메뉴 건너뛰기




Volumn 161, Issue , 1998, Pages 95-109

Ecto-enzyme and signaling functions of lymphocyte CD73

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE RECEPTOR; CELL ADHESION MOLECULE; ECTO 5' NUCLEOTIDASE; GLYCOSYLPHOSPHATIDYLINOSITOL; LYMPHOCYTE ANTIGEN; LYMPHOCYTE ENZYME;

EID: 0031933227     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01574.x     Document Type: Review
Times cited : (294)

References (133)
  • 1
    • 0016734225 scopus 로고
    • 5′-nucleotidase from smooth muscle of small intestine and from brain. Inhibition by nucleotides
    • Burger RM, Lowenstein JM. 5′-nucleotidase from smooth muscle of small intestine and from brain. Inhibition by nucleotides. Biochemistry 1975;14:2362-2366.
    • (1975) Biochemistry , vol.14 , pp. 2362-2366
    • Burger, R.M.1    Lowenstein, J.M.2
  • 2
    • 0019813150 scopus 로고
    • 5′-nucleotidase from rat heart
    • Naito Y, Lowenstein JM. 5′-nucleotidase from rat heart. Biochemistry 1981;20:5188-5194.
    • (1981) Biochemistry , vol.20 , pp. 5188-5194
    • Naito, Y.1    Lowenstein, J.M.2
  • 3
    • 0025055084 scopus 로고
    • Production and characterization of monoclonal antibodies to the glycosyl phosphatidylinositol-anchored lymphocyte differentiation antigen ecto-5′-nucleotidase (CD73)
    • Thompson LF, et al. Production and characterization of monoclonal antibodies to the glycosyl phosphatidylinositol-anchored lymphocyte differentiation antigen ecto-5′-nucleotidase (CD73). Tissue Antigens 1990;35:9-19.
    • (1990) Tissue Antigens , vol.35 , pp. 9-19
    • Thompson, L.F.1
  • 4
    • 0026729643 scopus 로고
    • 5′-nucleotidase: Molecular structure and functional aspects
    • Zimmermann H. 5′-nucleotidase: Molecular structure and functional aspects. Biochem J 1992;285:345-365.
    • (1992) Biochem J , vol.285 , pp. 345-365
    • Zimmermann, H.1
  • 5
    • 0016839152 scopus 로고
    • Human lymphocytes: 5′-nucleotidase-positive and -negative subpopulations
    • Silber R, Conklyn M, Grusky G, Zucker-Franklin D. Human lymphocytes: 5′-nucleotidase-positive and -negative subpopulations. J Clin Invest 1975;56:1324-1327.
    • (1975) J Clin Invest , vol.56 , pp. 1324-1327
    • Silber, R.1    Conklyn, M.2    Grusky, G.3    Zucker-Franklin, D.4
  • 7
    • 0016295491 scopus 로고
    • B-cell neoplasia in man
    • Salmon SE, Seligmann M. B-cell neoplasia in man. Lancet 1974;2:1230-1233.
    • (1974) Lancet , vol.2 , pp. 1230-1233
    • Salmon, S.E.1    Seligmann, M.2
  • 8
    • 0016289673 scopus 로고
    • Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. II. Properties and suitability as markers for the plasma membrane
    • DePierre JW, Karnovsky ML. Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. II. Properties and suitability as markers for the plasma membrane. J Biol Chem 1974;249:7121-7129.
    • (1974) J Biol Chem , vol.249 , pp. 7121-7129
    • DePierre, J.W.1    Karnovsky, M.L.2
  • 10
    • 0018088317 scopus 로고
    • Lymphocyte ecto-5′-nucleotidase deficiency in agammaglobulinemia
    • Edwards NL, Magilavy DB, Cassidy JT, Fox IH. Lymphocyte ecto-5′-nucleotidase deficiency in agammaglobulinemia. Science 1978;201:628-630.
    • (1978) Science , vol.201 , pp. 628-630
    • Edwards, N.L.1    Magilavy, D.B.2    Cassidy, J.T.3    Fox, I.H.4
  • 11
    • 0024538472 scopus 로고
    • Clinical and immunologic analyses of 103 patients with common variable immunodeficiency
    • Cunningham-Rundles C. Clinical and immunologic analyses of 103 patients with common variable immunodeficiency. J Clin Immunol 1989;9:22-33.
    • (1989) J Clin Immunol , vol.9 , pp. 22-33
    • Cunningham-Rundles, C.1
  • 12
    • 0025027433 scopus 로고
    • Phenotypic features and proliferative activity of B cell progenitors in X-linked agammaglobulinemia
    • Campana D, Farrant J, Inamdar N, Webster ADB, Janossy G. Phenotypic features and proliferative activity of B cell progenitors in X-linked agammaglobulinemia. J Immunol 1990;145:1675-1680.
    • (1990) J Immunol , vol.145 , pp. 1675-1680
    • Campana, D.1    Farrant, J.2    Inamdar, N.3    Webster, A.D.B.4    Janossy, G.5
  • 13
    • 0015515283 scopus 로고
    • Adenosine-deaminase deficiency in two patients with severely impaired cellular immunity
    • Giblett ER, Anderson JE, Cohen F, Pollara B, Meuwissen HJ. Adenosine-deaminase deficiency in two patients with severely impaired cellular immunity. Lancet 1972;2:1067-1069.
    • (1972) Lancet , vol.2 , pp. 1067-1069
    • Giblett, E.R.1    Anderson, J.E.2    Cohen, F.3    Pollara, B.4    Meuwissen, H.J.5
  • 14
    • 84919573117 scopus 로고
    • Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity
    • Giblett ER, Ammann AJ, Sandman R, Wara DW, Diamond LK. Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity. Lancet 1975;1:1010-1013.
    • (1975) Lancet , vol.1 , pp. 1010-1013
    • Giblett, E.R.1    Ammann, A.J.2    Sandman, R.3    Wara, D.W.4    Diamond, L.K.5
  • 15
    • 0018945982 scopus 로고
    • Lymphocyte 5′-nucleotidase deficiency in hypogammaglobulinemia: Clinical characteristics
    • Edwards NL, Cassidy JT, Fox IH. Lymphocyte 5′-nucleotidase deficiency in hypogammaglobulinemia: Clinical characteristics. Clin Immunol Immunopathol 1980;17: 76-88.
    • (1980) Clin Immunol Immunopathol , vol.17 , pp. 76-88
    • Edwards, N.L.1    Cassidy, J.T.2    Fox, I.H.3
  • 16
    • 0002377290 scopus 로고
    • Immunodeficiency diseases caused by adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency
    • Scriver CR, Beaudet AL, Sly WS, Valle D, eds. New York: McGraw-Hill, Inc.
    • Hershfield MS, Mitchell BS. Immunodeficiency diseases caused by adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The metabolic and molecular bases of inherited disease. New York: McGraw-Hill, Inc. 1995. p. 1725-1768.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1725-1768
    • Hershfield, M.S.1    Mitchell, B.S.2
  • 17
    • 0018582727 scopus 로고
    • Ecto-5′-nucleotidase activity in T and B lymphocytes from normal subjects and patients with congenital X-linked agammaglobulinemia
    • Thompson LF, et al. Ecto-5′-nucleotidase activity in T and B lymphocytes from normal subjects and patients with congenital X-linked agammaglobulinemia. J Immunol 1979;123:2475-2478.
    • (1979) J Immunol , vol.123 , pp. 2475-2478
    • Thompson, L.F.1
  • 19
    • 0023003428 scopus 로고
    • Ecto-5′-nucleotidase expression during human B cell development. An explanation for the heterogeneity in B lymphocyte ecto-5′-nucleotidase activity in patients with hypogammaglobulinemia
    • Thompson LF, Ruedi JM, O'Connor RD, Bastian JF. Ecto-5′-nucleotidase expression during human B cell development. An explanation for the heterogeneity in B lymphocyte ecto-5′-nucleotidase activity in patients with hypogammaglobulinemia. J Immunol 1986;137:2496-2500.
