메뉴 건너뛰기




Volumn 92, Issue 6, 2010, Pages 561-582

Emerging roles of secreted phospholipase A2 enzymes: Lessons from transgenic and knockout mice

Author keywords

Asthma; Atherosclerosis; Inflammation; Lipid mediator; Phospholipase A2

Indexed keywords

A 002; LY 329722; METHYLINDOXAM; MUCIN 2; PHOSPHOLIPASE A2 GROUP IB; PHOSPHOLIPASE A2 GROUP II; PHOSPHOLIPASE A2 GROUP III; PHOSPHOLIPASE A2 GROUP V; PHOSPHOLIPASE A2 GROUP X; PHOSPHOLIPASE A2 INHIBITOR; PHOSPHOLIPASE A2 RECEPTOR; PLACEBO; PRAVASTATIN; SECRETORY PHOSPHOLIPASE A2; UNCLASSIFIED DRUG; VARESPLADIB;

EID: 77953269931     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.03.015     Document Type: Review
Times cited : (128)

References (298)
  • 2
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase A2 structure/function, mechanism, and signaling
    • Burke J.E., Dennis E.A. Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res. 2009, (Suppl. 50):S237-S242.
    • (2009) J. Lipid Res. , Issue.SUPPL. 50
    • Burke, J.E.1    Dennis, E.A.2
  • 3
    • 0034739474 scopus 로고    scopus 로고
    • Increasing molecular diversity of secreted phospholipases A2 and their receptors and binding proteins
    • Valentin E., Lambeau G. Increasing molecular diversity of secreted phospholipases A2 and their receptors and binding proteins. Biochim. Biophys. Acta 2000, 1488:59-70.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 59-70
    • Valentin, E.1    Lambeau, G.2
  • 4
    • 0035222529 scopus 로고    scopus 로고
    • Diversity and regulatory functions of mammalian secretory phospholipases A2
    • Murakami M., Kudo I. Diversity and regulatory functions of mammalian secretory phospholipases A2. Adv. Immunol. 2001, 77:163-194.
    • (2001) Adv. Immunol. , vol.77 , pp. 163-194
    • Murakami, M.1    Kudo, I.2
  • 5
    • 49449090767 scopus 로고    scopus 로고
    • Biochemistry and physiology of mammalian secreted phospholipases A2
    • Lambeau G., Gelb M.H. Biochemistry and physiology of mammalian secreted phospholipases A2. Annu. Rev. Biochem. 2008, 77:495-520.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 495-520
    • Lambeau, G.1    Gelb, M.H.2
  • 6
    • 33750964517 scopus 로고    scopus 로고
    • Biochemical properties and pathophysiological roles of cytosolic phospholipase A2s
    • Kita Y., Ohto T., Uozumi N., Shimizu T. Biochemical properties and pathophysiological roles of cytosolic phospholipase A2s. Biochim. Biophys. Acta 2006, 1761:1317-1322.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1317-1322
    • Kita, Y.1    Ohto, T.2    Uozumi, N.3    Shimizu, T.4
  • 8
    • 52449101823 scopus 로고    scopus 로고
    • Group VI phospholipases A2: homeostatic phospholipases with significant potential as targets for novel therapeutics
    • Wilkins W.P., Barbour S.E. Group VI phospholipases A2: homeostatic phospholipases with significant potential as targets for novel therapeutics. Curr. Drug Targets 2008, 9:683-697.
    • (2008) Curr. Drug Targets , vol.9 , pp. 683-697
    • Wilkins, W.P.1    Barbour, S.E.2
  • 9
    • 53649086025 scopus 로고    scopus 로고
    • Role of Ca2+-independen t phospholipase A2 in cell growth and signaling
    • Hooks S.B., Cummings B.S. Role of Ca2+-independen t phospholipase A2 in cell growth and signaling. Biochem. Pharmacol. 2008, 76:1059-1067.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1059-1067
    • Hooks, S.B.1    Cummings, B.S.2
  • 10
    • 67650354215 scopus 로고    scopus 로고
    • Calcium-independent phospholipases in the heart: mediators of cellular signaling, bioenergetics, and ischemia- induced electrophysiologic dysfunction
    • Cedars A., Jenkins C.M., Mancuso D.J., Gross R.W. Calcium-independent phospholipases in the heart: mediators of cellular signaling, bioenergetics, and ischemia- induced electrophysiologic dysfunction. J. Cardiovasc. Pharmacol. 2009, 53:277-289.
    • (2009) J. Cardiovasc. Pharmacol. , vol.53 , pp. 277-289
    • Cedars, A.1    Jenkins, C.M.2    Mancuso, D.J.3    Gross, R.W.4
  • 11
    • 66349121084 scopus 로고    scopus 로고
    • Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions
    • Kienesberger P.C., Oberer M., Lass A., Zechner R. Mammalian patatin domain containing proteins: a family with diverse lipolytic activities involved in multiple biological functions. J. Lipid Res. 2009, (Suppl. 50):S63-S68.
    • (2009) J. Lipid Res. , Issue.SUPPL. 50
    • Kienesberger, P.C.1    Oberer, M.2    Lass, A.3    Zechner, R.4
  • 12
    • 0036669403 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolase
    • Arai H. Platelet-activating factor acetylhydrolase. Prostaglandins Other Lipid Mediat. 2002, 68-69:83-94.
    • (2002) Prostaglandins Other Lipid Mediat. , pp. 83-94
    • Arai, H.1
  • 14
    • 24944523382 scopus 로고    scopus 로고
    • Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2
    • Fisher A.B., Dodia C., Feinstein S.I., Ho Y.S. Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2. J. Lipid Res. 2005, 46:1248-1256.
    • (2005) J. Lipid Res. , vol.46 , pp. 1248-1256
    • Fisher, A.B.1    Dodia, C.2    Feinstein, S.I.3    Ho, Y.S.4
  • 15
    • 5644289431 scopus 로고    scopus 로고
    • Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages
    • Abe A., Hiraoka M., Wild S., Wilcoxen S.E., Paine R., Shayman J.A. Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages. J. Biol. Chem. 2004, 279:42605-42611.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42605-42611
    • Abe, A.1    Hiraoka, M.2    Wild, S.3    Wilcoxen, S.E.4    Paine, R.5    Shayman, J.A.6
  • 16
    • 54449092296 scopus 로고    scopus 로고
    • Identification and functional characterization of adipose-specific phospholipase A2 (AdPLA)
    • Duncan R.E., Sarkadi-Nagy E., Jaworski K., Ahmadian M., Sul H.S. Identification and functional characterization of adipose-specific phospholipase A2 (AdPLA). J. Biol. Chem. 2008, 283:25428-25436.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25428-25436
    • Duncan, R.E.1    Sarkadi-Nagy, E.2    Jaworski, K.3    Ahmadian, M.4    Sul, H.S.5
  • 17
    • 0031471709 scopus 로고    scopus 로고
    • Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2
    • Bonventre J.V., Huang Z., Taheri M.R., O'Leary E., Li E., Moskowitz M.A., Sapirstein A. Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2. Nature 1997, 390:622-625.
    • (1997) Nature , vol.390 , pp. 622-625
    • Bonventre, J.V.1    Huang, Z.2    Taheri, M.R.3    O'Leary, E.4    Li, E.5    Moskowitz, M.A.6    Sapirstein, A.7
  • 20
    • 4644235280 scopus 로고    scopus 로고
    • Male mice that do not express group VIA phospholipase A2 produce spermatozoa with impaired motility and have greatly reduced fertility
    • Bao S., Miller D.J., Ma Z., Wohltmann M., Eng G., Ramanadham S., Moley K., Turk J. Male mice that do not express group VIA phospholipase A2 produce spermatozoa with impaired motility and have greatly reduced fertility. J. Biol. Chem. 2004, 279:38194-38200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38194-38200
    • Bao, S.1    Miller, D.J.2    Ma, Z.3    Wohltmann, M.4    Eng, G.5    Ramanadham, S.6    Moley, K.7    Turk, J.8
  • 21
    • 38949151226 scopus 로고    scopus 로고
    • Glucose homeostasis, insulin secretion, and islet phospholipids in mice that overexpress iPLA2beta in pancreatic beta-cells and in i PLA2beta-null mice
    • Bao S., Jacobson D.A., Wohltmann M., Bohrer A., Jin W., Philipson L.H., Turk J. Glucose homeostasis, insulin secretion, and islet phospholipids in mice that overexpress iPLA2beta in pancreatic beta-cells and in i PLA2beta-null mice. Am. J. Physiol. Endocrinol. Metab. 2008, 294:E217-E229.
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.294
    • Bao, S.1    Jacobson, D.A.2    Wohltmann, M.3    Bohrer, A.4    Jin, W.5    Philipson, L.H.6    Turk, J.7
  • 22
    • 57749122054 scopus 로고    scopus 로고
    • Smooth muscle cell arachidonic acid release, migration, and proliferation are markedly attenuated in mice null forcalcium-independent phospholipase A2beta
    • Moon S.H., Jenkins C.M., Mancuso D.J., Turk J., Gross R.W. Smooth muscle cell arachidonic acid release, migration, and proliferation are markedly attenuated in mice null forcalcium-independent phospholipase A2beta. J. Biol. Chem. 2008, 283:33975-33987.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33975-33987
    • Moon, S.H.1    Jenkins, C.M.2    Mancuso, D.J.3    Turk, J.4    Gross, R.W.5
  • 23
    • 56349084706 scopus 로고    scopus 로고
    • Skeletal muscle group VIA phospholipase A2 (iPLA2beta): expression and role in fatty acid oxidation
    • Carper M.J., Zhang S., Turk J., Ramanadham S. Skeletal muscle group VIA phospholipase A2 (iPLA2beta): expression and role in fatty acid oxidation. Biochemistry 2008, 47:12241-12249.
    • (2008) Biochemistry , vol.47 , pp. 12241-12249
    • Carper, M.J.1    Zhang, S.2    Turk, J.3    Ramanadham, S.4
  • 24
    • 39549085125 scopus 로고    scopus 로고
    • Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystro phy caused by PLA2G6 mutations
    • Malik I., Turk J., Mancuso D.J., Montier L., Wohltmann M., Wozniak D.F., Schmidt R.E., Gross R.W., Kotzbauer P.T. Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystro phy caused by PLA2G6 mutations. Am. J. Pathol. 2008, 172:406-416.
    • (2008) Am. J. Pathol. , vol.172 , pp. 406-416
    • Malik, I.1    Turk, J.2    Mancuso, D.J.3    Montier, L.4    Wohltmann, M.5    Wozniak, D.F.6    Schmidt, R.E.7    Gross, R.W.8    Kotzbauer, P.T.9
  • 27
    • 36849074624 scopus 로고    scopus 로고
    • Genetic ablation of calcium-independent phospholipase A2 gamma leads toalterations in mitochondrial lipid metabolism and function resulting in a deficient mitochondrial bioenergetic phenotype
    • Mancuso D.J., Sims H.F., Han X., Jenkins C.M., Guan S.P., Yang K., Moon S.H., Pietka T., Abumrad N.A., Schlesinger P.H., Gross R.W. Genetic ablation of calcium-independent phospholipase A2 gamma leads toalterations in mitochondrial lipid metabolism and function resulting in a deficient mitochondrial bioenergetic phenotype. J. Biol. Chem. 2007, 282:34611-34622.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34611-34622
    • Mancuso, D.J.1    Sims, H.F.2    Han, X.3    Jenkins, C.M.4    Guan, S.P.5    Yang, K.6    Moon, S.H.7    Pietka, T.8    Abumrad, N.A.9    Schlesinger, P.H.10    Gross, R.W.11
  • 28
    • 72149127390 scopus 로고    scopus 로고
    • Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction
    • Mancuso D.J., Kotzbauer P., Wozniak D.F., Sims H.F., Jenkins C.M., Guan S., Han X., Yang K., Sun G., Malik I., Conyers S., Green K.G., Schmidt R.E., Gross R.W. Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction. J. Biol. Chem. 2009, 284:35632-35644.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35632-35644
    • Mancuso, D.J.1    Kotzbauer, P.2    Wozniak, D.F.3    Sims, H.F.4    Jenkins, C.M.5    Guan, S.6    Han, X.7    Yang, K.8    Sun, G.9    Malik, I.10    Conyers, S.11    Green, K.G.12    Schmidt, R.E.13    Gross, R.W.14
  • 30
    • 0842347414 scopus 로고    scopus 로고
    • Placental failure and impaired vasculogenesis result in embryonic lethality for neuropathy target esterase-deficient mice
    • Moser M., Li Y., Vaupel K., Kretzschmar D., Kluge R., Glynn P., Buettner R. Placental failure and impaired vasculogenesis result in embryonic lethality for neuropathy target esterase-deficient mice. Mol. Cell. Biol. 2004, 24:1667-1679.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1667-1679
    • Moser, M.1    Li, Y.2    Vaupel, K.3    Kretzschmar, D.4    Kluge, R.5    Glynn, P.6    Buettner, R.7
  • 31
    • 15244351250 scopus 로고    scopus 로고
    • Loss of Swiss cheese/neuropathy target esterase activity causes disruption of phosphatidylcholine homeostasis and neuronal and glial death in adult Drosophila
    • Muhlig-Versen M., da Cruz A.B., Tschape J.A., Moser M., Buttner R., Athenstaedt K., Glynn P., Kretzschmar D. Loss of Swiss cheese/neuropathy target esterase activity causes disruption of phosphatidylcholine homeostasis and neuronal and glial death in adult Drosophila. J. Neurosci. 2005, 25:2865-2873.
