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Volumn 88, Issue 6, 2006, Pages 693-699

Transcriptome analysis of expressed sequence tags from the venom glands of the fish Thalassophryne nattereri

Author keywords

Fish venom; Kininogenase; Lectin; Natterin; Thalassophryne nattereri; Transcriptome

Indexed keywords

CLUSTERIN; COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT PEPTIDE; COMPLEMENTARY DNA; LECTIN; TRANSCRIPTOME; CALCIUM BINDING PROTEIN; CHAPERONE; FISH PROTEIN; FISH VENOM;

EID: 33745345741     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.12.008     Document Type: Article
Times cited : (54)

References (48)
  • 1
    • 2442572097 scopus 로고    scopus 로고
    • Isolation of a haemorrhagic protein toxin (SA-HT) from the Indian venomous butterfish (Scatophagus argus, Linn) sting extract
    • Karmakar S., Muhuri D.C., Dasgupta S.C., Nagchaudhuri A.K., and Gomes A. Isolation of a haemorrhagic protein toxin (SA-HT) from the Indian venomous butterfish (Scatophagus argus, Linn) sting extract. Indian J. Exp. Biol. 42 (2004) 452-460
    • (2004) Indian J. Exp. Biol. , vol.42 , pp. 452-460
    • Karmakar, S.1    Muhuri, D.C.2    Dasgupta, S.C.3    Nagchaudhuri, A.K.4    Gomes, A.5
  • 2
    • 14844325770 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the first aquatic hyaluronidase, SFHYA1, from the venom of stonefish (Synanceja horrida)
    • Ng H.C., Ranganathan S., Chua K.L., and Khoo H.E. Cloning and molecular characterization of the first aquatic hyaluronidase, SFHYA1, from the venom of stonefish (Synanceja horrida). Gene 346 (2005) 71-81
    • (2005) Gene , vol.346 , pp. 71-81
    • Ng, H.C.1    Ranganathan, S.2    Chua, K.L.3    Khoo, H.E.4
  • 3
    • 0037131367 scopus 로고    scopus 로고
    • A neurosecretory protein isolated from stonefish (Synanceia trachynis) venom, forms nonselective pores in the membrane of NG108-15 cells
    • Ouanounou G., Malo M., Stinnakre J., Kreger A.S., and Molgo J.T. A neurosecretory protein isolated from stonefish (Synanceia trachynis) venom, forms nonselective pores in the membrane of NG108-15 cells. J. Biol. Chem. 277 (2002) 39119-39127
    • (2002) J. Biol. Chem. , vol.277 , pp. 39119-39127
    • Ouanounou, G.1    Malo, M.2    Stinnakre, J.3    Kreger, A.S.4    Molgo, J.T.5
  • 4
    • 0033991543 scopus 로고    scopus 로고
    • An investigation of the biological activity of bullrout (Notesthes robusta) venom
    • Hahn S.T., and O'Connor J.M. An investigation of the biological activity of bullrout (Notesthes robusta) venom. Toxicon 38 (2000) 79-89
    • (2000) Toxicon , vol.38 , pp. 79-89
    • Hahn, S.T.1    O'Connor, J.M.2
  • 5
    • 0031552060 scopus 로고    scopus 로고
    • Complete amino-acid sequence of the β-subunit of VTX from venom of the stonefish (Synanceia verrucosa) as identified from cDNA cloning experiments
    • Garnier P., Ducancel F., Ogawa T., Boulain J.C., Goudey-Perrière F., Perrière C., and Ménez A. Complete amino-acid sequence of the β-subunit of VTX from venom of the stonefish (Synanceia verrucosa) as identified from cDNA cloning experiments. Biochim. Biophys. Acta 1337 (1997) 1-5
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 1-5
    • Garnier, P.1    Ducancel, F.2    Ogawa, T.3    Boulain, J.C.4    Goudey-Perrière, F.5    Perrière, C.6    Ménez, A.7
  • 6
    • 0029817930 scopus 로고    scopus 로고
    • Stonustoxin is a novel lethal factor from stonefish (Synanceja horrida) venom cDNA cloning and characterization
    • Ghadessy F.G., Chen D., Kini R.M., Chung M.C.M., Khoo H.E., Jeyaseelan K., and Yuen R. Stonustoxin is a novel lethal factor from stonefish (Synanceja horrida) venom cDNA cloning and characterization. J. Biol. Chem. 271 (1996) 25575-25581
    • (1996) J. Biol. Chem. , vol.271 , pp. 25575-25581
    • Ghadessy, F.G.1    Chen, D.2    Kini, R.M.3    Chung, M.C.M.4    Khoo, H.E.5    Jeyaseelan, K.6    Yuen, R.7
