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Volumn 44, Issue 5, 2007, Pages 774-783

Molecular cloning and characterisation of sea bass (Dicentrarchus labrax L.) caspase-3 gene

Author keywords

Apoptosis; Caspase 3; Photobacterium damselae ssp. piscicida; Sea bass

Indexed keywords

AMINO ACID; ASPARTIC ACID; CASPASE 3; PENTAPEPTIDE;

EID: 33748785440     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.04.028     Document Type: Article
Times cited : (74)

References (33)
  • 1
    • 0030698056 scopus 로고    scopus 로고
    • Specific activation of the cysteine protease CPP32 during the negative selection of T cells in the thymus
    • Alam A., Braun M.Y., Hartgers F., Lesage S., Cohen L., Hugo P., Denis F., and Sekaly R.P. Specific activation of the cysteine protease CPP32 during the negative selection of T cells in the thymus. J. Exp. Med. 186 (1997) 1503-1512
    • (1997) J. Exp. Med. , vol.186 , pp. 1503-1512
    • Alam, A.1    Braun, M.Y.2    Hartgers, F.3    Lesage, S.4    Cohen, L.5    Hugo, P.6    Denis, F.7    Sekaly, R.P.8
  • 3
    • 0019363396 scopus 로고
    • Organization and expression of eucaryotic split genes coding for proteins
    • Breathnach R., and Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem. 50 (1981) 349-383
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 5
    • 4344630346 scopus 로고    scopus 로고
    • Translation inhibition during the induction of apoptosis: RNA or protein degradation?
    • Bushell M., Stoneley M., Sarnow P., and Willis A.E. Translation inhibition during the induction of apoptosis: RNA or protein degradation?. Biochem. Soc. Trans. 32 (2004) 606-610
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 606-610
    • Bushell, M.1    Stoneley, M.2    Sarnow, P.3    Willis, A.E.4
  • 7
    • 0038639727 scopus 로고    scopus 로고
    • Apoptosis of sea bass (Dicentrarchus labrax L.) neutrophils and macrophages induced by experimental infection with Photobacterium damselae subsp. piscicida
    • do Vale A., Marques F., and Silva M.T. Apoptosis of sea bass (Dicentrarchus labrax L.) neutrophils and macrophages induced by experimental infection with Photobacterium damselae subsp. piscicida. Fish Shellfish Immunol. 15 (2003) 129-144
    • (2003) Fish Shellfish Immunol. , vol.15 , pp. 129-144
    • do Vale, A.1    Marques, F.2    Silva, M.T.3
  • 8
    • 27944453406 scopus 로고    scopus 로고
    • AIP56, a novel plasmid-encoded virulence factor of Photobacterium damselae subsp. piscicida with apoptogenic activity against sea bass macrophages and neutrophils
    • do Vale A., Silva M.T., dos Santos N.M.S., Nascimento D.S., Reis-Rodrigues P., Costa-Ramos C., Ellis A.E., and Azevedo J.E. AIP56, a novel plasmid-encoded virulence factor of Photobacterium damselae subsp. piscicida with apoptogenic activity against sea bass macrophages and neutrophils. Mol. Microbiol. 58 (2005) 1025-1038
    • (2005) Mol. Microbiol. , vol.58 , pp. 1025-1038
    • do Vale, A.1    Silva, M.T.2    dos Santos, N.M.S.3    Nascimento, D.S.4    Reis-Rodrigues, P.5    Costa-Ramos, C.6    Ellis, A.E.7    Azevedo, J.E.8
  • 9
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme
    • Fernandes-Alnemri T., Litwack G., and Alnemri E. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J. Biol. Chem. 269 (1994) 30761-30764
    • (1994) J. Biol. Chem. , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.3
  • 10
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells
    • Fink S.L., and Cookson B.T. Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect. Immun. 73 (2005) 1907-1916
    • (2005) Infect. Immun. , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 11
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: a comprehensive update of caspase substrates
    • Fischer U., Janicke R.U., and Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10 (2003) 76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 12
    • 27744477444 scopus 로고    scopus 로고
    • Mammalian initiator apoptotic caspases
    • Ho P.-K., and Hawkins C.J. Mammalian initiator apoptotic caspases. FEBS J. 272 (2005) 5436-5453
    • (2005) FEBS J. , vol.272 , pp. 5436-5453
    • Ho, P.-K.1    Hawkins, C.J.2
  • 13
    • 0032990532 scopus 로고    scopus 로고
    • Caspases in T-cell receptor-induced thymocyte apoptosis
    • Jiang D., Zheng L., and Lenardo M.J. Caspases in T-cell receptor-induced thymocyte apoptosis. Cell Death Differ. 6 (1999) 402-411
    • (1999) Cell Death Differ. , vol.6 , pp. 402-411
    • Jiang, D.1    Zheng, L.2    Lenardo, M.J.3
  • 14
    • 0033999220 scopus 로고    scopus 로고
    • Caspase-3 and -6 expression and enzyme activity in hen granulosa cells
    • Johnson A.L., and Bridgham J.T. Caspase-3 and -6 expression and enzyme activity in hen granulosa cells. Biol. Reprod. 62 (2000) 589-598
    • (2000) Biol. Reprod. , vol.62 , pp. 589-598
    • Johnson, A.L.1    Bridgham, J.T.2
  • 17
    • 0030797727 scopus 로고    scopus 로고
    • Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death
    • Miller T.M., Moulder K.L., Knudson C.M., Creedon D.J., Deshmukh M., Korsmeyer S.J., and Johnson Jr. E.M. Bax deletion further orders the cell death pathway in cerebellar granule cells and suggests a caspase-independent pathway to cell death. J. Cell Biol. 139 (1997) 205-217
    • (1997) J. Cell Biol. , vol.139 , pp. 205-217
    • Miller, T.M.1    Moulder, K.L.2    Knudson, C.M.3    Creedon, D.J.4    Deshmukh, M.5    Korsmeyer, S.J.6    Johnson Jr., E.M.7
  • 18
    • 0028839234 scopus 로고
    • Accumulation of sequence-specific RNA-binding proteins in the cytosol of activated T cells undergoing RNA degradation and apoptosis
    • Mondino A., and Jenkins M.K. Accumulation of sequence-specific RNA-binding proteins in the cytosol of activated T cells undergoing RNA degradation and apoptosis. J. Biol. Chem. 270 (1995) 26593-26601
    • (1995) J. Biol. Chem. , vol.270 , pp. 26593-26601
    • Mondino, A.1    Jenkins, M.K.2
  • 21
    • 0038725685 scopus 로고    scopus 로고
    • Negative selection-clearing out the bad apples from the T-cell repertoire
    • Palmer E. Negative selection-clearing out the bad apples from the T-cell repertoire. Nat. Rev. Immunol. 3 (2003) 383-391
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 383-391
    • Palmer, E.1
  • 22
    • 2942722389 scopus 로고
    • Rearrangement of tryptophan residues in caspase-3 active site upon activation
    • Park I.S., Moon H.R., Seok H., and Lee M. Rearrangement of tryptophan residues in caspase-3 active site upon activation. Biochim. Biophys. Acta (1700) 5-9
    • (1700) Biochim. Biophys. Acta , pp. 5-9
    • Park, I.S.1    Moon, H.R.2    Seok, H.3    Lee, M.4
  • 23
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini R., Koivunen E., and Ruoslahti E. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130 (1995) 1189-1196
    • (1995) J. Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 24
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., and Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309 (1984) 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 25
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol. 12 (1996) 697-715
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 26
    • 0027537439 scopus 로고
    • Polymorphism and estimation of the number of MhcCyca class I and class II genes in laboratory strains of the common carp (Cyprinus carpio L.)
    • Stet R.J., van Erp S.H., Hermsen T., Sultmann H.A., and Egberts E. Polymorphism and estimation of the number of MhcCyca class I and class II genes in laboratory strains of the common carp (Cyprinus carpio L.). Dev. Comp. Immunol. 17 (1993) 141-156
    • (1993) Dev. Comp. Immunol. , vol.17 , pp. 141-156
    • Stet, R.J.1    van Erp, S.H.2    Hermsen, T.3    Sultmann, H.A.4    Egberts, E.5
  • 28
    • 33750877931 scopus 로고    scopus 로고
    • Molecular characterization of rabbit CPP32 and its function in vascular smooth muscle cell apoptosis
    • Wang H., and Keiser J.A. Molecular characterization of rabbit CPP32 and its function in vascular smooth muscle cell apoptosis. Am. J. Physiol. 274 (1998) H1132-H1140
    • (1998) Am. J. Physiol. , vol.274
    • Wang, H.1    Keiser, J.A.2
  • 29
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis
    • Wang X., Zelenski N.G., Yang J., Sakai J., Brown M.S., and Goldstein J.L. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J. 15 (1996) 1012-1020
    • (1996) EMBO J. , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 30
    • 0033575255 scopus 로고    scopus 로고
    • Suicidal tendencies: apoptotic cell death by caspase family proteinases
    • Wolf B.B., and Green D.R. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. 274 (1999) 20049-20052
    • (1999) J. Biol. Chem. , vol.274 , pp. 20049-20052
    • Wolf, B.B.1    Green, D.R.2
  • 31
  • 32
    • 0035890676 scopus 로고    scopus 로고
    • Characterization of zebrafish caspase-3 and induction of apoptosis through ceramide generation in fish fathead minnow tailbud cells and zebrafish embryo
    • Yabu T., Kishi S., Okazaki T., and Yamashita M. Characterization of zebrafish caspase-3 and induction of apoptosis through ceramide generation in fish fathead minnow tailbud cells and zebrafish embryo. Biochem. J. 360 (2001) 39-47
    • (2001) Biochem. J. , vol.360 , pp. 39-47
    • Yabu, T.1    Kishi, S.2    Okazaki, T.3    Yamashita, M.4
  • 33
    • 0035478060 scopus 로고    scopus 로고
    • Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury
    • Yakovlev A.G., Ota K., Wang G., Movsesyan V., Bao W.L., Yoshihara K., and Faden A.I. Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury. J. Neurosci. 21 (2001) 7439-7446
    • (2001) J. Neurosci. , vol.21 , pp. 7439-7446
    • Yakovlev, A.G.1    Ota, K.2    Wang, G.3    Movsesyan, V.4    Bao, W.L.5    Yoshihara, K.6    Faden, A.I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.