    • (2005) J. Neurosci. , vol.25 , pp. 2865-2873
    • Muhlig-Versen, M.1    da Cruz, A.B.2    Tschape, J.A.3    Moser, M.4    Buttner, R.5    Athenstaedt, K.6    Glynn, P.7    Kretzschmar, D.8
  • 36
    • 0037809246 scopus 로고    scopus 로고
    • Targeted disruption of intracellular type I platelet activating factor-acetylhydrolase catalytic subunits causes severe impairment in spermatogenesis
    • Koizumi H., Yamaguchi N., Hattori M., Ishikawa T.O., Aoki J., Taketo M.M., Inoue K., Arai H. Targeted disruption of intracellular type I platelet activating factor-acetylhydrolase catalytic subunits causes severe impairment in spermatogenesis. J. Biol. Chem. 2003, 278:12489-12494.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12489-12494
    • Koizumi, H.1    Yamaguchi, N.2    Hattori, M.3    Ishikawa, T.O.4    Aoki, J.5    Taketo, M.M.6    Inoue, K.7    Arai, H.8
  • 37
    • 38349107040 scopus 로고    scopus 로고
    • Protection against oxidative stress-induced hepatic injury by intracellular type II platelet-activating factor acetylhydrolase by metabolism of oxidized phospholipids in vivo
    • Kono N., Inoue T., Yoshida Y., Sato H., Matsusue T., Itabe H., Niki E., Aoki J., Arai H. Protection against oxidative stress-induced hepatic injury by intracellular type II platelet-activating factor acetylhydrolase by metabolism of oxidized phospholipids in vivo. J. Biol. Chem. 2008, 283:1628-1636.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1628-1636
    • Kono, N.1    Inoue, T.2    Yoshida, Y.3    Sato, H.4    Matsusue, T.5    Itabe, H.6    Niki, E.7    Aoki, J.8    Arai, H.9
  • 38
    • 0036745169 scopus 로고    scopus 로고
    • Reduction in the extent of atherosclerosis in apolipoprotein E-deficient mice induced by electroporation-mediated transfer of the human plasma platelet-activating factor acetylhydrolase gene into skeletal muscle
    • Hase M., Tanaka M., Yokota M., Yamada Y. Reduction in the extent of atherosclerosis in apolipoprotein E-deficient mice induced by electroporation-mediated transfer of the human plasma platelet-activating factor acetylhydrolase gene into skeletal muscle. Prostaglandins Other Lipid Mediat. 2002, 70:107-118.
    • (2002) Prostaglandins Other Lipid Mediat. , vol.70 , pp. 107-118
    • Hase, M.1    Tanaka, M.2    Yokota, M.3    Yamada, Y.4
  • 39
    • 0035933117 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of human platelet-activating factor-acetylhydrolase prevents injury-induced neointima formation and reduces spontaneous atherosclerosis in apolipoprotein E-deficient mice
    • Quarck R., De Geest B., Stengel D., Mertens A., Lox M., Theilmeier G., Michiels C., Raes M., Bult H., Collen D., Van Veldhoven P., Ninio E., Holvoet P. Adenovirus-mediated gene transfer of human platelet-activating factor-acetylhydrolase prevents injury-induced neointima formation and reduces spontaneous atherosclerosis in apolipoprotein E-deficient mice. Circulation 2001, 103:2495-2500.
    • (2001) Circulation , vol.103 , pp. 2495-2500
    • Quarck, R.1    De Geest, B.2    Stengel, D.3    Mertens, A.4    Lox, M.5    Theilmeier, G.6    Michiels, C.7    Raes, M.8    Bult, H.9    Collen, D.10    Van Veldhoven, P.11    Ninio, E.12    Holvoet, P.13
  • 43
    • 33644662758 scopus 로고    scopus 로고
    • Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress
    • Wang Y., Feinstein S.I., Manevich Y., Ho Y.S., Fisher A.B. Peroxiredoxin 6 gene-targeted mice show increased lung injury with paraquat-induced oxidative stress. Antioxid. Redox Signal. 2006, 8:229-237.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 229-237
    • Wang, Y.1    Feinstein, S.I.2    Manevich, Y.3    Ho, Y.S.4    Fisher, A.B.5
  • 45
    • 0141483322 scopus 로고    scopus 로고
    • Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity
    • Rouault M., Bollinger J.G., Lazdunski M., Gelb M.H., Lambeau G. Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry 2003, 42:11494-11503.
    • (2003) Biochemistry , vol.42 , pp. 11494-11503
    • Rouault, M.1    Bollinger, J.G.2    Lazdunski, M.3    Gelb, M.H.4    Lambeau, G.5
  • 46
    • 0032430262 scopus 로고    scopus 로고
    • Otoconin-90, the mammalian otoconial matrix protein, contains two domains of homology to se cretory phospholipase A2
    • Wang Y., Kowalski P.E., Thalmann I., Ornitz D.M., Mager D.L., Thalmann R. Otoconin-90, the mammalian otoconial matrix protein, contains two domains of homology to se cretory phospholipase A2. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:15345-15350.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15345-15350
    • Wang, Y.1    Kowalski, P.E.2    Thalmann, I.3    Ornitz, D.M.4    Mager, D.L.5    Thalmann, R.6
  • 47
    • 0033582330 scopus 로고    scopus 로고
    • Characterization of otoconin-95, the major protein of murine otoconia, provides insights into the formation of these inner ear biominerals
    • Verpy E., Leibovici M., Petit C. Characterization of otoconin-95, the major protein of murine otoconia, provides insights into the formation of these inner ear biominerals. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:529-534.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 529-534
    • Verpy, E.1    Leibovici, M.2    Petit, C.3
  • 48
    • 0033135012 scopus 로고    scopus 로고
    • Intergenic splicing between a HERV-H endogenous retrovirus and two adjacent human genes
    • Kowalski P.E., Freeman J.D., Mager D.L. Intergenic splicing between a HERV-H endogenous retrovirus and two adjacent human genes. Genomics 1999, 57:371-379.
    • (1999) Genomics , vol.57 , pp. 371-379
    • Kowalski, P.E.1    Freeman, J.D.2    Mager, D.L.3
  • 52
    • 33748465176 scopus 로고    scopus 로고
    • The proinflammatory mediator platelet activating factor is an effective substrate for human group X secreted phospholipase A2
    • Gora S., Lambeau G., Bollinger J.G., Gelb M., Ninio E., Karabina S.A. The proinflammatory mediator platelet activating factor is an effective substrate for human group X secreted phospholipase A2. Biochim. Biophys. Acta 2006, 1761:1093-1099.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1093-1099
    • Gora, S.1    Lambeau, G.2    Bollinger, J.G.3    Gelb, M.4    Ninio, E.5    Karabina, S.A.6
  • 53
    • 30044438111 scopus 로고    scopus 로고
    • Group V and X secretory phospholipase A2 prevents adenoviral infection in mammalian cells
    • Mitsuishi M., Masuda S., Kudo I., Murakami M. Group V and X secretory phospholipase A2 prevents adenoviral infection in mammalian cells. Biochem. J. 2006, 393:97-106.
    • (2006) Biochem. J. , vol.393 , pp. 97-106
    • Mitsuishi, M.1    Masuda, S.2    Kudo, I.3    Murakami, M.4
  • 54
    • 36749018033 scopus 로고    scopus 로고
    • Human group III phospholipase A2 suppresses adenovirus infection into host cells. Evidence that group III, V and X phospholipase A2s act on distinct cellular phospholipid molecular species
    • Mitsuishi M., Masuda S., Kudo I., Murakami M. Human group III phospholipase A2 suppresses adenovirus infection into host cells. Evidence that group III, V and X phospholipase A2s act on distinct cellular phospholipid molecular species. Biochim. Biophys. Acta 2007, 1771:1389-1396.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 1389-1396
    • Mitsuishi, M.1    Masuda, S.2    Kudo, I.3    Murakami, M.4
  • 55
    • 0028986238 scopus 로고
    • Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells
    • Fourcade O., Simon M.F., Viode C., Rugani N., Leballe F., Ragab A., Fournie B., Sarda L., Chap H. Secretory phospholipase A2 generates the novel lipid mediator lysophosphatidic acid in membrane microvesicles shed from activated cells. Cell 1995, 80:919-927.
    • (1995) Cell , vol.80 , pp. 919-927
    • Fourcade, O.1    Simon, M.F.2    Viode, C.3    Rugani, N.4    Leballe, F.5    Ragab, A.6    Fournie, B.7    Sarda, L.8    Chap, H.9
  • 56
    • 19044392084 scopus 로고    scopus 로고
    • Potent modification of low density lipoprotein by group X secretory phospholipase A2 is linked to macrophage foam cell formation
    • Hanasaki K., Yamada K., Yamamoto S., Ishimoto Y., Saiga A., Ono T., Ikeda M., Notoya M., Kamitani S., Arita H. Potent modification of low density lipoprotein by group X secretory phospholipase A2 is linked to macrophage foam cell formation. J. Biol. Chem. 2002, 277:29116-29124.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29116-29124
    • Hanasaki, K.1    Yamada, K.2    Yamamoto, S.3    Ishimoto, Y.4    Saiga, A.5    Ono, T.6    Ikeda, M.7    Notoya, M.8    Kamitani, S.9    Arita, H.10
  • 57
    • 0037771393 scopus 로고    scopus 로고
    • Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2
    • Chabot S., Koumanov K., Lambeau G., Gelb M.H., Chignard M., Whitsett J.A., Touqui L. Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2. J. Immunol. 2003, 171:995-1000.
    • (2003) J. Immunol. , vol.171 , pp. 995-1000
    • Chabot, S.1    Koumanov, K.2    Lambeau, G.3    Gelb, M.H.4    Chignard, M.5    Whitsett, J.A.6    Touqui, L.7
  • 58
    • 33845678939 scopus 로고    scopus 로고
    • Atherogenic properties of LDL particles modified by human group X secreted phospholipase A2 on human endothelial cell function
    • Karabina S.A., Brocheriou I., Le Naour G., Agrapart M., Durand H., Gelb M., Lambeau G., Ninio E. Atherogenic properties of LDL particles modified by human group X secreted phospholipase A2 on human endothelial cell function. Faseb J. 2006, 20:2547-2549.
    • (2006) Faseb J. , vol.20 , pp. 2547-2549
    • Karabina, S.A.1    Brocheriou, I.2    Le Naour, G.3    Agrapart, M.4    Durand, H.5    Gelb, M.6    Lambeau, G.7    Ninio, E.8
  • 59
    • 73349093412 scopus 로고    scopus 로고
    • Lipoprotein modification by secretory phospholipase A(2) enzymes contributes to the initiation and progression of atherosclerosis
    • Oorni K., Kovanen P.T. Lipoprotein modification by secretory phospholipase A(2) enzymes contributes to the initiation and progression of atherosclerosis. Curr. Opin. Lipidol. 2009, 20:421-427.
    • (2009) Curr. Opin. Lipidol. , vol.20 , pp. 421-427
    • Oorni, K.1    Kovanen, P.T.2
  • 60
    • 0033062090 scopus 로고    scopus 로고
    • Receptors for a growing family of secreted phospholipases A2
    • Lambeau G., Lazdunski M. Receptors for a growing family of secreted phospholipases A2. Trends Pharmacol. Sci. 1999, 20:162-170.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 162-170
    • Lambeau, G.1    Lazdunski, M.2
  • 61
    • 0033732562 scopus 로고    scopus 로고
    • What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2?
    • Valentin E., Lambeau G. What can venom phospholipases A2 tell us about the functional diversity of mammalian secreted phospholipases A2?. Biochimie 2000, 82:815-831.
    • (2000) Biochimie , vol.82 , pp. 815-831
    • Valentin, E.1    Lambeau, G.2
  • 62
    • 0035742201 scopus 로고    scopus 로고
    • Anticoagulant venom and mammalian secreted phospholipases A(2): protein- versus phospholipid-dependent mechanism of action
    • Mounier C.M., Bon C., Kini R.M. Anticoagulant venom and mammalian secreted phospholipases A(2): protein- versus phospholipid-dependent mechanism of action. Haemostasis 2001, 31:279-287.
    • (2001) Haemostasis , vol.31 , pp. 279-287
    • Mounier, C.M.1    Bon, C.2    Kini, R.M.3
  • 63
    • 35649004304 scopus 로고    scopus 로고
    • Understanding the molecular mechanism underlying the presynaptic toxicity of secreted phospholipases A2
    • Pungercar J., Krizaj I. Understanding the molecular mechanism underlying the presynaptic toxicity of secreted phospholipases A2. Toxicon 2007, 50:871-892.
    • (2007) Toxicon , vol.50 , pp. 871-892
    • Pungercar, J.1    Krizaj, I.2
  • 64
    • 0022923991 scopus 로고
    • Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung
    • Seilhamer J.J., Randall T.L., Yamanaka M., Johnson L.K. Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA 1986, 5:519-527.
    • (1986) DNA , vol.5 , pp. 519-527
    • Seilhamer, J.J.1    Randall, T.L.2    Yamanaka, M.3    Johnson, L.K.4
  • 67
    • 0035079697 scopus 로고    scopus 로고
    • Compensatory phospholipid digestion is required for cholesterol absorption in pancreatic phospholipase A (2)-deficient mice
    • Richmond B.L., Boileau A.C., Zheng S., Huggins K.W., Granholm N.A., Tso P., Hui D.Y. Compensatory phospholipid digestion is required for cholesterol absorption in pancreatic phospholipase A (2)-deficient mice. Gastroenterology 2001, 120:1193-1202.
    • (2001) Gastroenterology , vol.120 , pp. 1193-1202
    • Richmond, B.L.1    Boileau, A.C.2    Zheng, S.3    Huggins, K.W.4    Granholm, N.A.5    Tso, P.6    Hui, D.Y.7
  • 68
    • 0036838450 scopus 로고    scopus 로고
    • Protection against diet-induced obesity and obesity- related insulin resistance in Group 1B PLA2-deficient mice
    • Huggins K.W., Boileau A.C., Hui D.Y. Protection against diet-induced obesity and obesity- related insulin resistance in Group 1B PLA2-deficient mice. Am. J. Physiol. Endocrinol. Metab. 2002, 283:E994-E1001.
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • Huggins, K.W.1    Boileau, A.C.2    Hui, D.Y.3
  • 69
    • 33745309628 scopus 로고    scopus 로고
    • Group IB phospholipase A2-Mediated lysophospholipid absorption directly contributes to postprandial hyperglycemia
    • Labonte E.D., Kirby R.J., Schildmeyer N.M., Cannon A.M., Huggins K.W., Hui D.Y. Group IB phospholipase A2-Mediated lysophospholipid absorption directly contributes to postprandial hyperglycemia. Diabetes 2006, 55:935-941.