  • 7
    • 0033797683 scopus 로고    scopus 로고
    • Clinical and experimental studies regarding poisoning caused by a fish Thalassophryne nattereri (niquim)
    • Fonseca L.A., and Lopes-Ferreira M. Clinical and experimental studies regarding poisoning caused by a fish Thalassophryne nattereri (niquim). An. Bras. Dermatol. 75 (2000) 435-443
    • (2000) An. Bras. Dermatol. , vol.75 , pp. 435-443
    • Fonseca, L.A.1    Lopes-Ferreira, M.2
  • 8
    • 0031979107 scopus 로고    scopus 로고
    • Thalassophryne nattereri fish venom: biological and biochemical characterization and serum neutralization of its toxic activities
    • Lopes-Ferreira M., Barbaro K.C., Cardoso D.F., Moura-da-Silva A.M., and Mota I. Thalassophryne nattereri fish venom: biological and biochemical characterization and serum neutralization of its toxic activities. Toxicon 36 (1998) 405-410
    • (1998) Toxicon , vol.36 , pp. 405-410
    • Lopes-Ferreira, M.1    Barbaro, K.C.2    Cardoso, D.F.3    Moura-da-Silva, A.M.4    Mota, I.5
  • 13
    • 0026587734 scopus 로고
    • Gene expression in Echis carinatus (carpet viper) venom glands following milking
    • Paine M.J., Desmond H.P., Theakston R.D., and Crampton J.M. Gene expression in Echis carinatus (carpet viper) venom glands following milking. Toxicon 30 (1992) 379-386
    • (1992) Toxicon , vol.30 , pp. 379-386
    • Paine, M.J.1    Desmond, H.P.2    Theakston, R.D.3    Crampton, J.M.4
  • 15
    • 0037121083 scopus 로고    scopus 로고
    • A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs)
    • Junqueira de Azevedo I.M.J., and Ho P.L. A survey of gene expression and diversity in the venom glands of the pitviper snake Bothrops insularis through the generation of expressed sequence tags (ESTs). Gene 299 (2002) 279-291
    • (2002) Gene , vol.299 , pp. 279-291
    • Junqueira de Azevedo, I.M.J.1    Ho, P.L.2
  • 17
    • 0034982418 scopus 로고    scopus 로고
    • Software scripts for quality checking of high throughput nucleic acid sequencers
    • Lazo G.R., Tong J., Miller R., Hsia C., Rausch C., Kang Y., and Anderson O.D. Software scripts for quality checking of high throughput nucleic acid sequencers. Biotechniques 30 (2001) 1300-1305
    • (2001) Biotechniques , vol.30 , pp. 1300-1305
    • Lazo, G.R.1    Tong, J.2    Miller, R.3    Hsia, C.4    Rausch, C.5    Kang, Y.6    Anderson, O.D.7
  • 18
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: a DNA sequence assembly program
    • Huang X., and Madan A. CAP3: a DNA sequence assembly program. Genome Res. 9 (1999) 868-877
    • (1999) Genome Res. , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 21
    • 0034623005 scopus 로고    scopus 로고
    • T-coffee: a novel method for fast and accurate multiple sequence alignment
    • Notredame C., Higgins D.G., and Heringa J. T-coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302 (2000) 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 22
    • 0030776390 scopus 로고    scopus 로고
    • Identifying distantly related protein sequences
    • Pearson W.R. Identifying distantly related protein sequences. Comput. Appl. Biosci. 13 (1997) 325-332
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 325-332
    • Pearson, W.R.1
  • 23
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263 (1988) 9557-9560
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 24
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis W.I., Taylor M.E., and Drickamer K. The C-type lectin superfamily in the immune system. Immunol. Rev. 163 (1998) 19-34
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 25
    • 9744281932 scopus 로고    scopus 로고
    • Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
    • Ogawa T., Chijiwa T., Oda-Ueda N., and Ohno M. Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon 45 (2005) 1-14
