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Volumn 240, Issue 1, 2006, Pages 9-16

Oncogenic action of phospholipase A2 in prostate cancer

Author keywords

Annexin A1; Annexin A2; Cyclooxygenase; Cytosolic phospholipase A2; Eicosanoids; Lipoxygenase; Secreted phospholipase A2

Indexed keywords

ANDROGEN; HORMONE DERIVATIVE; LIPOCORTIN 1; LIPOCORTIN 2; LIPOXYGENASE; LIPOXYGENASE INHIBITOR; METRIBOLONE; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 INHIBITOR; PROSTAGLANDIN SYNTHASE; PROSTAGLANDIN SYNTHASE INHIBITOR; PYRROLIDINE DERIVATIVE;

EID: 33745860033     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2005.08.012     Document Type: Review
Times cited : (87)

References (61)
  • 1
    • 0025974356 scopus 로고
    • Carcinoma of the prostate
    • [see comments]
    • Gittes R.F. Carcinoma of the prostate. N. Engl. J. Med. 324 (1991) 236-245 [see comments]
    • (1991) N. Engl. J. Med. , vol.324 , pp. 236-245
    • Gittes, R.F.1
  • 2
    • 0023185591 scopus 로고
    • Carcinoma of the prostate. Hormonal therapy
    • Grayhack J.T., Keeler T.C., and Kozlowski J.M. Carcinoma of the prostate. Hormonal therapy. Cancer 60 (1987) 589-601
    • (1987) Cancer , vol.60 , pp. 589-601
    • Grayhack, J.T.1    Keeler, T.C.2    Kozlowski, J.M.3
  • 3
    • 0034637528 scopus 로고    scopus 로고
    • A distinct sequence (ATAAA)(n) separates methylated and unmethylated domains at the 5 '-end of the GSTP1 CpG island
    • Millar D.S., Paul C.L., Molloy P.L., and Clark S.J. A distinct sequence (ATAAA)(n) separates methylated and unmethylated domains at the 5 '-end of the GSTP1 CpG island. J. Biol. Chem. 275 (2000) 24893-24899
    • (2000) J. Biol. Chem. , vol.275 , pp. 24893-24899
    • Millar, D.S.1    Paul, C.L.2    Molloy, P.L.3    Clark, S.J.4
  • 4
    • 0033545329 scopus 로고    scopus 로고
    • Detailed methylation analysis of the glutathione S-transferase pi (GSTP1) gene in prostate cancer
    • Millar D.S., Ow K.K., Paul C.L., Russell P.J., Molloy P.L., and Clark S.J. Detailed methylation analysis of the glutathione S-transferase pi (GSTP1) gene in prostate cancer. Oncogene 18 (1999) 1313-1324
    • (1999) Oncogene , vol.18 , pp. 1313-1324
    • Millar, D.S.1    Ow, K.K.2    Paul, C.L.3    Russell, P.J.4    Molloy, P.L.5    Clark, S.J.6
  • 5
    • 0031012829 scopus 로고    scopus 로고
    • Glutathione s-transferase pi (gst-pi) class expression by immunohistochemistry in benign and malignant prostate tissue
    • Cookson M.S., Reuter V.E., Linkov I., and Fair W.R. Glutathione s-transferase pi (gst-pi) class expression by immunohistochemistry in benign and malignant prostate tissue. J. Urol. 157 (1997) 673-676
    • (1997) J. Urol. , vol.157 , pp. 673-676
    • Cookson, M.S.1    Reuter, V.E.2    Linkov, I.3    Fair, W.R.4
  • 6
    • 0035418338 scopus 로고    scopus 로고
    • Loss of annexin II heavy and light chains in prostate cancer and its precursors
    • Chetcuti A., Margan S.H., Russell P., Mann S., Millar D.S., Clark S.J., et al. Loss of annexin II heavy and light chains in prostate cancer and its precursors. Cancer Res. 61 (2001) 6331-6334
    • (2001) Cancer Res. , vol.61 , pp. 6331-6334
    • Chetcuti, A.1    Margan, S.H.2    Russell, P.3    Mann, S.4    Millar, D.S.5    Clark, S.J.6
  • 7
    • 0033676804 scopus 로고    scopus 로고
    • Loss of annexin 1 correlates with early onset of tumorigenesis in esophageal and prostate carcinoma
    • Paweletz C.P., Ornstein D.K., Roth M.J., Bichsel V.E., Gillespie J.W., Calvert V.S., et al. Loss of annexin 1 correlates with early onset of tumorigenesis in esophageal and prostate carcinoma. Cancer Res. 60 (2000) 6293-6297
    • (2000) Cancer Res. , vol.60 , pp. 6293-6297
    • Paweletz, C.P.1    Ornstein, D.K.2    Roth, M.J.3    Bichsel, V.E.4    Gillespie, J.W.5    Calvert, V.S.6
  • 9
    • 0028324464 scopus 로고    scopus 로고
    • Raynal P., Pollard H.B., Annexins - the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins [Review], Biochimica et Biophysica Acta - Reviews on Biomembranes 1197 (1994) 63-93.
