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Volumn 326, Issue 1-2, 2004, Pages 157-165

Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage

Author keywords

Antioxidant; Echinococcus granulosus; H2O2 tolerance; Peroxiredoxin gene superfamily; Thiol dependent peroxidase activity; Thioredoxin peroxidase

Indexed keywords

ANTIOXIDANT; ANTISERUM; COMPLEMENTARY DNA; GLUTATHIONE TRANSFERASE; HELMINTH RNA; HYBRID PROTEIN; HYDROGEN PEROXIDE; PEROXIDASE; PROTECTOR PROTEIN (MIXED FUNCTION OXIDASE SYSTEMS); PROTECTOR PROTEIN (MIXED-FUNCTION OXIDASE SYSTEMS); THIOREDOXIN PEROXIDASE;

EID: 0346056673     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2003.10.027     Document Type: Article
Times cited : (76)

References (31)
  • 1
    • 0035425182 scopus 로고    scopus 로고
    • Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin
    • Berggren M.I., Husbeck B., Samulitis B., Baker A.F., Gallegos A., Powis G. Thioredoxin peroxidase-1 (peroxiredoxin-1) is increased in thioredoxin-1 transfected cells and results in enhanced protection against apoptosis caused by hydrogen peroxide but not by other agents including dexamethasone, etoposide, and doxorubicin. Arch. Biochem. Biophys. 392:2001;103-109.
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 103-109
    • Berggren, M.I.1    Husbeck, B.2    Samulitis, B.3    Baker, A.F.4    Gallegos, A.5    Powis, G.6
  • 2
    • 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. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0033301995 scopus 로고    scopus 로고
    • From cytoprotection to tumor suppression: The multifactorial role of peroxiredoxins
    • Butterfield L.H., Merino A., Golub S.H., Shau H. From cytoprotection to tumor suppression: the multifactorial role of peroxiredoxins. Antioxid. Redox Signal. 1:1999;385-402.
    • (1999) Antioxid. Redox Signal. , vol.1 , pp. 385-402
    • Butterfield, L.H.1    Merino, A.2    Golub, S.H.3    Shau, H.4
  • 4
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269:1994;27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 5
    • 0028229670 scopus 로고
    • Dimerization of thiol-specific antioxidant and the essential role of cysteine 47
    • Chae H.Z., Uhm T.B., Rhee S.G. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl. Acad. Sci. U. S. A. 91:1994;7022-7026.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 7022-7026
    • Chae, H.Z.1    Uhm, T.B.2    Rhee, S.G.3
  • 6
    • 0022451604 scopus 로고
    • Detection of specific circulating antigen, immune complexes and antibodies in human hydatidosis from Turkana (Kenya) and Great Britain, by enzyme-immunoassay
    • Craig P.S. Detection of specific circulating antigen, immune complexes and antibodies in human hydatidosis from Turkana (Kenya) and Great Britain, by enzyme-immunoassay. Parasite Immunol. 8:1986;171-188.
    • (1986) Parasite Immunol. , vol.8 , pp. 171-188
    • Craig, P.S.1
  • 9
    • 0021189761 scopus 로고
    • Role of hydrogen peroxide in the neutrophil-mediated release of prostacyclin from cultured endothelial cells
    • Harlan J.M., Callahan K.S. Role of hydrogen peroxide in the neutrophil-mediated release of prostacyclin from cultured endothelial cells. J. Clin. Invest. 74:1984;442-448.
    • (1984) J. Clin. Invest. , vol.74 , pp. 442-448
    • Harlan, J.M.1    Callahan, K.S.2
  • 11
    • 1842295744 scopus 로고    scopus 로고
    • Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
    • Jin D.Y., Chae H.Z., Rhee S.G., Jeang K.T. Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. J. Biol. Chem. 272:1997;30952-30961.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30952-30961
    • Jin, D.Y.1    Chae, H.Z.2    Rhee, S.G.3    Jeang, K.T.4
  • 12
    • 0023929362 scopus 로고
    • The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system
    • Kim K., Kim I.H., Lee K.Y., Rhee S.G., Stadtman E.R. The isolation and purification of a specific "protector" protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system. J. Biol. Chem. 263:1988;4704-4711.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4704-4711
    • Kim, K.1    Kim, I.H.2    Lee, K.Y.3    Rhee, S.G.4    Stadtman, E.R.5
  • 14
    • 0034674703 scopus 로고    scopus 로고
    • Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells
    • Kim H., Lee T.H., Park E.S., Suh J.M., Park S.J., Chung H.K., Kwon O.Y., Kim Y.K., Ro H.K., Shong M. Role of peroxiredoxins in regulating intracellular hydrogen peroxide and hydrogen peroxide-induced apoptosis in thyroid cells. J. Biol. Chem. 275:2000;18266-18270.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18266-18270
