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Volumn 47, Issue 2, 2015, Pages 645-654

Molecular cloning, immunohistochemical localization, characterization and expression analysis of caspase-8 from the blunt snout bream (Megalobrama amblycephala) exposed to ammonia

Author keywords

Ammonia; Apoptosis; Caspase 8; Megalobrama amblycephala; Oxidative stress

Indexed keywords

AMMONIA; CASPASE 8; COMPLEMENTARY DNA; FISH PROTEIN; MESSENGER RNA; WATER POLLUTANT;

EID: 84945538602     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2015.10.016     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 27744477444 scopus 로고    scopus 로고
    • Mammalian initiator apoptotic caspases
    • Ho P.K., Hawkins C.J. Mammalian initiator apoptotic caspases. FEBS J. 2005, 272:5436-5453.
    • (2005) FEBS J. , vol.272 , pp. 5436-5453
    • Ho, P.K.1    Hawkins, C.J.2
  • 2
    • 54849407552 scopus 로고    scopus 로고
    • Characterisation of cDNAs of key genes involved in apoptosis in common carp (Cyprinus carpio L.)
    • Vidal M.C., Hoole D., Williams G.T. Characterisation of cDNAs of key genes involved in apoptosis in common carp (Cyprinus carpio L.). Fish Shellfish Immunol. 2008, 25:494-507.
    • (2008) Fish Shellfish Immunol. , vol.25 , pp. 494-507
    • Vidal, M.C.1    Hoole, D.2    Williams, G.T.3
  • 3
    • 84861652703 scopus 로고    scopus 로고
    • The central role of initiator caspase-9 in apoptosis signal transduction and the regulation of its activation and activity on the apoptosome
    • Wuerstle M.L., Laussmann M.A., Rehm M. The central role of initiator caspase-9 in apoptosis signal transduction and the regulation of its activation and activity on the apoptosome. Exp. Cell Res. 2012, 318:1213-1220.
    • (2012) Exp. Cell Res. , vol.318 , pp. 1213-1220
    • Wuerstle, M.L.1    Laussmann, M.A.2    Rehm, M.3
  • 4
    • 0042318707 scopus 로고    scopus 로고
    • Apoptosis e an introduction
    • Lawen A. Apoptosis e an introduction. Bioessays 2003, 25:888-896.
    • (2003) Bioessays , vol.25 , pp. 888-896
    • Lawen, A.1
  • 5
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998, 94:481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 6
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6
  • 7
    • 55949128738 scopus 로고    scopus 로고
    • Non-apoptotic functions of caspase-8
    • Maelfait J., Beyaert R. Non-apoptotic functions of caspase-8. Biochem. Pharmacol. 2008, 76:1365-1373.
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1365-1373
    • Maelfait, J.1    Beyaert, R.2
  • 8
    • 33748785440 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene
    • Reis M.I.R., Nascimento D.S., do Vale A., Silva M.T., dos Santos N.M.S. Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene. Mol. Immunol. 2006, 44:774-783.
    • (2006) Mol. Immunol. , vol.44 , pp. 774-783
    • Reis, M.I.R.1    Nascimento, D.S.2    do Vale, A.3    Silva, M.T.4    dos Santos, N.M.S.5
  • 9
    • 84884125631 scopus 로고    scopus 로고
    • Cadmium triggers kidney cell apoptosis of purse red common carp (Cyprinus carpio) without caspase-8 activation
    • Gao D., Xu Z., Zhang X.Y., Zhu C.C., Wang Y.N., Min W.P. Cadmium triggers kidney cell apoptosis of purse red common carp (Cyprinus carpio) without caspase-8 activation. Dev. Comp. Immunol. 2013, 41:728-737.
    • (2013) Dev. Comp. Immunol. , vol.41 , pp. 728-737
    • Gao, D.1    Xu, Z.2    Zhang, X.Y.3    Zhu, C.C.4    Wang, Y.N.5    Min, W.P.6
  • 10
    • 84928391426 scopus 로고    scopus 로고