    • (2006) Diabetes , vol.55 , pp. 935-941
    • Labonte, E.D.1    Kirby, R.J.2    Schildmeyer, N.M.3    Cannon, A.M.4    Huggins, K.W.5    Hui, D.Y.6
  • 71
    • 0033615737 scopus 로고    scopus 로고
    • On the diversity of secreted phospholipases A2. Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes
    • Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G. On the diversity of secreted phospholipases A2. Cloning, tissue distribution, and functional expression of two novel mouse group II enzymes. J. Biol. Chem. 1999, 274:31195-31202.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31195-31202
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 73
    • 34248183607 scopus 로고    scopus 로고
    • Human secretory phosp holipase A(2), group IB in normal eyes and in eye diseases
    • Kolko M., Prause J.U., Bazan N.G., Heegaard S. Human secretory phosp holipase A(2), group IB in normal eyes and in eye diseases. Acta Ophthalmol. Scand. 2007, 85:317-323.
    • (2007) Acta Ophthalmol. Scand. , vol.85 , pp. 317-323
    • Kolko, M.1    Prause, J.U.2    Bazan, N.G.3    Heegaard, S.4
  • 74
    • 0035348393 scopus 로고    scopus 로고
    • Helicobacter infection and phospholipase A2 enzymes: effect of Helicobacter felis-infection on the expr ession and activity of sPLA2 enzymes in mouse stomach
    • Ottlecz A., Romero J.J., Lichtenberger L.M. Helicobacter infection and phospholipase A2 enzymes: effect of Helicobacter felis-infection on the expr ession and activity of sPLA2 enzymes in mouse stomach. Mol. Cell. Biochem. 2001, 221:71-77.
    • (2001) Mol. Cell. Biochem. , vol.221 , pp. 71-77
    • Ottlecz, A.1    Romero, J.J.2    Lichtenberger, L.M.3
  • 77
    • 0024554009 scopus 로고
    • Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid
    • Seilhamer J.J., Pruzanski W., Vadas P., Plant S., Miller J.A., Kloss J., Johnson L.K. Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J. Biol. Chem. 1989, 264:5335-5338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5335-5338
    • Seilhamer, J.J.1    Pruzanski, W.2    Vadas, P.3    Plant, S.4    Miller, J.A.5    Kloss, J.6    Johnson, L.K.7
  • 78
    • 0025922776 scopus 로고
    • Phos pholipase A2-a mediator between proximal and distal effectors of inflammation
    • Pruzanski W., Vadas P. Phos pholipase A2-a mediator between proximal and distal effectors of inflammation. Immunol. Today 1991, 12:143-146.
    • (1991) Immunol. Today , vol.12 , pp. 143-146
    • Pruzanski, W.1    Vadas, P.2
  • 80
    • 0025288589 scopus 로고
    • Glucocorticoids suppress group II phospholipase A2 production by blocking mRNA synthesis and post-transcriptional expression
    • Nakano T., Ohara O., Teraoka H., Arita H. Glucocorticoids suppress group II phospholipase A2 production by blocking mRNA synthesis and post-transcriptional expression. J. Biol. Chem. 1990, 265:12745-12748.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12745-12748
    • Nakano, T.1    Ohara, O.2    Teraoka, H.3    Arita, H.4
  • 81
    • 0025923332 scopus 로고
    • Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response
    • Crowl R.M., Stoller T.J., Conroy R.R., Stoner C.R. Induction of phospholipase A2 gene expression in human hepatoma cells by mediators of the acute phase response. J. Biol. Chem. 1991, 266:2647-2651.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2647-2651
    • Crowl, R.M.1    Stoller, T.J.2    Conroy, R.R.3    Stoner, C.R.4
  • 82
    • 0025895754 scopus 로고
    • Inflammatory factors stimulate expression of group II phospholipaseA2 in rat cultured astrocytes. Two distinct pathways of the gene expression
    • Oka S., Arita H. Inflammatory factors stimulate expression of group II phospholipaseA2 in rat cultured astrocytes. Two distinct pathways of the gene expression. J. Biol. Chem. 1991, 266:9956-9960.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9956-9960
    • Oka, S.1    Arita, H.2
  • 83
    • 0027365347 scopus 로고
    • Cytokine-stimulated secretion of group II phospholipase A2 by rat mesangial cells. Its contribution to arachidonic acid release and prostaglandin synthesis by cultured rat glomerular cells
    • Pfeilschifter J., Schalkwijk C., Briner V.A., Van Den Bosch H. Cytokine-stimulated secretion of group II phospholipase A2 by rat mesangial cells. Its contribution to arachidonic acid release and prostaglandin synthesis by cultured rat glomerular cells. J. Clin. Invest. 1993, 92:2516-2523.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2516-2523
    • Pfeilschifter, J.1    Schalkwijk, C.2    Briner, V.A.3    Van Den Bosch, H.4
  • 84
    • 0034292346 scopus 로고    scopus 로고
    • Studies on a mechanism by which cytosolic phospholipase A2 regulates the expression and function of type IIA secretory phospholipase A2
    • Kuwata H., Yamamoto S., Miyazaki Y., Shimbara S., Nakatani Y., Suzuki H., Ueda N., Yamamoto S., Murakami M., Kudo I. Studies on a mechanism by which cytosolic phospholipase A2 regulates the expression and function of type IIA secretory phospholipase A2. J. Immunol. 2000, 165:4024-4031.
    • (2000) J. Immunol. , vol.165 , pp. 4024-4031
    • Kuwata, H.1    Yamamoto, S.2    Miyazaki, Y.3    Shimbara, S.4    Nakatani, Y.5    Suzuki, H.6    Ueda, N.7    Yamamoto, S.8    Murakami, M.9    Kudo, I.10
  • 85
    • 0033551608 scopus 로고    scopus 로고
    • Interleukin 1beta induces type II-secreted phospholipase A(2) gene in vascular smooth muscle cells by a nuclear factor kappaB and peroxisome proliferator-activated receptor-mediated process
    • Couturier C., Brouillet A., Couriaud C., Koumanov K., B ereziat G., Andreani M. Interleukin 1beta induces type II-secreted phospholipase A(2) gene in vascular smooth muscle cells by a nuclear factor kappaB and peroxisome proliferator-activated receptor-mediated process. J. Biol. Chem. 1999, 274:23085-23093.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23085-23093
    • Couturier, C.1    Brouillet, A.2    Couriaud, C.3    Koumanov, K.4    B ereziat, G.5    Andreani, M.6
  • 86
    • 0034725574 scopus 로고    scopus 로고
    • Interferon-gamma induces secretory group IIA phospholipase A2 in human arterial smooth muscle cells. Involvement of cell differentiation, STAT-3 activation, and modulation by other cytokines
    • Peilot H., Rosengren B., Bondjers G., Hurt-Camejo E. Interferon-gamma induces secretory group IIA phospholipase A2 in human arterial smooth muscle cells. Involvement of cell differentiation, STAT-3 activation, and modulation by other cytokines. J. Biol. Chem. 2000, 275:22895-22904.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22895-22904
    • Peilot, H.1    Rosengren, B.2    Bondjers, G.3    Hurt-Camejo, E.4
  • 87
    • 0034725716 scopus 로고    scopus 로고
    • Induction of secreted type IIA phospholipase A2 gene transcription by interleukin-1beta. Role of C/EBP factors
    • Massaad C., Paradon M., Jacques C., Salvat C., Bereziat G., Berenbaum F., Olivier J.L. Induction of secreted type IIA phospholipase A2 gene transcription by interleukin-1beta. Role of C/EBP factors. J. Biol. Chem. 2000, 275:22686-22694.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22686-22694
    • Massaad, C.1    Paradon, M.2    Jacques, C.3    Salvat, C.4    Bereziat, G.5    Berenbaum, F.6    Olivier, J.L.7
  • 88
    • 0035877603 scopus 로고    scopus 로고
    • Secretory phospholipase A2 mediates cooperative prostaglandin generation by growth factor and cytokine independently of preceding cytosolic phospholipase A2 expression i n rat gastric epithelial cells
    • Akiba S., Hatazawa R., Ono K., Kitatani K., Hayama M., Sato T. Secretory phospholipase A2 mediates cooperative prostaglandin generation by growth factor and cytokine independently of preceding cytosolic phospholipase A2 expression i n rat gastric epithelial cells. J. Biol. Chem. 2001, 276:21854-21862.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21854-21862
    • Akiba, S.1    Hatazawa, R.2    Ono, K.3    Kitatani, K.4    Hayama, M.5    Sato, T.6
  • 89
    • 0032486481 scopus 로고    scopus 로고
    • The functions of five distinct mammalian phospholipase A2s in regulating arachidonic acid re lease. Type IIA and type V secretory phospholipases A2 are functionally redundant and act in concert with cytosolic phospholipase A2
    • Murakami M., Shimbara S., Kambe T., Kuwata H., Winstead M.V., Tischfield J.A., Kudo I. The functions of five distinct mammalian phospholipase A2s in regulating arachidonic acid re lease. Type IIA and type V secretory phospholipases A2 are functionally redundant and act in concert with cytosolic phospholipase A2. J. Biol. Chem. 1998, 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
  • 90
    • 0033569895 scopus 로고    scopus 로고
    • Functional association of type IIA secretory phospholipase A2 with the glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan in the cyclooxygenase-2-mediated delayed prostanoid-biosynthetic pathway
    • Murakami M., Kambe T., Shimbara S., Yamamoto S., Kuwata H., Kudo I. Functional association of type IIA secretory phospholipase A2 with the glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan in the cyclooxygenase-2-mediated delayed prostanoid-biosynthetic pathway. J. Biol. Chem. 1999, 274:29927-29936.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29927-29936
    • Murakami, M.1    Kambe, T.2    Shimbara, S.3    Yamamoto, S.4    Kuwata, H.5    Kudo, I.6
  • 91
    • 0035971193 scopus 로고    scopus 로고
    • Distinct arachidonate-releasing functions of mammalian secreted phospholipases A2 in fibroblastic and mastocytoma cells through heparan sulfate shuttling and external plasma membrane mechanisms
    • Muraka mi M., Koduri R.S., Enomoto A., Shimbara S., Seki M., Yoshihara K., Singer A., Valentin E., Ghomashchi F., Lambeau G., Gelb M.H., Kudo I. Distinct arachidonate-releasing functions of mammalian secreted phospholipases A2 in fibroblastic and mastocytoma cells through heparan sulfate shuttling and external plasma membrane mechanisms. J. Biol. Chem. 2001, 276:10083-10096.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10083-10096
    • Muraka mi, M.1    Koduri, R.S.2    Enomoto, A.3    Shimbara, S.4    Seki, M.5    Yoshihara, K.6    Singer, A.7    Valentin, E.8    Ghomashchi, F.9    Lambeau, G.10    Gelb, M.H.11    Kudo, I.12
  • 92
    • 0031594888 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 is required for cytokine-induced expression of type IIA secretor y phospholipase A2 that mediates optimal cyclooxygenase-2-dependent delayed prostaglandin E2 generation in rat 3Y1 fibroblasts
    • Kuwata H., Nakatani Y., Murakami M., Kudo I. Cytosolic phospholipase A2 is required for cytokine-induced expression of type IIA secretor y phospholipase A2 that mediates optimal cyclooxygenase-2-dependent delayed prostaglandin E2 generation in rat 3Y1 fibroblasts. J. Biol. Chem. 1998, 273:1733-1740.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1733-1740
    • Kuwata, H.1    Nakatani, Y.2    Murakami, M.3    Kudo, I.4
  • 93
    • 0033610901 scopus 로고    scopus 로고
    • Action o f human group IIa secreted phospholipase A2 on cell membranes. Vesicle but not heparinoid binding determines rate of fatty acid release by exogenously added enzyme
    • Koduri R.S., Baker S.F., Snitko Y., Han S.K., Cho W., Wilton D.C., Gelb M.H. Action o f human group IIa secreted phospholipase A2 on cell membranes. Vesicle but not heparinoid binding determines rate of fatty acid release by exogenously added enzyme. J. Biol. Chem. 1998, 273:32142-32153.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32142-32153
    • Koduri, R.S.1    Baker, S.F.2    Snitko, Y.3    Han, S.K.4    Cho, W.5    Wilton, D.C.6    Gelb, M.H.7
  • 94
    • 2942614828 scopus 로고    scopus 로고
    • Arachidonic acid release from mammalian cells transfected with human groups IIA and X secreted phospholipase A2 occurs predominantly during the secretory process and with the involvement of cytosolic phospholipase A2-alpha
    • Mounier C.M., Ghomashchi F., Lindsay M.R., James S., Singer A.G., Parton R.G., Gelb M.H. Arachidonic acid release from mammalian cells transfected with human groups IIA and X secreted phospholipase A2 occurs predominantly during the secretory process and with the involvement of cytosolic phospholipase A2-alpha. J. Biol. Chem. 2004, 279:25024-25038.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25024-25038
    • Mounier, C.M.1    Ghomashchi, F.2    Lindsay, M.R.3    James, S.4    Singer, A.G.5    Parton, R.G.6    Gelb, M.H.7
  • 95
    • 0031560233 scopus 로고    scopus 로고
    • The perturbed membrane of cells undergoing apoptosis is susceptible to type II secretory phospholipase A2 to liberate arachidonic acid
    • Atsumi G., Murakami M., Tajima M., Shimbara S., Hara N., Kudo I. The perturbed membrane of cells undergoing apoptosis is susceptible to type II secretory phospholipase A2 to liberate arachidonic acid. Biochim. Biophys. Acta 1997, 1349:43-54.
    • (1997) Biochim. Biophys. Acta , vol.1349 , pp. 43-54
    • Atsumi, G.1    Murakami, M.2    Tajima, M.3    Shimbara, S.4    Hara, N.5    Kudo, I.6
  • 96
    • 0031051318 scopus 로고    scopus 로고
    • High specificity of human secretory class II phospholipase A2 for phosphatidic acid
    • Snitko Y., Yoon E.T., Cho W. High specificity of human secretory class II phospholipase A2 for phosphatidic acid. Biochem. J. 1997, 321:737-741.
