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Volumn 157, Issue 8, 1996, Pages 3341-3349

Cell Surface ADP-Ribosyltransferase Regulates Lymphocyte Function-Associated Molecule-1 (LFA-1) Function in T Cells

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; ARGININE; EPITOPE; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PHOSPHODIESTERASE;

EID: 0030587933     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (73)

References (37)
  • 1
    • 0001917915 scopus 로고
    • Cholera, the cholera enterotoxins, and the cholera enterotoxin-related enterotoxin family
    • P. Owen and T. J. Foster, eds. Elsevier Science Publishers, Biomedical Division, Amsterdam
    • Finkelstein, R. A. 1988. Cholera, the cholera enterotoxins, and the cholera enterotoxin-related enterotoxin family. In Immunochemical and Molecular Genetic-Analysis of Bacterial Pathogens. P. Owen and T. J. Foster, eds. Elsevier Science Publishers, Biomedical Division, Amsterdam, p. 85.
    • (1988) Immunochemical and Molecular Genetic-Analysis of Bacterial Pathogens , pp. 85
    • Finkelstein, R.A.1
  • 2
    • 0000921719 scopus 로고
    • Mono-ADP-ribosyltransferases and ADP-ribosylarginine hydrolases: A mono-ADP-ribosylation cycle in animal cells
    • J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, D.C.
    • Williamson, K. C., and J. Moss. 1990. Mono-ADP-ribosyltransferases and ADP-ribosylarginine hydrolases: a mono-ADP-ribosylation cycle in animal cells. In ADP-Rihosylating Toxins and G Proteins. J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, D.C., p. 493.
    • (1990) ADP-Rihosylating Toxins and G Proteins , pp. 493
    • Williamson, K.C.1    Moss, J.2
  • 4
    • 0002603319 scopus 로고
    • Diphtheria toxin: Structure and function of a cytocidal protein
    • J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, DC
    • Collier, R. J. 1990. Diphtheria toxin: structure and function of a cytocidal protein. In ADP-Ribosylating Toxins and G Proteins: Insights into Signal Transduction. J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, DC, p. 3.
    • (1990) ADP-Ribosylating Toxins and G Proteins: Insights into Signal Transduction , pp. 3
    • Collier, R.J.1
  • 5
    • 0003085965 scopus 로고
    • Pertussis toxin as a valuable probe for G-protein involvement in signal transduction
    • J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, DC
    • Ui, M. 1990. Pertussis toxin as a valuable probe for G-protein involvement in signal transduction. In ADP-Ribosylating Toxins and G Proteins: Insights into Signal Transduction. J. Moss and M. Vaughan, eds. American Society for Microbiology, Washington, DC, p. 45.
    • (1990) ADP-Ribosylating Toxins and G Proteins: Insights into Signal Transduction , pp. 45
    • Ui, M.1
  • 6
    • 0019332669 scopus 로고
    • Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes
    • Moss, J., S. J. Stanley, and P. A. Watkins. 1980. Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J. Biol. Chem. 255:1838.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1838
    • Moss, J.1    Stanley, S.J.2    Watkins, P.A.3
  • 7
    • 0021765287 scopus 로고
    • NAD:guanidine group-specific mono-ADP-ribosyltransferase activity in skeletal muscle
    • Soman, G., J. R. Mickelson, C. F. Louis, and D. J. Graves. 1984. NAD:guanidine group-specific mono-ADP-ribosyltransferase activity in skeletal muscle. Biochem. Biophys. Res. Commun. 120:973.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 973
    • Soman, G.1    Mickelson, J.R.2    Louis, C.F.3    Graves, D.J.4
  • 9
    • 0026014211 scopus 로고
    • Mono-ADP-ribosylation in brain: Purification and characterization of ADP-ribosyltransferases affecting actin from rat brain
    • Matsuyama, S., and S. Tsuyama. 1991. Mono-ADP-ribosylation in brain: purification and characterization of ADP-ribosyltransferases affecting actin from rat brain. J. Neurochem. 57:1380.