    • (1986) J Immunol , vol.137 , pp. 2496-2500
    • Thompson, L.F.1    Ruedi, J.M.2    O'Connor, R.D.3    Bastian, J.F.4
  • 21
    • 0021351201 scopus 로고
    • Lymphocyte ecto-5′-nucleotidase activity in infancy: Increasing activity in peripheral blood B cells precedes their ability to synthesize IgG in vitro
    • Bastian JF, Ruedi JM, MacPherson GA, Golembesky HE, O'Connor RD, Thompson LF. Lymphocyte ecto-5′-nucleotidase activity in infancy: increasing activity in peripheral blood B cells precedes their ability to synthesize IgG in vitro. J Immunol 1984;132:1767-1772.
    • (1984) J Immunol , vol.132 , pp. 1767-1772
    • Bastian, J.F.1    Ruedi, J.M.2    MacPherson, G.A.3    Golembesky, H.E.4    O'Connor, R.D.5    Thompson, L.F.6
  • 23
    • 0020696354 scopus 로고
    • Ecto-5′-nucleotidase activity in human T cell subsets. Decreased numbers of ecto-5′-nucleotidase positive cells from both OKT4+ and OKT8+ cells in patients with hypogammaglobulinemia
    • Thompson LF, Saxon A, O'Connor RD, Fox RI. Ecto-5′-nucleotidase activity in human T cell subsets. Decreased numbers of ecto-5′-nucleotidase positive cells from both OKT4+ and OKT8+ cells in patients with hypogammaglobulinemia. J Clin Invest 1983;71:892-899.
    • (1983) J Clin Invest , vol.71 , pp. 892-899
    • Thompson, L.F.1    Saxon, A.2    O'Connor, R.D.3    Fox, R.I.4
  • 24
    • 0017340224 scopus 로고
    • Quantitative measurements of T- and B-cell function in "variable" primary hypogammaglobulinemia: Evidence for a consistent B-cell defect
    • De La Concha EG, Oldham G, Webster ADB, Asherson GL, Platts-Mills TAE. Quantitative measurements of T- and B-cell function in "variable" primary hypogammaglobulinemia: evidence for a consistent B-cell defect. Clin Exp Immunol 1977;27:208-215.
    • (1977) Clin Exp Immunol , vol.27 , pp. 208-215
    • De La Concha, E.G.1    Oldham, G.2    Webster, A.D.B.3    Asherson, G.L.4    Platts-Mills, T.A.E.5
  • 25
    • 0027399081 scopus 로고
    • Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia
    • Tsukada S, et al. Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell 1993;71:279-290.
    • (1993) Cell , vol.71 , pp. 279-290
    • Tsukada, S.1
  • 26
    • 0018843739 scopus 로고
    • Histochemical evaluation of lymphocytes in hypogammaglobulinemia. Decreased number of 5′-nucleotidase-positive cells
    • Recker DP, Edwards NL, Fox IH. Histochemical evaluation of lymphocytes in hypogammaglobulinemia. Decreased number of 5′-nucleotidase-positive cells. J Lab Clin Med 1980;95:175-179.
    • (1980) J Lab Clin Med , vol.95 , pp. 175-179
    • Recker, D.P.1    Edwards, N.L.2    Fox, I.H.3
  • 27
    • 0018774326 scopus 로고
    • Histochemical studies for 5′-nucleotidase and alpha-naphthyl (non-specific) esterase in lymphocytes from patients with primary immunoglobulin deficiencies
    • Matamoros N, Horwitz DA, Newton C, Asherson GL, Webster ADB. Histochemical studies for 5′-nucleotidase and alpha-naphthyl (non-specific) esterase in lymphocytes from patients with primary immunoglobulin deficiencies. Clin Exp Immunol 1979;36:102-106.
    • (1979) Clin Exp Immunol , vol.36 , pp. 102-106
    • Matamoros, N.1    Horwitz, D.A.2    Newton, C.3    Asherson, G.L.4    Webster, A.D.B.5
  • 28
    • 0027501009 scopus 로고
    • lo (naive) CD8+ T lymphocytes
    • lo (naive) CD8+ T lymphocytes. J Immunol 1993;151:3961-3970.
    • (1993) J Immunol , vol.151 , pp. 3961-3970
    • Dianzani, U.1
  • 29
    • 1542696283 scopus 로고
    • Production of mAb to ecto-5′-nucleotidase: A glycosyl phosphatidylinositol-anchored differentiation antigen expressed on human T- and B-lymphocytes
    • Knapp W, et al. eds. New York: Oxford University Press
    • Thompson LF, Ruedi JM, Glass A, Lucas AH. Production of mAb to ecto-5′-nucleotidase: a glycosyl phosphatidylinositol-anchored differentiation antigen expressed on human T- and B-lymphocytes. In: Knapp W, et al. eds. Leucocyte Typing IV: white cell differentiation antigens. New York: Oxford University Press; 1989. p. 104-106.
    • (1989) Leucocyte Typing IV: White Cell Differentiation Antigens , pp. 104-106
    • Thompson, L.F.1    Ruedi, J.M.2    Glass, A.3    Lucas, A.H.4
  • 30
    • 0021275246 scopus 로고
    • Maternal isoimmunization resulting in an infant with combined immunodeficiency and fatal graft versus host disease
    • Bastian JF, Williams RA, Ornelas W, Tani P, Thompson LF. Maternal isoimmunization resulting in an infant with combined immunodeficiency and fatal graft versus host disease. Lancet 1984;1:1435-1437.
    • (1984) Lancet , vol.1 , pp. 1435-1437
    • Bastian, J.F.1    Williams, R.A.2    Ornelas, W.3    Tani, P.4    Thompson, L.F.5
  • 31
    • 0019498233 scopus 로고
    • Ecto-5′-nucleotidase deficiency: Association with adenosine deaminase deficiency and non-association with deoxyadenosine toxicity
    • Boss GR, Thompson LF, O'Connor RD, Ziering RW, Seegmiller JE. Ecto-5′-nucleotidase deficiency: Association with adenosine deaminase deficiency and non-association with deoxyadenosine toxicity. Clin Immunol Immunopathol 1981;19:1-7.
    • (1981) Clin Immunol Immunopathol , vol.19 , pp. 1-7
    • Boss, G.R.1    Thompson, L.F.2    O'Connor, R.D.3    Ziering, R.W.4    Seegmiller, J.E.5
  • 32
    • 0021750975 scopus 로고
    • Phenotype and function of engrafted maternal T cells in patients with severe combined immunodeficiency
    • Thompson LF, O'Connor RD, Bastian JF. Phenotype and function of engrafted maternal T cells in patients with severe combined immunodeficiency. J Immunol 1984;133:2513-2517.
    • (1984) J Immunol , vol.133 , pp. 2513-2517
    • Thompson, L.F.1    O'Connor, R.D.2    Bastian, J.F.3
  • 33
    • 0018912786 scopus 로고
    • Association of a lymphocyte purine enzyme deficiency (5′-nucleotidase) with combined immunodeficiency
    • Cohen A, Mansour A, Dosch H-M, Gelfand EW. Association of a lymphocyte purine enzyme deficiency (5′-nucleotidase) with combined immunodeficiency. Clin Immunol Immunopathol 1980;15: 245-250.
    • (1980) Clin Immunol Immunopathol , vol.15 , pp. 245-250
    • Cohen, A.1    Mansour, A.2    Dosch, H.-M.3    Gelfand, E.W.4
  • 34
    • 0021252765 scopus 로고
    • Absence of lymphocyte ecto-5′-nucleotidase in infants with reticuloendotheliosis and eosinophilia (Omenn's Syndrome)
    • Gelfand EW, McCurdy D, Rao CP, Cohen A. Absence of lymphocyte ecto-5′-nucleotidase in infants with reticuloendotheliosis and eosinophilia (Omenn's Syndrome). Blood 1984;63:1475-1480.
