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Volumn 15, Issue 2, 2004, Pages 270-277

Antigenic Prenylated Peptide Conjugates and Polyclonal Antibodies to Detect Protein Prenylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIGEN-ANTIBODY REACTIONS; ANTIGENS; BIOSYNTHESIS; BODY FLUIDS; ESTERS; FLUORESCENCE; MAMMALS; PEPTIDES;

EID: 1642416710     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc0342027     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0004323984 scopus 로고    scopus 로고
    • Essential techniques series (Rickwood, D., Ed.) VII vols., John Wiley & Sons, Oxford
    • Delves, P. J. (1997) Antibody Production. Essential techniques series (Rickwood, D., Ed.) VII vols., John Wiley & Sons, Oxford.
    • (1997) Antibody Production
    • Delves, P.J.1
  • 3
    • 0035844287 scopus 로고    scopus 로고
    • Isopentenyl pyrophosphate, a mycobacterial nonpeptidic antigen, triggers delayed and highly sustained signaling in human gamma delta T lymphocytes without inducing down-modulation of T cell antigen receptor
    • Lafont, V., Liautard, J., Sable-Teychene, M., Sainte-Marie, Y., and Favero, J. (2001) Isopentenyl pyrophosphate, a mycobacterial nonpeptidic antigen, triggers delayed and highly sustained signaling in human gamma delta T lymphocytes without inducing down-modulation of T cell antigen receptor. J. Biol. Chem. 276, 15961-15967.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15961-15967
    • Lafont, V.1    Liautard, J.2    Sable-Teychene, M.3    Sainte-Marie, Y.4    Favero, J.5
  • 4
    • 0035858979 scopus 로고    scopus 로고
    • Structure of a human gamma delta T-cell antigen receptor
    • Allison, T., Winter, C., Fournie, J., Bonneville, M., and Garboczi, D. (2001) Structure of a human gamma delta T-cell antigen receptor. Nature 411, 820-824.
    • (2001) Nature , vol.411 , pp. 820-824
    • Allison, T.1    Winter, C.2    Fournie, J.3    Bonneville, M.4    Garboczi, D.5
  • 5
    • 0034611752 scopus 로고    scopus 로고
    • Gamma (delta) T cells: Nonclassical ligands for nonclassical cells
    • Steele, C., Oppenheim, D., and Hayday, A. (2000) Gamma (delta) T cells: Nonclassical ligands for nonclassical cells. Curr. Biol. 10, R282-285.
    • (2000) Curr. Biol. , vol.10
    • Steele, C.1    Oppenheim, D.2    Hayday, A.3
  • 6
    • 0032710142 scopus 로고    scopus 로고
    • Recognition of nonpeptide prenyl pyrophosphate antigens by human gamma delta T cells
    • Morita, C., Lee, H., Leslie, D., Tanaka, Y., Bukowski, J., and Marker-Hermann, E. (1999) Recognition of nonpeptide prenyl pyrophosphate antigens by human gamma delta T cells. Microbes Infect. 1, 175-186.
    • (1999) Microbes Infect. , vol.1 , pp. 175-186
    • Morita, C.1    Lee, H.2    Leslie, D.3    Tanaka, Y.4    Bukowski, J.5    Marker-Hermann, E.6
  • 7
    • 0010159927 scopus 로고    scopus 로고
    • Human gamma delta T cells recognize alkylamines derived from microbes, edible plants, and tea: Implications for innate immunity
    • Bukowski, J., Morita, C., and Brenner, M. (1999) Human gamma delta T cells recognize alkylamines derived from microbes, edible plants, and tea: Implications for innate immunity. Immunity 11, 57-65.
    • (1999) Immunity , vol.11 , pp. 57-65
    • Bukowski, J.1    Morita, C.2    Brenner, M.3
  • 10
    • 0029995623 scopus 로고    scopus 로고
    • A polyreactive human anti-lipid A monoclonal antibody having cross reactivity to polysaccharide portions of Pseudomonas aeruginosa lipopolysaccharides
    • Yokota, S., Ohtsuka, H., Kohzuki, T., and Noguchi, H. (1996) A polyreactive human anti-lipid A monoclonal antibody having cross reactivity to polysaccharide portions of Pseudomonas aeruginosa lipopolysaccharides. FEMS Immunol. Med. Microbiol. 14, 31-38.
    • (1996) FEMS Immunol. Med. Microbiol. , vol.14 , pp. 31-38
    • Yokota, S.1    Ohtsuka, H.2    Kohzuki, T.3    Noguchi, H.4
  • 11
    • 0031951335 scopus 로고    scopus 로고
    • Anti-lipid A monoclonal antibody Centoxin (HA-1A) binds to a wide variety of hydrophobic ligands
    • Helmerhorst, E., Maaskant, J., and Appelmelk, B. (1998) Anti-lipid A monoclonal antibody Centoxin (HA-1A) binds to a wide variety of hydrophobic ligands. Infect. Immun. 66, 870-873.