    • (1991) J. Neurochem. , vol.57 , pp. 1380
    • Matsuyama, S.1    Tsuyama, S.2
  • 10
    • 0028131940 scopus 로고
    • Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase
    • Wang, J., E. Nemoto, A. Y. Kots, H. R. Kaslow, and G. Dennert. 1994. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J. Immunol. 153:4048.
    • (1994) J. Immunol. , vol.153 , pp. 4048
    • Wang, J.1    Nemoto, E.2    Kots, A.Y.3    Kaslow, H.R.4    Dennert, G.5
  • 11
    • 0030022789 scopus 로고    scopus 로고
    • Release of a glycosyl-phosphatidylinositol-anchored ADP-ribosyltransferase from cytotoxic T cells upon activation
    • Nemoto, E., S. Stohlman, and G. Dennert. 1996. Release of a glycosyl-phosphatidylinositol-anchored ADP-ribosyltransferase from cytotoxic T cells upon activation. J. Immunol. 156:85.
    • (1996) J. Immunol. , vol.156 , pp. 85
    • Nemoto, E.1    Stohlman, S.2    Dennert, G.3
  • 12
    • 0020520382 scopus 로고
    • Monoclonal cytotoxic T lymphocyte hybridomas capable of specific killing activity, antigenic responsiveness, and inducible interleukin secretion
    • Kaufmann, Y., and G. Berke. 1983. Monoclonal cytotoxic T lymphocyte hybridomas capable of specific killing activity, antigenic responsiveness, and inducible interleukin secretion. J. Immunol. 131:50.
    • (1983) J. Immunol. , vol.131 , pp. 50
    • Kaufmann, Y.1    Berke, G.2
  • 13
    • 0027295575 scopus 로고
    • CTX-B inhibits CTL cytotoxicity, and cytoskeleton movements
    • Sugawara, S., H. R. Kaslow, and G. Dennert. 1993. CTX-B inhibits CTL cytotoxicity, and cytoskeleton movements. Immunopharmacology 26:93.
    • (1993) Immunopharmacology , vol.26 , pp. 93
    • Sugawara, S.1    Kaslow, H.R.2    Dennert, G.3
  • 14
    • 0022453692 scopus 로고
    • A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1
    • Rothlein, R., M. L. Dustin, S. D. Marlin, and T. A. Springer. 1986. A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1. J. Immunol. 137: 1270.
    • (1986) J. Immunol. , vol.137 , pp. 1270
    • Rothlein, R.1    Dustin, M.L.2    Marlin, S.D.3    Springer, T.A.4
  • 15
    • 0021917674 scopus 로고
    • Transmembrane signaling by the T cell antigen receptor: Perturbation of the T3-amigen receptor complex generates inositol phosphates, and releases calcium ions from intracellular stores
    • Imboden, J. B., and J. D. Stobo. 1985. Transmembrane signaling by the T cell antigen receptor: perturbation of the T3-amigen receptor complex generates inositol phosphates, and releases calcium ions from intracellular stores. J. Exp. Med. 161:446.
    • (1985) J. Exp. Med. , vol.161 , pp. 446
    • Imboden, J.B.1    Stobo, J.D.2
  • 16
    • 0031059054 scopus 로고    scopus 로고
    • Molecular cloning of a functional murine arginine specific mono-ADP-ribosyltransferase and its expression in lymphoid cells
    • In press
    • Yu, Y., S. Okamoto, E. Nemoto, and G. Dennert. 1996. Molecular cloning of a functional murine arginine specific mono-ADP-ribosyltransferase and its expression in lymphoid cells. DNA Cell Biol. In press.
    • (1996) DNA Cell Biol.
    • Yu, Y.1    Okamoto, S.2    Nemoto, E.3    Dennert, G.4
  • 18
    • 0019448315 scopus 로고
    • Monoclonal antibody to a novel lymphocyte function-associated antigen (LFA-1): Mechanism of blockade of T lymphocyte-mediated killing and effects on other T and B lymphocyte functions
    • Davignon, D., E. Martz, T. Reynolds, K. Kurzinger, and T. A. Springer. 1981. Monoclonal antibody to a novel lymphocyte function-associated antigen (LFA-1): mechanism of blockade of T lymphocyte-mediated killing and effects on other T and B lymphocyte functions. J. Immunol. 127:590.