    • (1984) Blood , vol.63 , pp. 1475-1480
    • Gelfand, E.W.1    McCurdy, D.2    Rao, C.P.3    Cohen, A.4
  • 35
    • 0022371024 scopus 로고
    • Reduced ecto-5′-nucleoudase activity and enhanced OKT10 and HLA-DR expression on CD8 (T suppressor/cytotoxic) lymphocytes in the acquired immune deficiency syndrome: Evidence of CD8 cell immaturity
    • Salazar-Gonzalez JF, Moody DJ, Giorgi JV, Martinez-Maza O, Mitsuyasu RT, Fahey JL. Reduced ecto-5′-nucleoudase activity and enhanced OKT10 and HLA-DR expression on CD8 (T suppressor/cytotoxic) lymphocytes in the acquired immune deficiency syndrome: Evidence of CD8 cell immaturity. J Immunol 1985;135:1778-1785.
    • (1985) J Immunol , vol.135 , pp. 1778-1785
    • Salazar-Gonzalez, J.F.1    Moody, D.J.2    Giorgi, J.V.3    Martinez-Maza, O.4    Mitsuyasu, R.T.5    Fahey, J.L.6
  • 36
    • 0021687132 scopus 로고
    • Decreased 5′ nucleotidase activity in lymphocytes from asymptomatic sexually active homosexual men and patients with the acquired immune deficiency syndrome
    • Murray JL, Reuben JM, Munn CG, Mansell PW, Newell GR, Hersh EM. Decreased 5′ nucleotidase activity in lymphocytes from asymptomatic sexually active homosexual men and patients with the acquired immune deficiency syndrome. Blood 1984;64:1016-1021.
    • (1984) Blood , vol.64 , pp. 1016-1021
    • Murray, J.L.1    Reuben, J.M.2    Munn, C.G.3    Mansell, P.W.4    Newell, G.R.5    Hersh, E.M.6
  • 37
    • 0028830744 scopus 로고
    • A signaling pathway governing early thymocyte maturation
    • Anderson SJ, Perlmutter RM. A signaling pathway governing early thymocyte maturation. Immunol Today 1995;16:99-105.
    • (1995) Immunol Today , vol.16 , pp. 99-105
    • Anderson, S.J.1    Perlmutter, R.M.2
  • 38
    • 0028288925 scopus 로고
    • Lymphocyte ontogeny and activation in gene targeted mutant mice
    • Pfeffer K, Mak TW. Lymphocyte ontogeny and activation in gene targeted mutant mice. Annu Rev Immunol 1994;12:367-411.
    • (1994) Annu Rev Immunol , vol.12 , pp. 367-411
    • Pfeffer, K.1    Mak, T.W.2
  • 39
    • 0023545332 scopus 로고
    • Distribution of ecto-5′-nucleotidase on subsets of human T and B lymphocytes as detected by indirect immunofluorescence using goat antibodies
    • Thompson LF, Ruedi JM, Low MG, Clement LT. Distribution of ecto-5′-nucleotidase on subsets of human T and B lymphocytes as detected by indirect immunofluorescence using goat antibodies. J Immunol 1987;139:4042-4048.
    • (1987) J Immunol , vol.139 , pp. 4042-4048
    • Thompson, L.F.1    Ruedi, J.M.2    Low, M.G.3    Clement, L.T.4
  • 40
    • 0021261638 scopus 로고
    • Development and properties of a monoclonal antibody specific for human ecto-5′-nucleotidase
    • Kummer U, et al. Development and properties of a monoclonal antibody specific for human ecto-5′-nucleotidase. Immunobiology 1984;166:203-211.
    • (1984) Immunobiology , vol.166 , pp. 203-211
    • Kummer, U.1
  • 42
    • 0024428731 scopus 로고
    • Increased density of ecto-5′-nucleotidase antigen on leukemic T cells from patients with cutaneous T cell lymphoma and adult T cell leukemia/lymphoma
    • Fukunaga Y, et al. Increased density of ecto-5′-nucleotidase antigen on leukemic T cells from patients with cutaneous T cell lymphoma and adult T cell leukemia/lymphoma. Blood 1989;74:2486-2492.
    • (1989) Blood , vol.74 , pp. 2486-2492
    • Fukunaga, Y.1
  • 43
    • 0038720665 scopus 로고
    • CD73 workshop panel report
    • Schlossman SF, et al. eds. New York City: Oxford University Press, Inc.
    • Thompson LF, Laurent AB, Franklin MK, Gutensohn W, Resta R. CD73 workshop panel report. In: Schlossman SF, et al. eds. Leucocyte Typing V. New York City: Oxford University Press, Inc. 1995. p. 564-567.
    • (1995) Leucocyte Typing V , pp. 564-567
    • Thompson, L.F.1    Laurent, A.B.2    Franklin, M.K.3    Gutensohn, W.4    Resta, R.5
  • 44
    • 0027440443 scopus 로고
    • Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium
    • Airas L, Salmi M, Jalkanen S. Lymphocyte-vascular adhesion protein-2 is a novel 70-kDa molecule involved in lymphocyte adhesion to vascular endothelium. J Immunol 1993;151:4228-4238.
    • (1993) J Immunol , vol.151 , pp. 4228-4238
    • Airas, L.1    Salmi, M.2    Jalkanen, S.3
  • 45
    • 0025643373 scopus 로고
    • Immunolocalization of ecto-5′-nucleotidase in the kidney by a monoclonal antibody
    • Gandhi R, LeHir M, Kaissling B. Immunolocalization of ecto-5′-nucleotidase in the kidney by a monoclonal antibody. Histochemistry 1990;95:165-174.
    • (1990) Histochemistry , vol.95 , pp. 165-174
    • Gandhi, R.1    Lehir, M.2    Kaissling, B.3
  • 46
    • 0019985373 scopus 로고
    • Distribution of terminal deoxynucleotidyl transferase and purine degradative and synthetic enzymes in subpopulations of human thymocytes
    • Ma DDF, et al. Distribution of terminal deoxynucleotidyl transferase and purine degradative and synthetic enzymes in subpopulations of human thymocytes. J Immunol 1982;129:1430-1435.
    • (1982) J Immunol , vol.129 , pp. 1430-1435
    • Ma, D.D.F.1
  • 47
    • 0027520073 scopus 로고
    • Murine ecto-5′-nucleotidase (CD73): CDNA cloning and tissue distribution
    • Resta R, et al. Murine ecto-5′-nucleotidase (CD73): cDNA cloning and tissue distribution. Gene 1993;133:171-177.
    • (1993) Gene , vol.133 , pp. 171-177
    • Resta, R.1
  • 48
    • 0020668382 scopus 로고
    • Activity of cell-detached 5′-nucleotidase in thymocytes of various densities
    • Oleinik BV, Tarasova AA, Bezvershenko IA. Activity of cell-detached 5′-nucleotidase in thymocytes of various densities. Tsitologiia 1983;25:106-110.
    • (1983) Tsitologiia , vol.25 , pp. 106-110
    • Oleinik, B.V.1    Tarasova, A.A.2    Bezvershenko, I.A.3
  • 49
    • 0022474832 scopus 로고
    • Differential expression of ecto-5′-nucleotidase activity by functionally and phenotypically distinct subpopulations of human Leu-2+/T8+ lymphocytes
    • Dianzani U, Massaia M, Pileri A, Grossi CE, Clement LT. Differential expression of ecto-5′-nucleotidase activity by functionally and phenotypically distinct subpopulations of human Leu-2+/T8+ lymphocytes. J Immunol 1986;137:484-489.
    • (1986) J Immunol , vol.137 , pp. 484-489
    • Dianzani, U.1    Massaia, M.2    Pileri, A.3    Grossi, C.E.4    Clement, L.T.5
  • 50
    • 0029817963 scopus 로고    scopus 로고
    • CD73 mediates adhesion of B cells to follicular dendritic cells
    • Airas L, Jalkanen S. CD73 mediates adhesion of B cells to follicular dendritic cells. Blood 1996;88:1755-1764.