  • 10
    • 0028928357 scopus 로고
    • The S100 protein family: history, function, and expression
    • Zimmer D.B., Cornwall E.H., Landar A., and Song W. The S100 protein family: history, function, and expression. Brain Res. Bull. 37 (1995) 417-429
    • (1995) Brain Res. Bull. , vol.37 , pp. 417-429
    • Zimmer, D.B.1    Cornwall, E.H.2    Landar, A.3    Song, W.4
  • 11
    • 0025939163 scopus 로고
    • Perspectives in S-100 protein biology
    • Donato R. Perspectives in S-100 protein biology. Cell Calcium 12 (1991) 713-726
    • (1991) Cell Calcium , vol.12 , pp. 713-726
    • Donato, R.1
  • 13
    • 0030022110 scopus 로고    scopus 로고
    • Annexin II up-regulates cellular levels of P11 protein by a post-translational mechanism
    • Puisieux A., Ji J.W., and Ozturk M. Annexin II up-regulates cellular levels of P11 protein by a post-translational mechanism. Biochem. J. 313 (1996) 51-55
    • (1996) Biochem. J. , vol.313 , pp. 51-55
    • Puisieux, A.1    Ji, J.W.2    Ozturk, M.3
  • 14
    • 0141483322 scopus 로고    scopus 로고
    • Rouault M., Bollinger J.G., Lazdunski M., Gelb M.H., Lambeau G., Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity, Biochemistry (Mosc) September 13 (2003) ASAP Article.
  • 15
  • 16
    • 0035823620 scopus 로고    scopus 로고
    • A novel group IIA phospholipase A(2) interacts with v-Src oncoprotein from RSV-transformed hamster cells
    • Mizenina O., Musatkina E., Yanushevich Y., Rodina A., Krasilnikov M., de Gunzburg J., et al. A novel group IIA phospholipase A(2) interacts with v-Src oncoprotein from RSV-transformed hamster cells. J. Biol. Chem. 276 (2001) 34006-34012
    • (2001) J. Biol. Chem. , vol.276 , pp. 34006-34012
    • Mizenina, O.1    Musatkina, E.2    Yanushevich, Y.3    Rodina, A.4    Krasilnikov, M.5    de Gunzburg, J.6
  • 17
    • 0034739474 scopus 로고    scopus 로고
    • Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins
    • Valentin E., and Lambeau G. Increasing molecular diversity of secreted phospholipases A(2) and their receptors and binding proteins. Biochim. Biophys. Acta 1488 (2000) 59-70
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 59-70
    • Valentin, E.1    Lambeau, G.2
  • 18
    • 0034739463 scopus 로고    scopus 로고
    • The expanding superfamily of phospholipase A(2) enzymes: classification and characterization
    • Six D.A., and Dennis E.A. The expanding superfamily of phospholipase A(2) enzymes: classification and characterization. Biochim. Biophys. Acta 1488 (2000) 1-19
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 1-19
    • Six, D.A.1    Dennis, E.A.2
  • 19
    • 21644470823 scopus 로고    scopus 로고
    • Identification of novel cytosolic phospholipase A2s, murine cPLA2d, e, and t, which form a gene cluster with cPLA2b
    • Ohto T., Uozumi N., Hirabayashi T., and Shimizu T. Identification of novel cytosolic phospholipase A2s, murine cPLA2d, e, and t, which form a gene cluster with cPLA2b. J. Biol. Chem. 280 (2005) 24576-24583
    • (2005) J. Biol. Chem. , vol.280 , pp. 24576-24583
    • Ohto, T.1    Uozumi, N.2    Hirabayashi, T.3    Shimizu, T.4
  • 20
    • 0035793464 scopus 로고    scopus 로고
    • Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model
    • Kim S., Ko J., Kim J.H., Choi E.C., and Na D.S. Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model. FEBS Lett. 489 (2001) 243-248
    • (2001) FEBS Lett. , vol.489 , pp. 243-248