    • (2005) Toxicon , vol.45 , pp. 1-14
    • Ogawa, T.1    Chijiwa, T.2    Oda-Ueda, N.3    Ohno, M.4
  • 26
    • 15844399859 scopus 로고    scopus 로고
    • A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins
    • Armstrong P.B., Swarnakar S., Srimal S., Misquith S., Hahn E.A., Aimes R.T., and Quigley J.P. A cytolytic function for a sialic acid-binding lectin that is a member of the pentraxin family of proteins. J. Biol. Chem. 271 (1996) 14717-14721
    • (1996) J. Biol. Chem. , vol.271 , pp. 14717-14721
    • Armstrong, P.B.1    Swarnakar, S.2    Srimal, S.3    Misquith, S.4    Hahn, E.A.5    Aimes, R.T.6    Quigley, J.P.7
  • 27
    • 4344713294 scopus 로고    scopus 로고
    • Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism
    • Uchida T., Yamasaki T., Eto S., Sugawara H., Kurisu G., Nakagawa A., Kusunoki M., and Hatakeyama T. Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism. J. Biol. Chem. 279 (2004) 37133-37141
    • (2004) J. Biol. Chem. , vol.279 , pp. 37133-37141
    • Uchida, T.1    Yamasaki, T.2    Eto, S.3    Sugawara, H.4    Kurisu, G.5    Nakagawa, A.6    Kusunoki, M.7    Hatakeyama, T.8
  • 28
    • 0023644774 scopus 로고
    • The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins
    • Giga Y., Ikai A., and Takahashi K. The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins. J. Biol. Chem. 262 (1987) 6197-6203
    • (1987) J. Biol. Chem. , vol.262 , pp. 6197-6203
    • Giga, Y.1    Ikai, A.2    Takahashi, K.3
  • 29
    • 11144223270 scopus 로고    scopus 로고
    • Purification of a myotoxin from the toadfish Thalassophryne maculosa (Gunter) venom
    • Sosa-Rosales J.I., D'Suze G., Salazar V., Fox J., and Sevcik C. Purification of a myotoxin from the toadfish Thalassophryne maculosa (Gunter) venom. Toxicon 45 (2005) 147-153
    • (2005) Toxicon , vol.45 , pp. 147-153
    • Sosa-Rosales, J.I.1    D'Suze, G.2    Salazar, V.3    Fox, J.4    Sevcik, C.5
  • 30
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 31
    • 0026271025 scopus 로고
    • The role of heat-shock proteins as molecular chaperones
    • Welch W.J. The role of heat-shock proteins as molecular chaperones. Curr. Opin. Cell Biol. 3 (1991) 1033-1038
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 1033-1038
    • Welch, W.J.1
  • 32
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: building bridges in protein folding
    • Freedman R.B., Hirst T.R., and Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19 (1994) 331-336
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 33
    • 0031954077 scopus 로고    scopus 로고
    • Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase
    • Freedman R.B., Gane P.J., Hawkins H.C., Hlodan R., McLaughlin S.H., and Parry J.W. Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase. Biol. Chem. 379 (1998) 321-328
    • (1998) Biol. Chem. , vol.379 , pp. 321-328
    • Freedman, R.B.1    Gane, P.J.2    Hawkins, H.C.3    Hlodan, R.4    McLaughlin, S.H.5    Parry, J.W.6
  • 35
    • 0033548566 scopus 로고    scopus 로고
    • Clusterin has chaperone-like activity similar to that of small heat shock proteins
    • Humphreys D.T., Carver J.A., Easterbrook-Smith S.B., and Wilson M.R. Clusterin has chaperone-like activity similar to that of small heat shock proteins. J. Biol. Chem. 274 (1999) 6875-6881
    • (1999) J. Biol. Chem. , vol.274 , pp. 6875-6881
    • Humphreys, D.T.1    Carver, J.A.2    Easterbrook-Smith, S.B.3    Wilson, M.R.4
  • 36
    • 0034719136 scopus 로고    scopus 로고
    • Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state
    • Poon S., Easterbrook-Smith S.B., Rybchyn M.S., Carver J.A., and Wilson M.R. Clusterin is an ATP-independent chaperone with very broad substrate specificity that stabilizes stressed proteins in a folding-competent state. Biochemistry 39 (2000) 15953-15960
