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Volumn 1627, Issue 2-3, 2003, Pages 111-120

Molecular cloning of an α-enolase from the human filarial parasite Onchocerca volvulus that binds human plasminogen

Author keywords

Filaria; IgG antibody; Onchocerca volvulus; Plasminogen binding; Enolase

Indexed keywords

ENOLASE; PLASMINOGEN;

EID: 0037786554     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(03)00083-6     Document Type: Article
Times cited : (105)

References (37)
  • 1
    • 0003680447 scopus 로고
    • (third report)
    • WHO Expert Committee on Onchocerciasis World Health Organization. Tech. Rep. Ser. 752:1987;1-167. (third report).
    • (1987) Tech. Rep. Ser. , vol.752 , pp. 1-167
  • 3
    • 0034947535 scopus 로고    scopus 로고
    • Multifunctional alpha-enolase: Its role in diseases
    • Pancholi V. Multifunctional alpha-enolase: its role in diseases. Cell. Mol. Life Sci. 58:2001;902-920.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 902-920
    • Pancholi, V.1
  • 4
    • 0022295671 scopus 로고
    • Tau-crystallin from the turtle lens: Purification and partial characterization
    • Williams L.A., Ding L., Horwitz J., Piatigorsky J. Tau-crystallin from the turtle lens: purification and partial characterization. Exp. Eye Res. 40:1985;741-749.
    • (1985) Exp. Eye Res. , vol.40 , pp. 741-749
    • Williams, L.A.1    Ding, L.2    Horwitz, J.3    Piatigorsky, J.4
  • 5
    • 0025945872 scopus 로고
    • Neuronal survival factor from bovine brain is identical to neuron-specific enolase
    • Takei N., Kondo J., Nagaike K., Oshawa K., Kato K., Kohsaka S. Neuronal survival factor from bovine brain is identical to neuron-specific enolase. J. Neurochem. 57:1991;1178-1184.
    • (1991) J. Neurochem. , vol.57 , pp. 1178-1184
    • Takei, N.1    Kondo, J.2    Nagaike, K.3    Oshawa, K.4    Kato, K.5    Kohsaka, S.6
  • 6
    • 0026768249 scopus 로고
    • Characterization of the interaction of yeast enolase with polynucleotides
    • Al-Giery A.G., Brewer J.M. Characterization of the interaction of yeast enolase with polynucleotides. Biochim. Biophys. Acta. 1159:1992;134-140.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 134-140
    • Al-Giery, A.G.1    Brewer, J.M.2
  • 8
    • 0347758959 scopus 로고    scopus 로고
    • Generation of a highly immunogenic recombinant enolase of the human opportunistic pathogen Candida albicans
    • Sandini S., Melchionnaã R., Arancia S., Gomez M.J., La Valle R. Generation of a highly immunogenic recombinant enolase of the human opportunistic pathogen Candida albicans. Biotechnol. Appl. Biochem. 29:1999;223-227.
    • (1999) Biotechnol. Appl. Biochem. , vol.29 , pp. 223-227
    • Sandini, S.1    Melchionnaã, R.2    Arancia, S.3    Gomez, M.J.4    La Valle, R.5
  • 9
    • 0034931519 scopus 로고    scopus 로고
    • α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • Bergmann S., Rohde M., Chhatwal G.S., Hammerschmidt S. α-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol. Microbiol. 40:2001;1273-1287.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 10
    • 0016809359 scopus 로고
    • Molecular biology of human plasminogen: II. Metabolism in physiological and some pathological conditions in man
    • Collen D., Verstraete M. Molecular biology of human plasminogen: II. Metabolism in physiological and some pathological conditions in man. Thromb. Diath. Haemorrh. 34:1975;403-408.
    • (1975) Thromb. Diath. Haemorrh. , vol.34 , pp. 403-408
    • Collen, D.1    Verstraete, M.2
  • 11
    • 0024146930 scopus 로고
    • Cell-associated plasminogen activation: Regulation and physiological functions
    • Saksela O., Rifkin D.B. Cell-associated plasminogen activation: regulation and physiological functions. Annu. Rev. Cell Biol. 4:1988;93-126.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 93-126
    • Saksela, O.1    Rifkin, D.B.2
  • 13
    • 0031754465 scopus 로고    scopus 로고
    • Onchocerca volvulus: Microfilariae secrete elastinolytic and males nonelastinolytic matrix-degrading serine and metalloproteases