    • Kim, S.1    Ko, J.2    Kim, J.H.3    Choi, E.C.4    Na, D.S.5
  • 21
    • 0030814032 scopus 로고    scopus 로고
    • P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2
    • Wu T., Angus C.W., Yao X.L., Logun C., and Shelhamer J.H. P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2. J. Biol. Chem. 272 (1997) 17145-17153
    • (1997) J. Biol. Chem. , vol.272 , pp. 17145-17153
    • Wu, T.1    Angus, C.W.2    Yao, X.L.3    Logun, C.4    Shelhamer, J.H.5
  • 22
    • 0023821674 scopus 로고
    • Ca2+-dependent phospholipid- (and membrane-) binding proteins
    • Klee C.B. Ca2+-dependent phospholipid- (and membrane-) binding proteins. Biochemistry 27 (1988) 6645-6653
    • (1988) Biochemistry , vol.27 , pp. 6645-6653
    • Klee, C.B.1
  • 23
    • 0033546309 scopus 로고    scopus 로고
    • Dexamethasone alters arachidonate release from human epithelial cells by induction of p11 protein synthesis and inhibition of phospholipase A2 activity
    • Yao X.L., Cowan M.J., Gladwin M.T., Lawrence M.M., Angus C.W., and Shelhamer J.H. Dexamethasone alters arachidonate release from human epithelial cells by induction of p11 protein synthesis and inhibition of phospholipase A2 activity. J. Biol. Chem. 274 (1999) 17202-17208
    • (1999) J. Biol. Chem. , vol.274 , pp. 17202-17208
    • Yao, X.L.1    Cowan, M.J.2    Gladwin, M.T.3    Lawrence, M.M.4    Angus, C.W.5    Shelhamer, J.H.6
  • 24
    • 0023644562 scopus 로고
    • Inhibition of phospholipase A2 by "lipocortins" and calpactins. An effect of binding to substrate phospholipids
    • Davidson F.F., Dennis E.A., Powell M., and Glenney Jr. J.R. Inhibition of phospholipase A2 by "lipocortins" and calpactins. An effect of binding to substrate phospholipids. J. Biol. Chem. 262 (1987) 1698-1705
    • (1987) J. Biol. Chem. , vol.262 , pp. 1698-1705
    • Davidson, F.F.1    Dennis, E.A.2    Powell, M.3    Glenney Jr., J.R.4
  • 25
    • 0023654840 scopus 로고
    • Characterization of lipocortin I and an immunologically unrelated 33-kDa protein as epidermal growth factor receptor/kinase substrates and phospholipase A2 inhibitors
    • Haigler H.T., Schlaepfer D.D., and Burgess W.H. Characterization of lipocortin I and an immunologically unrelated 33-kDa protein as epidermal growth factor receptor/kinase substrates and phospholipase A2 inhibitors. J. Biol. Chem. 262 (1987) 6921-6930
    • (1987) J. Biol. Chem. , vol.262 , pp. 6921-6930
    • Haigler, H.T.1    Schlaepfer, D.D.2    Burgess, W.H.3
  • 26
    • 0023196365 scopus 로고
    • Lipocortin inhibition of extracellular and intracellular phospholipases A2 is substrate concentration dependent
    • Aarsman A.J., Mynbeek G., van den Bosch H., Rothhut B., Prieur B., Comera C., et al. Lipocortin inhibition of extracellular and intracellular phospholipases A2 is substrate concentration dependent. FEBS Lett. 219 (1987) 176-180
    • (1987) FEBS Lett. , vol.219 , pp. 176-180
    • Aarsman, A.J.1    Mynbeek, G.2    van den Bosch, H.3    Rothhut, B.4    Prieur, B.5    Comera, C.6
  • 27
    • 0024268328 scopus 로고
    • Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor
    • Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W., and de Haen C. Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor. J. Biol. Chem. 263 (1988) 18657-18663
    • (1988) J. Biol. Chem. , vol.263 , pp. 18657-18663
    • Ahn, N.G.1    Teller, D.C.2    Bienkowski, M.J.3    McMullen, B.A.4    Lipkin, E.W.5    de Haen, C.6