    • Kim, H.1    Lee, T.H.2    Park, E.S.3    Suh, J.M.4    Park, S.J.5    Chung, H.K.6    Kwon, O.Y.7    Kim, Y.K.8    Ro, H.K.9    Shong, M.10
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0027259213 scopus 로고
    • Removal of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo
    • Lim Y.S., Cha M.K., Kim H.K., Uhm T.B., Park J.W., Kim K., Kim I.H. Removal of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem. Biophys. Res. Commun. 192:1993;273-280.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 273-280
    • Lim, Y.S.1    Cha, M.K.2    Kim, H.K.3    Uhm, T.B.4    Park, J.W.5    Kim, K.6    Kim, I.H.7
  • 18
    • 0029886243 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity
    • Netto L.E.S., Chae H.Z., Kang S.W., Rhee S.G., Stadtman E.R. Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. TSA possesses thiol peroxidase activity. J. Biol. Chem. 271:1996;15315-15321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15315-15321
    • Netto, L.E.S.1    Chae, H.Z.2    Kang, S.W.3    Rhee, S.G.4    Stadtman, E.R.5
  • 19
    • 0029560827 scopus 로고
    • Early events in erythroid differentiation: Accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B)
    • Rabilloud T., Berthier R., Vincon M., Ferbus D., Goubin G., Lawrence J.J. Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B). Biochem. J. 312:1995;699-705.
    • (1995) Biochem. J. , vol.312 , pp. 699-705
    • Rabilloud, T.1    Berthier, R.2    Vincon, M.3    Ferbus, D.4    Goubin, G.5    Lawrence, J.J.6
  • 21
    • 0031577466 scopus 로고    scopus 로고
    • A protein with a novel calcium-binding domain associated with calcareous corpuscles in Echinococcus granulosus
    • Rodrigues J.J., Ferreira H.B., Farias S.E., Zaha A. A protein with a novel calcium-binding domain associated with calcareous corpuscles in Echinococcus granulosus. Biochem. Biophys. Res. Commun. 237:1997;451-456.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 451-456
    • Rodrigues, J.J.1    Ferreira, H.B.2    Farias, S.E.3    Zaha, A.4
  • 23
    • 0346908614 scopus 로고    scopus 로고
    • Molecular Cloning. a Laboratory Manual
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Sambrook J., Russell D.W. Molecular Cloning. A Laboratory Manual. 3rd ed. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2001) 3rd Ed.
    • Sambrook, J.1    Russell, D.W.2
  • 24
    • 0028904691 scopus 로고
    • Antioxidant function of recombinant human natural killer enhancing factor
    • Sauri H., Butterfield L., Kim A., Shau H. Antioxidant function of recombinant human natural killer enhancing factor. Biochem. Biophys. Res. Commun. 208:1995;964-969.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 964-969
    • Sauri, H.1    Butterfield, L.2    Kim, A.3    Shau, H.4
  • 27
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 28
    • 0035151727 scopus 로고    scopus 로고
    • Further studies on an intermediate host murine model showing that a primary Echinococcus granulosus infection is protective against subsequent oncospheral challenge
    • Zhang W., You H., Zhang Z., Turson G., Hasyet A., McManus D.P. Further studies on an intermediate host murine model showing that a primary Echinococcus granulosus infection is protective against subsequent oncospheral challenge. Parasitol. Int. 50:2001;279-283.
    • (2001) Parasitol. Int. , vol.50 , pp. 279-283
    • Zhang, W.1    You, H.2    Zhang, Z.3    Turson, G.4    Hasyet, A.5    McManus, D.P.6
  • 29
    • 0037237660 scopus 로고    scopus 로고
    • Concepts in immunology and diagnosis of hydatid disease
    • Zhang W., Li J., McManus D.P. Concepts in immunology and diagnosis of hydatid disease. Clin. Microbiol. Rev. 16:2003;18-36.
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 18-36
    • Zhang, W.1    Li, J.2    McManus, D.P.3
  • 31
    • 0345967823 scopus 로고    scopus 로고
    • Immunoglobulin profiles in a murine intermediate host model of resistance for Echinococcus granulosus infection
    • Zhang W., You H., Li J., Zhang Z., Turson G., Aili H., Wang J., McManus D.P. Immunoglobulin profiles in a murine intermediate host model of resistance for Echinococcus granulosus infection. Parasite Immunol. 25:2003;161-168.
    • (2003) Parasite Immunol. , vol.25 , pp. 161-168
    • Zhang, W.1    You, H.2    Li, J.3    Zhang, Z.4    Turson, G.5    Aili, H.6    Wang, J.7    McManus, D.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.