    • (1981) J. Immunol. , vol.127 , pp. 590
    • Davignon, D.1    Martz, E.2    Reynolds, T.3    Kurzinger, K.4    Springer, T.A.5
  • 19
    • 0027264855 scopus 로고
    • Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase
    • McDonald, L. J., and J. Moss. 1993. Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 90:6238.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6238
    • McDonald, L.J.1    Moss, J.2
  • 20
    • 0022330322 scopus 로고
    • Modification of proteins by mono(ADP-ribosylation) in vivo
    • Payne, D. M., E. L. Jacobson, J. Moss, and M. K. Jacobson. 1985. Modification of proteins by mono(ADP-ribosylation) in vivo. Biochemistry 24:7540.
    • (1985) Biochemistry , vol.24 , pp. 7540
    • Payne, D.M.1    Jacobson, E.L.2    Moss, J.3    Jacobson, M.K.4
  • 21
    • 0023773267 scopus 로고
    • ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions
    • Meyer, T., R. Koch, W. Fanick, and H. Hilz. 1988. ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions. Biol. Chem. Hoppe-Seyler 369:579.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 579
    • Meyer, T.1    Koch, R.2    Fanick, W.3    Hilz, H.4
  • 24
    • 0024358179 scopus 로고
    • Heterogeneous distribution and transmembrane signaling properties of lymphocyte function-associated antigen (LFA-1) in human lymphocyte subsets
    • Pardi, R., J. R. Bender, C. Dettori, E. Giannazza, and E. G. Engleman. 1989. Heterogeneous distribution and transmembrane signaling properties of lymphocyte function-associated antigen (LFA-1) in human lymphocyte subsets. J. Immunol. 143:3157.
    • (1989) J. Immunol. , vol.143 , pp. 3157
    • Pardi, R.1    Bender, J.R.2    Dettori, C.3    Giannazza, E.4    Engleman, E.G.5
  • 25
    • 0024443411 scopus 로고
    • T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin, M. L., and T. A. Springer. 1989. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 341:619.
    • (1989) Nature , vol.341 , pp. 619
    • Dustin, M.L.1    Springer, T.A.2
  • 26
    • 0025907110 scopus 로고
    • Induction of LFA-1-mediated homotypic adhesions in promonocytic U-937 cells occurs independently of cell differentiation
    • Cabanas, C., P. Lastres, T. Bellon, P. Aller, C. G. Figdor, A. Corbi, and C. Bernabeu. 1991. Induction of LFA-1-mediated homotypic adhesions in promonocytic U-937 cells occurs independently of cell differentiation. Biochim. Biophys. Acta 1092:165.
    • (1991) Biochim. Biophys. Acta , vol.1092 , pp. 165
    • Cabanas, C.1    Lastres, P.2    Bellon, T.3    Aller, P.4    Figdor, C.G.5    Corbi, A.6    Bernabeu, C.7
  • 27
    • 0025195765 scopus 로고
    • Roles of adhesion molecules in T-cell recognition: Fundamental similarities between four integrins on resting human T cells (LFA-1, VLA-4, VLA-5, VLA-6) in expression, binding, and costimulation
    • Shimizu, Y., G. A. Van-Seventer, K. J. Horgan, and S. Shaw. 1990. Roles of adhesion molecules in T-cell recognition: fundamental similarities between four integrins on resting human T cells (LFA-1, VLA-4, VLA-5, VLA-6) in expression, binding, and costimulation. Immunol. Rev. 114:109.
    • (1990) Immunol. Rev. , vol.114 , pp. 109
    • Shimizu, Y.1    Van-Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 28
    • 0026672994 scopus 로고
    • Monoclonal antibodies targeting murine LFA-1 induce LFA-1/ICAM-1-independent homotypic lymphocyte aggregation
    • Wuthrich, R. P. 1992. Monoclonal antibodies targeting murine LFA-1 induce LFA-1/ICAM-1-independent homotypic lymphocyte aggregation. Cell. Immunol 144:22.