  • 28
    • 0034018418 scopus 로고    scopus 로고
    • Structure-function analyses of eicosanoid receptors. Physiologic and therapeutic implications
    • Breyer R.M., Kennedy C.R., Zhang Y., and Breyer M.D. Structure-function analyses of eicosanoid receptors. Physiologic and therapeutic implications. Ann. NY Acad. Sci. 905 (2000) 221-231
    • (2000) Ann. NY Acad. Sci. , vol.905 , pp. 221-231
    • Breyer, R.M.1    Kennedy, C.R.2    Zhang, Y.3    Breyer, M.D.4
  • 29
    • 0036896107 scopus 로고    scopus 로고
    • 5(S)-Hydroxy-6,8,11,14-E,Z,Z,Z-eicosatetraenoate stimulates PC3 cell signaling and growth by a receptor-dependent mechanism
    • O'Flaherty J.T., Rogers L.C., Chadwell B.A., Owen J.S., Rao A., Cramer S.D., and Daniel L.W. 5(S)-Hydroxy-6,8,11,14-E,Z,Z,Z-eicosatetraenoate stimulates PC3 cell signaling and growth by a receptor-dependent mechanism. Cancer Res. 62 (2002) 6817-6819
    • (2002) Cancer Res. , vol.62 , pp. 6817-6819
    • O'Flaherty, J.T.1    Rogers, L.C.2    Chadwell, B.A.3    Owen, J.S.4    Rao, A.5    Cramer, S.D.6    Daniel, L.W.7
  • 30
    • 0030614354 scopus 로고    scopus 로고
    • The growing phospholipase A2 superfamily of signal transduction enzymes
    • Dennis E.A. The growing phospholipase A2 superfamily of signal transduction enzymes. Trends Biochem. Sci. 22 (1997) 1-2
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 1-2
    • Dennis, E.A.1
  • 31
    • 0035028449 scopus 로고    scopus 로고
    • Fukushima N., Ishii I., Contos J.J., Weiner J.A., Chun J., Lysophospholipid receptors.[erratum appears in Annu Rev Pharmacol Toxicol 2002;42:vii], Annual Review of Pharmacology & Toxicology. 41 (2001) 507-534.
  • 32
    • 0031445523 scopus 로고    scopus 로고
    • Role of cytosolic phospholipase A2 in allergic response and parturition
    • Uozumi N., Kume K., Nagase T., Nakatani N., Ishii S., Tashiro F., et al. Role of cytosolic phospholipase A2 in allergic response and parturition. Nature 390 (1997) 618-622
    • (1997) Nature , vol.390 , pp. 618-622
    • Uozumi, N.1    Kume, K.2    Nagase, T.3    Nakatani, N.4    Ishii, S.5    Tashiro, F.6
  • 33
    • 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., and Sapirstein A. Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2. Nature 390 (1997) 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
  • 34
    • 0034739477 scopus 로고    scopus 로고
    • Specific physiological roles of cytosolic phospholipase A(2) as defined by gene knockouts
    • Sapirstein A., and Bonventre J.V. Specific physiological roles of cytosolic phospholipase A(2) as defined by gene knockouts. Biochim. Biophys. Acta 1488 (2000) 139-148
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 139-148
    • Sapirstein, A.1    Bonventre, J.V.2
  • 35
    • 0036669685 scopus 로고    scopus 로고
    • Roles for cytosolic phospholipase A2alpha as revealed by gene-targeted mice
    • Uozumi N., and Shimizu T. Roles for cytosolic phospholipase A2alpha as revealed by gene-targeted mice. Prostaglandins Other Lipid Mediat. 68-69 (2002) 59-69
    • (2002) Prostaglandins Other Lipid Mediat. , vol.68-69 , pp. 59-69
    • Uozumi, N.1    Shimizu, T.2
  • 36
    • 0038399752 scopus 로고    scopus 로고
    • Phospholipase A(2) isoforms: a perspective
    • Chakraborti S. Phospholipase A(2) isoforms: a perspective. Cell. Signal. 15 (2003) 637-665
    • (2003) Cell. Signal. , vol.15 , pp. 637-665