    • (1997) Biochem. J. , vol.321 , pp. 737-741
    • Snitko, Y.1    Yoon, E.T.2    Cho, W.3
  • 99
    • 0031921970 scopus 로고    scopus 로고
    • Mice lacking secretory phospholipase A2 show altered apoptosis and differentiation with Helicobacter felis infection
    • Wang T.C., Goldenring J.R., Dangler C., Ito S., Mueller A., Jeon W.K., Koh T.J., Fox J.G. Mice lacking secretory phospholipase A2 show altered apoptosis and differentiation with Helicobacter felis infection. Gastroenterology 1998, 114:675-689.
    • (1998) Gastroenterology , vol.114 , pp. 675-689
    • Wang, T.C.1    Goldenring, J.R.2    Dangler, C.3    Ito, S.4    Mueller, A.5    Jeon, W.K.6    Koh, T.J.7    Fox, J.G.8
  • 100
    • 0033966580 scopus 로고    scopus 로고
    • Expression analysis of the group IIA secretory phospholipase A2 in mice with differential susceptibility to azoxymethane-induced colon tumorigenesis
    • Papanikolaou A., Wang Q.S., Mulherkar R., Bolt A., Rosenberg D.W. Expression analysis of the group IIA secretory phospholipase A2 in mice with differential susceptibility to azoxymethane-induced colon tumorigenesis. Carcinogenesis 2000, 21:133-138.
    • (2000) Carcinogenesis , vol.21 , pp. 133-138
    • Papanikolaou, A.1    Wang, Q.S.2    Mulherkar, R.3    Bolt, A.4    Rosenberg, D.W.5
  • 102
    • 0037025894 scopus 로고    scopus 로고
    • Discrete role for cytosolic phospholipase A(2)alpha in platelets: studies using single and double mutant mice of cytosolic and group IIA secretory phospholipase A(2)
    • Wong D.A., Kita Y., Uozumi N., Shimizu T. Discrete role for cytosolic phospholipase A(2)alpha in platelets: studies using single and double mutant mice of cytosolic and group IIA secretory phospholipase A(2). J. Exp. Med. 2002, 196:349-357.
    • (2002) J. Exp. Med. , vol.196 , pp. 349-357
    • Wong, D.A.1    Kita, Y.2    Uozumi, N.3    Shimizu, T.4
  • 107
    • 0028828611 scopus 로고
    • Absence of secretory ph ospholipase A2 gene alterations in human colorectal cancer
    • Riggins G.J., Markowitz S., Wilson J.K., Vogelstein B., Kinzler K.W. Absence of secretory ph ospholipase A2 gene alterations in human colorectal cancer. Cancer Res. 1995, 55:5184-5186.
    • (1995) Cancer Res. , vol.55 , pp. 5184-5186
    • Riggins, G.J.1    Markowitz, S.2    Wilson, J.K.3    Vogelstein, B.4    Kinzler, K.W.5
  • 108
    • 0030882943 scopus 로고    scopus 로고
    • Loss of the PLA2G2A gene in a sporadic colorectal tumor of a patien t with a PLA2G2A germline mutation and absence of PLA2G2A germline alterations in patients with FAP
    • Nimmrich I., Friedl W., Kruse R., Pietsch S., Hentsch S., Deuter R., Winde G., Muller O. Loss of the PLA2G2A gene in a sporadic colorectal tumor of a patien t with a PLA2G2A germline mutation and absence of PLA2G2A germline alterations in patients with FAP. Hum. Genet. 1997, 100:345-349.
    • (1997) Hum. Genet. , vol.100 , pp. 345-349
    • Nimmrich, I.1    Friedl, W.2    Kruse, R.3    Pietsch, S.4    Hentsch, S.5    Deuter, R.6    Winde, G.7    Muller, O.8
  • 109
    • 33846886980 scopus 로고    scopus 로고
    • Impact of Phospholipase A2 group IIa gene polymorphism on phenotypic features of patients with familial adenomatous polyposis
    • Yanaru-Fujisawa R., Matsumoto T., Kukita Y., Nakamura S., Yao T., Hayashi K., Iida M. Impact of Phospholipase A2 group IIa gene polymorphism on phenotypic features of patients with familial adenomatous polyposis. Dis. Colon Rectum 2007, 50:223-231.
    • (2007) Dis. Colon Rectum , vol.50 , pp. 223-231
    • Yanaru-Fujisawa, R.1    Matsumoto, T.2    Kukita, Y.3    Nakamura, S.4    Yao, T.5    Hayashi, K.6    Iida, M.7
  • 117
    • 61349123574 scopus 로고    scopus 로고
    • Group IIA phospholipase A as a prognostic marker in prostate cancer: relevance to clinicopathological variables and disease-specific mortality
    • Mirtti T., Laine V.J., Hiekkanen H., Hurme S., Rowe O., Nevalainen T.J., Kallajoki M., Alanen K. Group IIA phospholipase A as a prognostic marker in prostate cancer: relevance to clinicopathological variables and disease-specific mortality. Apmis 2009, 117:151-161.
    • (2009) Apmis , vol.117 , pp. 151-161
    • Mirtti, T.1    Laine, V.J.2    Hiekkanen, H.3    Hurme, S.4    Rowe, O.5    Nevalainen, T.J.6    Kallajoki, M.7    Alanen, K.8
  • 118
    • 0029882783 scopus 로고    scopus 로고
    • Expression of humangroup II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate
    • Grass D.S., Felkner R.H., Chiang M.Y., Wallace R.E., Nevalainen T.J., Bennett C.F., Swanson M.E. Expression of humangroup II PLA2 in transgenic mice results in epidermal hyperplasia in the absence of inflammatory infiltrate. J. Clin. Invest. 1996, 97:2233-2241.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2233-2241
    • Grass, D.S.1    Felkner, R.H.2    Chiang, M.Y.3    Wallace, R.E.4    Nevalainen, T.J.5    Bennett, C.F.6    Swanson, M.E.7
  • 119
    • 0037417127 scopus 로고    scopus 로고
    • Expression of enhancing factor/phospholipase A2 in skin results in abnormal epidermis and increased sensitivity to chemical carcinogenesis
    • Mulherkar R., Kirtane B.M., Ramchandani A., Mansukhani N.P., Kannan S., Naresh K.N. Expression of enhancing factor/phospholipase A2 in skin results in abnormal epidermis and increased sensitivity to chemical carcinogenesis. Oncogene 2003, 22:1936-1944.
    • (2003) Oncogene , vol.22 , pp. 1936-1944
    • Mulherkar, R.1    Kirtane, B.M.2    Ramchandani, A.3    Mansukhani, N.P.4    Kannan, S.5    Naresh, K.N.6
  • 120
  • 122
    • 0031596818 scopus 로고    scopus 로고
    • Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears
    • Qu X.D., Lehrer R.I. Secretory phospholipase A2 is the principal bactericide for staphylococci and other gram-positive bacteria in human tears. Infect. Immun. 1998, 66:2791-2797.
    • (1998) Infect. Immun. , vol.66 , pp. 2791-2797
    • Qu, X.D.1    Lehrer, R.I.2
  • 123
    • 0025949682 scopus 로고
    • Detection of 14-kDa group II phospholipase A2 in human seminal plasma
    • Takayama K., Hara S., Kudo I., Inoue K. Detection of 14-kDa group II phospholipase A2 in human seminal plasma. Biochem. Biophys. Res. Commun. 1991, 178:1505-1511.
    • (1991) Biochem. Biophys. Res. Commun. , vol.178 , pp. 1505-1511
    • Takayama, K.1    Hara, S.2    Kudo, I.3    Inoue, K.4
  • 124
    • 0032145843 scopus 로고    scopus 로고
    • Mobilization of potent plasma bactericidal activity during systemic bacterial challenge. Role of group IIA phospholipase A2
    • Weinrauch Y., Abad C., Liang N.S., Lowry S.F., Weiss J. Mobilization of potent plasma bactericidal activity during systemic bacterial challenge. Role of group IIA phospholipase A2. J. Clin. Invest. 1998, 102:633-638.
    • (1998) J. Clin. Invest. , vol.102 , pp. 633-638
    • Weinrauch, Y.1    Abad, C.2    Liang, N.S.3    Lowry, S.F.4    Weiss, J.5
  • 125
    • 0033104949 scopus 로고    scopus 로고
    • Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria
    • Foreman-Wykert A.K., Weinrauch Y., Elsbach P., Weiss J. Cell-wall determinants of the bactericidal action of group IIA phospholipase A2 against Gram-positive bacteria. J. Clin. Invest. 1999, 103:715-721.
    • (1999) J. Clin. Invest. , vol.103 , pp. 715-721
    • Foreman-Wykert, A.K.1    Weinrauch, Y.2    Elsbach, P.3    Weiss, J.4
  • 126
    • 0033564947 scopus 로고    scopus 로고
    • Protection by group II phospholipase A2 against Staphylococcus aureus
    • Laine V.J., Grass D.S., Nevalainen T.J. Protection by group II phospholipase A2 against Staphylococcus aureus. J. Immunol. 1999, 162:7402-7408.
    • (1999) J. Immunol. , vol.162 , pp. 7402-7408
    • Laine, V.J.1    Grass, D.S.2    Nevalainen, T.J.3
  • 127
    • 0033966028 scopus 로고    scopus 로고
    • Resistance of transgenic mice expressing human group II phospholipase A2 to Escherichia coli infection
    • Laine V.J., Grass D.S., Nevalainen T.J. Resistance of transgenic mice expressing human group II phospholipase A2 to Escherichia coli infection. Infect. Immun. 2000, 68:87-92.
    • (2000) Infect. Immun. , vol.68 , pp. 87-92
    • Laine, V.J.1    Grass, D.S.2    Nevalainen, T.J.3
  • 129
    • 0347298784 scopus 로고    scopus 로고
    • Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus
    • Koprivnjak T., Peschel A., Gelb M.H., Liang N.S., Weiss J.P. Role of charge properties of bacterial envelope in bactericidal action of human group IIA phospholipase A2 against Staphylococcus aureus. J. Biol. Chem. 2002, 277:47636-47644.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47636-47644
    • Koprivnjak, T.1    Peschel, A.2    Gelb, M.H.3    Liang, N.S.4    Weiss, J.P.5
  • 132
    • 0032701519 scopus 로고    scopus 로고
    • Secreted phosp holipases A2, a new class of HIV inhibitors that block virus entry into host cells
    • Fenard D., Lambeau G., Valentin E., Lefebvre J.C., Lazdunski M., Doglio A. Secreted phosp holipases A2, a new class of HIV inhibitors that block virus entry into host cells. J. Clin. Invest. 1999, 104:611-618.
    • (1999) J. Clin. Invest. , vol.104 , pp. 611-618
    • Fenard, D.1    Lambeau, G.2    Valentin, E.3    Lefebvre, J.C.4    Lazdunski, M.5    Doglio, A.6
  • 133
    • 0031956684 scopus 로고    scopus 로고
    • Ultrastructural localization of secretory type II phospholipase A2 in atherosclerotic and nonatherosclerotic regions of human arteries
    • Romano M., Romano E., Bjorkerud S., Hurt-Camejo E. Ultrastructural localization of secretory type II phospholipase A2 in atherosclerotic and nonatherosclerotic regions of human arteries. Arterioscler. Thromb. Vasc. Biol. 1998, 18:519-525.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 519-525
    • Romano, M.1    Romano, E.2    Bjorkerud, S.3    Hurt-Camejo, E.4
  • 136
    • 0142124857 scopus 로고    scopus 로고
    • New phospholipase A(2) isozymes with a potential role in atherosclerosis
    • Murakami M., Kudo I. New phospholipase A(2) isozymes with a potential role in atherosclerosis. Curr. Opin. Lipidol. 2003, 14:431-436.
    • (2003) Curr. Opin. Lipidol. , vol.14 , pp. 431-436
    • Murakami, M.1    Kudo, I.2
  • 138
    • 23444442916 scopus 로고    scopus 로고
    • Secretory phospholipase A2 enzymes in atherogenesis
    • Webb N.R. Secretory phospholipase A2 enzymes in atherogenesis. Curr. Opin. Lipidol. 2005, 16:341-344.
    • (2005) Curr. Opin. Lipidol. , vol.16 , pp. 341-344
    • Webb, N.R.1
  • 139
    • 23044484743 scopus 로고    scopus 로고
    • The role of phospholipases in lipid modification and atherosclerosis
    • Ghesquiere S.A., Hofker M.H., de Winther M.P. The role of phospholipases in lipid modification and atherosclerosis. Cardiovasc. Toxicol. 2005, 5:161-182.
    • (2005) Cardiovasc. Toxicol. , vol.5 , pp. 161-182
    • Ghesquiere, S.A.1    Hofker, M.H.2    de Winther, M.P.3
  • 140
    • 60249101701 scopus 로고    scopus 로고
    • Effects of 1-H-indole-3-glyoxamide (A-002) on concentration of secretory phospholipase A2 (PLASMA study): a phase II double-blind, randomised, placebo-controlled trial
    • Rosenson R.S., Hislop C., McConnell D., Elliott M., Stasiv Y., Wang N., Waters D.D. Effects of 1-H-indole-3-glyoxamide (A-002) on concentration of secretory phospholipase A2 (PLASMA study): a phase II double-blind, randomised, placebo-controlled trial. Lancet 2009, 373:649-658.
    • (2009) Lancet , vol.373 , pp. 649-658
    • Rosenson, R.S.1    Hislop, C.2    McConnell, D.3    Elliott, M.4    Stasiv, Y.5    Wang, N.6    Waters, D.D.7
  • 141
    • 58549103715 scopus 로고    scopus 로고
    • Future role for selective phospholipase A2 inhibitors in the prevention of atherosclerotic cardiovascular disease
    • Rosenson R.S. Future role for selective phospholipase A2 inhibitors in the prevention of atherosclerotic cardiovascular disease. Cardiovasc. Drugs Ther. 2009, 23:93-101.
    • (2009) Cardiovasc. Drugs Ther. , vol.23 , pp. 93-101
    • Rosenson, R.S.1
  • 144
    • 58549118043 scopus 로고    scopus 로고
    • Lipoprotein-associated and secre tory phospholipase A2 in cardiovascular disease: the epidemiological evidence
    • Koenig W., Khuseyinova N. Lipoprotein-associated and secre tory phospholipase A2 in cardiovascular disease: the epidemiological evidence. Cardiovasc. Drugs Ther. 2009, 23:85-92.