    • (1996) Blood , vol.88 , pp. 1755-1764
    • Airas, L.1    Jalkanen, S.2
  • 51
    • 0018128739 scopus 로고
    • 5′-nucleotidase activity in subpopulations of rat lymphocytes
    • Barton RW, Goldschneider I. 5′-nucleotidase activity in subpopulations of rat lymphocytes. J Immunol 1978;121:2329-2334.
    • (1978) J Immunol , vol.121 , pp. 2329-2334
    • Barton, R.W.1    Goldschneider, I.2
  • 52
    • 0024594290 scopus 로고
    • Functional characterization of ecto-5′-nucleotidase positive and negative human T lymphocytes
    • Thompson LF, Ruedi JM. Functional characterization of ecto-5′-nucleotidase positive and negative human T lymphocytes. J Immunol 1989;142:1518-1522.
    • (1989) J Immunol , vol.142 , pp. 1518-1522
    • Thompson, L.F.1    Ruedi, J.M.2
  • 53
    • 0023681163 scopus 로고
    • Synthesis of immunoglobulin G by pokeweed mitogen- or Epstein-Barr virus-stimulated human B cells in vitro is restricted to the ecto-5′-nucleotidase positive subset
    • Thompson LF, Ruedi JM. Synthesis of immunoglobulin G by pokeweed mitogen- or Epstein-Barr virus-stimulated human B cells in vitro is restricted to the ecto-5′-nucleotidase positive subset. J Clin Invest 1988;82:902-905.
    • (1988) J Clin Invest , vol.82 , pp. 902-905
    • Thompson, L.F.1    Ruedi, J.M.2
  • 54
    • 0025787038 scopus 로고
    • Expression of 5′-nucleotidase (CD73) related to other differentiation antigens in leukemias of B-cell lineage
    • Pieters R, et al. Expression of 5′-nucleotidase (CD73) related to other differentiation antigens in leukemias of B-cell lineage. Blood 1991;78:488-492.
    • (1991) Blood , vol.78 , pp. 488-492
    • Pieters, R.1
  • 55
    • 0022355056 scopus 로고
    • Prognostic value of 5′nucleotidase in acute lymphoblastic leukemia with the common-all phenotype
    • Veerman AJP, Hogeman PHG, van Zantwijk CH, Bezemer PD. Prognostic value of 5′nucleotidase in acute lymphoblastic leukemia with the common-all phenotype. Leuk Res 1985;9:1227-1229.
    • (1985) Leuk Res , vol.9 , pp. 1227-1229
    • Veerman, A.J.P.1    Hogeman, P.H.G.2    Van Zantwijk, C.H.3    Bezemer, P.D.4
  • 56
    • 0025086770 scopus 로고
    • Prognostic implication of ecto-5′-nucleotidase activity in acute lymphoblastic leukemia
    • Gutensohn W, Thiel E. Prognostic implication of ecto-5′-nucleotidase activity in acute lymphoblastic leukemia. Cancer 1990;66:1755-1758.
    • (1990) Cancer , vol.66 , pp. 1755-1758
    • Gutensohn, W.1    Thiel, E.2
  • 57
    • 0026806087 scopus 로고
    • Relation of 5′-nucleotidase and phosphatase activities with immunophenoptype, drug resistance and dinical prognosis in childhood leukemia
    • Pieters R, et al. Relation of 5′-nucleotidase and phosphatase activities with immunophenoptype, drug resistance and dinical prognosis in childhood leukemia. Leuk Res 1992;16:873-880.
    • (1992) Leuk Res , vol.16 , pp. 873-880
    • Pieters, R.1
  • 59
    • 0029835821 scopus 로고    scopus 로고
    • Evidence for the involvement of ecto-5′-nucleotidase (CD73) in drug resistance
    • Ujházy P, et al. Evidence for the involvement of ecto-5′-nucleotidase (CD73) in drug resistance. Int J Cancer 1996;68:493-500.
    • (1996) Int J Cancer , vol.68 , pp. 493-500
    • Ujházy, P.1
  • 60
    • 0018859942 scopus 로고
    • Selective release of plasma-membrane enzymes from rat hepatocytes by a phosphatidylinositol-specific phospholipase C
    • Shukla SD, Coleman R, Finean JB, Michell RH. Selective release of plasma-membrane enzymes from rat hepatocytes by a phosphatidylinositol-specific phospholipase C. Biochem J 1980;187:277-280.
    • (1980) Biochem J , vol.187 , pp. 277-280
    • Shukla, S.D.1    Coleman, R.2    Finean, J.B.3    Michell, R.H.4
  • 62
    • 0025709722 scopus 로고
    • Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form
    • Misumi Y, Ogata S, Ohkubo K, Hirose S, Ikehara Y. Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form. Eur J Biochem 1990;191:563-569.
    • (1990) Eur J Biochem , vol.191 , pp. 563-569
    • Misumi, Y.1    Ogata, S.2    Ohkubo, K.3    Hirose, S.4    Ikehara, Y.5
  • 63
    • 0026681419 scopus 로고
    • Soluble low-Km 5′-nucleotidase from electric-ray (Torpedo marmorata) electric organ and bovine cerebral cortex is derived from the glycosyl-phosphatidylinositol-anchored ecto-enzyme by phospholipase C cleavage
    • Vogel M, Kowalewski H, Zimmermann H, Hooper NM, Turner AJ. Soluble low-Km 5′-nucleotidase from electric-ray (Torpedo marmorata) electric organ and bovine cerebral cortex is derived from the glycosyl-phosphatidylinositol-anchored ecto-enzyme by phospholipase C cleavage. Biochem J 1992;284:621-624.
    • (1992) Biochem J , vol.284 , pp. 621-624
    • Vogel, M.1    Kowalewski, H.2    Zimmermann, H.3    Hooper, N.M.4    Turner, A.J.5
  • 64
    • 0025004134 scopus 로고
    • Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid
    • Misumi Y, Ogata S, Hirose S, Ikehara Y. Primary structure of rat liver 5′-nucleotidase deduced from the cDNA. Presence of the COOH-terminal hydrophobic domain for possible post-translational modification by glycophospholipid. J Biol Chem 1990;265:2178-2183.
    • (1990) J Biol Chem , vol.265 , pp. 2178-2183
    • Misumi, Y.1    Ogata, S.2    Hirose, S.3    Ikehara, Y.4
  • 65
    • 0027316045 scopus 로고
    • Purification and cDNA cloning of bovine liver 5′-nucleotidase, a GPI-anchored protein, and its expression in COS cells
    • Tokyo
    • Suzuki K, et al. Purification and cDNA cloning of bovine liver 5′-nucleotidase, a GPI-anchored protein, and its expression in COS cells. J Biochem (Tokyo) 1993;113:607-613.
    • (1993) J Biochem , vol.113 , pp. 607-613
    • Suzuki, K.1
  • 66
    • 0026343113 scopus 로고
    • 5′-Nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes
    • Volknandt W, Vogel M, Pevsner J, Misumi Y, Ikehara Y, Zimmermann H. 5′-Nucleotidase from the electric ray electric lobe. Primary structure and relation to mammalian and procaryotic enzymes. Eur J Biochem 1991;202:855-861.
    • (1991) Eur J Biochem , vol.202 , pp. 855-861
    • Volknandt, W.1    Vogel, M.2    Pevsner, J.3    Misumi, Y.4    Ikehara, Y.5    Zimmermann, H.6
  • 67
    • 0026013817 scopus 로고
    • Phosphatidylinositol membrane anchors and T-cell activation
    • Robinson PJ. Phosphatidylinositol membrane anchors and T-cell activation. Immunol Today 1991;12:35-41.
    • (1991) Immunol Today , vol.12 , pp. 35-41
    • Robinson, P.J.1
  • 68
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown D. The tyrosine kinase connection: how GPI-anchored proteins activate T cells. Curr Opin Immunol 1993;5:349-354.