    • Haffner A., Guilavogui A.Z., Tischendorf F.W., Brattig N.W. Onchocerca volvulus: microfilariae secrete elastinolytic and males nonelastinolytic matrix-degrading serine and metalloproteases. Exp. Parasitol. 90:1998;26-33.
    • (1998) Exp. Parasitol. , vol.90 , pp. 26-33
    • Haffner, A.1    Guilavogui, A.Z.2    Tischendorf, F.W.3    Brattig, N.W.4
  • 15
    • 0030850151 scopus 로고    scopus 로고
    • Characterization of the human immune responses to the cytosolic superoxide dismutase and glutathione S-transferase from Onchocerca volvulus
    • Brattig N.W., Henkle-Dührsen K., Hounkpatin S., Kruppa T., Liebau E., Zipfel P.F. Characterization of the human immune responses to the cytosolic superoxide dismutase and glutathione S-transferase from Onchocerca volvulus. Trop. Med. Int. Health. 2:1997;788-798.
    • (1997) Trop. Med. Int. Health , vol.2 , pp. 788-798
    • Brattig, N.W.1    Henkle-Dührsen, K.2    Hounkpatin, S.3    Kruppa, T.4    Liebau, E.5    Zipfel, P.F.6
  • 16
    • 0033884629 scopus 로고    scopus 로고
    • Humoral responses to a secretory Onchocerca volvulus protein: Differences in the pattern of antibody isotypes to recombinant Ov20/OvS1 in generalized and hyperreactive onchocerciasis
    • Mpagi J.L., Büttner D.W., Tischendorf F.W., Erttmann K.D., Brattig N.W. Humoral responses to a secretory Onchocerca volvulus protein: differences in the pattern of antibody isotypes to recombinant Ov20/OvS1 in generalized and hyperreactive onchocerciasis. Parasite Immunol. 22:2000;455-460.
    • (2000) Parasite Immunol. , vol.22 , pp. 455-460
    • Mpagi, J.L.1    Büttner, D.W.2    Tischendorf, F.W.3    Erttmann, K.D.4    Brattig, N.W.5
  • 17
    • 0030987978 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing
    • Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R. Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing. Electrophoresis. 18:1997;557-562.
    • (1997) Electrophoresis , vol.18 , pp. 557-562
    • Bini, L.1    Heid, H.2    Liberatori, S.3    Geier, G.4    Pallini, V.5    Zwilling, R.6
  • 18
    • 0027527241 scopus 로고
    • Cloning and functional expression of a Schistosoma japonicum cDNA homologous to the enolase gene family
    • Waine G.J., Becker M., Kalinna B., Yang W., McManus D.P. Cloning and functional expression of a Schistosoma japonicum cDNA homologous to the enolase gene family. Biochem. Biophys. Res. Commun. 195:1993;1211-1217.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 1211-1217
    • Waine, G.J.1    Becker, M.2    Kalinna, B.3    Yang, W.4    McManus, D.P.5
  • 19
    • 0028058605 scopus 로고
    • RNA trans-splicing in Fasciola hepatica. Identification of a spliced leader (SL) RNA and SL sequences on mRNAs
    • Davis R.E., Singh H., Botka C., Hardwick C., Ashraf el Meanawy M., Villanueva J. RNA trans-splicing in Fasciola hepatica. Identification of a spliced leader (SL) RNA and SL sequences on mRNAs. J. Biol. Chem. 269:1994;20026-20030.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20026-20030
    • Davis, R.E.1    Singh, H.2    Botka, C.3    Hardwick, C.4    Ashraf el Meanawy, M.5    Villanueva, J.6
  • 20
    • 0025122165 scopus 로고
    • The nucleotide sequence of a Drosophila melanogaster enolase gene
    • Bishop J.G., Corces V.G. The nucleotide sequence of a Drosophila melanogaster enolase gene. Nucleic Acids Res. 18:1990;191.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 191
    • Bishop, J.G.1    Corces, V.G.2
  • 21
    • 0038464170 scopus 로고
    • Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase
    • Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C. Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase. Proc. Natl. Acad. Sci. U. S. A. 83:1986;6741-6745.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 6741-6745
    • Giallongo, A.1    Feo, S.2    Moore, R.3    Croce, C.M.4    Showe, L.C.5
  • 23
    • 0030827288 scopus 로고    scopus 로고
    • Mechanism of enolase: The crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution
    • Zhang E., Brewer J.M., Minor W., Carreira L.A., Lebioda L. Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution. Biochemistry. 36:1997;12526-12534.
