메뉴 건너뛰기




Volumn 34, Issue 5, 2010, Pages 538-545

Identification and functional characterization of a human sTRAIL homolog, CasTRAIL, in an invertebrate oyster Crassostrea ariakensis

Author keywords

Anti RLO immune; CasTRAIL; Oyster Crassostrea ariakensis; Tumor necrosis factor related apoptosis inducing ligand (TRAIL)

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; MEMBRANE PROTEIN;

EID: 77953398614     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2009.12.014     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 0034255259 scopus 로고    scopus 로고
    • B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1
    • Shu H.B., Johnson H. B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1. Proc Natl Acad Sci USA 2000, 97:9156-9161.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9156-9161
    • Shu, H.B.1    Johnson, H.2
  • 2
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti R.M., Marsters S.A., Ruppert S., Donahue C.J., Moore A., Ashkenazi A. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem 1996, 271:12687-12690.
    • (1996) J Biol Chem , vol.271 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3    Donahue, C.J.4    Moore, A.5    Ashkenazi, A.6
  • 3
    • 0029310492 scopus 로고
    • The TNF ligand superfamily and its relevance for human diseases
    • Gruss H.J., Dower S.K. The TNF ligand superfamily and its relevance for human diseases. Cytokines Mol Ther 1995, 1:75-105.
    • (1995) Cytokines Mol Ther , vol.1 , pp. 75-105
    • Gruss, H.J.1    Dower, S.K.2
  • 4
    • 0034037333 scopus 로고    scopus 로고
    • Apoptosis induced by death receptors
    • Schneider P., Tschopp J. Apoptosis induced by death receptors. Pharm Acta Helv 2000, 74:281-286.
    • (2000) Pharm Acta Helv , vol.74 , pp. 281-286
    • Schneider, P.1    Tschopp, J.2
  • 5
    • 0030943324 scopus 로고    scopus 로고
    • Interleukin 1 beta-converting enzyme related proteases/caspases are involved in TRAIL-induced apoptosis of myeloma and leukemia cells
    • Mariani S.M., Matiba B., Armandola E.A., Krammer P.H. Interleukin 1 beta-converting enzyme related proteases/caspases are involved in TRAIL-induced apoptosis of myeloma and leukemia cells. J Cell Biol 1997, 137:221-229.
    • (1997) J Cell Biol , vol.137 , pp. 221-229
    • Mariani, S.M.1    Matiba, B.2    Armandola, E.A.3    Krammer, P.H.4
  • 6
    • 43349084615 scopus 로고    scopus 로고
    • TNF-related apoptosis-inducing ligand (TRAIL) is expressed throughout myeloid development, resulting in a broad distribution among neutrophil granules
    • Simons M.P., Leidal K.G., Nauseef W.M., Griffith T.S. TNF-related apoptosis-inducing ligand (TRAIL) is expressed throughout myeloid development, resulting in a broad distribution among neutrophil granules. J Leukoc Biol 2008, 83(3):621-629.
    • (2008) J Leukoc Biol , vol.83 , Issue.3 , pp. 621-629
    • Simons, M.P.1    Leidal, K.G.2    Nauseef, W.M.3    Griffith, T.S.4
  • 7
    • 0346792725 scopus 로고    scopus 로고
    • TRAIL and apoptosis induction by TNF-family death receptors
    • Wang S., El-Deiry W.S. TRAIL and apoptosis induction by TNF-family death receptors. Oncogene 2003, 22:8628-8633.
    • (2003) Oncogene , vol.22 , pp. 8628-8633
    • Wang, S.1    El-Deiry, W.S.2
  • 8
    • 3142735020 scopus 로고    scopus 로고
    • Apo2 ligand/tumor necrosis factor-related apoptosis-inducing ligand cooperates with chemotherapy to inhibit orthotopic lung tumor growth and improve survival
    • Jin H., Yang R., Fong S., Totpal K., Lawrence D., Zheng Z., et al. Apo2 ligand/tumor necrosis factor-related apoptosis-inducing ligand cooperates with chemotherapy to inhibit orthotopic lung tumor growth and improve survival. Cancer Res 2004, 64:4900-4905.