    • (1993) Curr Opin Immunol , vol.5 , pp. 349-354
    • Brown, D.1
  • 69
    • 0014940795 scopus 로고
    • Preparation and properties of 5′-nucleotidase from smooth muscle of small intestine
    • Burger RM, Lowenstein JM. Preparation and properties of 5′-nucleotidase from smooth muscle of small intestine. J Biol Chem 1970;245:6274-6280.
    • (1970) J Biol Chem , vol.245 , pp. 6274-6280
    • Burger, R.M.1    Lowenstein, J.M.2
  • 70
    • 0022622216 scopus 로고
    • Human placental cytoplasmic 5′-nucleotidase
    • Madrid-Marina V, Fox IH. Human placental cytoplasmic 5′-nucleotidase. J Biol Chem 1986;261:444-452.
    • (1986) J Biol Chem , vol.261 , pp. 444-452
    • Madrid-Marina, V.1    Fox, I.H.2
  • 71
    • 0024592380 scopus 로고
    • Human placental ecto-5′-nucleotidase: Isoforms and chemical crosslinking products of the membrane-bound and isolated enzyme
    • Buschette-Brambrink S, Gutensohn W. Human placental ecto-5′-nucleotidase: isoforms and chemical crosslinking products of the membrane-bound and isolated enzyme. Biol Chem Hoppe Seyler 1989;370:67-74.
    • (1989) Biol Chem Hoppe Seyler , vol.370 , pp. 67-74
    • Buschette-Brambrink, S.1    Gutensohn, W.2
  • 72
    • 0023227996 scopus 로고
    • Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C
    • Thompson LF, Ruedi JM, Low MG. Purification of 5′-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C. Biochem Biophys Res Commun 1987;145: 118-125.
    • (1987) Biochem Biophys Res Commun , vol.145 , pp. 118-125
    • Thompson, L.F.1    Ruedi, J.M.2    Low, M.G.3
  • 73
    • 0028838712 scopus 로고
    • CD73 is involved in lymphocyte binding to the endothelium: Characterization of lymphocyte vascular adhesion protein 2 identifies it as CD73
    • Airas L, et al. CD73 is involved in lymphocyte binding to the endothelium: Characterization of lymphocyte vascular adhesion protein 2 identifies it as CD73. J Exp Med 1995;182:1603-1608.
    • (1995) J Exp Med , vol.182 , pp. 1603-1608
    • Airas, L.1
  • 74
    • 0023389627 scopus 로고
    • Purification, characterization and cellular localization of 5′-nucleotidase from Torpedo electric organ
    • Grondai EJM, Zimmermann H. Purification, characterization and cellular localization of 5′-nucleotidase from Torpedo electric organ. Biochem J 1987;245:805-810.
    • (1987) Biochem J , vol.245 , pp. 805-810
    • Grondai, E.J.M.1    Zimmermann, H.2
  • 75
    • 0024317286 scopus 로고
    • Regional localization of human ecto-5′-nucleotidase to chromosome 6q14-q21
    • Boyle JM, Hey Y, Grzeschik K-H. Thompson L, Munro E, Fox M. Regional localization of human ecto-5′-nucleotidase to chromosome 6q14-q21. Hum Genet 1989;83:179-180.
    • (1989) Hum Genet , vol.83 , pp. 179-180
    • Boyle, J.M.1    Hey, Y.2    Grzeschik, K.-H.3    Thompson, L.4    Munro, E.5    Fox, M.6
  • 76
    • 0025072285 scopus 로고
    • Glycosylation and processing of carbohydrate side chains of ecto-5′-nucleotidase in cultured human chorionic cells
    • Burgemeister R, Danescu I, Gutensohn W. Glycosylation and processing of carbohydrate side chains of ecto-5′-nucleotidase in cultured human chorionic cells. Biol Chem Hoppe Seyler 1990;371:355-361.
    • (1990) Biol Chem Hoppe Seyler , vol.371 , pp. 355-361
    • Burgemeister, R.1    Danescu, I.2    Gutensohn, W.3
  • 77
    • 0021009420 scopus 로고
    • Purification and properties of bovine liver plasma membrane 5′-nucleotidase
    • Harb J, Meflah K, Duflos Y, Bernard S. Purification and properties of bovine liver plasma membrane 5′-nucleotidase. Eur J Biochem 1983;137:131-138.
    • (1983) Eur J Biochem , vol.137 , pp. 131-138
    • Harb, J.1    Meflah, K.2    Duflos, Y.3    Bernard, S.4
  • 78
    • 17344372126 scopus 로고
    • Structure-function relationships in the CD73 molecule
    • Schlossman SF, et al. eds. New York City: Oxford University Press, Inc.
    • Gutensohn W, Resta R, Misumi Y, Ikehara Y, Thompson LF. Structure-function relationships in the CD73 molecule. In: Schlossman SF, et al. eds. Leucocyte Typing V. New York City: Oxford University Press, Inc. 1995. p. 567-568.
    • (1995) Leucocyte Typing V , pp. 567-568
    • Gutensohn, W.1    Resta, R.2    Misumi, Y.3    Ikehara, Y.4    Thompson, L.F.5
  • 79
    • 0031025034 scopus 로고    scopus 로고
    • Insights into thymic purine metabolism and adenosine deaminase deficiency revealed by transgenic mice over expressing ecto-5′-nucleotidase (CD73)
    • Resta R, et al. Insights into thymic purine metabolism and adenosine deaminase deficiency revealed by transgenic mice over expressing ecto-5′-nucleotidase (CD73). J Clin Invest 1997;99:676-683.
    • (1997) J Clin Invest , vol.99 , pp. 676-683
    • Resta, R.1
  • 80
    • 0026646193 scopus 로고
    • Adenosine levels in the postimplantation mouse uterus: Quantitation by HPLC-fluorometric detection and spatiotemporal regulation by 5′-nucleotidase and adenosine deaminase
    • Blackburn MR, Gao X, Airhart MJ, Skalko RG, Thompson LF, Knudsen TB. Adenosine levels in the postimplantation mouse uterus: quantitation by HPLC-fluorometric detection and spatiotemporal regulation by 5′-nucleotidase and adenosine deaminase. Dev Dyn 1992;194:155-168.
    • (1992) Dev Dyn , vol.194 , pp. 155-168
    • Blackburn, M.R.1    Gao, X.2    Airhart, M.J.3    Skalko, R.G.4    Thompson, L.F.5    Knudsen, T.B.6
  • 81
    • 0025944542 scopus 로고
    • Adenosine in vertebrate retina: Localization, receptor characterization, and function
    • Blazynski C, Perez MR. Adenosine in vertebrate retina: Localization, receptor characterization, and function. Cell Mol Neurobiol 1991;11:463-484.
    • (1991) Cell Mol Neurobiol , vol.11 , pp. 463-484
    • Blazynski, C.1    Perez, M.R.2
  • 82
    • 0019509057 scopus 로고
    • An immunomorphologic study of adenosine deaminase distribution in human thymus tissue, normal lymphocytes, and hematopoietic cell lines
    • Chechik BE, Schrader WP, Minowada J. An immunomorphologic study of adenosine deaminase distribution in human thymus tissue, normal lymphocytes, and hematopoietic cell lines. J Immunol 1981;126:1003-1007.
    • (1981) J Immunol , vol.126 , pp. 1003-1007
    • Chechik, B.E.1    Schrader, W.P.2    Minowada, J.3
  • 83
    • 0031570040 scopus 로고    scopus 로고
    • Adenosine metabolism during phorbol myristate acetate-mediated induction of HL-60 cell difference - Changes in expression pattern of adenosine kinase, adenosine deaminase, and 5′-nucleotidase
    • Spychala J, Mitchell BS, Barankiewicz J. Adenosine metabolism during phorbol myristate acetate-mediated induction of HL-60 cell difference - Changes in expression pattern of adenosine kinase, adenosine deaminase, and 5′-nucleotidase. J Immunol 1997;158:4947-4952.
