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Volumn 111, Issue 6, 1999, Pages 516-524

Phospholipase A2 enzymes in eicosanoid generation

Author keywords

Arachidonic acid; Enzymes; Leukotrienes; Phospholipases; Prostaglandins

Indexed keywords

AMINO ACID; ARACHIDONIC ACID; CALCIUM; FATTY ACID; GLYCEROPHOSPHOLIPID; ICOSANOID; LEUKOTRIENE; PHOSPHOLIPASE A2; PROSTANOID; CELL SURFACE RECEPTOR; ISOENZYME; MEMBRANE LIPID; PHOSPHOLIPASE A; PHOSPHOLIPASE A2 RECEPTOR; PHOSPHOLIPID; TUMOR PROTEIN;

EID: 0033219838     PISSN: 1081650X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1525-1381.1999.99321.x     Document Type: Review
Times cited : (62)

References (67)
  • 1
    • 0028338536 scopus 로고
    • Diversity of group types, regulation, and function of phospholipase A2.
    • 1 Dennis E.A. Diversity of group types, regulation, and function of phospholipase A 2. J. Biol. Chem. 269: 13057 13060, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 13057-13060
    • Dennis, E.A.1
  • 2
    • 0030614354 scopus 로고    scopus 로고
    • The growing phospholipase A2 superfamily of signal transduction enzymes.
    • 2 Dennis E.A. The growing phospholipase A 2 superfamily of signal transduction enzymes. Trends Biochem. Sci. 2: 1 2, 1997.
    • (1997) Trends Biochem. Sci , vol.2 , pp. 1-2
    • Dennis, E.A.1
  • 4
    • 0030798853 scopus 로고    scopus 로고
    • A reassessment of the low molecular weight phospholipase A2 gene family in mammals.
    • 4 Tischfield J.A. A reassessment of the low molecular weight phospholipase A 2 gene family in mammals. J. Biol. Chem. 272: 17247 17250, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 17247-17250
    • Tischfield, J.A.1
  • 5
    • 0030836586 scopus 로고    scopus 로고
    • Properties and regulation of cytosolic phospholipase A2.
    • 5 Leslie C.C. Properties and regulation of cytosolic phospholipase A 2. J. Biol. Chem. 272: 16709 16712, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 16709-16712
    • Leslie, C.C.1
  • 6
    • 0031010112 scopus 로고    scopus 로고
    • Function and inhibition of intracellular calcium‐independent phospholipase A2.
    • 6 Balsinde J. & Dennis E.A. Function and inhibition of intracellular calcium‐independent phospholipase A 2. J. Biol. Chem. 272: 16069 16072, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 16069-16072
    • Balsinde, J.1    Dennis, E.A.2
  • 9
    • 0024554009 scopus 로고
    • Cloning and expression of phospholipase A2 present in rheumatoid arthritic synovial fluid.
    • 9 Seilhamer J.J., Pruzanski W., Vadas P., et al. Cloning and expression of phospholipase A 2 present in rheumatoid arthritic synovial fluid. J. Biol. Chem. 264: 5335 5338, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 5335-5338
    • Seilhamer, J.J.1    Pruzanski, W.2    Vadas, P.3
  • 10
    • 0029861006 scopus 로고    scopus 로고
    • Type II phospholipase A2 associated with cell surfaces via C‐terminal heparin‐binding lysine residues augments stimulus‐initiated delayed prostaglandin generation.
    • 10 Murakami M., Nakatani Y., Kudo I. Type II phospholipase A 2 associated with cell surfaces via C‐terminal heparin‐binding lysine residues augments stimulus‐initiated delayed prostaglandin generation. J. Biol. Chem. 271: 30041 30051, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 30041-30051
    • Murakami, M.1    Nakatani, Y.2    Kudo, I.3
  • 11
    • 0029860085 scopus 로고    scopus 로고
    • Binding of human phospholipase A2 to proteoglycans, differential effect of glycosaminoglycans on enzyme activity.