    • (2004) Cancer Res , vol.64 , pp. 4900-4905
    • Jin, H.1    Yang, R.2    Fong, S.3    Totpal, K.4    Lawrence, D.5    Zheng, Z.6
  • 9
    • 30344462991 scopus 로고    scopus 로고
    • Interferon-alfa enhances TRAIL-mediated apoptosis by up-regulating caspase-8 transcription in human hepatoma cells
    • Liedtke C., Gröger N., Manns M.P., Trautwein C. Interferon-alfa enhances TRAIL-mediated apoptosis by up-regulating caspase-8 transcription in human hepatoma cells. J Hepatol 2006, 44:342-349.
    • (2006) J Hepatol , vol.44 , pp. 342-349
    • Liedtke, C.1    Gröger, N.2    Manns, M.P.3    Trautwein, C.4
  • 10
    • 0034061453 scopus 로고    scopus 로고
    • Lipopolysaccharide induces expression of Apo2 ligand/TRAIL in human monocytes and macrophages
    • Halaas O., Vik R., Ashkenazi A., Espevik T. Lipopolysaccharide induces expression of Apo2 ligand/TRAIL in human monocytes and macrophages. Scand J Immunol 2000, 51:244-250.
    • (2000) Scand J Immunol , vol.51 , pp. 244-250
    • Halaas, O.1    Vik, R.2    Ashkenazi, A.3    Espevik, T.4
  • 11
    • 35348880300 scopus 로고    scopus 로고
    • Neutrophils and TRAIL: insights into BCG immunotherapy for bladder cancer
    • Simons M.P., Nauseef W.M., Griffith T.S. Neutrophils and TRAIL: insights into BCG immunotherapy for bladder cancer. Immunol Res 2007, 39:79-93.
    • (2007) Immunol Res , vol.39 , pp. 79-93
    • Simons, M.P.1    Nauseef, W.M.2    Griffith, T.S.3
  • 12
    • 70449491806 scopus 로고    scopus 로고
    • The emerging role of TRAIL as key regulator of inflammatory responses
    • Collison A., Foster P.S., Mattes J. The emerging role of TRAIL as key regulator of inflammatory responses. Clin Exp Pharmacol Physiol 2009, 36:1049-1053.
    • (2009) Clin Exp Pharmacol Physiol , vol.36 , pp. 1049-1053
    • Collison, A.1    Foster, P.S.2    Mattes, J.3
  • 13
    • 34447132223 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) pathway signaling
    • Thorburn A. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) pathway signaling. J Thoracic Oncol 2007, 2:461-465.
    • (2007) J Thoracic Oncol , vol.2 , pp. 461-465
    • Thorburn, A.1
  • 14
    • 32044447468 scopus 로고    scopus 로고
    • Characterization and expression analysis of TNF-related apoptosis inducing ligand (TRAIL) in grass carp Ctenopharyngodon idella
    • Chang M.X., Nie P., Xie H.X., Wang G.L., Gao Y. Characterization and expression analysis of TNF-related apoptosis inducing ligand (TRAIL) in grass carp Ctenopharyngodon idella. Vet Immunol Immunopathol 2006, 110:51-63.
    • (2006) Vet Immunol Immunopathol , vol.110 , pp. 51-63
    • Chang, M.X.1    Nie, P.2    Xie, H.X.3    Wang, G.L.4    Gao, Y.5
  • 15
    • 38349131974 scopus 로고    scopus 로고
    • TRAIL in the mandarin fish Siniperca chuatsi: gene and its apoptotic effect in HeLa cells
    • Gao Y., Chang M.X., Sun B.J., Nie P. TRAIL in the mandarin fish Siniperca chuatsi: gene and its apoptotic effect in HeLa cells. Fish Shellfish Immunol 2008, 24:55-66.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 55-66
    • Gao, Y.1    Chang, M.X.2    Sun, B.J.3    Nie, P.4
  • 16
    • 0037124314 scopus 로고    scopus 로고
    • Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway
    • Igaki T., Kanda H., Yamamoto-Goto Y., Kanuka H., Kuranaga E., Aigaki T., et al. Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway. EMBO J 2002, 21:3009-3018.
    • (2002) EMBO J , vol.21 , pp. 3009-3018
    • Igaki, T.1    Kanda, H.2    Yamamoto-Goto, Y.3    Kanuka, H.4    Kuranaga, E.5    Aigaki, T.6
  • 17
    • 0042066408 scopus 로고    scopus 로고
    • Eiger and its receptor, Wengen, comprise a TNF-like system in Drosophila
    • Kauppila S., Maaty W.S.A., Chen P., Tomar R.S., Eby M.T., Chapo J., et al. Eiger and its receptor, Wengen, comprise a TNF-like system in Drosophila. Oncogene 2003, 22:4860-4867.