    • (1997) J Immunol , vol.158 , pp. 4947-4952
    • Spychala, J.1    Mitchell, B.S.2    Barankiewicz, J.3
  • 84
    • 0029559205 scopus 로고
    • Isolation and characterization of the promoter of the human 5′-nucleotidase (CD73)-encoding gene
    • Hansen KR, Resta R, Webb CF, Thompson LF. Isolation and characterization of the promoter of the human 5′-nucleotidase (CD73)-encoding gene. Gene 1995;167:307-312.
    • (1995) Gene , vol.167 , pp. 307-312
    • Hansen, K.R.1    Resta, R.2    Webb, C.F.3    Thompson, L.F.4
  • 85
    • 0030588705 scopus 로고    scopus 로고
    • Selective induction of CD73 expression in human lymphocytes by CD38 ligation - A novel pathway linking signal transducers with ecto-enzyme activities
    • Peola S, Borrione P, Matera L, Malavasi F, Pileri A, Massaia M. Selective induction of CD73 expression in human lymphocytes by CD38 ligation - A novel pathway linking signal transducers with ecto-enzyme activities. J Immunol 1996;157:4354-4362.
    • (1996) J Immunol , vol.157 , pp. 4354-4362
    • Peola, S.1    Borrione, P.2    Matera, L.3    Malavasi, F.4    Pileri, A.5    Massaia, M.6
  • 86
    • 0016819538 scopus 로고
    • Action of 5′-nucleotidase in the uptake of adenosine from AMP by human lymphocytes
    • Fleit H, Conklyn M, Stebbins RD, Silber R. Action of 5′-nucleotidase in the uptake of adenosine from AMP by human lymphocytes. J Biol Chem 1975;23:8889-8892.
    • (1975) J Biol Chem , vol.23 , pp. 8889-8892
    • Fleit, H.1    Conklyn, M.2    Stebbins, R.D.3    Silber, R.4
  • 87
    • 0021809695 scopus 로고
    • Ecto-5′-nucleotidase can provide the total purine requirements of mitogen-stimulated human T cells and rapidly dividing human B lymphoblastoid cells
    • Thompson LF. Ecto-5′-nucleotidase can provide the total purine requirements of mitogen-stimulated human T cells and rapidly dividing human B lymphoblastoid cells. J Immunol 1985;134:3794-3797.
    • (1985) J Immunol , vol.134 , pp. 3794-3797
    • Thompson, L.F.1
  • 88
    • 0016261604 scopus 로고
    • Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. I. Evidence for an ecto-adenosine monophosphatase, adenosine triphosphatase, and -p-nitrophenyl phosphates
    • DePierre TW, Karnovsky ML. Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. I. Evidence for an ecto-adenosine monophosphatase, adenosine triphosphatase, and -p-nitrophenyl phosphates. J Biol Chem 1974;249:7111-7120.
    • (1974) J Biol Chem , vol.249 , pp. 7111-7120
    • DePierre, T.W.1    Karnovsky, M.L.2
  • 89
    • 0025326815 scopus 로고
    • Cardiovascular purinoceptors
    • Olsson RA, Pearson D. Cardiovascular purinoceptors. Physiol Rev 1990;70:761-845.
    • (1990) Physiol Rev , vol.70 , pp. 761-845
    • Olsson, R.A.1    Pearson, D.2
  • 90
    • 0024214165 scopus 로고
    • Adenosine receptors: Clinical implications and biochemical mechanisms
    • Ramkumar V, Pierson G, Stiles G. Adenosine receptors: clinical implications and biochemical mechanisms. Prog Drug Res 1988;32:195-247.
    • (1988) Prog Drug Res , vol.32 , pp. 195-247
    • Ramkumar, V.1    Pierson, G.2    Stiles, G.3
  • 91
    • 0022397930 scopus 로고
    • Adenosine: A physiologic modulator of superoxide anion generation by human neutrophils. Adenosine acts via an A2 receptor on human neutrophils
    • Cronstein BN, Rosenstein ED, Kramer SB, Weissmann G, Hirschhorn R. Adenosine: A physiologic modulator of superoxide anion generation by human neutrophils. Adenosine acts via an A2 receptor on human neutrophils. J Immunol 1985;135:1366-1371.
    • (1985) J Immunol , vol.135 , pp. 1366-1371
    • Cronstein, B.N.1    Rosenstein, E.D.2    Kramer, S.B.3    Weissmann, G.4    Hirschhorn, R.5
  • 92
    • 0027337474 scopus 로고
    • 3 adenosine receptor is the unique adenosine receptor which facilitates release of allergic mediators in mast cells
    • 3 adenosine receptor is the unique adenosine receptor which facilitates release of allergic mediators in mast cells. J Biol Chem 1993;268:16887-16890.
    • (1993) J Biol Chem , vol.268 , pp. 16887-16890
    • Ramkumar, V.1    Stiles, G.L.2    Beaven, M.A.3    Ali, H.4
  • 94
    • 33748918019 scopus 로고    scopus 로고
    • Adenosine receptor expression in developing murine thymus
    • Abstract
    • Jiang H, Puffinbarger NK, Resta R, Thompson LF. Adenosine receptor expression in developing murine thymus. FASEB J 1996;10:A1047(Abstract).
    • (1996) FASEB J , vol.10
    • Jiang, H.1    Puffinbarger, N.K.2    Resta, R.3    Thompson, L.F.4
  • 95
    • 0029018445 scopus 로고
    • Production and characterization of multiple antigenic peptide antibodies to the adenosine A-2b receptor
    • Puffinbarger NK, et al. Production and characterization of multiple antigenic peptide antibodies to the adenosine A-2b receptor. Mol Pharmacol 1995;47:1126-1132.
    • (1995) Mol Pharmacol , vol.47 , pp. 1126-1132
    • Puffinbarger, N.K.1
  • 98
    • 0026732707 scopus 로고
    • Molecular cloning and characterization of an adenosine receptor: The A3 adenosine receptor
    • Zhou Q, Li C, Olah ME, Johnson RA, Stiles GL, Civelli O. Molecular cloning and characterization of an adenosine receptor: The A3 adenosine receptor. Proc Natl Acad Sci USA 1992;89:7432-7436.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7432-7436
    • Zhou, Q.1    Li, C.2    Olah, M.E.3    Johnson, R.A.4    Stiles, G.L.5    Civelli, O.6
  • 99
    • 0027258364 scopus 로고
    • 5′-AMP is the neutrophil derived paracrine factor that elicits chloride secretion from T84 intestinal epithelial cell monolayers
    • Madara JL, et al. 5′-AMP is the neutrophil derived paracrine factor that elicits chloride secretion from T84 intestinal epithelial cell monolayers. J Clin Invest 1993;91:2320-2325.
    • (1993) J Clin Invest , vol.91 , pp. 2320-2325
    • Madara, J.L.1
  • 100
    • 0028985715 scopus 로고
    • 2b adenosine receptor mediates cAMP responses to adenosine receptor agonists in human intestinal epithelia
    • 2b adenosine receptor mediates cAMP responses to adenosine receptor agonists in human intestinal epithelia. J Biol Chem 1995;270:2387-2394.
    • (1995) J Biol Chem , vol.270 , pp. 2387-2394
    • Strohmeier, G.R.1    Reppert, S.M.2    Lencer, W.I.3    Madara, J.L.4
  • 101
    • 0027471927 scopus 로고
    • Ishemic preconditioning increases adenosine release and 5′-nucleotidase activity during myocardial ischemia and reperfusion in dogs
    • Kitakaze M, Masatsugu H, Takashima S, Sato H, Michitoshi I, Kamada T. Ishemic preconditioning increases adenosine release and 5′-nucleotidase activity during myocardial ischemia and reperfusion in dogs. Circulation 1993;87:208-215.