    • (2009) Cardiovasc. Drugs Ther. , vol.23 , pp. 85-92
    • Koenig, W.1    Khuseyinova, N.2
  • 145
    • 72949102004 scopus 로고    scopus 로고
    • Association between type II secretory phospholipase A2 plasma concentrations and activity and cardiovascular events in patients with coronary heart disease
    • Koenig W., Vossen C.Y., Mallat Z., Brenner H., Benessiano J., Rothenbacher D. Association between type II secretory phospholipase A2 plasma concentrations and activity and cardiovascular events in patients with coronary heart disease. Eur. Heart J. 2009, 30:2742-2748.
    • (2009) Eur. Heart J. , vol.30 , pp. 2742-2748
    • Koenig, W.1    Vossen, C.Y.2    Mallat, Z.3    Brenner, H.4    Benessiano, J.5    Rothenbacher, D.6
  • 146
    • 0035676862 scopus 로고    scopus 로고
    • Elevated levels of small, low-density lipoprotein with high affinity for arterial matrix components in patients with rheumatoid arthritis: possible contribution of phospholipase A2 to this atherogenic profile
    • Hurt-Camejo E., Paredes S., Masana L., Camejo G., Sartipy P., Rosengren B., Pedreno J., Vallve J.C., Benito P., Wiklund O. Elevated levels of small, low-density lipoprotein with high affinity for arterial matrix components in patients with rheumatoid arthritis: possible contribution of phospholipase A2 to this atherogenic profile. Arthritis Rheum. 2001, 44:2761-2767.
    • (2001) Arthritis Rheum. , vol.44 , pp. 2761-2767
    • Hurt-Camejo, E.1    Paredes, S.2    Masana, L.3    Camejo, G.4    Sartipy, P.5    Rosengren, B.6    Pedreno, J.7    Vallve, J.C.8    Benito, P.9    Wiklund, O.10
  • 147
    • 0034737779 scopus 로고    scopus 로고
    • Molecular basis for the association of group IIA phospholipase A2 and decorin in human atherosclerotic lesions
    • Sartipy P., Johansen B., Gasvik K., Hurt-Camejo E. Molecular basis for the association of group IIA phospholipase A2 and decorin in human atherosclerotic lesions. Circ. Res. 2000, 86:707-714.
    • (2000) Circ. Res. , vol.86 , pp. 707-714
    • Sartipy, P.1    Johansen, B.2    Gasvik, K.3    Hurt-Camejo, E.4
  • 149
    • 1842475761 scopus 로고    scopus 로고
    • Group V sPLA2 hydrolysis of low-density lipoprotein results in spontaneous particle aggregation and promotes macrophage foam cell formation
    • Wooton-Kee C.R., Boya novsky B.B., Nasser M.S., de Villiers W.J., Webb N.R. Group V sPLA2 hydrolysis of low-density lipoprotein results in spontaneous particle aggregation and promotes macrophage foam cell formation. Arterioscler. Thromb. Vasc. Biol. 2004, 24:762-767.
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 762-767
    • Wooton-Kee, C.R.1    Boya novsky, B.B.2    Nasser, M.S.3    de Villiers, W.J.4    Webb, N.R.5
  • 155
    • 0033615728 scopus 로고    scopus 로고
    • Different functional aspects of the group II subfamily (Types IIA and V) and type X secretory phospholipase A2s in regulating arachidonic acid release and prostaglandin generation. Implications of cyclooxygenase-2 induction and phospholipid scramblase-mediated cellular membrane perturbation
    • Murak ami M., Kambe T., Shimbara S., Higashino K., Hanasaki K., Arita H., Horiguchi M., Arita M., Arai H., Inoue K., Kudo I. Different functional aspects of the group II subfamily (Types IIA and V) and type X secretory phospholipase A2s in regulating arachidonic acid release and prostaglandin generation. Implications of cyclooxygenase-2 induction and phospholipid scramblase-mediated cellular membrane perturbation. J. Biol. Chem. 1999, 274:31435-31444.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31435-31444
    • Murak ami, M.1    Kambe, T.2    Shimbara, S.3    Higashino, K.4    Hanasaki, K.5    Arita, H.6    Horiguchi, M.7    Arita, M.8    Arai, H.9    Inoue, K.10    Kudo, I.11
  • 157
    • 0035815731 scopus 로고    scopus 로고
    • Mechanism of human group V phospholipase A2 (PLA2)-induced leukotriene biosynthesis in human neutrophils. A potential role of heparan sulfate binding in PLA2 internalization and degradation
    • Kim K.P., Rafter J.D., Bittova L., Han S.K., Snitko Y., Munoz N.M., Leff A.R., Cho W. Mechanism of human group V phospholipase A2 (PLA2)-induced leukotriene biosynthesis in human neutrophils. A potential role of heparan sulfate binding in PLA2 internalization and degradation. J. Biol. Chem. 2001, 276:11126-11134.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11126-11134
    • Kim, K.P.1    Rafter, J.D.2    Bittova, L.3    Han, S.K.4    Snitko, Y.5    Munoz, N.M.6    Leff, A.R.7    Cho, W.8
  • 159
    • 0037184110 scopus 로고    scopus 로고
    • Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2
    • Kim Y.J., Kim K.P., Han S.K., Munoz N.M., Zhu X., Sano H., Leff A.R., Cho W. Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2. J. Biol. Chem. 2002, 277:36479-36488.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36479-36488
    • Kim, Y.J.1    Kim, K.P.2    Han, S.K.3    Munoz, N.M.4    Zhu, X.5    Sano, H.6    Leff, A.R.7    Cho, W.8
  • 160
    • 33744998946 scopus 로고    scopus 로고
    • Systematic evaluation of transcellular activities of secretory phospholipases A2. High activity of group V phospholipases A2 to induce eicosanoid biosynthesis in neighboring inflammatory cells
    • Wijewickrama G.T., Kim J.H., Kim Y.J., Abraham A., Oh Y., Ananthanarayanan B., Kwatia M., Ackerman S.J., Cho W. Systematic evaluation of transcellular activities of secretory phospholipases A2. High activity of group V phospholipases A2 to induce eicosanoid biosynthesis in neighboring inflammatory cells. J. Biol. Chem. 2006, 281:10935-10944.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10935-10944
    • Wijewickrama, G.T.1    Kim, J.H.2    Kim, Y.J.3    Abraham, A.4    Oh, Y.5    Ananthanarayanan, B.6    Kwatia, M.7    Ackerman, S.J.8    Cho, W.9
  • 161
    • 0031712651 scopus 로고    scopus 로고
    • Expression and characterization of human group V phospholipase A2
    • Chen Y., Dennis E.A. Expression and characterization of human group V phospholipase A2. Biochim. Biophys. Acta 1998, 1394:57-64.
    • (1998) Biochim. Biophys. Acta , vol.1394 , pp. 57-64
    • Chen, Y.1    Dennis, E.A.2
  • 162
    • 23944471373 scopus 로고    scopus 로고
    • Differential hydrolysis of molecular species of lipoprotein phosphatidylcholine by groups IIA, V and X secretory phospholipases A2
    • Pruzanski W., Lambeau G., Lazdunski M., Cho W., Kopilov J., Kuksis A. Differential hydrolysis of molecular species of lipoprotein phosphatidylcholine by groups IIA, V and X secretory phospholipases A2. Biochim. Biophys. Acta 2005, 1736:38-50.
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 38-50
    • Pruzanski, W.1    Lambeau, G.2    Lazdunski, M.3    Cho, W.4    Kopilov, J.5    Kuksis, A.6
  • 163
    • 1942469349 scopus 로고    scopus 로고
    • Role of group V phospholipase A2 in zymosan-induced eicosanoid generation and vascular permeability revealed by targeted gene disruption
    • Satake Y., Diaz B.L., Balestrieri B., Lam B.K., Kanaoka Y., Grusby M.J., Arm J.P. Role of group V phospholipase A2 in zymosan-induced eicosanoid generation and vascular permeability revealed by targeted gene disruption. J. Biol. Chem. 2004, 279:16488-16494.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16488-16494
    • Satake, Y.1    Diaz, B.L.2    Balestrieri, B.3    Lam, B.K.4    Kanaoka, Y.5    Grusby, M.J.6    Arm, J.P.7
  • 164
    • 33751396595 scopus 로고    scopus 로고
    • Group V secretory phospholipase A2 amplifies the induction of cyclooxygenase 2 and delayed prostaglandin D2 generation in mouse bone marrow culture-derivedmast cells in a strain-dependent manner
    • Diaz B.L., Satake Y., Kikawada E., Balestrieri B., Arm J.P. Group V secretory phospholipase A2 amplifies the induction of cyclooxygenase 2 and delayed prostaglandin D2 generation in mouse bone marrow culture-derivedmast cells in a strain-dependent manner. Biochim. Biophys. Acta 2006, 1761:1489-1497.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1489-1497
    • Diaz, B.L.1    Satake, Y.2    Kikawada, E.3    Balestrieri, B.4    Arm, J.P.5
  • 165
    • 34547104852 scopus 로고    scopus 로고
    • Group V secretory PLA2 regulates TLR2-dependent eicosanoid generation in mouse mast cells through amplification of ERK and c PLA2alpha activation
    • Kikawada E., Bonventre J.V., Arm J.P. Group V secretory PLA2 regulates TLR2-dependent eicosanoid generation in mouse mast cells through amplification of ERK and c PLA2alpha activation. Blood 2007, 110:561-567.
    • (2007) Blood , vol.110 , pp. 561-567
    • Kikawada, E.1    Bonventre, J.V.2    Arm, J.P.3
  • 166
    • 0029860316 scopus 로고    scopus 로고
    • A heparin-sensitive phospholipase A2 and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase ofprostaglandin D2 generation in mouse bone marrow-derived mast cells
    • Bingham C.r., Murakami M., Fujishima H., Hunt J.E., Austen K.F., Arm J.P. A heparin-sensitive phospholipase A2 and prostaglandin endoperoxide synthase-2 are functionally linked in the delayed phase ofprostaglandin D2 generation in mouse bone marrow-derived mast cells. J. Biol. Chem. 1996, 271:25936-25944.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25936-25944
    • Bingham, C.1    Murakami, M.2    Fujishima, H.3    Hunt, J.E.4    Austen, K.F.5    Arm, J.P.6
  • 167
    • 0031184060 scopus 로고    scopus 로고
    • Cyclooxygenase-2-dependent delayed prostaglandin D2 generation is initiated by nerve growth factor in rat peritoneal mast cells: its augmentation by extracellular type II secretory phospholipase A2
    • Murakami M., Tada K., Nakajima K., Kudo I. Cyclooxygenase-2-dependent delayed prostaglandin D2 generation is initiated by nerve growth factor in rat peritoneal mast cells: its augmentation by extracellular type II secretory phospholipase A2. J. Immunol. 1997, 159:439-446.
    • (1997) J. Immunol. , vol.159 , pp. 439-446
    • Murakami, M.1    Tada, K.2    Nakajima, K.3    Kudo, I.4
  • 168
    • 0034292359 scopus 로고    scopus 로고
    • Redundant and segregated functions of granule-a ssociated heparin-binding group II subfamily of secretory phospholipases A2 in the regulation of degranulation and prostaglandin D2 synthesis in mast cells
    • Enomoto A., Murakami M., Valentin E., Lambeau G., Gelb M.H., Kudo I. Redundant and segregated functions of granule-a ssociated heparin-binding group II subfamily of secretory phospholipases A2 in the regulation of degranulation and prostaglandin D2 synthesis in mast cells. J. Immunol. 2000, 165:4007-4014.
    • (2000) J. Immunol. , vol.165 , pp. 4007-4014
    • Enomoto, A.1    Murakami, M.2    Valentin, E.3    Lambeau, G.4    Gelb, M.H.5    Kudo, I.6
  • 170
    • 33646538505 scopus 로고    scopus 로고
    • Group V secretory phospholipase A2 translocates to the phagosome after zymosan stimulation of mouse peritoneal macrophages and regulates phagocytosis
    • Balestrieri B., Hsu V.W., Gilbert H., Leslie C.C., Han W.K., Bonventre J.V., Arm J.P. Group V secretory phospholipase A2 translocates to the phagosome after zymosan stimulation of mouse peritoneal macrophages and regulates phagocytosis. J. Biol. Chem. 2006, 281:6691-6698.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6691-6698
    • Balestrieri, B.1    Hsu, V.W.2    Gilbert, H.3    Leslie, C.C.4    Han, W.K.5    Bonventre, J.V.6    Arm, J.P.7
  • 171
    • 65249115433 scopus 로고    scopus 로고
    • Group V secretory phospholipase A2 modulates phagosome maturation and regulates the innate immune response against Candida albicans
    • Balestrieri B., Maekawa A., Xing W., Gelb M.H., Katz H.R., Arm J.P. Group V secretory phospholipase A2 modulates phagosome maturation and regulates the innate immune response against Candida albicans. J. Immunol. 2009, 182:4891-4898.
    • (2009) J. Immunol. , vol.182 , pp. 4891-4898
    • Balestrieri, B.1    Maekawa, A.2    Xing, W.3    Gelb, M.H.4    Katz, H.R.5    Arm, J.P.6
  • 174
    • 17144363202 scopus 로고    scopus 로고
    • Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandin-synthetic function in human lung-derived cells
    • Masuda S., Murakami M., Mitsuishi M., Komiyama K., Ishikawa Y., Ishii T., Kudo I. Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandin-synthetic function in human lung-derived cells. Biochem. J. 2005, 387:27-38.