    • Chakraborti, S.1
  • 37
    • 16644382118 scopus 로고    scopus 로고
    • Regulatory mechanism and physiological role of cytosolic phospholipase A2
    • Hirabayashi T., Murayama T., and Shimizu T. Regulatory mechanism and physiological role of cytosolic phospholipase A2. Biol. Pharm. Bull. 27 (2004) 1168-1173
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 1168-1173
    • Hirabayashi, T.1    Murayama, T.2    Shimizu, T.3
  • 38
    • 0027513175 scopus 로고
    • New insights on mammalian phospholipase A2(s); comparison of arachidonoyl-selective and -nonselective enzymes
    • Mayer R.J., and Marshall L.A. New insights on mammalian phospholipase A2(s); comparison of arachidonoyl-selective and -nonselective enzymes. FASEB J. 7 (1993) 339-348
    • (1993) FASEB J. , vol.7 , pp. 339-348
    • Mayer, R.J.1    Marshall, L.A.2
  • 39
    • 0028169417 scopus 로고
    • Phospholipase A2 enzymes: regulation and physiological role
    • Mukherjee A.B., Miele L., and Pattabiraman N. Phospholipase A2 enzymes: regulation and physiological role. Biochem. Pharmacol. 48 (1994) 1-10
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1-10
    • Mukherjee, A.B.1    Miele, L.2    Pattabiraman, N.3
  • 40
    • 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., and 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. 279 (2004) 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
  • 41
    • 0033178693 scopus 로고    scopus 로고
    • Regulation of type V phospholipase A2 expression and function by proinflammatory stimuli
    • Sawada H., Murakami M., Enomoto A., Shimbara S., and Kudo I. Regulation of type V phospholipase A2 expression and function by proinflammatory stimuli. Eur. J. Biochem. 263 (1999) 826-835
    • (1999) Eur. J. Biochem. , vol.263 , pp. 826-835
    • Sawada, H.1    Murakami, M.2    Enomoto, A.3    Shimbara, S.4    Kudo, I.5
  • 42
    • 0034292359 scopus 로고    scopus 로고
    • Redundant and segregated functions of granule-associated 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., and Kudo I. Redundant and segregated functions of granule-associated heparin-binding group II subfamily of secretory phospholipases A2 in the regulation of degranulation and prostaglandin D2 synthesis in mast cells. J. Immunol. 165 (2000) 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
  • 43
    • 0036213281 scopus 로고    scopus 로고
    • Phospholipase A2
    • Murakami M., and Kudo I. Phospholipase A2. J. Biochem. 131 (2002) 285-292
    • (2002) J. Biochem. , vol.131 , pp. 285-292
    • Murakami, M.1    Kudo, I.2
  • 44
    • 0030006530 scopus 로고    scopus 로고
    • Increased phospholipid fatty acid remodeling in human and rat prostatic adenocarcinoma tissues
    • Faas F.H., Dang A.Q., Pollard M., Hong X.M., Fan K., Luckert P.H., and Schutz M. Increased phospholipid fatty acid remodeling in human and rat prostatic adenocarcinoma tissues. J. Urol. 156 (1996) 243-248
    • (1996) J. Urol. , vol.156 , pp. 243-248
    • Faas, F.H.1    Dang, A.Q.2    Pollard, M.3    Hong, X.M.4    Fan, K.5    Luckert, P.H.6    Schutz, M.7
  • 45
    • 0033781990 scopus 로고    scopus 로고
    • Cytoplasmic induction and over-expression of cyclooxygenase-2 in human prostate cancer: implications for prevention and treatment