    • Effects of ammonia exposure on apoptosis, oxidative stress andimmune response in pufferfish (Takifugu obscurus)
    • Cheng C.H., Yang F.F., Ling R.Z., Liao S.A., Miao Y.T., Ye C.X., Wang A.L. Effects of ammonia exposure on apoptosis, oxidative stress andimmune response in pufferfish (Takifugu obscurus). Aquat. Toxicol. 2015, 164:61-71.
    • (2015) Aquat. Toxicol. , vol.164 , pp. 61-71
    • Cheng, C.H.1    Yang, F.F.2    Ling, R.Z.3    Liao, S.A.4    Miao, Y.T.5    Ye, C.X.6    Wang, A.L.7
  • 12
    • 33845582464 scopus 로고    scopus 로고
    • Ammonia in estuaries and effect on fish
    • Eddy F.B. Ammonia in estuaries and effect on fish. J. Fish Biol. 2005, 67:1495-1513.
    • (2005) J. Fish Biol. , vol.67 , pp. 1495-1513
    • Eddy, F.B.1
  • 13
    • 46149083696 scopus 로고    scopus 로고
    • Sublethal ammonia exposure of Nile tilapia (Oreochromis niloticus L.): effects on gill liver and kidney histology
    • Benli A.C.K., Köksal G., Özkul A. Sublethal ammonia exposure of Nile tilapia (Oreochromis niloticus L.): effects on gill liver and kidney histology. Chemosphere 2008, 72:1355-1358.
    • (2008) Chemosphere , vol.72 , pp. 1355-1358
    • Benli, A.C.K.1    Köksal, G.2    Özkul, A.3
  • 14
    • 84897484196 scopus 로고    scopus 로고
    • Effects of ammoniastress, dietary linseed oil and Edwardsiella ictaluri challenge on juveniledarkbarbel catfish Pelteobagrus vachelli
    • Li M., Yu N., Qin J.G., Li E., Du Z.Y., Chen L.Q. Effects of ammoniastress, dietary linseed oil and Edwardsiella ictaluri challenge on juveniledarkbarbel catfish Pelteobagrus vachelli. Fish Shellfish Immunol. 2014, 38:158-165.
    • (2014) Fish Shellfish Immunol. , vol.38 , pp. 158-165
    • Li, M.1    Yu, N.2    Qin, J.G.3    Li, E.4    Du, Z.Y.5    Chen, L.Q.6
  • 15
    • 0035888288 scopus 로고    scopus 로고
    • Ammonia-induced production of free radicals in primary cultures of rat astrocytes
    • Murthy C.R.K., Rama Rao K.V., Bai G., Norenberg M.D. Ammonia-induced production of free radicals in primary cultures of rat astrocytes. J. Neurosci. Res. 2001, 66:282-288.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 282-288
    • Murthy, C.R.K.1    Rama Rao, K.V.2    Bai, G.3    Norenberg, M.D.4
  • 18
    • 77955057057 scopus 로고    scopus 로고
    • Molecular cloning of sea bass (Dicentrarchus labrax L.) caspase-8 gene and its involvement in Photobacterium damselae ssp. piscicida triggered apoptosis
    • Reis M.I.R., Costa-Ramos C., do Vale A., dos Santos N.M.S. Molecular cloning of sea bass (Dicentrarchus labrax L.) caspase-8 gene and its involvement in Photobacterium damselae ssp. piscicida triggered apoptosis. Fish Shellfish Immunol. 2010, 29:58-65.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 58-65
    • Reis, M.I.R.1    Costa-Ramos, C.2    do Vale, A.3    dos Santos, N.M.S.4
  • 19
    • 84891151306 scopus 로고    scopus 로고
    • Pathological observation of bacterial septicemia in Megalobrama amblycephala
    • (in chinese)
    • He L.J., Liao L.K., Yuan J.F., Tang H.Y., Wu Q., Zhang G.W. Pathological observation of bacterial septicemia in Megalobrama amblycephala. J. Southwest Univ. 2006, 3:483-490. (in chinese).
    • (2006) J. Southwest Univ. , vol.3 , pp. 483-490
    • He, L.J.1    Liao, L.K.2    Yuan, J.F.3    Tang, H.Y.4    Wu, Q.5    Zhang, G.W.6
  • 20
    • 84945562642 scopus 로고    scopus 로고
    • Acute effects of ammonia exposure on histopathology of gill, liver and kidney in juvenile Megalobrama amblycephala and the post-exposure recovery
    • (In Chinese)