    • (2000) Biochemistry , vol.39 , pp. 15953-15960
    • Poon, S.1    Easterbrook-Smith, S.B.2    Rybchyn, M.S.3    Carver, J.A.4    Wilson, M.R.5
  • 37
    • 0028947053 scopus 로고
    • PCR differential display identifies a rat brain mRNA that is transcriptionally regulated by cocaine and amphetamine
    • Douglass J., McKinzie A.A., and Couceyro P. PCR differential display identifies a rat brain mRNA that is transcriptionally regulated by cocaine and amphetamine. Neurosci. 15 (1995) 2471-2481
    • (1995) Neurosci. , vol.15 , pp. 2471-2481
    • Douglass, J.1    McKinzie, A.A.2    Couceyro, P.3
  • 38
    • 0034704344 scopus 로고    scopus 로고
    • Effects of CART peptides on food consumption, feeding and associated behaviors in the goldfish, Carassius auratus: actions on neuropeptide Y- and orexin A-induced feeding
    • Volkoff H., and Peter R.E. Effects of CART peptides on food consumption, feeding and associated behaviors in the goldfish, Carassius auratus: actions on neuropeptide Y- and orexin A-induced feeding. Brain Res. 887 (2000) 125-133
    • (2000) Brain Res. , vol.887 , pp. 125-133
    • Volkoff, H.1    Peter, R.E.2
  • 40
    • 0032577534 scopus 로고    scopus 로고
    • Purification and characterization of a new hypothalamic satiety peptide, cocaine and amphetamine regulated transcript (CART), produced in yeast
    • Thim L., Nielsen P.F., Judge M.E., Andersen A.S., Diers I., Egel-Mitani M., and Hastrup S. Purification and characterization of a new hypothalamic satiety peptide, cocaine and amphetamine regulated transcript (CART), produced in yeast. FEBS Lett. 428 (1998) 263-268
    • (1998) FEBS Lett. , vol.428 , pp. 263-268
    • Thim, L.1    Nielsen, P.F.2    Judge, M.E.3    Andersen, A.S.4    Diers, I.5    Egel-Mitani, M.6    Hastrup, S.7
  • 41
    • 0030797958 scopus 로고    scopus 로고
    • Further studies on the anatomical distribution of CART by in situ hybridization
    • Couceyro P.R., Koylu E.O., and Kuhar M.J. Further studies on the anatomical distribution of CART by in situ hybridization. J. Chem. Neuroanat. 12 (1997) 229-241
    • (1997) J. Chem. Neuroanat. , vol.12 , pp. 229-241
    • Couceyro, P.R.1    Koylu, E.O.2    Kuhar, M.J.3
  • 42
    • 0033550726 scopus 로고    scopus 로고
    • Recombinant CART peptide induces c-Fos expression in central areas involved in control of feeding behaviour
    • Vrang N., Tang-Christensen M., Larsen P.J., and Kristensen P. Recombinant CART peptide induces c-Fos expression in central areas involved in control of feeding behaviour. Brain Res. 818 (1999) 499-509
    • (1999) Brain Res. , vol.818 , pp. 499-509
    • Vrang, N.1    Tang-Christensen, M.2    Larsen, P.J.3    Kristensen, P.4
  • 43
    • 0030611786 scopus 로고    scopus 로고
    • 2+ and the regulation of neurotransmitter secretion
    • 2+ and the regulation of neurotransmitter secretion. Curr. Opin. Neurobiol. 7 (1997) 316-322
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 316-322
    • Bennett, M.K.1
  • 46
    • 0023580129 scopus 로고
    • Differential distribution of immunoreactive S-100a and S-100b proteins in normal nonnervous human tissues
    • Haimoto H., Hosoda S., and Kato K. Differential distribution of immunoreactive S-100a and S-100b proteins in normal nonnervous human tissues. Lab. Invest. 57 (1987) 489-498
    • (1987) Lab. Invest. , vol.57 , pp. 489-498
    • Haimoto, H.1    Hosoda, S.2    Kato, K.3
  • 47
    • 0030052283 scopus 로고    scopus 로고
    • Calcium-dependent binding of S100C to the N-terminal domain of annexin I
    • Mailliard W.S., Haigler H.T., and Schlaepfer D.D. Calcium-dependent binding of S100C to the N-terminal domain of annexin I. J. Biol. Chem. 271 (1996) 719-725
    • (1996) J. Biol. Chem. , vol.271 , pp. 719-725
    • Mailliard, W.S.1    Haigler, H.T.2    Schlaepfer, D.D.3


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