    • Madaan S., Abel P.D., Chaudhary K.S., Hewitt R., Stott M.A., Stamp G.W., and Lalani E.N. Cytoplasmic induction and over-expression of cyclooxygenase-2 in human prostate cancer: implications for prevention and treatment. BJU Int. 86 (2000) 736-741
    • (2000) BJU Int. , vol.86 , pp. 736-741
    • Madaan, S.1    Abel, P.D.2    Chaudhary, K.S.3    Hewitt, R.4    Stott, M.A.5    Stamp, G.W.6    Lalani, E.N.7
  • 46
    • 0035893745 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is up-regulated in proliferative inflammatory atrophy of the prostate, but not in prostate carcinoma
    • Zha S., Gage W.R., Sauvageot J., Saria E.A., Putzi M.J., and Ewing C.M. Cyclooxygenase-2 is up-regulated in proliferative inflammatory atrophy of the prostate, but not in prostate carcinoma. Cancer Res. 61 (2001) 8617-8623
    • (2001) Cancer Res. , vol.61 , pp. 8617-8623
    • Zha, S.1    Gage, W.R.2    Sauvageot, J.3    Saria, E.A.4    Putzi, M.J.5    Ewing, C.M.6
  • 47
    • 0034646688 scopus 로고    scopus 로고
    • The cyclooxygenase-2 inhibitor celecoxib induces apoptosis by blocking Akt activation in human prostate cancer cells independently of Bcl-2
    • Hsu A.L., Ching T.T., Wang D.S., Song X., Rangnekar V.M., and Chen C.S. The cyclooxygenase-2 inhibitor celecoxib induces apoptosis by blocking Akt activation in human prostate cancer cells independently of Bcl-2. J. Biol. Chem. 275 (2000) 11397-11403
    • (2000) J. Biol. Chem. , vol.275 , pp. 11397-11403
    • Hsu, A.L.1    Ching, T.T.2    Wang, D.S.3    Song, X.4    Rangnekar, V.M.5    Chen, C.S.6
  • 49
    • 0032573175 scopus 로고    scopus 로고
    • Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells
    • Ghosh J., and Myers C.E. Inhibition of arachidonate 5-lipoxygenase triggers massive apoptosis in human prostate cancer cells. Proc. Natl. Acad. Sci. USA 95 (1998) 13182-13187
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13182-13187
    • Ghosh, J.1    Myers, C.E.2
  • 50
    • 0022623468 scopus 로고
    • Prostaglandin modulation of prostate tumor growth and metastases
    • Ablin R.J., and Shaw M.W. Prostaglandin modulation of prostate tumor growth and metastases. Anticancer Res. 6 (1986) 327-328
    • (1986) Anticancer Res. , vol.6 , pp. 327-328
    • Ablin, R.J.1    Shaw, M.W.2
  • 51
    • 0025871331 scopus 로고
    • Effects of fatty acids and eicosanoid synthesis inhibitors on the growth of two human prostate cancer cell lines
    • Rose D.P., and Connolly J.M. Effects of fatty acids and eicosanoid synthesis inhibitors on the growth of two human prostate cancer cell lines. Prostate 18 (1991) 243-254
    • (1991) Prostate , vol.18 , pp. 243-254
    • Rose, D.P.1    Connolly, J.M.2
  • 52
    • 0027959058 scopus 로고
    • 12(S)-HETE enhancement of prostate tumor cell invasion - selective role of PKC-alpha
    • Liu B., Maher R.J., Hannun Y.A., Porter A.T., and Honn K.V. 12(S)-HETE enhancement of prostate tumor cell invasion - selective role of PKC-alpha. J. Natl. Cancer. Inst. 86 (1994) 1145-1151
    • (1994) J. Natl. Cancer. Inst. , vol.86 , pp. 1145-1151
    • Liu, B.1    Maher, R.J.2    Hannun, Y.A.3    Porter, A.T.4    Honn, K.V.5
  • 53
    • 0027978551 scopus 로고
    • Recombinant human uteroglobin inhibits the in vitro invasiveness of human metastatic prostate tumor cells and the release of arachidonic acid stimulated by fibroblast-conditioned medium