    • (2003) Oncogene , vol.22 , pp. 4860-4867
    • Kauppila, S.1    Maaty, W.S.A.2    Chen, P.3    Tomar, R.S.4    Eby, M.T.5    Chapo, J.6
  • 20
    • 46149091038 scopus 로고    scopus 로고
    • A novel tumor necrosis factor ligand superfamily member (CsTL) from Ciona savignyi: molecular identification and expression analysis
    • Zhang X., Luan W., Jin S., Xiang J. A novel tumor necrosis factor ligand superfamily member (CsTL) from Ciona savignyi: molecular identification and expression analysis. Dev Comp Immunol 2008, 32:1362-1373.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1362-1373
    • Zhang, X.1    Luan, W.2    Jin, S.3    Xiang, J.4
  • 21
    • 64749107745 scopus 로고    scopus 로고
    • First molluscan TNF-alpha homologue of the TNF superfamily in disk abalone: molecular characterization and expression analysis
    • De Zoysa M., Jung S., Lee J. First molluscan TNF-alpha homologue of the TNF superfamily in disk abalone: molecular characterization and expression analysis. Fish Shellfish Immunol 2009, 32:625-631.
    • (2009) Fish Shellfish Immunol , vol.32 , pp. 625-631
    • De Zoysa, M.1    Jung, S.2    Lee, J.3
  • 22
    • 68649099889 scopus 로고    scopus 로고
    • A novel Fas ligand in mollusk abalone: molecular characterization, immune responses and biological activity of the recombinant protein
    • De Zoysa M., Nikapitiya C., Moon D.O., Whang I., Kim G.Y., Lee J. A novel Fas ligand in mollusk abalone: molecular characterization, immune responses and biological activity of the recombinant protein. Fish Shellfish Immunol 2009, 27:423-432.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 423-432
    • De Zoysa, M.1    Nikapitiya, C.2    Moon, D.O.3    Whang, I.4    Kim, G.Y.5    Lee, J.6
  • 23
    • 34248215727 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative lipopolysaccharide-induced TNFα factor (LITAF) gene homologue from Zhikong scallop Chlamys farreri
    • Yu Y.D., Qiu L.M., Song L.S., Zhao J.M., Ni D.J., Zhang Y., et al. Molecular cloning and characterization of a putative lipopolysaccharide-induced TNFα factor (LITAF) gene homologue from Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 2007, 23:419-429.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 419-429
    • Yu, Y.D.1    Qiu, L.M.2    Song, L.S.3    Zhao, J.M.4    Ni, D.J.5    Zhang, Y.6
  • 24
    • 38349095852 scopus 로고    scopus 로고
    • Cloning, characterization and expression analysis of the gene for putative lipopolysaccharide-induced TNF-a factor of the Pacific oyster, Crassostrea gigas
    • Park E.M., Kim Y.O., Nam B.H., Kong H.J., Kim W.J., Lee S.J., et al. Cloning, characterization and expression analysis of the gene for putative lipopolysaccharide-induced TNF-a factor of the Pacific oyster, Crassostrea gigas. Fish Shellfish Immunol 2008, 24:11-17.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 11-17
    • Park, E.M.1    Kim, Y.O.2    Nam, B.H.3    Kong, H.J.4    Kim, W.J.5    Lee, S.J.6
  • 25
    • 68949147766 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of a putative LPS-induced TNF-alpha factor (LITAF) from pearl oyster Pinctada fucata
    • Zhang D., Jiang J., Jiang S., Ma J., Su T., Qiu L., et al. Molecular characterization and expression analysis of a putative LPS-induced TNF-alpha factor (LITAF) from pearl oyster Pinctada fucata. Fish Shellfish Immunol 2009, 27:391-396.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 391-396
    • Zhang, D.1    Jiang, J.2    Jiang, S.3    Ma, J.4    Su, T.5    Qiu, L.6
  • 26
    • 0034496824 scopus 로고    scopus 로고
    • A Piscirickettsia salmonis-like organism in grouper, Epinephelus melanostigma, in Taiwan
    • Chen S.C., Wang P.C., Tung M.C., Thompson K., Adams A. A Piscirickettsia salmonis-like organism in grouper, Epinephelus melanostigma, in Taiwan. J Fish Dis 2000, 23:415-418.