    • 11 Sartipy P., Johansen B., Camejo G., et al. Binding of human phospholipase A 2 to proteoglycans, differential effect of glycosaminoglycans on enzyme activity. J. Biol. Chem. 271: 26307 26314, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 26307-26314
    • Sartipy, P.1    Johansen, B.2    Camejo, G.3
  • 12
    • 0029995054 scopus 로고    scopus 로고
    • Low‐molecular weight, calcium‐dependent phospholipase A 2 genes are linked and map to homologous chromosome regions in mouse and human.
    • 12 Tischfield J.A., Xia Y.‐R., Shih D.M., et al. Low‐molecular weight, calcium‐dependent phospholipase A  2 genes are linked and map to homologous chromosome regions in mouse and human. Genomics 32: 328 333, 1996.
    • (1996) Genomics , vol.32 , pp. 328-333
    • Tischfield, J.A.1    Xia, Y.‐R.2    Shih, D.M.3
  • 13
    • 0028998255 scopus 로고
    • The secretory phospholipase A2 gene is a candidate for the Mom1 locus, a major modifier of Apc Min‐induced intestinal neoplasia.
    • 13 MacPhee M., Chepenik K.P., Liddell R., et al. The secretory phospholipase A 2 gene is a candidate for the Mom1 locus, a major modifier of Apc Min‐induced intestinal neoplasia. Cell 81: 957 966, 1995.
    • (1995) Cell , vol.81 , pp. 957-966
    • MacPhee, M.1    Chepenik, K.P.2    Liddell, R.3
  • 14
    • 0029152947 scopus 로고
    • A natural disruption of the secretory group II phospholipase A 2 gene in inbred mouse strains.
    • 14 Kennedy B.P., Payette P., Mudgett J., et al. A natural disruption of the secretory group II phospholipase A  2 gene in inbred mouse strains. J. Biol. Chem. 270: 22378 22385, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 22378-22385
    • Kennedy, B.P.1    Payette, P.2    Mudgett, J.3
  • 15
    • 0028828611 scopus 로고
    • Absence of secretory phospholipase A2 gene alterations in human colorectal cancer.
    • 15 Riggins G.J., Markowitz S., Wilson J.K., et al. Absence of secretory phospholipase A 2 gene alterations in human colorectal cancer. Cancer Res. 55: 5184 5186, 1995.
    • (1995) Cancer Res , vol.55 , pp. 5184-5186
    • Riggins, G.J.1    Markowitz, S.2    Wilson, J.K.3
  • 16
    • 0031730346 scopus 로고    scopus 로고
    • Gene expression of cyclooxygenase‐2, group II and cytosolic phospholipase A2 in human colon cancer.
    • 16 Dimberg J., Samuelsson A., Hugander A., Soderkvist P. Gene expression of cyclooxygenase‐2, group II and cytosolic phospholipase A 2 in human colon cancer. Anticancer Res. 18: 3283 3287, 1998.
    • (1998) Anticancer Res , vol.18 , pp. 3283-3287
    • Dimberg, J.1    Samuelsson, A.2    Hugander, A.3    Soderkvist, P.4
  • 17
    • 0029882783 scopus 로고    scopus 로고
    • Expression of human group II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate.
    • 17 Grass D.S., Felkner R.H., Chiang M.‐Y., et al. Expression of human group II PLA 2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate. J. Clin. Invest. 97: 2233 2241, 1996.
    • (1996) J. Clin. Invest , vol.97 , pp. 2233-2241
    • Grass, D.S.1    Felkner, R.H.2    Chiang, M.‐Y.3
  • 19
    • 0029860316 scopus 로고    scopus 로고
    • A heparin‐sensitive phospholipase A2 and prostaglandin endoperoxide synthase‐2 are functionally linked in the delayed phase of prostaglandin D2 generation in mouse bone marrow‐derived mast cells.
    • 19 Bingham III C.O., Murakami M., Fujishima H., et al. A heparin‐sensitive phospholipase A 2 and prostaglandin endoperoxide synthase‐2 are functionally linked in the delayed phase of prostaglandin D 2 generation in mouse bone marrow‐derived mast cells. J. Biol. Chem. 271: 25936 25944, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 25936-25944
    • Bingham, C.O.1    Murakami, M.2    Fujishima, H.3
  • 21
    • 0027992088 scopus 로고
    • Cloning and characterization of novel rat and mouse low molecular weight Ca2+‐dependent phospholipase A2s containing 16 cysteines.