    • (1998) Infect. Immun. , vol.66 , pp. 870-873
    • Helmerhorst, E.1    Maaskant, J.2    Appelmelk, B.3
  • 12
    • 0030202483 scopus 로고    scopus 로고
    • The antiphospholipid/cofactor syndromes
    • Alarcon-Segovia, D., and Cabral, A. (1996) The antiphospholipid/cofactor syndromes. J. Rheumatol. 238, 1319-1321.
    • (1996) J. Rheumatol. , vol.238 , pp. 1319-1321
    • Alarcon-Segovia, D.1    Cabral, A.2
  • 13
    • 0025744815 scopus 로고
    • Immunology and clinical importance of antiphospholipid antibodies
    • McNeil, H., Chesterman, C., and Krilis, S. (1991) Immunology and clinical importance of antiphospholipid antibodies. Adv. Immunol. 49, 193-280.
    • (1991) Adv. Immunol. , vol.49 , pp. 193-280
    • McNeil, H.1    Chesterman, C.2    Krilis, S.3
  • 14
    • 0024366194 scopus 로고
    • Effective production of monoclonal antibodies against phosphatidylserine: Stereospecific recognition of phosphatidylserine by monoclonal antibody
    • Umeda, M., Igarashi, K., Nam, K., and Inoue, K. (1989) Effective production of monoclonal antibodies against phosphatidylserine: Stereospecific recognition of phosphatidylserine by monoclonal antibody. J. Immunol. 143, 2273-2279.
    • (1989) J. Immunol. , vol.143 , pp. 2273-2279
    • Umeda, M.1    Igarashi, K.2    Nam, K.3    Inoue, K.4
  • 15
    • 0032031777 scopus 로고    scopus 로고
    • Synthesis of disulfide-containing phospholipid analogues for the preparation of headgroup-specific lipid antigens: Generation of phosphatidylserine antibodies
    • Diaz, C., Balasubramanian, K., and Schroit, A. (1998) Synthesis of disulfide-containing phospholipid analogues for the preparation of headgroup-specific lipid antigens: generation of phosphatidylserine antibodies. Bioconjugate Chem. 9, 250-254.
    • (1998) Bioconjugate Chem. , vol.9 , pp. 250-254
    • Diaz, C.1    Balasubramanian, K.2    Schroit, A.3
  • 16
    • 0029004822 scopus 로고
    • Monoclonal anti-PS antibody reactivity against human first-trimester placental trophoblasts
    • Katsuragawa, H., Rote, N., Inoue, T., Narukawa, S., Kanzaki, H., and Mori, T. (1995) Monoclonal anti-PS antibody reactivity against human first-trimester placental trophoblasts. J. Obstet. Gynecol. 172, 1592-1597.
    • (1995) J. Obstet. Gynecol. , vol.172 , pp. 1592-1597
    • Katsuragawa, H.1    Rote, N.2    Inoue, T.3    Narukawa, S.4    Kanzaki, H.5    Mori, T.6
  • 17
    • 0023944481 scopus 로고
    • Demonstration of high specificity antibodies against phosphatidylserine
    • Maneta-Peyret, L., Bessoule, J., Geffard, M., and Cassagne, C. (1988) Demonstration of high specificity antibodies against phosphatidylserine. J. Immunol. Methods 108, 123-127.
    • (1988) J. Immunol. Methods , vol.108 , pp. 123-127
    • Maneta-Peyret, L.1    Bessoule, J.2    Geffard, M.3    Cassagne, C.4
  • 18
    • 0032845528 scopus 로고    scopus 로고
    • Generation of phosphatidylinositol-specific antibodies and their characterization
    • Thomas, C., Steel, J., Prestwich, G., and Schiavo, G. (1999) Generation of phosphatidylinositol-specific antibodies and their characterization. Biochem. Soc. Trans. 27, 648-652.
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 648-652
    • Thomas, C.1    Steel, J.2    Prestwich, G.3    Schiavo, G.4
  • 21
    • 0034672686 scopus 로고    scopus 로고
    • Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking
    • Sinensky, M. (2000) Functional aspects of polyisoprenoid protein substituents: Roles in protein-protein interaction and trafficking. Biochim. Biophys. Acta 1529, 203-209.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 203-209
    • Sinensky, M.1
  • 22
    • 0034630098 scopus 로고    scopus 로고
    • Recent advances in the study of prenylated proteins
    • Sinensky, M. (2000) Recent advances in the study of prenylated proteins. Biochim. Biophys. Acta 1484, 93-106.