    • (2005) Biochem. J. , vol.387 , pp. 27-38
    • Masuda, S.1    Murakami, M.2    Mitsuishi, M.3    Komiyama, K.4    Ishikawa, Y.5    Ishii, T.6    Kudo, I.7
  • 175
    • 41949093677 scopus 로고    scopus 로고
    • A catalytic ally independent physiological function for human acute phase protein group IIA phospholipase A2: cellular uptake facilitates cell debris removal
    • Birts C.N., Barton C.H., Wilton D.C. A catalytic ally independent physiological function for human acute phase protein group IIA phospholipase A2: cellular uptake facilitates cell debris removal. J. Biol. Chem. 2008, 283:5034-5045.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5034-5045
    • Birts, C.N.1    Barton, C.H.2    Wilton, D.C.3
  • 180
    • 38449093436 scopus 로고    scopus 로고
    • Prostaglandin I2-IP signaling blocks allergic pulmonary inflammation by preventing recruitment of CD4+ Th2 cells into the airways in a mouse model of asthma
    • Jaffar Z., Ferrini M.E., Buford M.C., Fitzgerald G.A., Roberts K. Prostaglandin I2-IP signaling blocks allergic pulmonary inflammation by preventing recruitment of CD4+ Th2 cells into the airways in a mouse model of asthma. J. Immunol. 2007, 179:6193-6203.
    • (2007) J. Immunol. , vol.179 , pp. 6193-6203
    • Jaffar, Z.1    Ferrini, M.E.2    Buford, M.C.3    Fitzgerald, G.A.4    Roberts, K.5
  • 182
    • 0030835266 scopus 로고    scopus 로고
    • 5-Lipoxygenase products are necessary for ovalbumin-induced airway responsiveness in mice
    • 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. 1997, 272:L1053-L1058.
    • (1997) Am. J. Physiol. , vol.272
    • Irvin, C.G.1    Tu, Y.P.2    Sheller, J.R.3    Funk, C.D.4
  • 187
    • 47849086917 scopus 로고    scopus 로고
    • Resolvin E1 regulates interleukin 23, interferon-gamma and lipoxin A4 to promote the resolution of allergic airway inflammation
    • Haworth O., Cernadas M., Yang R., Serhan C.N., Levy B.D. Resolvin E1 regulates interleukin 23, interferon-gamma and lipoxin A4 to promote the resolution of allergic airway inflammation. Nat. Immunol. 2008, 9:873-879.
    • (2008) Nat. Immunol. , vol.9 , pp. 873-879
    • Haworth, O.1    Cernadas, M.2    Yang, R.3    Serhan, C.N.4    Levy, B.D.5
  • 188
    • 2442674091 scopus 로고    scopus 로고
    • Platelet-activating factor receptor develops airway hyperresponsiveness independently of airway inflammation in a murine asthma model
    • Ishii S., Nagase T., Shindou H., Takizawa H., Ouchi Y., Shimizu T. Platelet-activating factor receptor develops airway hyperresponsiveness independently of airway inflammation in a murine asthma model. J. Immunol. 2004, 172:7095-7102.
    • (2004) J. Immunol. , vol.172 , pp. 7095-7102
    • Ishii, S.1    Nagase, T.2    Shindou, H.3    Takizawa, H.4    Ouchi, Y.5    Shimizu, T.6
  • 189
    • 49449112039 scopus 로고    scopus 로고
    • Deletion of secretory group V phospholipase A2 attenuates cell migration and airway hyperresponsiveness in immunosensitized mice
    • Munoz N.M., Meliton A.Y., Arm J.P., Bonventre J.V., Cho W., Leff A.R. Deletion of secretory group V phospholipase A2 attenuates cell migration and airway hyperresponsiveness in immunosensitized mice. J. Immunol. 2007, 179:4800-4807.
    • (2007) J. Immunol. , vol.179 , pp. 4800-4807
    • Munoz, N.M.1    Meliton, A.Y.2    Arm, J.P.3    Bonventre, J.V.4    Cho, W.5    Leff, A.R.6
  • 192
    • 0035750309 scopus 로고    scopus 로고
    • Mammalian secreted phospholipases A2 and their pathophysiological significance in inflammatory diseases
    • Touqui L., Alaoui-El-Azher M. Mammalian secreted phospholipases A2 and their pathophysiological significance in inflammatory diseases. Curr. Mol. Med. 2001, 1:739-754.
    • (2001) Curr. Mol. Med. , vol.1 , pp. 739-754
    • Touqui, L.1    Alaoui-El-Azher, M.2
  • 193
    • 0032530764 scopus 로고    scopus 로고
    • Generation of lyso-phospholipids from surfactant in acute lung injury is mediated by type-II phosphol ipase A2 and inhibited by a direct surfactant protein A-phospholipase A2 protein interaction
    • Arbibe L., Koumanov K., Vial D., Rougeot C., Faure G., Havet N., Longacre S., Vargaftig B.B., Bereziat G., Voelker D.R., Wolf C., Touqui L. Generation of lyso-phospholipids from surfactant in acute lung injury is mediated by type-II phosphol ipase A2 and inhibited by a direct surfactant protein A-phospholipase A2 protein interaction. J. Clin. Invest. 1998, 102:1152-1160.
    • (1998) J. Clin. Invest. , vol.102 , pp. 1152-1160
    • Arbibe, L.1    Koumanov, K.2    Vial, D.3    Rougeot, C.4    Faure, G.5    Havet, N.6    Longacre, S.7    Vargaftig, B.B.8    Bereziat, G.9    Voelker, D.R.10    Wolf, C.11    Touqui, L.12
  • 195
    • 33646748549 scopus 로고    scopus 로고
    • The first potent inhibitor of Mammalian group X secreted phospholipase A2: elucidation of sites for enhanced binding
    • Smart B.P., Oslund R.C., Walsh L.A., Gelb M.H. The first potent inhibitor of Mammalian group X secreted phospholipase A2: elucidation of sites for enhanced binding. J. Med. Chem. 2006, 49:2858-2860.
    • (2006) J. Med. Chem. , vol.49 , pp. 2858-2860
    • Smart, B.P.1    Oslund, R.C.2    Walsh, L.A.3    Gelb, M.H.4
  • 199
    • 0037117723 scopus 로고    scopus 로고
    • Role of group IIa and group V secretory phospholipases A(2) in the metabolism of lipoproteins. Substrate specificities of the enzymes and the regulation of their activities by sphingomyelin
    • Gesquiere L., Cho W., Subbaiah P.V. Role of group IIa and group V secretory phospholipases A(2) in the metabolism of lipoproteins. Substrate specificities of the enzymes and the regulation of their activities by sphingomyelin. Biochemistry 2002, 41:4911-4920.
    • (2002) Biochemistry , vol.41 , pp. 4911-4920
    • Gesquiere, L.1    Cho, W.2    Subbaiah, P.V.3
  • 200
    • 25444491572 scopus 로고    scopus 로고
    • Group V secretory phospholipase A2-modified low density lipoprotein promotes foam cell formation by a SR-A- and CD36-independent process that involves cellular proteoglycans
    • Boyanovsky B.B., van der Westhuyzen D.R., Webb N.R. Group V secretory phospholipase A2-modified low density lipoprotein promotes foam cell formation by a SR-A- and CD36-independent process that involves cellular proteoglycans. J. Biol. Chem. 2005, 280:32746-32752.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32746-32752
    • Boyanovsky, B.B.1    van der Westhuyzen, D.R.2    Webb, N.R.3
  • 202
    • 33745959648 scopus 로고    scopus 로고
    • Inflammation and atherosclerosis: group IIa and Group V sPLA2 are not redundant
    • de Beer F.C., Webb N.R. Inflammation and atherosclerosis: group IIa and Group V sPLA2 are not redundant. Arterioscler. Thromb. Vasc. Biol. 2006, 26:1421-1422.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1421-1422
    • de Beer, F.C.1    Webb, N.R.2
  • 203
    • 33751092532 scopus 로고    scopus 로고
    • Distinctiveness of secretory phospholipase A2 group IIA and V suggesting unique roles in atherosclerosis
    • Rosengren B., Jonsson-Rylander A.C., Peilot H., Camejo G., Hurt-Camejo E. Distinctiveness of secretory phospholipase A2 group IIA and V suggesting unique roles in atherosclerosis. Biochim. Biophys. Acta 2006, 1761:1301-1308.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1301-1308
    • Rosengren, B.1    Jonsson-Rylander, A.C.2    Peilot, H.3    Camejo, G.4    Hurt-Camejo, E.5
  • 205
    • 34447344534 scopus 로고    scopus 로고
    • Tagging SNP haplotype analysis of the secretory PLA2-V gene, PLA2G5, shows strong association with LDL and oxLDL levels, suggesting functional distinction from sPLA2-IIA: results from the UDACS study
    • Wootton P.T., Arora N.L., Drenos F., Thompson S.R., Cooper J.A., Stephens J.W., Hurel S.J., Hurt-Camejo E., Wiklund O., Humphries S.E., Talmud P.J. Tagging SNP haplotype analysis of the secretory PLA2-V gene, PLA2G5, shows strong association with LDL and oxLDL levels, suggesting functional distinction from sPLA2-IIA: results from the UDACS study. Hum. Mol. Genet. 2007, 16:1437-1444.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1437-1444
    • Wootton, P.T.1    Arora, N.L.2    Drenos, F.3    Thompson, S.R.4    Cooper, J.A.5    Stephens, J.W.6    Hurel, S.J.7    Hurt-Camejo, E.8    Wiklund, O.9    Humphries, S.E.10    Talmud, P.J.11
  • 207
    • 77953273219 scopus 로고    scopus 로고
    • Varespladib (A-002), a secretory phospholipase A2 inhibitor, reduces atherosclerosis and Aneurysm formation in ApoE-/- mice, J. Cardiovasc. Pharmacol. in press
    • H. Fraser, C. Hislop, R.M. Christie, H.L. Rick, C.A. Reidy, M.L. Chouinard, P.I. Eacho, K.E. Gould, J. Trias, Varespladib (A-002), a secretory phospholipase A2 inhibitor, reduces atherosclerosis and Aneurysm formation in ApoE-/- mice, J. Cardiovasc. Pharmacol. in press.
    • Fraser, H.1    Hislop, C.2    Christie, R.M.3    Rick, H.L.4    Reidy, C.A.5    Chouinard, M.L.6    Eacho, P.I.7    Gould, K.E.8    Trias, J.9
  • 209
    • 69249088914 scopus 로고    scopus 로고
    • Varespladib methyl, an oral phospholipase A2 inhibitor for the potential treatment of coronary artery disease
    • Kar akas M., Koenig W. Varespladib methyl, an oral phospholipase A2 inhibitor for the potential treatment of coronary artery disease. IDrugs 2009, 12:585-592.
    • (2009) IDrugs , vol.12 , pp. 585-592
    • Kar akas, M.1    Koenig, W.2
  • 211
    • 26444495116 scopus 로고    scopus 로고
    • Diverse cellular localizations of secretory phospholipase A2 enzymes in several human tissues
    • Masuda S., Murakami M., Ishikawa Y., Ishii T., Kudo I. Diverse cellular localizations of secretory phospholipase A2 enzymes in several human tissues. Biochim. Biophys. Acta 2005, 1736:200-210.
    • (2005) Biochim. Biophys. Acta , vol.1736 , pp. 200-210
    • Masuda, S.1    Murakami, M.2    Ishikawa, Y.3    Ishii, T.4    Kudo, I.5
  • 212
    • 0030905731 scopus 로고    scopus 로고
    • Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2
    • Cupillard L., Koumanov K., Mattéi M.G., Lazdunski M., Lambeau G. Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J. Biol. Chem. 1997, 272:15745-15752.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15745-15752
    • Cupillard, L.1    Koumanov, K.2    Mattéi, M.G.3    Lazdunski, M.4    Lambeau, G.5
  • 214
    • 0034282662 scopus 로고    scopus 로고
    • Mouse group X secretory phospholipase A2 induces a potent release of a rachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor
    • Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T., Nakano K., Fujii N., Ishizaki J., Arita H., Hanasaki K. Mouse group X secretory phospholipase A2 induces a potent release of a rachidonic acid from spleen cells and acts as a ligand for the phospholipase A2 receptor. Arch. Biochem. Biophys. 2000, 381:31-42.
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 31-42
    • Morioka, Y.1    Saiga, A.2    Yokota, Y.3    Suzuki, N.4    Ikeda, M.5    Ono, T.6    Nakano, K.7    Fujii, N.8    Ishizaki, J.9    Arita, H.10    Hanasaki, K.11
  • 215
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: from protein traffic to embryogenesis and disease
    • Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell. Biol. 2002, 3:753-766.
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 218
    • 0037047328 scopus 로고    scopus 로고
    • Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes
    • Pan Y.H., Yu B.Z., Singer A.G., Ghomashchi F., Lambeau G., Gelb M.H., Jain M.K., Bahnson B.J. Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes. J. Biol. Chem. 2002, 277:29086-29093.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29086-29093
    • Pan, Y.H.1    Yu, B.Z.2    Singer, A.G.3    Ghomashchi, F.4    Lambeau, G.5    Gelb, M.H.6    Jain, M.K.7    Bahnson, B.J.8
  • 219
    • 0034603037 scopus 로고    scopus 로고
    • Exogenously added human group X secreted phospholipase A2 but not the group IB, IIA, and V enzymes efficiently release arachidonic acid from adherent mammalian cells
    • Bezzine S., Koduri R.S., Valentin E., Murakami M., Kudo I., Ghomashchi F., Sadilek M., Lambeau G., Gelb M.H. Exogenously added human group X secreted phospholipase A2 but not the group IB, IIA, and V enzymes efficiently release arachidonic acid from adherent mammalian cells. J. Biol. Chem. 2000, 275:3179-3191.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3179-3191
    • Bezzine, S.1    Koduri, R.S.2    Valentin, E.3    Murakami, M.4    Kudo, I.5    Ghomashchi, F.6    Sadilek, M.7    Lambeau, G.8    Gelb, M.H.9
  • 220
    • 0034731425 scopus 로고    scopus 로고
    • Potential role of group X secretory phospholipase A2 in cyclooxygenase-2-dependent PGE2 formation during colon tumorigenesis
    • Morioka Y., Ikeda M., Saiga A., Fujii N., Ishimoto Y., Arita H., Hanasaki K. Potential role of group X secretory phospholipase A2 in cyclooxygenase-2-dependent PGE2 formation during colon tumorigenesis. FEBS Lett. 2000, 487:262-266.