    • 21 Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A. Cloning and characterization of novel rat and mouse low molecular weight Ca 2+ ‐dependent phospholipase A 2 s containing 16 cysteines. J. Biol. Chem. 269: 23018 23024, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 23018-23024
    • Chen, J.1    Engle, S.J.2    Seilhamer, J.J.3    Tischfield, J.A.4
  • 22
    • 0030757375 scopus 로고    scopus 로고
    • Detection of secretory phospholipase A2s related to but not identical to type IIA isozyme in cultured mast cells.
    • 22 Murakami M., Tada K., Shimbara S., et al. Detection of secretory phospholipase A 2 s related to but not identical to type IIA isozyme in cultured mast cells. FEBS Lett. 413: 249 254, 1997.
    • (1997) FEBS Lett , vol.413 , pp. 249-254
    • Murakami, M.1    Tada, K.2    Shimbara, S.3
  • 23
    • 0032486481 scopus 로고    scopus 로고
    • The functions of five distinct 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.
    • 23 Murakami M., Shimbara S., Kambe T., et al. The functions of five distinct phospholipase A 2 s in regulating arachidonic acid release. Type IIa and type V secretory phospholipase A 2 s are functionally redundant and act in concert with cytosolic phospholipase A 2. J. Biol. Chem. 273: 14411 14423, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 14411-14423
    • Murakami, M.1    Shimbara, S.2    Kambe, T.3
  • 24
    • 0027934181 scopus 로고
    • Cloning and recombinant expression of a novel human low molecular weight Ca2+‐dependent phospholipase A2.
    • 24 Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A. Cloning and recombinant expression of a novel human low molecular weight Ca 2+ ‐dependent phospholipase A 2. J. Biol. Chem. 269: 2365 2368, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 2365-2368
    • Chen, J.1    Engle, S.J.2    Seilhamer, J.J.3    Tischfield, J.A.4
  • 25
    • 0030905731 scopus 로고    scopus 로고
    • Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2.
    • 25 Cupillard L., Koumanov K., Mattei M.G., et al. Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A 2. J. Biol. Chem. 272: 15745 15752, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 15745-15752
    • Cupillard, L.1    Koumanov, K.2    Mattei, M.G.3
  • 26
    • 0031010458 scopus 로고    scopus 로고
    • Analysis of the secretory phospholipase A2 that mediates prostaglandin production in mast cells.
    • 26 Reddy S.T., Winstead M.V., Tischfield J.A., Herschman H.R. Analysis of the secretory phospholipase A 2 that mediates prostaglandin production in mast cells. J. Biol. Chem. 272: 13591 13596, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 13591-13596
    • Reddy, S.T.1    Winstead, M.V.2    Tischfield, J.A.3    Herschman, H.R.4
  • 27
    • 0029753778 scopus 로고    scopus 로고
    • Novel group V phospholipase A2 involved in arachidonic acid mobilization in murine P388D1 macrophages.
    • 27 Balboa M.A., Balsinde J., Winstead M.V., et al. Novel group V phospholipase A 2 involved in arachidonic acid mobilization in murine P388D1 macrophages. J. Biol. Chem. 271: 32381 32384, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 32381-32384
    • Balboa, M.A.1    Balsinde, J.2    Winstead, M.V.3
  • 28
    • 0029862974 scopus 로고    scopus 로고
    • Distinct roles in signal transduction for each of the phospholipase A2 enzymes present in P388D1 macrophages.
    • 28 Balsinde J. & Denis E.A. Distinct roles in signal transduction for each of the phospholipase A 2 enzymes present in P388D1 macrophages. J. Biol. Chem. 271: 6758 6765, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 6758-6765
    • Balsinde, J.1    Denis, E.A.2
  • 29
    • 0024340136 scopus 로고
    • Identification and properties of very high affinity brain membrane‐binding sites for a neurotoxic phospholipase from taipan venom.