    • (1992) Cell. Immunol , vol.144 , pp. 22
    • Wuthrich, R.P.1
  • 29
    • 0025314483 scopus 로고
    • The LFA-1 ligand ICAM-1 provides an important costimulatory signal for T cell receptor-mediated activation of resting T cells
    • Van Seventer, G. A., Y. Shimizu, K. J. Horgan, and S. Shaw. 1990. The LFA-1 ligand ICAM-1 provides an important costimulatory signal for T cell receptor-mediated activation of resting T cells. J. Immunol. 144:4579.
    • (1990) J. Immunol. , vol.144 , pp. 4579
    • Van Seventer, G.A.1    Shimizu, Y.2    Horgan, K.J.3    Shaw, S.4
  • 30
    • 0024348184 scopus 로고
    • Leucocyte adhesion to cells. Molecular basis, physiological relevance, and abnormalities
    • Patarroyo, M., and M. W. Makgoba. 1989. Leucocyte adhesion to cells. Molecular basis, physiological relevance, and abnormalities. Scand. J. Immunol. 30: 129.
    • (1989) Scand. J. Immunol. , vol.30 , pp. 129
    • Patarroyo, M.1    Makgoba, M.W.2
  • 33
    • 0027331555 scopus 로고
    • 7 as substrate for a glycophosphatidylinositol anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • 7 as substrate for a glycophosphatidylinositol anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J. Biol. Chem. 268:25273.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25273
    • Zolkiewska, A.1    Moss, J.2
  • 34
    • 0026080687 scopus 로고
    • Chromosomal localization, DNA polymorphism, and expression of RT-6, the mouse homologue of rat T lymphocyte differentiation marker RT6
    • Prochazka, M., H. R. Gaskins, E. H. Leiter, F. Koch-Nolte, F. Haag, and H.-G. Thiele. 1991. Chromosomal localization, DNA polymorphism, and expression of RT-6, the mouse homologue of rat T lymphocyte differentiation marker RT6. Immunogenetics 33:152.
    • (1991) Immunogenetics , vol.33 , pp. 152
    • Prochazka, M.1    Gaskins, H.R.2    Leiter, E.H.3    Koch-Nolte, F.4    Haag, F.5    Thiele, H.-G.6
  • 35
    • 0028983937 scopus 로고
    • Both allelic forms of the rat T cell differentiation marker RT6 display nicotinamide adenine dinucleotide (NAD)-glycohydrolase activity, yet only RT6.2 is capable of automodification upon incubation with NAD
    • Haag, F., V. Andersen, S. Karsten, F. Koch-Nolte, and H.-G. Thiele. 1995. Both allelic forms of the rat T cell differentiation marker RT6 display nicotinamide adenine dinucleotide (NAD)-glycohydrolase activity, yet only RT6.2 is capable of automodification upon incubation with NAD. Eur. J. Immunol. 25:2355.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2355
    • Haag, F.1    Andersen, V.2    Karsten, S.3    Koch-Nolte, F.4    Thiele, H.-G.5
  • 36
    • 0029980483 scopus 로고    scopus 로고
    • Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins
    • Koch-Nolte, F., D. Petersen, S. Balasubramanian, F. Haag, D. Kahlke, T. Willer, R. Kastelein, F. Bazan, and H.-G. Thiele. 1996. Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl)transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271:1.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1
    • Koch-Nolte, F.1    Petersen, D.2    Balasubramanian, S.3    Haag, F.4    Kahlke, D.5    Willer, T.6    Kastelein, R.7    Bazan, F.8    Thiele, H.-G.9
  • 37
    • 0024801641 scopus 로고
    • Constitutive and stimulus-induced phosphorylation of CD11/CD18 leukocyte adhesion molecules
    • Chatila, T. A., R. S. Geha, and M. A. Arnaout. 1989. Constitutive and stimulus-induced phosphorylation of CD11/CD18 leukocyte adhesion molecules. J. Cell. Biol. 109:3435.
    • (1989) J. Cell. Biol. , vol.109 , pp. 3435
    • Chatila, T.A.1    Geha, R.S.2    Arnaout, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.