    • (2000) FEBS Lett. , vol.487 , pp. 262-266
    • Morioka, Y.1    Ikeda, M.2    Saiga, A.3    Fujii, N.4    Ishimoto, Y.5    Arita, H.6    Hanasaki, K.7
  • 221
    • 0035135395 scopus 로고    scopus 로고
    • Characterization of group X phospholipase A2 as the major enzyme secreted by human keratinocytes and its regulation by the phorbol ester TPA
    • Schadow A., Scholz K., Lambeau G., Gelb M.H., Furstenberger G., Pfeilschifter J., Kaszkin M. Characterization of group X phospholipase A2 as the major enzyme secreted by human keratinocytes and its regulation by the phorbol ester TPA. J. Invest. Dermatol. 2001, 116:31-39.
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 31-39
    • Schadow, A.1    Scholz, K.2    Lambeau, G.3    Gelb, M.H.4    Furstenberger, G.5    Pfeilschifter, J.6    Kaszkin, M.7
  • 224
    • 0037591839 scopus 로고    scopus 로고
    • Cross-talk between cytosolic phospholipase A2 alpha (cPLA2 alpha) and secretory phospholipase A2 (sPLA2) in hydrogen peroxide-induced arachidonic acid release in murine mesangial cells: sPLA2 regulates cPLA2 alpha activity that is responsible for arachidonic acid release
    • Han W.K., Sapirstein A., Hung C.C., Alessandrini A., Bonventre J.V. Cross-talk between cytosolic phospholipase A2 alpha (cPLA2 alpha) and secretory phospholipase A2 (sPLA2) in hydrogen peroxide-induced arachidonic acid release in murine mesangial cells: sPLA2 regulates cPLA2 alpha activity that is responsible for arachidonic acid release. J. Biol. Chem. 2003, 278:24153-24163.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24153-24163
    • Han, W.K.1    Sapirstein, A.2    Hung, C.C.3    Alessandrini, A.4    Bonventre, J.V.5
  • 225
    • 13844269166 scopus 로고    scopus 로고
    • Group X secretory phospholipase A2 can induce arachidonic acid release and eicosanoid production without activation of cytosolic phospholipase A2 alpha
    • Saiga A., Uozumi N., Ono T., Seno K., Ishimoto Y., Arita H., Shimizu T., Hanasaki K. Group X secretory phospholipase A2 can induce arachidonic acid release and eicosanoid production without activation of cytosolic phospholipase A2 alpha. Prostaglandins Other Lipid Mediat. 2005, 75:79-89.
    • (2005) Prostaglandins Other Lipid Mediat. , vol.75 , pp. 79-89
    • Saiga, A.1    Uozumi, N.2    Ono, T.3    Seno, K.4    Ishimoto, Y.5    Arita, H.6    Shimizu, T.7    Hanasaki, K.8
  • 226
    • 42649089790 scopus 로고    scopus 로고
    • Resolving inflammation: dual anti-inflammatory and pro-resolution lipid mediators
    • Serhan C.N., Chiang N., Van Dyke T.E. Resolving inflammation: dual anti-inflammatory and pro-resolution lipid mediators. Nat. Rev. Immunol. 2008, 8:349-361.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 349-361
    • Serhan, C.N.1    Chiang, N.2    Van Dyke, T.E.3
  • 229
    • 33846833931 scopus 로고    scopus 로고
    • Differential behavior of sPLA2-V and s PLA2-X in human neutrophils
    • Solodkin-Szaingurten I., Levy R., Hadad N. Differential behavior of sPLA2-V and s PLA2-X in human neutrophils. Biochim. Biophys. Acta 2007, 1771:155-163.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 155-163
    • Solodkin-Szaingurten, I.1    Levy, R.2    Hadad, N.3
  • 231
    • 33847786698 scopus 로고    scopus 로고
    • Role of sphingomyelin and ceramide in the regulation of the activity and fatty acid specificity of group V secretory phospholipase A2
    • Singh D.K., Gesquiere L.R., Subbaiah P.V. Role of sphingomyelin and ceramide in the regulation of the activity and fatty acid specificity of group V secretory phospholipase A2. Arch. Biochem. Biophys. 2007, 459:280-287.
    • (2007) Arch. Biochem. Biophys. , vol.459 , pp. 280-287
    • Singh, D.K.1    Gesquiere, L.R.2    Subbaiah, P.V.3
  • 232
    • 0142200309 scopus 로고    scopus 로고
    • Group V and X secretory phospholipase A2s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions
    • Ishimoto Y., Yamada K., Yamamoto S., Ono T., Notoya M., Hanasaki K. Group V and X secretory phospholipase A2s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions. Biochim. Biophys. Acta 2003, 1642:129-138.
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 129-138
    • Ishimoto, Y.1    Yamada, K.2    Yamamoto, S.3    Ono, T.4    Notoya, M.5    Hanasaki, K.6
  • 233
    • 67649424740 scopus 로고    scopus 로고
    • Molecular and functional characterization of polymorphisms in the secreted phospholipase A2 group X gene: relevance to coronary artery disease
    • Gora S., Perret C., Jemel I., Nicaud V., Lambeau G., Cambien F., Ninio E., Blankenberg S., Tiret L., Karabina S.A. Molecular and functional characterization of polymorphisms in the secreted phospholipase A2 group X gene: relevance to coronary artery disease. J. Mol. Med. 2009, 87:723-733.
    • (2009) J. Mol. Med. , vol.87 , pp. 723-733
    • Gora, S.1    Perret, C.2    Jemel, I.3    Nicaud, V.4    Lambeau, G.5    Cambien, F.6    Ninio, E.7    Blankenberg, S.8    Tiret, L.9    Karabina, S.A.10
  • 236
    • 34249816501 scopus 로고    scopus 로고
    • Sperm phospholipases and acrosomal exocytosis
    • Roldan E.R., Shi Q.X. Sperm phospholipases and acrosomal exocytosis. Front. Biosci. 2007, 12:89-104.
    • (2007) Front. Biosci. , vol.12 , pp. 89-104
    • Roldan, E.R.1    Shi, Q.X.2
  • 237
    • 0037190128 scopus 로고    scopus 로고
    • Expression of cytosolic and group X secretory phospholipaseA(2) genes in human colorectal adenocarcinomas
    • Osterstrom A., Dimberg J., Fransen K., Soderkvist P. Expression of cytosolic and group X secretory phospholipaseA(2) genes in human colorectal adenocarcinomas. Cancer Lett. 2002, 182:175-182.
    • (2002) Cancer Lett. , vol.182 , pp. 175-182
    • Osterstrom, A.1    Dimberg, J.2    Fransen, K.3    Soderkvist, P.4
  • 238
    • 38949163648 scopus 로고    scopus 로고
    • Distinct expression pattern of the full set of secreted phospholipases A2 in human colore ctal adenocarcinomas: sPLA2-III as a biomarker candidate
    • Mounier C.M., Wendum D., Greenspan E., Flejou J.F., Rosenberg D.W., Lambeau G. Distinct expression pattern of the full set of secreted phospholipases A2 in human colore ctal adenocarcinomas: sPLA2-III as a biomarker candidate. Br. J. Cancer 2008, 98:587-595.
    • (2008) Br. J. Cancer , vol.98 , pp. 587-595
    • Mounier, C.M.1    Wendum, D.2    Greenspan, E.3    Flejou, J.F.4    Rosenberg, D.W.5    Lambeau, G.6
  • 239
    • 0034602149 scopus 로고    scopus 로고
    • Suppression of intestinal polyposis in ApcDelta 716 knockout mice by an additio nal mutation in the cytosolic phospholipase A2 gene
    • Takaku K., Sonoshita M., Sasaki N., Uozumi N., Doi Y., Shimizu T., Taketo M.M. Suppression of intestinal polyposis in ApcDelta 716 knockout mice by an additio nal mutation in the cytosolic phospholipase A2 gene. J. Biol. Chem. 2000, 275:34013-34016.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34013-34016
    • Takaku, K.1    Sonoshita, M.2    Sasaki, N.3    Uozumi, N.4    Doi, Y.5    Shimizu, T.6    Taketo, M.M.7
  • 240
    • 0034677892 scopus 로고    scopus 로고
    • Novel human secreted phospholipase A2 with homology to the group III bee venom enzyme
    • Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G. Novel human secreted phospholipase A2 with homology to the group III bee venom enzyme. J. Biol. Chem. 2000, 275:7492-7496.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7492-7496
    • Valentin, E.1    Ghomashchi, F.2    Gelb, M.H.3    Lazdunski, M.4    Lambeau, G.5
  • 242
    • 21644487435 scopus 로고    scopus 로고
    • Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholi pase A2
    • Murakami M., Masuda S., Shimbara S., Ishikawa Y., Ishii T., Kudo I. Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholi pase A2. J. Biol. Chem. 2005, 280:24987-24998.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24987-24998
    • Murakami, M.1    Masuda, S.2    Shimbara, S.3    Ishikawa, Y.4    Ishii, T.5    Kudo, I.6
  • 245
    • 0027992088 scopus 로고
    • Cloning and characterization of novel rat and mouse low molecular weight Ca2+-dependent phospholipases A2 containing 16 cysteines
    • Chen J., Engle S.J., Seilhamer J.J., T ischfield J.A. Cloning and characterization of novel rat and mouse low molecular weight Ca2+-dependent phospholipases A2 containing 16 cysteines. J. Biol. Chem. 1994, 269:23018-23024.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23018-23024
    • Chen, J.1    Engle, S.J.2    Seilhamer, J.J.3    T ischfield, J.A.4
  • 246
    • 0031035805 scopus 로고    scopus 로고
    • Localization of group IIc low molecular weight phospholipase A2 mRNA to meiotic cells in the mouse
    • Chen J., Shao C., Lazar V., Srivastava C.H., Lee W.H., Tischfield J.A. Localization of group IIc low molecular weight phospholipase A2 mRNA to meiotic cells in the mouse. J. Cell. Biochem. 1997, 64:369-375.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 369-375
    • Chen, J.1    Shao, C.2    Lazar, V.3    Srivastava, C.H.4    Lee, W.H.5    Tischfield, J.A.6
  • 250
    • 0034139619 scopus 로고    scopus 로고
    • SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency
    • Shakhov A.N., Rubtsov A.V., Lyakhov I.G., Tumanov A.V., Nedospasov S.A. SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000, 1:191-199.
    • (2000) Genes Immun. , vol.1 , pp. 191-199
    • Shakhov, A.N.1    Rubtsov, A.V.2    Lyakhov, I.G.3    Tumanov, A.V.4    Nedospasov, S.A.5
  • 252
    • 33646132893 scopus 로고    scopus 로고
    • Interferon gamma-induced gene expression of the novel secretory phospholipase A2 type IID in human monocyte-derived macrophages is inhibited by lipopolysaccharide
    • Lindbom J., Ljungman A.G., Tagesson C. Interferon gamma-induced gene expression of the novel secretory phospholipase A2 type IID in human monocyte-derived macrophages is inhibited by lipopolysaccharide. Inflammation 2005, 29:108-117.
    • (2005) Inflammation , vol.29 , pp. 108-117
    • Lindbom, J.1    Ljungman, A.G.2    Tagesson, C.3
  • 258
    • 0034704143 scopus 로고    scopus 로고
    • Cloning and recombinant expression of a structurally novel human secreted phospholipase A2
    • Gelb M.H., Valentin E., Ghoma shchi F., Lazdunski M., Lambeau G. Cloning and recombinant expression of a structurally novel human secreted phospholipase A2. J. Biol. Chem. 2000, 275:39823-39826.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39823-39826
    • Gelb, M.H.1    Valentin, E.2    Ghoma shchi, F.3    Lazdunski, M.4    Lambeau, G.5
  • 260
    • 33644817721 scopus 로고    scopus 로고
    • Antibacterial effects of human group IIA and group XIIA pho spholipase A2 against Helicobacter pylori in vitro
    • Huhtinen H.T., Gronroos J.O., Gronroos J.M., Uksila J., Gelb M.H., Nevalainen T.J., Laine V.J. Antibacterial effects of human group IIA and group XIIA pho spholipase A2 against Helicobacter pylori in vitro. Apmis 2006, 114:127-130.
    • (2006) Apmis , vol.114 , pp. 127-130
    • Huhtinen, H.T.1    Gronroos, J.O.2    Gronroos, J.M.3    Uksila, J.4    Gelb, M.H.5    Nevalainen, T.J.6    Laine, V.J.7
  • 261
    • 17644420004 scopus 로고    scopus 로고
    • Induction of ectopic olfactory structures and bone morphogenetic protein inhibition by Rossy, a group XII secreted phospholipase A2
    • Munoz-Sanjuan I., Brivanlou A.H. Induction of ectopic olfactory structures and bone morphogenetic protein inhibition by Rossy, a group XII secreted phospholipase A2. Mol. Cell. Biol. 2005, 25:3608-3619.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3608-3619
    • Munoz-Sanjuan, I.1    Brivanlou, A.H.2
  • 262
    • 34047126302 scopus 로고    scopus 로고
    • Gene targeting reveals the role of Oc90 as the essential organizer of the otoconial organic matrix
    • Zhao X., Yang H., Yamoah E.N., Lundberg Y.W. Gene targeting reveals the role of Oc90 as the essential organizer of the otoconial organic matrix. Dev. Biol. 2007, 304:508-524.
    • (2007) Dev. Biol. , vol.304 , pp. 508-524
    • Zhao, X.1    Yang, H.2    Yamoah, E.N.3    Lundberg, Y.W.4
  • 263
    • 41949116366 scopus 로고    scopus 로고
    • Otoconin-90 deletion leads to imbalance but normal hearing: a comparison with other otoconia mutants
    • Zhao X., Jones S.M., Yamoah E.N., Lundberg Y.W. Otoconin-90 deletion leads to imbalance but normal hearing: a comparison with other otoconia mutants. Neuroscience 2008, 153:289-299.
    • (2008) Neuroscience , vol.153 , pp. 289-299
    • Zhao, X.1    Jones, S.M.2    Yamoah, E.N.3    Lundberg, Y.W.4
  • 264
    • 0027277037 scopus 로고
    • Otoconin-22, the major protein of aragonitic frog otoconia, is a homolog of phospholipase A2
    • Pote K.G., Hauer C.R.I., Michel H., Shabanowitz J., Hunt D.F., Kretsinger R.H. Otoconin-22, the major protein of aragonitic frog otoconia, is a homolog of phospholipase A2. Biochemistry 1993, 32:5017-5024.
