-551
    • Bozza, P.T.1    Magalhaes, K.G.2    Weller, P.F.3
  • 44
    • 59649083719 scopus 로고    scopus 로고
    • Cell and molecular biology of nuclear actin
    • Hofmann W.A. Cell and molecular biology of nuclear actin. Int. Rev. Cell Mol. Biol. 273 (2009) 219-263
    • (2009) Int. Rev. Cell Mol. Biol. , vol.273 , pp. 219-263
    • Hofmann, W.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.