    • (1993) Circulation , vol.87 , pp. 208-215
    • Kitakaze, M.1    Masatsugu, H.2    Takashima, S.3    Sato, H.4    Michitoshi, I.5    Kamada, T.6
  • 102
    • 0028212002 scopus 로고
    • Infarct size-limiting effect of ischemic preconditioning is blunted by inhibition of 5′-nucleotidase activity and attenuation of adenosine release
    • Kitakaze M, et al. Infarct size-limiting effect of ischemic preconditioning is blunted by inhibition of 5′-nucleotidase activity and attenuation of adenosine release. Circulation 1994;89:1237-1246.
    • (1994) Circulation , vol.89 , pp. 1237-1246
    • Kitakaze, M.1
  • 103
    • 0025024913 scopus 로고
    • Agents that elevate cAMP stimulate DNA fragmentation in thymocytes
    • McConkey DJ, Orrenius S, Jondal M. Agents that elevate cAMP stimulate DNA fragmentation in thymocytes. J Immunol 1990;145:1227-1230.
    • (1990) J Immunol , vol.145 , pp. 1227-1230
    • McConkey, D.J.1    Orrenius, S.2    Jondal, M.3
  • 104
    • 0025230674 scopus 로고
    • Adenosine receptor-mediated accumulation of cyclic AMP-induced T lymphocyte death through internucleosomal DNA cleavage
    • Kizaki H, Suzuki K, Tadakuma T, Ishimura Y. Adenosine receptor-mediated accumulation of cyclic AMP-induced T lymphocyte death through internucleosomal DNA cleavage. J Biol Chem 1990;265:5280-5284.
    • (1990) J Biol Chem , vol.265 , pp. 5280-5284
    • Kizaki, H.1    Suzuki, K.2    Tadakuma, T.3    Ishimura, Y.4
  • 105
    • 0030025256 scopus 로고    scopus 로고
    • Block of T lymphocyte differentiation by activation of the cAMP-dependent signal transduction pathway
    • Lalli E, Sassone-Corsi P, Ceredig R. Block of T lymphocyte differentiation by activation of the cAMP-dependent signal transduction pathway. EMBO J 1996;15:528-537.
    • (1996) EMBO J , vol.15 , pp. 528-537
    • Lalli, E.1    Sassone-Corsi, P.2    Ceredig, R.3
  • 106
    • 0030837064 scopus 로고    scopus 로고
    • SCID: The role of adenosine deaminase deficiency
    • Resta R, Thompson LF. SCID: the role of adenosine deaminase deficiency. Immunol Today 1997;18:371-374.
    • (1997) Immunol Today , vol.18 , pp. 371-374
    • Resta, R.1    Thompson, L.F.2
  • 107
    • 0029005278 scopus 로고
    • Disruption of the adenosine deaminase gene causes hepatocellular impairment and perinatal lethality in mice
    • Wakamiya M, et al. Disruption of the adenosine deaminase gene causes hepatocellular impairment and perinatal lethality in mice. Proc Natl Acad Sci USA 1995;92:3673-3677.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3673-3677
    • Wakamiya, M.1
  • 108
    • 0029039360 scopus 로고
    • Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death
    • Migchielsen AAJ, et al. Adenosine-deaminase-deficient mice die perinatally and exhibit liver-cell degeneration, atelectasis and small intestinal cell death. Nat Genet 1995;10:279-287.
    • (1995) Nat Genet , vol.10 , pp. 279-287
    • Migchielsen, A.A.J.1
  • 109
    • 0029946223 scopus 로고    scopus 로고
    • Metabolic and immunologic consequences of limited adenosine deaminase expression in mice
    • Blackburn MR, Datta SK, Wakamiya M, Vartabedian BS, Kellems RE. Metabolic and immunologic consequences of limited adenosine deaminase expression in mice. J Biol Chem 1996;271:15203-15210.
    • (1996) J Biol Chem , vol.271 , pp. 15203-15210
    • Blackburn, M.R.1    Datta, S.K.2    Wakamiya, M.3    Vartabedian, B.S.4    Kellems, R.E.5
  • 110
    • 0030878807 scopus 로고    scopus 로고
    • Role of A2a extracellular adenosine receptor-mediated signaling in adenosine-mediated inhibition of T-cell activation and expansion
    • Huang S, Apasov S, Koshiba M, Sitkovsky M. Role of A2a extracellular adenosine receptor-mediated signaling in adenosine-mediated inhibition of T-cell activation and expansion. Blood 1997;90:1600-1610.
    • (1997) Blood , vol.90 , pp. 1600-1610
    • Huang, S.1    Apasov, S.2    Koshiba, M.3    Sitkovsky, M.4
  • 111
    • 0024456069 scopus 로고
    • Antibodies to 5′-nucleotidase (CD73), a glycosyl-phosphatidylinositol-anchored protein, cause human peripheral blood T cells to proliferate
    • Thompson LF, Ruedi JM, Glass A, Low MG, Lucas AH. Antibodies to 5′-nucleotidase (CD73), a glycosyl-phosphatidylinositol-anchored protein, cause human peripheral blood T cells to proliferate. J Immunol 1989;143:1815-1821.
    • (1989) J Immunol , vol.143 , pp. 1815-1821
    • Thompson, L.F.1    Ruedi, J.M.2    Glass, A.3    Low, M.G.4    Lucas, A.H.5
  • 112
    • 0025053145 scopus 로고
    • Human T cell activation: Synergy between CD73 (ecto-5′-nucleotidase) and signals delivered through CD8 and CD2 molecules
    • Massaia M, et al. Human T cell activation: synergy between CD73 (ecto-5′-nucleotidase) and signals delivered through CD8 and CD2 molecules. J Immunol 1990;145:1664-1674.
    • (1990) J Immunol , vol.145 , pp. 1664-1674
    • Massaia, M.1
  • 113
    • 0021840708 scopus 로고
    • Human T cell activation. A new activation pathway used by a major T cell population via a disulfide-bonded dimer of a 44 kilodalton polypeptide (9.3 antigen)
    • Hara T, Fu SM, Hansen JA. Human T cell activation. A new activation pathway used by a major T cell population via a disulfide-bonded dimer of a 44 kilodalton polypeptide (9.3 antigen). J Exp Med 1985;161:1513-1524.
    • (1985) J Exp Med , vol.161 , pp. 1513-1524
    • Hara, T.1    Fu, S.M.2    Hansen, J.A.3
  • 114
    • 0022990811 scopus 로고
    • Anchoring of membrane proteins via phosphatidylinositol is deficient in two classes of Thy-1 negative mutant lymphoma cells
    • Conzelmann A, Spiazzi A, Hyman R, Bron C. Anchoring of membrane proteins via phosphatidylinositol is deficient in two classes of Thy-1 negative mutant lymphoma cells. EMBO J 1986;5:3291-3296.
    • (1986) EMBO J , vol.5 , pp. 3291-3296
    • Conzelmann, A.1    Spiazzi, A.2    Hyman, R.3    Bron, C.4
  • 115
    • 0022453690 scopus 로고
    • The expression, function, and ontogeny of a novel T cell-activating protein, TAP, in the thymus
    • Yeh ETH, Reiser H, Benacerraf B, Rock KL. The expression, function, and ontogeny of a novel T cell-activating protein, TAP, in the thymus. J Immunol 1986;137:1232-1238.
    • (1986) J Immunol , vol.137 , pp. 1232-1238
    • Yeh, E.T.H.1    Reiser, H.2    Benacerraf, B.3    Rock, K.L.4
  • 116
    • 0029073090 scopus 로고
    • Distinct roles for the costimulaotry ligands B7-1 and B7-2 in T helper cell differentiation?
    • Thompson CB. Distinct roles for the costimulaotry ligands B7-1 and B7-2 in T helper cell differentiation? Cell 1995;81:979-982.
    • (1995) Cell , vol.81 , pp. 979-982
    • Thompson, C.B.1
  • 117
    • 0022500156 scopus 로고
    • Role of Ly-6 in lymphocyte activation. Induction of T cell activation by monoclonal anti-Ly-6 antibodies
    • Malek TR, Ortega G, Chan C, Kroczek RA, Shevach EM. Role of Ly-6 in lymphocyte activation. Induction of T cell activation by monoclonal anti-Ly-6 antibodies. J Exp Med 1986;164:709-722.