    • (2000) Biochim. Biophys. Acta , vol.1484 , pp. 93-106
    • Sinensky, M.1
  • 23
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F., and Casey, P. (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65, 241-269.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 241-269
    • Zhang, F.1    Casey, P.2
  • 24
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley, A. (2001) Rho family proteins: coordinating cell responses. Trends Cell Biol. 11, 471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.1
  • 25
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A. (2001) Rho GTPases and cell migration. J. Cell Sci. 114, 2713-2722.
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.1
  • 26
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley, A. (2001) Rho proteins: linking signaling with membrane trafficking. Traffic 2, 303-310.
    • (2001) Traffic , vol.2 , pp. 303-310
    • Ridley, A.1
  • 27
    • 0032949552 scopus 로고    scopus 로고
    • Localization of isoprenylated antigen of hepatitis delta virus by anti-farnesyl antibodies
    • Lin, H., Hsu, S., Wu, J., Sheen, I., Yan, B., and Syu, W. (1999) Localization of isoprenylated antigen of hepatitis delta virus by anti-farnesyl antibodies. J. Gen. Virol. 80, 91-96.
    • (1999) J. Gen. Virol. , vol.80 , pp. 91-96
    • Lin, H.1    Hsu, S.2    Wu, J.3    Sheen, I.4    Yan, B.5    Syu, W.6
  • 28
    • 0034633651 scopus 로고    scopus 로고
    • RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: Evidenced in vivo by an anti-farnesyl cysteine antibody
    • Baron, R., Fourcade, E., Lajoie-Mazenc, I., Allal, C., Couderc, B., Barbaras, R., Favre, G., Faye, J., and Pradines, A. (2000) RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: evidenced in vivo by an anti-farnesyl cysteine antibody. Proc. Natl. Acad. Sci. U.S.A. 97, 11626-11631.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11626-11631
    • Baron, R.1    Fourcade, E.2    Lajoie-Mazenc, I.3    Allal, C.4    Couderc, B.5    Barbaras, R.6    Favre, G.7    Faye, J.8    Pradines, A.9
  • 29
    • 0142003638 scopus 로고
    • Total synthesis of δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV), a biosynthetic precursor of penicillins and cephalosporins
    • Wolfe, S., and Jokinen, M. G. (1979) Total synthesis of δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine (ACV), a biosynthetic precursor of penicillins and cephalosporins. Can. J. Chem. 57, 1388-1396.
    • (1979) Can. J. Chem. , vol.57 , pp. 1388-1396
    • Wolfe, S.1    Jokinen, M.G.2
  • 30
    • 0009328237 scopus 로고
    • Comparative sulfhydryl reaction pathways of chlorooxirane and chloroacetaldehyde
    • Joseph, J. T., Elmore, J. D., and Wong, J. L. (1990) Comparative sulfhydryl reaction pathways of chlorooxirane and chloroacetaldehyde. J. Org. Chem. 55, 471-474.
    • (1990) J. Org. Chem. , vol.55 , pp. 471-474
    • Joseph, J.T.1    Elmore, J.D.2    Wong, J.L.3
  • 31
    • 0032483144 scopus 로고    scopus 로고
    • Design and synthesis of thiol-reactive lipopeptides
    • Boeckler, C., Frisch, B., and Schuber, F. (1998) Design and synthesis of thiol-reactive lipopeptides. Bioorg. Med. Chem. Lett. 8, 2055-2058.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 2055-2058
    • Boeckler, C.1    Frisch, B.2    Schuber, F.3
  • 32
    • 45249127652 scopus 로고
    • Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking of protecting groups in peptide synthesis
    • Pearson, D. A., Blanchette, M., Baker, M. L., and Guindon, C. A. (1989) Trialkylsilanes as scavengers for the trifluoroacetic acid deblocking of protecting groups in peptide synthesis. Tetrahedron Lett. 30, 2739-2742.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 2739-2742
    • Pearson, D.A.1    Blanchette, M.2    Baker, M.L.3    Guindon, C.A.4
  • 33
    • 0026554482 scopus 로고
    • Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst
    • Xue, C. B., Becker, J. M., and Naider, F. (1992) Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst. Tetrahedron Lett. 33, 1435-1438.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 1435-1438
    • Xue, C.B.1    Becker, J.M.2    Naider, F.3
  • 34
    • 0033200301 scopus 로고    scopus 로고
    • Synthesis and selective cytotoxicity of a hyaluronic acid-antitumor bioconjugate
    • Luo, Y., and Prestwich, G. D. (1999) Synthesis and selective cytotoxicity of a hyaluronic acid-antitumor bioconjugate. Bioconjugate Chem. 10, 755-763.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 755-763
    • Luo, Y.1    Prestwich, G.D.2
  • 36
    • 0037045255 scopus 로고    scopus 로고
    • Didehydrogeranylgeranyl (AAGG): A fluorescent probe for protein prenylation
    • Liu, X., and Prestwich, G. (2002) Didehydrogeranylgeranyl (AAGG): A fluorescent probe for protein prenylation. J. Am. Chem. Soc. 124, 20-21.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 20-21
    • Liu, X.1    Prestwich, G.2
  • 37
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban, A., David, S., Bjorkesten, L., Andersson, C., Sloge, E., Lewis, S., and Currie, I. (2003) A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 3, 36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.2    Bjorkesten, L.3    Andersson, C.4    Sloge, E.5    Lewis, S.6    Currie, I.7
  • 38
    • 0035491770 scopus 로고    scopus 로고
    • Fluorescent dual colour 2D-protein gel electrophoresis for rapid detection of differences in protein pattern with standard image analysis software
    • Von, E. F., Gawriljuk, A., Fiedler, W., Ernst, G., Claussen, U., Klose, J., and Romer, I. (2001) Fluorescent dual colour 2D-protein gel electrophoresis for rapid detection of differences in protein pattern with standard image analysis software. Int. J. Mol. Med. 8, 373-377.