    • 29 Lambeau G., Barhanin J., Schweitz S., et al. Identification and properties of very high affinity brain membrane‐binding sites for a neurotoxic phospholipase from taipan venom. J. Biol. Chem. 264: 11503 11510, 1989.
    • (1989) J. Biol. Chem , vol.264 , pp. 11503-11510
    • Lambeau, G.1    Barhanin, J.2    Schweitz, S.3
  • 30
    • 0025300683 scopus 로고
    • Identification and purification of a very high affinity binding protein for toxic phospholipase A2s in skeletal muscle.
    • 30 Lambeau G., Schmid‐Alliana A., Luzdunski M., Barhanin J. Identification and purification of a very high affinity binding protein for toxic phospholipase A 2 s in skeletal muscle. J. Biol. Chem. 265: 9526 9532, 1990.
    • (1990) J. Biol. Chem , vol.265 , pp. 9526-9532
    • Lambeau, G.1    Schmid‐Alliana, A.2    Luzdunski, M.3    Barhanin, J.4
  • 31
    • 0028954284 scopus 로고
    • The human 180‐kDa receptor for secretory phospholipases A2: Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization.
    • 31 Ancian P., Lambeau G., Mattei M.G., Luzdunski M. The human 180‐kDa receptor for secretory phospholipases A 2: Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization. J. Biol. Chem. 270: 8963 8970, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 8963-8970
    • Ancian, P.1    Lambeau, G.2    Mattei, M.G.3    Luzdunski, M.4
  • 32
    • 0028941455 scopus 로고
    • Structural elements of secretory phospholipases A2 involved in the binding to M‐type receptors.
    • 32 Lambeau G., Ancian P., Nicolas J.P., et al. Structural elements of secretory phospholipases A 2 involved in the binding to M‐type receptors. J. Biol. Chem. 270: 5534 5540, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 5534-5540
    • Lambeau, G.1    Ancian, P.2    Nicolas, J.P.3
  • 33
    • 0028084979 scopus 로고
    • Cloning and expression of a membrane receptor for secretory phospholipases A2.
    • 33 Lambeau G., Ancian P., Barhanin J., Lazdunski M. Cloning and expression of a membrane receptor for secretory phospholipases A 2. J. Biol. Chem. 269: 1575 1578, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 1575-1578
    • Lambeau, G.1    Ancian, P.2    Barhanin, J.3    Lazdunski, M.4
  • 34
    • 0033548622 scopus 로고    scopus 로고
    • Both group IB and group IIA secreted phospholipases A2 are natural ligands of the mouse 180‐kDa M‐type receptor.
    • 34 Cupillard L., Mulherkar R., Gomez N., et al. Both group IB and group IIA secreted phospholipases A 2 are natural ligands of the mouse 180‐kDa M‐type receptor. J. Biol. Chem. 274: 7043 7051, 1999.
    • (1999) J. Biol. Chem , vol.274 , pp. 7043-7051
    • Cupillard, L.1    Mulherkar, R.2    Gomez, N.3
  • 35
    • 0031689398 scopus 로고    scopus 로고
    • Mechanisms that account for the selective release of arachidonic acid from intact cells by secretory phospholipase A2.
    • 35 Fonteh A.N., Samet J.M., Surette M., et al. Mechanisms that account for the selective release of arachidonic acid from intact cells by secretory phospholipase A 2. Biochim. Biophys. Acta 1393: 253 266, 1998.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 253-266
    • Fonteh, A.N.1    Samet, J.M.2    Surette, M.3
  • 36
    • 0028339812 scopus 로고
    • Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca2+‐dependent lipid‐binding domain and a Ca2+‐independent catalytic domain.
    • 36 Nalefski E.A., Sultzman L.A., Martin D.M., et al. Delineation of two functionally distinct domains of cytosolic phospholipase A 2, a regulatory Ca 2+ ‐dependent lipid‐binding domain and a Ca 2+ ‐independent catalytic domain. J. Biol. Chem. 269: 18239 18249, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 18239-18249
    • Nalefski, E.A.1    Sultzman, L.A.2    Martin, D.M.3
  • 37
    • 0031941133 scopus 로고    scopus 로고
    • Group IV cytosolic phospholipase A2 binds with high affinity and specificity to phosphatidylinositol 4,5‐bisphosphate, resulting in dramatic increases in activity.