    • Zhang W.X., Sun S.M., Ge X.P., Zhu J., Li B., Miao L.H., Xia S.L., Zhang Q., Jiang X.J. Acute effects of ammonia exposure on histopathology of gill, liver and kidney in juvenile Megalobrama amblycephala and the post-exposure recovery. J. Fish. China 2014, 38:228-236. (In Chinese).
    • (2014) J. Fish. China , vol.38 , pp. 228-236
    • Zhang, W.X.1    Sun, S.M.2    Ge, X.P.3    Zhu, J.4    Li, B.5    Miao, L.H.6    Xia, S.L.7    Zhang, Q.8    Jiang, X.J.9
  • 21
    • 77955551022 scopus 로고    scopus 로고
    • Oxidative stress and antioxidantenzymes in liver and white muscle of Nile tilapia juveniles in chronic ammonia exposure
    • Hegazi M.M., Attia Z.I., Ashour O.A. Oxidative stress and antioxidantenzymes in liver and white muscle of Nile tilapia juveniles in chronic ammonia exposure. Aquat. Toxicol. 2010, 99:118-125.
    • (2010) Aquat. Toxicol. , vol.99 , pp. 118-125
    • Hegazi, M.M.1    Attia, Z.I.2    Ashour, O.A.3
  • 22
    • 84864697201 scopus 로고    scopus 로고
    • Transcriptome analysis and SSR/SNP markers information of the blunt snout bream (Megalobrama amblycephala)
    • Gao Z., Luo W., Liu H., Zeng C., Liu X., Yi S.K., et al. Transcriptome analysis and SSR/SNP markers information of the blunt snout bream (Megalobrama amblycephala). PLoS One 2012, 7:e42637.
    • (2012) PLoS One , vol.7 , pp. e42637
    • Gao, Z.1    Luo, W.2    Liu, H.3    Zeng, C.4    Liu, X.5    Yi, S.K.6
  • 23
    • 84887075420 scopus 로고    scopus 로고
    • Nitrite-induced hepatotoxicity in bluntsnout bream (Megalobrama amblycephala): the mechanistic insight from transcriptome to physiology analysis
    • Sun S., Ge X., Xuan F., Zhu J., Nu N. Nitrite-induced hepatotoxicity in bluntsnout bream (Megalobrama amblycephala): the mechanistic insight from transcriptome to physiology analysis. Environ. Toxicol. Pharmacol. 2014, 159:69-77.
    • (2014) Environ. Toxicol. Pharmacol. , vol.159 , pp. 69-77
    • Sun, S.1    Ge, X.2    Xuan, F.3    Zhu, J.4    Nu, N.5
  • 26
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel F.C., Hellbardt S., Behrmann I., Germer M., Pawlita M., Krammer P.H., Peter M.E. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 1995, 14:5579-5588.
    • (1995) EMBO J. , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 27
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl S.J., Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 2004, 5:897-907.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 28
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326:1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 30
    • 0032522871 scopus 로고    scopus 로고
    • Molecular cloning and characterization of mouse caspase-8
    • Sakamaki K., Tsukumo S., Yonehara S. Molecular cloning and characterization of mouse caspase-8. Eur. J. Biochem. 1998, 253:399-405.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 399-405
    • Sakamaki, K.1    Tsukumo, S.2    Yonehara, S.3
  • 31
    • 0034997803 scopus 로고    scopus 로고
    • Oxidative stress and antioxidant defenses in goldfish Carassius auratus during anoxia and reoxygenation
    • Lushchak V., Lushchak L., Mota A. Oxidative stress and antioxidant defenses in goldfish Carassius auratus during anoxia and reoxygenation. Am. J. Physiol. 2001, 280:100-107.
    • (2001) Am. J. Physiol. , vol.280 , pp. 100-107
    • Lushchak, V.1    Lushchak, L.2    Mota, A.3
  • 32
    • 5044223163 scopus 로고    scopus 로고
    • Peroxidation in muscle and liver tissues from fish in a contaminated river due to a petroleum refinery industry
