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Volumn 200, Issue 1, 2004, Pages 15-23

Temperature-induced change of variant surface antigen expression in Paramecium involves antigen release into the culture medium with considerable delay between transcription and surface expression

Author keywords

Cilia; Immobilization antigens; Paramecium; Protozoa; Variant surface antigens

Indexed keywords

ANTIGEN EXPRESSION; ARTICLE; CELL MEMBRANE; CELL SURFACE; CONTROLLED STUDY; GENETIC TRANSCRIPTION; MOLECULAR WEIGHT; NONHUMAN; PARAMECIUM; SOMATIC CELL; SURFACE PROPERTY; TEMPERATURE SENSITIVITY; WESTERN BLOTTING;

EID: 4444346057     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-004-0690-y     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0021024183 scopus 로고
    • Physiological and mutational protein variations in the ciliary membrane of Paramecium
    • Adoutte, A., Ling, K.Y., Chang, S., Huang, F., Kung, C. 1983. Physiological and mutational protein variations in the ciliary membrane of Paramecium. Exp. Cell Res. 148:387-404
    • (1983) Exp. Cell Res. , vol.148 , pp. 387-404
    • Adoutte, A.1    Ling, K.Y.2    Chang, S.3    Huang, F.4    Kung, C.5
  • 2
    • 0005519211 scopus 로고
    • Uneven distribution of surface antigens during antigenic variation in Paramecium primaurelia
    • Antony, C., Capdeville, Y. 1989. Uneven distribution of surface antigens during antigenic variation in Paramecium primaurelia. J. Cell Sci. 92:205-215
    • (1989) J. Cell Sci. , vol.92 , pp. 205-215
    • Antony, C.1    Capdeville, Y.2
  • 3
    • 0026486580 scopus 로고
    • Structural comparisons between the soluble and the GPI-anchored forms of the Paramecium temperature-specific 156G surface antigen
    • Assouz, N., Capdeville, Y. 1992. Structural comparisons between the soluble and the GPI-anchored forms of the Paramecium temperature-specific 156G surface antigen. Biol. Cell 75:217-223
    • (1992) Biol. Cell , vol.75 , pp. 217-223
    • Assouz, N.1    Capdeville, Y.2
  • 4
    • 0021311630 scopus 로고
    • Antibody-induced membrane fusion in Paramecium
    • Barnett, A., Steers, E. 1984. Antibody-induced membrane fusion in Paramecium. J. Cell Sci. 65:153-162
    • (1984) J. Cell Sci. , vol.65 , pp. 153-162
    • Barnett, A.1    Steers, E.2
  • 6
    • 0344701076 scopus 로고    scopus 로고
    • The lipid moiety of the GPI-anchor of the major plasma membrane proteins in Paramecium primaurelia is a ceramide: Variation of the amide-linked fatty acid composition as a function of growth
    • Benwakrim, A., Trémolière., A., Labarre, J., Capdeville, Y. 1998. The lipid moiety of the GPI-anchor of the major plasma membrane proteins in Paramecium primaurelia is a ceramide: variation of the amide-linked fatty acid composition as a function of growth. Protist 149:39-50
    • (1998) Protist , vol.149 , pp. 39-50
    • Benwakrim, A.1    Trémolière, A.2    Labarre, J.3    Capdeville, Y.4
  • 7
    • 0034232515 scopus 로고    scopus 로고
    • Proteases involved in erythrocyte invasion by the malaria parasite: Function and potential as chemotherapeutic targets
    • Blackman, M.J. 2000. Proteases involved in erythrocyte invasion by the malaria parasite: Function and potential as chemotherapeutic targets. Curr. Drug Targets 1:59-83
    • (2000) Curr. Drug Targets , vol.1 , pp. 59-83
    • Blackman, M.J.1
  • 8
    • 0002235158 scopus 로고    scopus 로고
    • Ciliate genetics