    • 37 Mosoir M., Six D.A., Dennis E.A. Group IV cytosolic phospholipase A2 binds with high affinity and specificity to phosphatidylinositol 4,5‐bisphosphate, resulting in dramatic increases in activity. J. Biol. Chem. 273: 2184 2191, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 2184-2191
    • Mosoir, M.1    Six, D.A.2    Dennis, E.A.3
  • 38
    • 0029020361 scopus 로고
    • Translocation of the 85‐kDa phospholipase A2 from the cytosol to the nuclear envelope in rat basophilic leukemia cells stimulated with calcium ionophore or IgE/antigen.
    • 38 Glover S., De Carvalho M.S., Bayburt T., et al. Translocation of the 85‐kDa phospholipase A 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.
    • (1995) J. Biol. Chem , vol.270 , pp. 15359-15367
    • Glover, S.1    De Carvalho, M.S.2    Bayburt, T.3
  • 39
    • 0027519767 scopus 로고
    • Redistribution of 5‐lipoxygenase and cytosolic phospholipase A2 to the nuclear fraction upon macrophage activation.
    • 39 Peters‐Golden M. & McNish R.W. Redistribution of 5‐lipoxygenase and cytosolic phospholipase A 2 to the nuclear fraction upon macrophage activation. Biochem. Biophys. Res. Commun. 196: 147 153, 1993.
    • (1993) Biochem. Biophys. Res. Commun , vol.196 , pp. 147-153
    • Peters‐Golden, M.1    McNish, R.W.2
  • 40
    • 0033582441 scopus 로고    scopus 로고
    • Critical duration of intracellular Ca2+ response required for continuous translocation and activation of cytosolic phospholipase A2.
    • 40 Hirabayashi T., Kume K., Hirose K., et al. Critical duration of intracellular Ca 2+ response required for continuous translocation and activation of cytosolic phospholipase A 2. J. Biol. Chem. 274: 5163 5169, 1999.
    • (1999) J. Biol. Chem , vol.274 , pp. 5163-5169
    • Hirabayashi, T.1    Kume, K.2    Hirose, K.3
  • 41
    • 0032478733 scopus 로고    scopus 로고
    • The role of calcium and phosphorylation of cytosolic phospholipase A2 in regulating arachidonic acid release in macrophages.
    • 41 Qiu Z.H., Gijon M.A., De Carvalho M.S., et al. The role of calcium and phosphorylation of cytosolic phospholipase A 2 in regulating arachidonic acid release in macrophages. J. Biol. Chem. 273: 8203 8211, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 8203-8211
    • Qiu, Z.H.1    Gijon, M.A.2    De Carvalho, M.S.3
  • 42
    • 0027338999 scopus 로고
    • cPLA2 is phosphorylated and activated by MAP kinase.
    • 42 Lin L.L., Wartmann M., Lin A.Y., et al. cPLA 2 is phosphorylated and activated by MAP kinase. Cell 72: 269 278, 1993.
    • (1993) Cell , vol.72 , pp. 269-278
    • Lin, L.L.1    Wartmann, M.2    Lin, A.Y.3
  • 43
    • 0029862747 scopus 로고    scopus 로고
    • Identification of phosphorylation sites of human 85‐kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes.
    • 43 De Carvalho M.G., McCormack A.L., Olson E., et al. Identification of phosphorylation sites of human 85‐kDa cytosolic phospholipase A 2 expressed in insect cells and present in human monocytes. J. Biol. Chem. 271: 6987 6997, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 6987-6997
    • De Carvalho, M.G.1    McCormack, A.L.2    Olson, E.3
  • 44
    • 0028987885 scopus 로고
    • Cytosolic phospholipase A2 gene in human and rat: Chromosomal localization and polymorphic markers.
    • 44 Tay A., Simon J.S., Squire J., et al. Cytosolic phospholipase A 2 gene in human and rat: Chromosomal localization and polymorphic markers. Genomics 26: 138 141, 1995.