    • (2001) Int. J. Mol. Med. , vol.8 , pp. 373-377
    • Von, E.F.1    Gawriljuk, A.2    Fiedler, W.3    Ernst, G.4    Claussen, U.5    Klose, J.6    Romer, I.7
  • 39
    • 0036907867 scopus 로고    scopus 로고
    • Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli
    • Yan, J., Devenish, A., Wait, R., Stone, T., Lewis, S., and Fowler, S. (2002) Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2, 1682-1698.
    • (2002) Proteomics , vol.2 , pp. 1682-1698
    • Yan, J.1    Devenish, A.2    Wait, R.3    Stone, T.4    Lewis, S.5    Fowler, S.6
  • 40
    • 0036638067 scopus 로고    scopus 로고
    • Quantitative evaluation of proteins in one- and two-dimensional polyacrylamide gels using a fluorescent stain
    • Nishihara, J., and Champion, K. (2002) Quantitative evaluation of proteins in one- and two-dimensional polyacrylamide gels using a fluorescent stain. Electrophoresis 23, 2203-2215.
    • (2002) Electrophoresis , vol.23 , pp. 2203-2215
    • Nishihara, J.1    Champion, K.2
  • 42
    • 0034062812 scopus 로고    scopus 로고
    • H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway
    • Apolloni, A., Prior, I., Lindsay, M., Parton, R., and Hancock, J. (2000) H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway. Mol. Cell Biol. 20, 2475-2487.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2475-2487
    • Apolloni, A.1    Prior, I.2    Lindsay, M.3    Parton, R.4    Hancock, J.5
  • 43
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D., Silletti, J., Murphy, G., D'Eustachio, P., Rush, M., and Philips, M. (2001) Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152, 111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.6
  • 45
    • 0026039147 scopus 로고
    • Synchronization of tumor and normal cells from G1 to multiple cell cycles by lovastatin
    • Keyomarsi, K., Sandoval, L., Band, V., and Pardee, A. (1991) Synchronization of tumor and normal cells from G1 to multiple cell cycles by lovastatin. Cancer Res. 51, 3602-3609.
    • (1991) Cancer Res. , vol.51 , pp. 3602-3609
    • Keyomarsi, K.1    Sandoval, L.2    Band, V.3    Pardee, A.4
  • 46
    • 0034602515 scopus 로고    scopus 로고
    • Lovastatin arrests CHO cells between the origin decision point and the restriction point
    • Wu, J., and Gilbert, D. (2000) Lovastatin arrests CHO cells between the origin decision point and the restriction point. FEBS Lett. 484, 108-112.
    • (2000) FEBS Lett. , vol.484 , pp. 108-112
    • Wu, J.1    Gilbert, D.2
  • 48
    • 0035967798 scopus 로고    scopus 로고
    • Dose-dependent effects of lovastatin on cell cycle progression. Distinct requirement of cholesterol and nonsterol mevalonate derivatives
    • Martinez-Botas, J., Ferruelo, A., Suarez, Y., Fernandez, C., Gomez-Coronado, D., and Lasuncion, M. (2001) Dose-dependent effects of lovastatin on cell cycle progression. Distinct requirement of cholesterol and nonsterol mevalonate derivatives. Biochim. Biophys. Acta 1532, 185-194.
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 185-194
    • Martinez-Botas, J.1    Ferruelo, A.2    Suarez, Y.3    Fernandez, C.4    Gomez-Coronado, D.5    Lasuncion, M.6


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