    • Avci A., Kacmaz M., Durak I. Peroxidation in muscle and liver tissues from fish in a contaminated river due to a petroleum refinery industry. Ecotoxicol. Environ. Saf. 2005, 6:101-105.
    • (2005) Ecotoxicol. Environ. Saf. , vol.6 , pp. 101-105
    • Avci, A.1    Kacmaz, M.2    Durak, I.3
  • 33
    • 52049116278 scopus 로고    scopus 로고
    • Caspases: determination of their activities in apoptotic cells
    • Vaculova A., Zhivotovsky B. Caspases: determination of their activities in apoptotic cells. Methods Enzymol. 2008, 442:157-181.
    • (2008) Methods Enzymol. , vol.442 , pp. 157-181
    • Vaculova, A.1    Zhivotovsky, B.2
  • 35
    • 84872620495 scopus 로고    scopus 로고
    • Embryonic exposure to cis-bifenthrin enantioselectively induces the transcription of genes related to oxidative stress apoptosis and immunotoxicity in zebrafish (Danio rerio)
    • Jin Y., Pan X., Cao L., Ma B., Fu Z. Embryonic exposure to cis-bifenthrin enantioselectively induces the transcription of genes related to oxidative stress apoptosis and immunotoxicity in zebrafish (Danio rerio). Fish Shellfish Immunol. 2013, 34:717-723.
    • (2013) Fish Shellfish Immunol. , vol.34 , pp. 717-723
    • Jin, Y.1    Pan, X.2    Cao, L.3    Ma, B.4    Fu, Z.5
  • 36
    • 17844398504 scopus 로고    scopus 로고
    • Dynamic expression of caspase-2, -3, -8, and -9 proteins and enzyme activity, but not messenger ribonucleic acid, in the monkey corpus luteum during the menstrual cycle
    • Peluffo M.C., Young K.A., Stouffer R.L. Dynamic expression of caspase-2, -3, -8, and -9 proteins and enzyme activity, but not messenger ribonucleic acid, in the monkey corpus luteum during the menstrual cycle. J. Clin. Endocrinol. Metab. 2005, 90:2327-2335.
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 2327-2335
    • Peluffo, M.C.1    Young, K.A.2    Stouffer, R.L.3
  • 37
    • 41549163827 scopus 로고    scopus 로고
    • MRNA expression of Bcl-2, Bax, caspase-3 and -7 cannot be used as a marker for apoptosis in bovine blastocysts
    • Vandaele L., Goossens K., Peelman L., Van Soom A. mRNA expression of Bcl-2, Bax, caspase-3 and -7 cannot be used as a marker for apoptosis in bovine blastocysts. Anim. Reprod. Sci. 2008, 106:168-173.
    • (2008) Anim. Reprod. Sci. , vol.106 , pp. 168-173
    • Vandaele, L.1    Goossens, K.2    Peelman, L.3    Van Soom, A.4
  • 38
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: intracellular signaling by proteolysis
    • Salvesen G.S., Dixit V.M. Caspases: intracellular signaling by proteolysis. Cell 1997, 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 40
    • 0033647484 scopus 로고    scopus 로고
    • Caspase-8 in apoptosis: the beginning of "the end"?
    • Kruidering M., Evan G.I. Caspase-8 in apoptosis: the beginning of "the end"?. IUBMB Life 2000, 50:85-90.
    • (2000) IUBMB Life , vol.50 , pp. 85-90
    • Kruidering, M.1    Evan, G.I.2
  • 42
    • 59149106633 scopus 로고    scopus 로고
    • Tracing the accumulation and effects of mercury uptake in the previtellogenic ovary of crucian carp, Carassius auratus gibelio by autometallography and caspase-3 immunohistochemistry
    • Zarnescu O. Tracing the accumulation and effects of mercury uptake in the previtellogenic ovary of crucian carp, Carassius auratus gibelio by autometallography and caspase-3 immunohistochemistry. Histol. Histopathol. 2009, 24:141-148.
    • (2009) Histol. Histopathol. , vol.24 , pp. 141-148
    • Zarnescu, O.1


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