    • (1995) Genomics , vol.26 , pp. 138-141
    • Tay, A.1    Simon, J.S.2    Squire, J.3
  • 45
    • 0027944170 scopus 로고
    • Assignment of the human prostaglandin‐endoperoxide synthase 2 (PTGS2) gene to 1q25 by fluorescence in situ hybridization.
    • 45 Tay A., Squire J.A., Goldberg H., Skorecki K. Assignment of the human prostaglandin‐endoperoxide synthase 2 (PTGS2) gene to 1q25 by fluorescence in situ hybridization. Genomics 23: 718 719, 1994.
    • (1994) Genomics , vol.23 , pp. 718-719
    • Tay, A.1    Squire, J.A.2    Goldberg, H.3    Skorecki, K.4
  • 47
    • 0029133572 scopus 로고
    • Interleukin‐3 regulates development of the 5‐lipoxygenase/leukotriene C4 synthase pathway in mouse mast cells.
    • 47 Murakami M., Austen K.F., Bingham III C.O., et al. Interleukin‐3 regulates development of the 5‐lipoxygenase/leukotriene C 4 synthase pathway in mouse mast cells. J. Biol. Chem. 270: 22653 22656, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 22653-22656
    • Murakami, M.1    Austen, K.F.2    Bingham, C.O.3
  • 48
    • 0028854929 scopus 로고
    • c‐kit ligand mediates increased expression of cytosolic phospholipase A2, prostaglandin endoperoxide synthase‐1, and hematopoietic prostaglandin D2 synthase and increased IgE‐dependent prostaglandin D2 generation in immature mouse mast cells.
    • 48 Murakami M., Matsumoto R., Urade Y., et al. c‐ kit ligand mediates increased expression of cytosolic phospholipase A 2, prostaglandin endoperoxide synthase‐1, and hematopoietic prostaglandin D 2 synthase and increased IgE‐dependent prostaglandin D 2 generation in immature mouse mast cells. J. Biol. Chem. 270: 3239 3246, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 3239-3246
    • Murakami, M.1    Matsumoto, R.2    Urade, Y.3
  • 49
    • 0029866745 scopus 로고    scopus 로고
    • Inhibition of monocyte chemotaxis to C‐C chemokines by antisense oligonucleotide for cytosolic phospholipase A2.
    • 49 Locati M., Lamorte G., Luini W., et al. Inhibition of monocyte chemotaxis to C‐C chemokines by antisense oligonucleotide for cytosolic phospholipase A 2. J. Biol. Chem. 271: 6010 6016, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 6010-6016
    • Locati, M.1    Lamorte, G.2    Luini, W.3
  • 50
    • 0030810224 scopus 로고    scopus 로고
    • Cytosolic 85‐kDa phospholipase A2‐mediated release of arachidonic acid is critical for proliferation of vascular smooth muscle cells.
    • 50 Anderson K.M., Roshak A., Winkler J.D., et al. Cytosolic 85‐kDa phospholipase A 2 ‐mediated release of arachidonic acid is critical for proliferation of vascular smooth muscle cells. J. Biol. Chem. 272: 30504 30511, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 30504-30511
    • Anderson, K.M.1    Roshak, A.2    Winkler, J.D.3
  • 51
    • 0031471709 scopus 로고    scopus 로고
    • Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2.
    • 51 Bonventre J.V., Huang Z., Taheri M.R., et al. Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A 2. Nature 390: 622 625, 1997.
    • (1997) Nature , vol.390 , pp. 622-625
    • Bonventre, J.V.1    Huang, Z.2    Taheri, M.R.3
  • 52
    • 0031445523 scopus 로고    scopus 로고
    • Role of cytosolic phospholipase A2 in allergic response and parturition.
    • 52 Uozumi N., Kume K., Nagase T., et al. Role of cytosolic phospholipase A 2 in allergic response and parturition. Nature 390: 618 622, 1997.
    • (1997) Nature , vol.390 , pp. 618-622
    • Uozumi, N.1    Kume, K.2    Nagase, T.3
  • 53
    • 0030835266 scopus 로고    scopus 로고
    • 5‐Lipoxygenase products are necessary for ovalbumin‐induced airway responsiveness in mice.