    • (1986) J Exp Med , vol.164 , pp. 709-722
    • Malek, T.R.1    Ortega, G.2    Chan, C.3    Kroczek, R.A.4    Shevach, E.M.5
  • 118
    • 0024322167 scopus 로고
    • Anti-Qa-2-induced T cell activation: The parameters of activation, the definition of mitogenic and nonmitogenic antibodies, and the differential effects on CD4+ vs CD8+ T cells
    • Hahn AB, Soloski MJ. Anti-Qa-2-induced T cell activation: the parameters of activation, the definition of mitogenic and nonmitogenic antibodies, and the differential effects on CD4+ vs CD8+ T cells. J Immunol 1989;143:407-413.
    • (1989) J Immunol , vol.143 , pp. 407-413
    • Hahn, A.B.1    Soloski, M.J.2
  • 119
    • 0023154034 scopus 로고
    • Polyclonal activation of rat T lymphocytes by RT6 alloantisera
    • Wonigeit K, Schwinzer R. Polyclonal activation of rat T lymphocytes by RT6 alloantisera. Transplant Proc 1987;XIX: 296-299.
    • (1987) Transplant Proc , vol.19 , pp. 296-299
    • Wonigeit, K.1    Schwinzer, R.2
  • 120
    • 0027155120 scopus 로고
    • Identification of the T cell surface signal-transducing glycoprotein sgp-60 as CD48, a counter-receptor for mouse CD2
    • Kato K, Tamura N, Okumura K, Yagita H. Identification of the T cell surface signal-transducing glycoprotein sgp-60 as CD48, a counter-receptor for mouse CD2. Eur J Immunol 1993;23:1412-1415.
    • (1993) Eur J Immunol , vol.23 , pp. 1412-1415
    • Kato, K.1    Tamura, N.2    Okumura, K.3    Yagita, H.4
  • 121
    • 0023681070 scopus 로고
    • Decay-accelerating factor functions as a signal transducing molecule for human T cells
    • Davis LS, Patel SS, Atkinson JP, Lipsky PE. Decay-accelerating factor functions as a signal transducing molecule for human T cells. J Immunol 1988;141:2246-2252.
    • (1988) J Immunol , vol.141 , pp. 2246-2252
    • Davis, L.S.1    Patel, S.S.2    Atkinson, J.P.3    Lipsky, P.E.4
  • 122
    • 0024414253 scopus 로고
    • 20 KDa homologous restriction factor of complement resembles T cell activating protein
    • Okada H, et al. 20 KDa homologous restriction factor of complement resembles T cell activating protein. Biochem Biophys Res Commun 1989;162: 1553-1559.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 1553-1559
    • Okada, H.1
  • 123
    • 0028342990 scopus 로고
    • Glycosyl phosphatidylinositol membrane anchor is not required for T cell activation through CD73
    • Resta R, et al. Glycosyl phosphatidylinositol membrane anchor is not required for T cell activation through CD73. J Immunol 1994;153:1046-1053.
    • (1994) J Immunol , vol.153 , pp. 1046-1053
    • Resta, R.1
  • 124
    • 0028940901 scopus 로고
    • Ecto-5′-nucleotidase activity is not required for T cell activation through CD73
    • Gutensohn W, Resta R, Misumi Y, Ikehara Y, Thompson LF. Ecto-5′-nucleotidase activity is not required for T cell activation through CD73. Cell Immunol 1995;161:213-217.
    • (1995) Cell Immunol , vol.161 , pp. 213-217
    • Gutensohn, W.1    Resta, R.2    Misumi, Y.3    Ikehara, Y.4    Thompson, L.F.5
  • 125
    • 0025781252 scopus 로고
    • Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ
    • Vogel M, Kowalewski HJ, Zimmermann H, Janetzko A, Margolis RU, Wollny HE. Association of the HNK-1 epitope with 5′-nucleotidase from Torpedo marmorata (electric ray) electric organ. Biochem J 1991;278:199-202.
    • (1991) Biochem J , vol.278 , pp. 199-202
    • Vogel, M.1    Kowalewski, H.J.2    Zimmermann, H.3    Janetzko, A.4    Margolis, R.U.5    Wollny, H.E.6
  • 126
    • 0024458171 scopus 로고
    • Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin
    • Stochaj U, Dieckhoff J, Mollenhauer J, Cramer M, Mannherz HG. Evidence for the direct interaction of chicken gizzard 5′-nucleotidase with laminin and fibronectin. Biochim Biophys Acta 1989;992:385-392.
    • (1989) Biochim Biophys Acta , vol.992 , pp. 385-392
    • Stochaj, U.1    Dieckhoff, J.2    Mollenhauer, J.3    Cramer, M.4    Mannherz, H.G.5
  • 127
    • 0022466757 scopus 로고
    • The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5′-nucleotidase from chicken gizzard smooth muscle
    • Dieckhoff J, Mollenhauer J, Kuhl U, Niggemeyer B, von der Mark K, Mannherz HG. The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5′-nucleotidase from chicken gizzard smooth muscle. FEBS Lett 1986;195:82-86.
    • (1986) FEBS Lett , vol.195 , pp. 82-86
    • Dieckhoff, J.1    Mollenhauer, J.2    Kuhl, U.3    Niggemeyer, B.4    Von Der Mark, K.5    Mannherz, H.G.6
  • 128
    • 0025218067 scopus 로고
    • Chicken gizzard 5′-nucleotidase is a receptor for the extracellular matrix component fibronectin
    • Stochaj U, Richter H, Mannherz HG. Chicken gizzard 5′-nucleotidase is a receptor for the extracellular matrix component fibronectin. Eur J Cell Biol 1990;51:335-338.
    • (1990) Eur J Cell Biol , vol.51 , pp. 335-338
    • Stochaj, U.1    Richter, H.2    Mannherz, H.G.3
  • 130
    • 0026457327 scopus 로고
    • Signal transduction through decay-accelerating factor. Interaction of glycosylphosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn
    • Shenoy-Scaria AM, Kwong J, Fujita T, Olszowy MW, Shaw AS, Lublin DM. Signal transduction through decay-accelerating factor. Interaction of glycosylphosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn. J Immunol 1992;149:3535-3541.
    • (1992) J Immunol , vol.149 , pp. 3535-3541
    • Shenoy-Scaria, A.M.1    Kwong, J.2    Fujita, T.3    Olszowy, M.W.4    Shaw, A.S.5    Lublin, D.M.6
  • 131
    • 0026090037 scopus 로고
    • The glycosyl phosphatidylinositol anchor is critical for Ly-6A/E-mediated T cell activation
    • Su B, Waneck GL, Flavell RA, Bothwell ALM. The glycosyl phosphatidylinositol anchor is critical for Ly-6A/E-mediated T cell activation. J Cell Biol 1991;112:377-384.
    • (1991) J Cell Biol , vol.112 , pp. 377-384
    • Su, B.1    Waneck, G.L.2    Flavell, R.A.3    Bothwell, A.L.M.4
  • 132
    • 0024449097 scopus 로고
    • A glycophospholipid anchor is required for Qa-2-mediated T cell activation
    • Robinson PJ, Millrain M, Antoniou J, Simpson E, Mellor AL. A glycophospholipid anchor is required for Qa-2-mediated T cell activation. Nature 1989;342:85-87.
    • (1989) Nature , vol.342 , pp. 85-87
    • Robinson, P.J.1    Millrain, M.2    Antoniou, J.3    Simpson, E.4    Mellor, A.L.5
  • 133
    • 0026076574 scopus 로고
    • Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins
    • Zhang F, et al. Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins. J Cell Biol 1991;115:75-84.
    • (1991) J Cell Biol , vol.115 , pp. 75-84
    • Zhang, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.