    • (2000) J Fish Dis , vol.23 , pp. 415-418
    • Chen, S.C.1    Wang, P.C.2    Tung, M.C.3    Thompson, K.4    Adams, A.5
  • 27
    • 0016139551 scopus 로고
    • Rickettsia-like organism causing disease in a crangonid amphipod from Florida
    • Federici B.A., Hazard E.I., Anthony D.W. Rickettsia-like organism causing disease in a crangonid amphipod from Florida. Appl Microbiol 1974, 28:885-886.
    • (1974) Appl Microbiol , vol.28 , pp. 885-886
    • Federici, B.A.1    Hazard, E.I.2    Anthony, D.W.3
  • 28
    • 0006487623 scopus 로고    scopus 로고
    • Studies on rickettsia-like organism disease of the tropical marine pearl oyster. I. The fine structure and morphogenesis of Pinctada maxima pathogen rickettsia-like organism
    • Wu X.Z., Pan J.P. Studies on rickettsia-like organism disease of the tropical marine pearl oyster. I. The fine structure and morphogenesis of Pinctada maxima pathogen rickettsia-like organism. J Invertebr Pathol 1999, 73:162-172.
    • (1999) J Invertebr Pathol , vol.73 , pp. 162-172
    • Wu, X.Z.1    Pan, J.P.2
  • 29
    • 3242660004 scopus 로고    scopus 로고
    • Histology, ultrastructure and morphogenesis of a rickettsia-like organism causing disease in the oyster, Crassostrea ariakensis Gould
    • Sun J.F., Wu X.Z. Histology, ultrastructure and morphogenesis of a rickettsia-like organism causing disease in the oyster, Crassostrea ariakensis Gould. J Invertebr Pathol 2004, 86:77-86.
    • (2004) J Invertebr Pathol , vol.86 , pp. 77-86
    • Sun, J.F.1    Wu, X.Z.2
  • 30
    • 49649126823 scopus 로고    scopus 로고
    • Characterization and function of CREB homologue from Crassostrea ariakensis stimulated by rickettsia-like organism
    • Zhu B.J., Wu X.Z. Characterization and function of CREB homologue from Crassostrea ariakensis stimulated by rickettsia-like organism. Dev Comp Immunol 2008, 32:1572-1581.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1572-1581
    • Zhu, B.J.1    Wu, X.Z.2
  • 31
    • 67650442054 scopus 로고    scopus 로고
    • Tolliod-like gene in Crassostrea ariakensis: molecular cloning, structural characterization and expression by RLO stimulation
    • Yang S., Wu X. Tolliod-like gene in Crassostrea ariakensis: molecular cloning, structural characterization and expression by RLO stimulation. Fish Shellfish Immunol 2009, 27:130-135.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 130-135
    • Yang, S.1    Wu, X.2
  • 32
    • 43449128830 scopus 로고    scopus 로고
    • Identification of outer membrane protein ompR from rickettsia-like organism and induction of immune response in Crassostrea ariakensis
    • Zhu B.J., Wu X.Z. Identification of outer membrane protein ompR from rickettsia-like organism and induction of immune response in Crassostrea ariakensis. Mol Immunol 2008, 45:3198-3204.
    • (2008) Mol Immunol , vol.45 , pp. 3198-3204
    • Zhu, B.J.1    Wu, X.Z.2
  • 33
    • 28944438403 scopus 로고    scopus 로고
    • Purification and antigenic characteristics of a rickettsia-like organism from the oyster Crassostrea ariakensis
    • Wu X., Sun J., Zhang W., Wen B. Purification and antigenic characteristics of a rickettsia-like organism from the oyster Crassostrea ariakensis. Dis Aquat Organ 2005, 67:149-154.
    • (2005) Dis Aquat Organ , vol.67 , pp. 149-154
    • Wu, X.1    Sun, J.2    Zhang, W.3    Wen, B.4
  • 34
    • 3142765578 scopus 로고    scopus 로고
    • Expression of gonadotropin-releasing hormone receptor and effect of gonadotropin-releasing hormone analogue on proliferation of cultured gastric smooth muscle cells of rats
    • Chen L., He H.X., Sun X.D., Zhao J., Liu L.H., Huang W.Q., et al. Expression of gonadotropin-releasing hormone receptor and effect of gonadotropin-releasing hormone analogue on proliferation of cultured gastric smooth muscle cells of rats. World J Gastroenterol 2004, 10:1780-1784.