    • 53 Irvin C.G., Tu Y.P., Sheller J.R., Funk C.D. 5‐Lipoxygenase products are necessary for ovalbumin‐induced airway responsiveness in mice. Am. J. Physiol. 272: L1053 L1058, 1997.
    • (1997) Am. J. Physiol , vol.272 , pp. L1053-L1058
    • Irvin, C.G.1    Tu, Y.P.2    Sheller, J.R.3    Funk, C.D.4
  • 54
    • 0032555643 scopus 로고    scopus 로고
    • A novel calcium‐independent phospholipase A2, cPLA2‐γ, that is prenylated and contains homology to cPLA2.
    • 54 Underwood K.W., Song C., Kriz R.W., et al. A novel calcium‐independent phospholipase A 2, cPLA 2 ‐γ, that is prenylated and contains homology to cPLA 2. J. Biol. Chem. 273: 21926 21932, 1999.
    • (1999) J. Biol. Chem , vol.273 , pp. 21926-21932
    • Underwood, K.W.1    Song, C.2    Kriz, R.W.3
  • 55
    • 0027504207 scopus 로고
    • 5‐lipoxygenase and 5‐lipoxygenase activating protein are localized in the nuclear envelope of activated human leukocytes.
    • 55 Woods J.W., Evans J.F., Ethier D., et al. 5‐lipoxygenase and 5‐lipoxygenase activating protein are localized in the nuclear envelope of activated human leukocytes. J. Exp. Med. 178: 1935 1946, 1993.
    • (1993) J. Exp. Med , vol.178 , pp. 1935-1946
    • Woods, J.W.1    Evans, J.F.2    Ethier, D.3
  • 56
    • 0027958828 scopus 로고
    • Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A 4.
    • 56 Lam B.K., Penrose J.F., Freeman G.J., Austen K.F. Expression cloning of a cDNA for human leukotriene C 4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A  4. Proc. Natl. Acad. Sci. U.S.A. 91: 7663 7667, 1994.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 7663-7667
    • Lam, B.K.1    Penrose, J.F.2    Freeman, G.J.3    Austen, K.F.4
  • 57
    • 0031744790 scopus 로고    scopus 로고
    • Cell biology of the 5‐lipoxygenase pathway.
    • 57 Peters‐Golden M. Cell biology of the 5‐lipoxygenase pathway. Am. J. Respir. Crit. Care Med. 157: S227 S231, 1998.
    • (1998) Am. J. Respir. Crit. Care Med , vol.157 , pp. S227-S231
    • Peters‐Golden, M.1
  • 58
    • 0032540344 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin endoperoxide H synthases‐1 and ‐2 by immunoelectron microscopy.
    • 58 Spencer A.G., Woods J.W., Arakawa T., et al. Subcellular localization of prostaglandin endoperoxide H synthases‐1 and ‐2 by immunoelectron microscopy. J. Biol. Chem. 273: 9886 9893, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 9886-9893
    • Spencer, A.G.1    Woods, J.W.2    Arakawa, T.3
  • 59
    • 0030930401 scopus 로고    scopus 로고
    • Eosinophil lipid bodies: Specific, inducible intracellular sites for enhanced eicosanoid formation.
    • 59 Bozza P.T., Yu W., Penrose J.F., et al. Eosinophil lipid bodies: Specific, inducible intracellular sites for enhanced eicosanoid formation. J. Exp. Med. 186: 909 920, 1997.
    • (1997) J. Exp. Med , vol.186 , pp. 909-920
    • Bozza, P.T.1    Yu, W.2    Penrose, J.F.3
  • 60
    • 0031889388 scopus 로고    scopus 로고
    • Co‐compartmentalization of MAP kinases and cytosolic phospholipase A2 at cytoplasmic arachidonate‐rich lipid bodies.
    • 60 Yu W., Bozza P.T., Tzizik D.M., et al. Co‐compartmentalization of MAP kinases and cytosolic phospholipase A 2 at cytoplasmic arachidonate‐rich lipid bodies. Am. J. Pathol. 152: 759 769, 1998.