    • Hausmann, K., Bradbury, P.C. (editors) Gustav Fischer Verlag. Stuttgart, Jena
    • Bleyman, L.K. 1996. Ciliate genetics. In: Ciliates - Cells, Organisms. Hausmann, K., Bradbury, P.C. (editors) pp. 291-324, Gustav Fischer Verlag. Stuttgart, Jena
    • (1996) Ciliates - Cells, Organisms , pp. 291-324
    • Bleyman, L.K.1
  • 9
    • 0033846583 scopus 로고    scopus 로고
    • Paramecium GPI proteins: Variability of expression and localization
    • Capdeville, Y. 2000. Paramecium GPI proteins: variability of expression and localization. Protist 151:161-169
    • (2000) Protist , vol.151 , pp. 161-169
    • Capdeville, Y.1
  • 10
    • 0029848441 scopus 로고    scopus 로고
    • The major ciliary membrane proteins in Paramecium primaurelia are all glycosylphosphatidylinositol-anchored proteins
    • Capdeville, Y., Benwakrim, A. 1996. The major ciliary membrane proteins in Paramecium primaurelia are all glycosylphosphatidylinositol-anchored proteins. Eur. J. Cell Biol. 70:339-346
    • (1996) Eur. J. Cell Biol. , vol.70 , pp. 339-346
    • Capdeville, Y.1    Benwakrim, A.2
  • 11
    • 0000065322 scopus 로고
    • Allelic antigen and membrane-anchor epitopes of Paramecium primaurelia surface antigens
    • Capdeville, Y., Caron, F., Antony, C., Deregnaucourt, C., Keller, A.M. 1987. Allelic antigen and membrane-anchor epitopes of Paramecium primaurelia surface antigens. J. Cell Sci. 88:553-562
    • (1987) J. Cell Sci. , vol.88 , pp. 553-562
    • Capdeville, Y.1    Caron, F.2    Antony, C.3    Deregnaucourt, C.4    Keller, A.M.5
  • 12
    • 0035005160 scopus 로고    scopus 로고
    • The I-antigens of Ichthyophthirius multifiliis are GPI-anchored proteins
    • Clark, T.G., Gao, Y., Gaertig, J., Wang, X., Cheng, G. 2001. The I-antigens of Ichthyophthirius multifiliis are GPI-anchored proteins. J. Eukaryot. Microbiol. 48:332-337
    • (2001) J. Eukaryot. Microbiol. , vol.48 , pp. 332-337
    • Clark, T.G.1    Gao, Y.2    Gaertig, J.3    Wang, X.4    Cheng, G.5
  • 14
    • 0345560185 scopus 로고
    • Turnover of the GPI-anchored surface antigen in Paramecium. Partial release of its acylated form into the culture medium
    • Deregnaucourt, C. 1992. Turnover of the GPI-anchored surface antigen in Paramecium. Partial release of its acylated form into the culture medium. Eur. J. Protistol. 28:220-225
    • (1992) Eur. J. Protistol. , vol.28 , pp. 220-225
    • Deregnaucourt, C.1
  • 15
    • 0033624164 scopus 로고    scopus 로고
    • Targeted disruption of the glycosylphosphatidylinositol-anchored surface antigen SAG3 gene in Toxoplasma gondii decreases host cell adhesion and drastically reduces virulence in mice
    • Dzierszinski, F., Mortuaire, M., Crebron-Delauw, M.F., Tomavo, S. 2000. Targeted disruption of the glycosylphosphatidylinositol-anchored surface antigen SAG3 gene in Toxoplasma gondii decreases host cell adhesion and drastically reduces virulence in mice. Mol. Microbiol. 37:574-582
    • (2000) Mol. Microbiol. , vol.37 , pp. 574-582
    • Dzierszinski, F.1    Mortuaire, M.2    Crebron-Delauw, M.F.3    Tomavo, S.4
  • 16
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson, M.A.J. 1999. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112:2799-2809
    • (1999) J. Cell Sci. , vol.112 , pp. 2799-2809
    • Ferguson, M.A.J.1
  • 17
    • 0344428151 scopus 로고    scopus 로고
    • Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells
    • Flötenmeyer, M., Momayezi, M., Plattner, H. 1999. Immunolabeling analysis of biosynthetic and degradative pathways of cell surface components (glycocalyx) in Paramecium cells. Eur. J. Cell Biol. 78:67-77
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 67-77
    • Flötenmeyer, M.1    Momayezi, M.2    Plattner, H.3
  • 18
    • 0038267453 scopus 로고    scopus 로고
    • A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage
    • Howell, S.A., Wells, I., Fleck, S.L., Kettleborough, C., Collins, C.R., Blackman, M.J. 2003. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. J. Biol. Chem. 278:23890-23898
    • (2003) J. Biol. Chem. , vol.278 , pp. 23890-23898
    • Howell, S.A.1    Wells, I.2    Fleck, S.L.3    Kettleborough, C.4    Collins, C.R.5    Blackman, M.J.6
  • 19
    • 37049061924 scopus 로고
    • Immobilization antigen in heterozygous clones of Paramecium aurelia
    • Jones, I.G. 1965. Immobilization antigen in heterozygous clones of Paramecium aurelia. Nature 207:769
    • (1965) Nature , vol.207 , pp. 769
    • Jones, I.G.1
  • 20
    • 0035868758 scopus 로고    scopus 로고
    • Genetically controlled expression of surface variant antigens in free-living protozoa
    • Kusch, J., Schmidt, H.J. 2001. Genetically controlled expression of surface variant antigens in free-living protozoa. J. Membrane Biol. 180:101-109
    • (2001) J. Membrane Biol. , vol.180 , pp. 101-109
    • Kusch, J.1    Schmidt, H.J.2
  • 21
    • 0037346805 scopus 로고    scopus 로고
    • Essential roles for GPI-anchored proteins in african trypanosomes revealed using mutants deficient in GPI8
    • Lillico, S., Field, M.C., Blundell, P., Coombs, G.H., Mottram, J.C. 2003. Essential roles for GPI-anchored proteins in african trypanosomes revealed using mutants deficient in GPI8. Mol. Biol. Cell 14:1182-1194
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1182-1194
    • Lillico, S.1    Field, M.C.2    Blundell, P.3    Coombs, G.H.4    Mottram, J.C.5
  • 22
    • 0035746007 scopus 로고    scopus 로고
    • Glycophosphatidylinositol-anchored proteins in Paramecium tetraurelia: Possible role in chemoresponse
    • Paquette, C.A., Rakochy, V., Bush, A., Van Houten, J.L. 2001. Glycophosphatidylinositol-anchored proteins in Paramecium tetraurelia: possible role in chemoresponse. J. Exp. Biol. 204:2899-2910
    • (2001) J. Exp. Biol. , vol.204 , pp. 2899-2910
    • Paquette, C.A.1    Rakochy, V.2    Bush, A.3    Van Houten, J.L.4
  • 23
    • 70449285258 scopus 로고
    • Studies on the immobilization antigens of Paramecium. II. Isolation
    • Preer, J.R. 1959. Studies on the immobilization antigens of Paramecium. II. Isolation. J. Immunol. 83:378-384
    • (1959) J. Immunol. , vol.83 , pp. 378-384
    • Preer, J.R.1
  • 25
    • 0023442573 scopus 로고
    • Molecular biology of the genes for immobilization antigens in Paramecium
    • Preer, J.B., Preer, L.B., Rudman, B., Barnett, A. 1987. Molecular biology of the genes for immobilization antigens in Paramecium. J. Protozool. 34:418-423
    • (1987) J. Protozool. , vol.34 , pp. 418-423
    • Preer, J.B.1    Preer, L.B.2    Rudman, B.3    Barnett, A.4
  • 27
    • 0041552320 scopus 로고
    • Development mechanisms in Paramecium
    • Sonneborn, T.M. 1947. Development mechanisms in Paramecium. Growth Symp. 11:291-307
    • (1947) Growth Symp. , vol.11 , pp. 291-307
    • Sonneborn, T.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.