    • (1997) Biochemistry , vol.36 , pp. 12526-12534
    • Zhang, E.1    Brewer, J.M.2    Minor, W.3    Carreira, L.A.4    Lebioda, L.5
  • 25
    • 0030009782 scopus 로고    scopus 로고
    • A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: Structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution
    • Larsen T.M., Wedekind J.E., Rayment I., Reed G.H. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry. 35:1996;4349-4358.
    • (1996) Biochemistry , vol.35 , pp. 4349-4358
    • Larsen, T.M.1    Wedekind, J.E.2    Rayment, I.3    Reed, G.H.4
  • 26
    • 0024270534 scopus 로고
    • The morphology of adult Onchocerca volvulus based on electron microscopy
    • Franz M. The morphology of adult Onchocerca volvulus based on electron microscopy. Trop. Med. Parasitol. 39:1988;359-366.
    • (1988) Trop. Med. Parasitol. , vol.39 , pp. 359-366
    • Franz, M.1
  • 27
    • 0024211899 scopus 로고
    • Histological examination of adult Onchocerca volvulus and comparison with the collagenase technique
    • Büttner D.W., Albiez E.J., von Essen J., Erichsen J. Histological examination of adult Onchocerca volvulus and comparison with the collagenase technique. Trop. Med. Parasitol. 39:1988;390-417.
    • (1988) Trop. Med. Parasitol. , vol.39 , pp. 390-417
    • Büttner, D.W.1    Albiez, E.J.2    Von Essen, J.3    Erichsen, J.4
  • 28
    • 0020691524 scopus 로고
    • The fine structure of adult Onchocerca volvulus: III. The cuticle, the interchordal hypodermis and the muscle cells of the female worm
    • Franz M., Büttner D.W. The fine structure of adult Onchocerca volvulus: III. The cuticle, the interchordal hypodermis and the muscle cells of the female worm. Tropenmed. Parasitol. 34:1983;61-69.
    • (1983) Tropenmed. Parasitol. , vol.34 , pp. 61-69
    • Franz, M.1    Büttner, D.W.2
  • 29
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle M.D., Lottenberg R. Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77:1997;1-10.
    • (1997) Thromb. Haemost. , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2
  • 30
    • 0033103020 scopus 로고    scopus 로고
    • Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes
    • Eberhard T., Kronvall G., Ullberg M. Surface bound plasmin promotes migration of Streptococcus pneumoniae through reconstituted basement membranes. Microb. Pathog. 26:1999;175-181.
    • (1999) Microb. Pathog. , vol.26 , pp. 175-181
    • Eberhard, T.1    Kronvall, G.2    Ullberg, M.3
  • 31
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi V., Fischetti V. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J. Exp. Med. 176:1992;415-426.
    • (1992) J. Exp. Med. , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.2
  • 34
    • 0027397616 scopus 로고
    • Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform
    • Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I. Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform. Arterioscler. Thromb. 13:1993;264-275.
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 264-275
    • Bottalico, L.A.1    Kendrick, N.C.2    Keller, A.3    Li, Y.4    Tabas, I.5
  • 36
    • 0031927997 scopus 로고    scopus 로고
    • Onchocerca volvulus: Ultrastructural localization of two glutathione S-transferases
    • Wildenburg G., Liebau E., Henkle-Dührsen K. Onchocerca volvulus: ultrastructural localization of two glutathione S-transferases. Exp. Parasitol. 88:1998;34-42.
    • (1998) Exp. Parasitol. , vol.88 , pp. 34-42
    • Wildenburg, G.1    Liebau, E.2    Henkle-Dührsen, K.3
  • 37
    • 0035189168 scopus 로고    scopus 로고
    • Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus
    • Sommer A., Nimtz M., Conradt H.S., Brattig N., Boettcher K., Fischer P., Walter R.D., Liebau E. Structural analysis and antibody response to the extracellular glutathione S-transferases from Onchocerca volvulus. Infect. Immun. 69:2001;7718-7728.
    • (2001) Infect. Immun. , vol.69 , pp. 7718-7728
    • Sommer, A.1    Nimtz, M.2    Conradt, H.S.3    Brattig, N.4    Boettcher, K.5    Fischer, P.6    Walter, R.D.7    Liebau, E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.