    • (1998) Am. J. Pathol , vol.152 , pp. 759-769
    • Yu, W.1    Bozza, P.T.2    Tzizik, D.M.3
  • 61
    • 0026507442 scopus 로고
    • Detection of three distinct phospholipases A2 in cultured mast cells.
    • 61 Murakami M., Kudo I., Umeda M., et al. Detection of three distinct phospholipases A 2 in cultured mast cells. J. Biochem. (Tokyo) 111: 175 181, 1992.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 175-181
    • Murakami, M.1    Kudo, I.2    Umeda, M.3
  • 62
    • 0028177226 scopus 로고
    • The localization of phospholipase A2 in the secretory granule.
    • 62 Chock S.P., Schumauder‐Chock E.A., Cordella‐Miele E., et al. The localization of phospholipase A 2 in the secretory granule. Biochem. J. 300: 619 622, 1994.
    • (1994) Biochem. J , vol.300 , pp. 619-622
    • Chock, S.P.1    Schumauder‐Chock, E.A.2    Cordella‐Miele, E.3
  • 63
    • 0028558828 scopus 로고
    • Levels and localization of group II phospholipase A2 and annexin I in interleukin‐ and dexamethasone‐treated rat mesangial cells: Evidence against annexin mediation of the dexamethasone‐induced inhibition of group II phospholipases A2.
    • 63 Vervoordeldonk M.J., Schalkwijk C.G., Vishwanath B.S., et al. Levels and localization of group II phospholipase A 2 and annexin I in interleukin‐ and dexamethasone‐treated rat mesangial cells: Evidence against annexin mediation of the dexamethasone‐induced inhibition of group II phospholipases A 2. Biochim. Biophys. Acta 1224: 541 550, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1224 , pp. 541-550
    • Vervoordeldonk, M.J.1    Schalkwijk, C.G.2    Vishwanath, B.S.3
  • 64
    • 0033608869 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 is essential for both the immediate and the delayed phases of eicosanoid generation in mouse bone marrow‐derived mast cells.
    • 64 Fujishima H., Sanchez R., Bingham III C.O., et al. Cytosolic phospholipase A 2 is essential for both the immediate and the delayed phases of eicosanoid generation in mouse bone marrow‐derived mast cells. Proc. Natl. Acad. Sci. U.S.A. 96: 4803 4807, 1999.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 4803-4807
    • Fujishima, H.1    Sanchez, R.2    Bingham, C.O.3
  • 65
    • 0030609846 scopus 로고    scopus 로고
    • Prostaglandin E2 amplifies cytosolic phospholipase A2‐ and cyclooxygenase‐2‐dependent delayed prostaglandin E2 generation in mouse osteoblastic cells. Enhancement by secretory phospholipase A2.
    • 65 Murakami M., Kuwata H., Amakasu Y., et al. Prostaglandin E 2 amplifies cytosolic phospholipase A 2 ‐ and cyclooxygenase‐2‐dependent delayed prostaglandin E 2 generation in mouse osteoblastic cells. Enhancement by secretory phospholipase A 2. J. Biol. Chem. 272: 19891 19897, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 19891-19897
    • Murakami, M.1    Kuwata, H.2    Amakasu, Y.3
  • 66
    • 0025983603 scopus 로고
    • Eicosanoid generation from antigen‐primed mast cells by extracellular mammalian 14‐kDa group II phospholipase A2.
    • 66 Murakami M., Kudo I., Inoue K. Eicosanoid generation from antigen‐primed mast cells by extracellular mammalian 14‐kDa group II phospholipase A 2. FEBS Lett. 294: 247 251, 1991.
    • (1991) FEBS Lett , vol.294 , pp. 247-251
    • Murakami, M.1    Kudo, I.2    Inoue, K.3
  • 67
    • 85120587918 scopus 로고    scopus 로고
    • 67 Bingham III C.O., Fijneman R.J.A., Friend D.S., et al. Low molecular weight group IIA and group V phospholipase A  2 enzymes have different intracellular locations in mouse bone marrow‐derived mast cells. J. Biol. Chem., in press.


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