    • Leyton J., Manyak M.J., Mukherjee A.B., Miele L., Mantile G., and Patierno S.R. Recombinant human uteroglobin inhibits the in vitro invasiveness of human metastatic prostate tumor cells and the release of arachidonic acid stimulated by fibroblast-conditioned medium. Cancer Res. 54 (1994) 3696-3699
    • (1994) Cancer Res. , vol.54 , pp. 3696-3699
    • Leyton, J.1    Manyak, M.J.2    Mukherjee, A.B.3    Miele, L.4    Mantile, G.5    Patierno, S.R.6
  • 54
    • 16344389993 scopus 로고    scopus 로고
    • Celecoxib inhibits prostate cancer growth: evidence of a cyclooxygenase-2-independent mechanism
    • Patel M.I., Subbaramaiah K., Du B., Chang M., Yang P., Newman R.A., et al. Celecoxib inhibits prostate cancer growth: evidence of a cyclooxygenase-2-independent mechanism. Clin. Cancer Res. 11 (2005) 1999-2007
    • (2005) Clin. Cancer Res. , vol.11 , pp. 1999-2007
    • Patel, M.I.1    Subbaramaiah, K.2    Du, B.3    Chang, M.4    Yang, P.5    Newman, R.A.6
  • 55
    • 0034739464 scopus 로고    scopus 로고
    • Nevalainen T.J., Haapamaki M.M., Gronroos J.M., Roles of secretory phospholipases A(2) in inflammatory diseases and trauma [Review], Biochimica et Biophysica Acta Molecular & Cell Biology of Lipids 1488 (2000) 83-90.
  • 56
    • 0036110406 scopus 로고    scopus 로고
    • Huhtinen H.T., Gronroos J.M., Haapamaki M.M., Nevalainen T.J., Source of group II phospholipase A(2) in gastric juice. Roles of secretory phospholipases A(2) in inflammatory diseases and trauma [Review], Scandinavian Journal of Clinical & Laboratory Investigation 62 (2002) 123-128..
  • 57
    • 0032101889 scopus 로고    scopus 로고
    • Group II phospholipase A2 in human male reproductive organs and genital tumors
    • Kallajoki M., Alanen K.A., Nevalainen M., and Nevalainen T.J. Group II phospholipase A2 in human male reproductive organs and genital tumors. Prostate 35 (1998) 263-272
    • (1998) Prostate , vol.35 , pp. 263-272
    • Kallajoki, M.1    Alanen, K.A.2    Nevalainen, M.3    Nevalainen, T.J.4
  • 59
    • 0036171520 scopus 로고    scopus 로고
    • Expression of group IIA secretory phospholipase A2 is elevated in prostatic intraepithelial neoplasia and adenocarcinoma
    • Jiang J.Z., Neubauer B.L., Graff J.R., Chedid M., Thomas J.E., and Roehm N.W. Expression of group IIA secretory phospholipase A2 is elevated in prostatic intraepithelial neoplasia and adenocarcinoma. Am. J. Pathol. 160 (2002) 667-671
    • (2002) Am. J. Pathol. , vol.160 , pp. 667-671
    • Jiang, J.Z.1    Neubauer, B.L.2    Graff, J.R.3    Chedid, M.4    Thomas, J.E.5    Roehm, N.W.6
  • 60
    • 4944224570 scopus 로고    scopus 로고
    • Oncogenic action of secreted phospholipase A2 in prostate cancer
    • Sved P., Scott K.F., McLeod D., King N., Singh J., Tsatralis T., et al. Oncogenic action of secreted phospholipase A2 in prostate cancer. Cancer Res. 64 (2004) 6934-6940
    • (2004) Cancer Res. , vol.64 , pp. 6934-6940
    • Sved, P.1    Scott, K.F.2    McLeod, D.3    King, N.4    Singh, J.5    Tsatralis, T.6
  • 61
    • 0033178693 scopus 로고    scopus 로고
    • Regulation of type V phospholipase A2 expression and function by proinflammatory stimuli
    • Sawada H., Murakami M., Enomoto A., Shimbara S., and Kudo I. Regulation of type V phospholipase A2 expression and function by proinflammatory stimuli. Eur. J. Biochem. 263 (1999) 826-835
    • (1999) Eur. J. Biochem. , vol.263 , pp. 826-835
    • Sawada, H.1    Murakami, M.2    Enomoto, A.3    Shimbara, S.4    Kudo, I.5


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