    • (2004) World J Gastroenterol , vol.10 , pp. 1780-1784
    • Chen, L.1    He, H.X.2    Sun, X.D.3    Zhao, J.4    Liu, L.H.5    Huang, W.Q.6
  • 36
    • 0037084394 scopus 로고    scopus 로고
    • P35-sensitive caspases, MAP kinases and Rho modulate beta-adrenergic induction of apoptosis in mollusc immune cells
    • Lacoste A., Cueff A., Poulet S.A. P35-sensitive caspases, MAP kinases and Rho modulate beta-adrenergic induction of apoptosis in mollusc immune cells. J Cell Sci 2002, 115:761-768.
    • (2002) J Cell Sci , vol.115 , pp. 761-768
    • Lacoste, A.1    Cueff, A.2    Poulet, S.A.3
  • 37
    • 0037097751 scopus 로고    scopus 로고
    • Bacteria-hemocyte interactions and phagocytosis in marine bivalves
    • Canesi L., Gallo G., Gavioli M., Pruzzo C. Bacteria-hemocyte interactions and phagocytosis in marine bivalves. Microsc Res Tech 2002, 57:469-476.
    • (2002) Microsc Res Tech , vol.57 , pp. 469-476
    • Canesi, L.1    Gallo, G.2    Gavioli, M.3    Pruzzo, C.4
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 0034617304 scopus 로고    scopus 로고
    • Cysteine 230 is essential for the structure and activity of the cytotoxic ligand TRAIL
    • Bodmer J.L., Meier P., Tschopp J., Schneider P. Cysteine 230 is essential for the structure and activity of the cytotoxic ligand TRAIL. J Biol Chem 2000, 275:20632-20637.
    • (2000) J Biol Chem , vol.275 , pp. 20632-20637
    • Bodmer, J.L.1    Meier, P.2    Tschopp, J.3    Schneider, P.4
  • 40
    • 2942647708 scopus 로고
    • Higher Education Press, Beijing, China
    • Jiang J. Invertebrate zoology 1982, Higher Education Press, Beijing, China.
    • (1982) Invertebrate zoology
    • Jiang, J.1
  • 41
    • 0035844129 scopus 로고    scopus 로고
    • MAPK/ERK overrides the apoptotic signaling from Fas, TNF, and TRAIL receptors
    • Tran S.E., Holmstrom T.H., Ahonen M., Kahari V.M., Eriksson J.E. MAPK/ERK overrides the apoptotic signaling from Fas, TNF, and TRAIL receptors. J Biol Chem 2001, 276:16484-16490.
    • (2001) J Biol Chem , vol.276 , pp. 16484-16490
    • Tran, S.E.1    Holmstrom, T.H.2    Ahonen, M.3    Kahari, V.M.4    Eriksson, J.E.5
  • 42
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeaud J., Davis R.J., Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 1995, 270:1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 43
    • 41449095631 scopus 로고    scopus 로고
    • Requirement of caspases and p38 MAPK for TRAIL-mediated ICAM-1 expression by human astroglial cells
    • Choi K., Song S., Choi C. Requirement of caspases and p38 MAPK for TRAIL-mediated ICAM-1 expression by human astroglial cells. Immunol Lett 2008, 117:168-173.
    • (2008) Immunol Lett , vol.117 , pp. 168-173
    • Choi, K.1    Song, S.2    Choi, C.3
  • 44
    • 0347364696 scopus 로고    scopus 로고
    • NK cell TRAIL eliminates immature dendritic cells in vivo and limits dendritic cell vaccination efficacy
    • Hayakawa Y., Screpanti V., Yagita H., Grandien A., Ljunggren H.G., Smyth M.J., et al. NK cell TRAIL eliminates immature dendritic cells in vivo and limits dendritic cell vaccination efficacy. J Immunol 2004, 172:123-129.
    • (2004) J Immunol , vol.172 , pp. 123-129
    • Hayakawa, Y.1    Screpanti, V.2    Yagita, H.3    Grandien, A.4    Ljunggren, H.G.5    Smyth, M.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.