    • (1993) Biochemistry , vol.32 , pp. 5017-5024
    • Pote, K.G.1    Hauer, C.R.I.2    Michel, H.3    Shabanowitz, J.4    Hunt, D.F.5    Kretsinger, R.H.6
  • 265
    • 2442700237 scopus 로고    scopus 로고
    • Developmental expression of otoconin-22 in the bullfrog endolymphatic sac and in nerear
    • Yaoi Y., Onda T., Hidaka Y., Yajima S., Suzuki M., Tanaka S. Developmental expression of otoconin-22 in the bullfrog endolymphatic sac and in nerear. J. Histochem. Cytochem. 2004, 52:663-670.
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 663-670
    • Yaoi, Y.1    Onda, T.2    Hidaka, Y.3    Yajima, S.4    Suzuki, M.5    Tanaka, S.6
  • 266
    • 38849178115 scopus 로고    scopus 로고
    • Otoc1: a novel otoconin-90 ortholog required for otolith mineralization in zebrafish
    • Petko J.A., Millimaki B.B., Canfield V.A., Riley B.B., Levenson R. Otoc1: a novel otoconin-90 ortholog required for otolith mineralization in zebrafish. Dev. Neurobiol. 2008, 68:209-222.
    • (2008) Dev. Neurobiol. , vol.68 , pp. 209-222
    • Petko, J.A.1    Millimaki, B.B.2    Canfield, V.A.3    Riley, B.B.4    Levenson, R.5
  • 267
    • 0037709970 scopus 로고    scopus 로고
    • Interaction of low molecular weight group IIA phospholipase A2 with apoptotic human T cells: role of heparan sulfate proteoglycans
    • Boilard E., Bourgoin S.G., Bernatchez C., Poubelle P.E., Surette M.E. Interaction of low molecular weight group IIA phospholipase A2 with apoptotic human T cells: role of heparan sulfate proteoglycans. Faseb J. 2003, 17:1068-1080.
    • (2003) Faseb J. , vol.17 , pp. 1068-1080
    • Boilard, E.1    Bourgoin, S.G.2    Bernatchez, C.3    Poubelle, P.E.4    Surette, M.E.5
  • 268
    • 0036669794 scopus 로고    scopus 로고
    • Phospholipase A2 receptor: a regulator of biological functions of secretory phospholipase A2
    • Hanasaki K., Arita H. Phospholipase A2 receptor: a regulator of biological functions of secretory phospholipase A2. Prostaglandins Other Lipid Mediat. 2002, 68-69:71-82.
    • (2002) Prostaglandins Other Lipid Mediat. , vol.68-69 , pp. 71-82
    • Hanasaki, K.1    Arita, H.2
  • 269
    • 1042287027 scopus 로고    scopus 로고
    • Natural phospholipase A2 myotoxin inhibitor proteins from snakes, mammals and plants
    • Lizano S., Domont G., Perales J. Natural phospholipase A2 myotoxin inhibitor proteins from snakes, mammals and plants. Toxicon 2003, 42:963-977.
    • (2003) Toxicon , vol.42 , pp. 963-977
    • Lizano, S.1    Domont, G.2    Perales, J.3
  • 270
    • 27644566534 scopus 로고    scopus 로고
    • Secretory phospholipases A2 in inflammatory and allergic diseases: not just enzymes
    • Triggiani M., Granata F., Giannattasio G., Marone G. Secretory phospholipases A2 in inflammatory and allergic diseases: not just enzymes. J. Allergy Clin. Immunol. 2005, 116:1000-1006.
    • (2005) J. Allergy Clin. Immunol. , vol.116 , pp. 1000-1006
    • Triggiani, M.1    Granata, F.2    Giannattasio, G.3    Marone, G.4
  • 271
    • 42449097135 scopus 로고    scopus 로고
    • Catalytically inactive phospholipase A2 homologue binds to vascular endothelial growth factor receptor-2 via a C-terminal loop region
    • Fujis awa D., Yamazaki Y., Lomonte B., Morita T. Catalytically inactive phospholipase A2 homologue binds to vascular endothelial growth factor receptor-2 via a C-terminal loop region. Biochem. J. 2008, 411:515-522.
    • (2008) Biochem. J. , vol.411 , pp. 515-522
    • Fujis awa, D.1    Yamazaki, Y.2    Lomonte, B.3    Morita, T.4
  • 272
    • 54449088685 scopus 로고    scopus 로고
    • Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in an integrin-dependent manner
    • Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S., Liu F.T., Takada Y.K., Takada Y. Pro-inflammatory secretory phospholipase A2 type IIA binds to integrins alphavbeta3 and alpha4beta1 and induces proliferation of monocytic cells in an integrin-dependent manner. J. Biol. Chem. 2008, 283:26107-26115.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26107-26115
    • Saegusa, J.1    Akakura, N.2    Wu, C.Y.3    Hoogland, C.4    Ma, Z.5    Lam, K.S.6    Liu, F.T.7    Takada, Y.K.8    Takada, Y.9
  • 276
    • 0041529693 scopus 로고    scopus 로고
    • Potentiation of TNFalpha -induced sPLA2-IIA expression in mesangial cells by an autocrine loop involving secreted phospholipase A2 and PPARalpha activation
    • Beck S., Lambeau G., Scholz-Pedretti K., Gelb M.H., Janssen M.J., Edwards S.H., Wilton D.C., Pfeilschifter J., Kaszkin M. Potentiation of TNFalpha -induced sPLA2-IIA expression in mesangial cells by an autocrine loop involving secreted phospholipase A2 and PPARalpha activation. J. Biol. Chem. 2003, 278:29799-29812.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29799-29812
    • Beck, S.1    Lambeau, G.2    Scholz-Pedretti, K.3    Gelb, M.H.4    Janssen, M.J.5    Edwards, S.H.6    Wilton, D.C.7    Pfeilschifter, J.8    Kaszkin, M.9
  • 277
    • 70350130979 scopus 로고    scopus 로고
    • Secreted phospholipase A2-IIA modulates key regulators of proliferation on astrocytoma cells
    • Martin R., Hernandez M., Ibeas E., Fuentes L., Salicio V., Arnes M., Nieto M.L. Secreted phospholipase A2-IIA modulates key regulators of proliferation on astrocytoma cells. J. Neurochem. 2009, 111:988-999.
    • (2009) J. Neurochem. , vol.111 , pp. 988-999
    • Martin, R.1    Hernandez, M.2    Ibeas, E.3    Fuentes, L.4    Salicio, V.5    Arnes, M.6    Nieto, M.L.7
  • 278
    • 0025300683 scopus 로고
    • Identification and purification of a very high affinity binding protein for toxic phospholipases A2 in skeletal muscle
    • Lambeau G., Schmid-Alliana A., Lazdunski M., Barhanin J. Identification and purification of a very high affinity binding protein for toxic phospholipases A2 in skeletal muscle. J. Biol. Chem. 1990, 265:9526-9532.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9526-9532
    • Lambeau, G.1    Schmid-Alliana, A.2    Lazdunski, M.3    Barhanin, J.4
  • 279
    • 43049176187 scopus 로고    scopus 로고
    • Extended and bent conformations of the mannose receptor family
    • Llorca O. Extended and bent conformations of the mannose receptor family. Cell. Mol. Life Sci. 2008, 65:1302-1310.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1302-1310
    • Llorca, O.1
  • 282
    • 0028084979 scopus 로고
    • Cloning and expression of a membrane receptor for secretory phospholipases A2
    • Lambea u G., Ancian P., Barhanin J., Lazdunski M. Cloning and expression of a membrane receptor for secretory phospholipases A2. J. Biol. Chem. 1994, 269:1575-1578.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1575-1578
    • Lambea u, G.1    Ancian, P.2    Barhanin, J.3    Lazdunski, M.4
  • 283
    • 0028954284 scopus 로고
    • The human 180-kDa receptor for secretory ph ospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization
    • Ancian P., Lambeau G., Mattéi M.G., Lazdunski M. The human 180-kDa receptor for secretory ph ospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization. J. Biol. Chem. 1995, 270:8963-8970.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8963-8970
    • Ancian, P.1    Lambeau, G.2    Mattéi, M.G.3    Lazdunski, M.4
  • 284
    • 2442511057 scopus 로고    scopus 로고
    • The chicken yolk sac IgY receptor, a functional eq uivalent of the mammalian MHC-related Fc receptor, is a phospholipase A2 receptor homolog
    • West A.P., Herr A.B., Bjorkman P.J. The chicken yolk sac IgY receptor, a functional eq uivalent of the mammalian MHC-related Fc receptor, is a phospholipase A2 receptor homolog. Immunity 2004, 20:601-610.
    • (2004) Immunity , vol.20 , pp. 601-610
    • West, A.P.1    Herr, A.B.2    Bjorkman, P.J.3
  • 285
    • 0028176838 scopus 로고
    • Inhibition of Trimeresurus flavoviridis phospholipase A2 by lung surfactant protein A (SP-A)
    • Fisher A.B., Dodia C., Chander A., Beers M.F., Bates S.R. Inhibition of Trimeresurus flavoviridis phospholipase A2 by lung surfactant protein A (SP-A). Biochim. Biophys. Acta 1994, 1211:256-262.
    • (1994) Biochim. Biophys. Acta , vol.1211 , pp. 256-262
    • Fisher, A.B.1    Dodia, C.2    Chander, A.3    Beers, M.F.4    Bates, S.R.5
  • 286
    • 27844495183 scopus 로고    scopus 로고
    • Mapping the region of the alpha-type phospholipase A2 inhibitor responsible for its inhibitory activity
    • Okumura K., Ohno A., Nishida M., Hayashi K., Ikeda K., Inoue S. Mapping the region of the alpha-type phospholipase A2 inhibitor responsible for its inhibitory activity. J. Biol. Chem. 2005, 280:37651-37659.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37651-37659
    • Okumura, K.1    Ohno, A.2    Nishida, M.3    Hayashi, K.4    Ikeda, K.5    Inoue, S.6
  • 287
    • 0030028070 scopus 로고    scopus 로고
    • Endocytic properties of the M-type 180-kDa receptor for secretory phospholipases A2
    • Zvaritch E., Lambeau G., Lazdunski M. Endocytic properties of the M-type 180-kDa receptor for secretory phospholipases A2. J. Biol. Chem. 1996, 271:250-257.
    • (1996) J. Biol. Chem. , vol.271 , pp. 250-257
    • Zvaritch, E.1    Lambeau, G.2    Lazdunski, M.3
  • 288
    • 0031466963 scopus 로고    scopus 로고
    • Resi stance to endotoxic shock in phospholipase A2 receptor-deficient mice
    • Hanasaki K., Yokota Y., Ishizaki J., Itoh T., Arita H. Resi stance to endotoxic shock in phospholipase A2 receptor-deficient mice. J. Biol. Chem. 1997, 272:32792-32797.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32792-32797
    • Hanasaki, K.1    Yokota, Y.2    Ishizaki, J.3    Itoh, T.4    Arita, H.5
  • 289
    • 61849129365 scopus 로고    scopus 로고
    • The M-type receptor PLA2R regulates senescence through the p53 pathway
    • Augert A., Payre C., de Launoit Y., Gil J., Lambeau G., Bernard D. The M-type receptor PLA2R regulates senescence through the p53 pathway. EMBO Rep. 2009, 10:271-277.
    • (2009) EMBO Rep. , vol.10 , pp. 271-277
    • Augert, A.1    Payre, C.2    de Launoit, Y.3    Gil, J.4    Lambeau, G.5    Bernard, D.6
  • 290
    • 64849104126 scopus 로고    scopus 로고
    • Induction of cellular senescence by secretory phospholipase A2 in human dermal fibroblasts through an ROS-mediated p53 pathway
    • Kim H.J., Kim K.S., Kim S.H., Baek S.H., Kim H.Y., Lee C., Kim J.R. Induction of cellular senescence by secretory phospholipase A2 in human dermal fibroblasts through an ROS-mediated p53 pathway. J. Gerontol. A. Biol. Sci. Med. Sci. 2009, 64:351-362.
    • (2009) J. Gerontol. A. Biol. Sci. Med. Sci. , vol.64 , pp. 351-362
    • Kim, H.J.1    Kim, K.S.2    Kim, S.H.3    Baek, S.H.4    Kim, H.Y.5    Lee, C.6    Kim, J.R.7
  • 293
    • 0020261362 scopus 로고
    • Novel intestinal phospholipase A2: purification and some molecular characteristics
    • Verger R., Ferrato F., Mansbach C.M., Pieroni G. Novel intestinal phospholipase A2: purification and some molecular characteristics. Biochemistry 1982, 21:6883-6889.
    • (1982) Biochemistry , vol.21 , pp. 6883-6889
    • Verger, R.1    Ferrato, F.2    Mansbach, C.M.3    Pieroni, G.4
  • 294
    • 0022814387 scopus 로고
    • Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis
    • Stefanski E., Pruzanski W., Sternby B., Vadas P. Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis. J. Biochem. 1986, 100:1297-1303.
    • (1986) J. Biochem. , vol.100 , pp. 1297-1303
    • Stefanski, E.1    Pruzanski, W.2    Sternby, B.3    Vadas, P.4
  • 295
    • 0022894807 scopus 로고
    • Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate
    • Forst S., Weiss J., Elsbach P., Maraganore J.M., Reardon I., Heinrikson R.L. Structural and functional properties of a phospholipase A2 purified from an inflammatory exudate. Biochemistry 1986, 25:8381-8385.
    • (1986) Biochemistry , vol.25 , pp. 8381-8385
    • Forst, S.1    Weiss, J.2    Elsbach, P.3    Maraganore, J.M.4    Reardon, I.5    Heinrikson, R.L.6
  • 296
  • 297
    • 27944472180 scopus 로고    scopus 로고
    • Inhibitors of secretory phospholipase A2 group IIA
    • Reid R.C. Inhibitors of secretory phospholipase A2 group IIA. Curr. Med. Chem. 2005, 12:3011-3026.
    • (2005) Curr. Med. Chem. , vol.12 , pp. 3011-3026
    • Reid, R.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.