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Volumn 158, Issue 10, 1997, Pages 4947-4952

Adenosine Metabolism during Phorbol Myristate Acetate-Mediated Induction of HL-60 Cell Differentiation: Changes in Expression Pattern of Adenosine Kinase, Adenosine Deaminase, and 5′-Nucleotidase

Author keywords

[No Author keywords available]

Indexed keywords

5' NUCLEOTIDASE; ADENINE; ADENOSINE; ADENOSINE DEAMINASE; ADENOSINE KINASE; HYPOXANTHINE; MESSENGER RNA; PHORBOL 13 ACETATE 12 MYRISTATE; PURINE DERIVATIVE;

EID: 0031570040     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (33)

References (60)
  • 1
    • 0014768311 scopus 로고
    • Effect of cyclic 3′5′-adenosine monophosphate and theophylline on lymphocyte transformation
    • Hirschhorn, R., J. Grossman, and G. Weismann. 1970. Effect of cyclic 3′5′-adenosine monophosphate and theophylline on lymphocyte transformation. Proc. Soc. Exp. Biol. Med. 113:1361.
    • (1970) Proc. Soc. Exp. Biol. Med. , vol.113 , pp. 1361
    • Hirschhorn, R.1    Grossman, J.2    Weismann, G.3
  • 2
    • 0020081679 scopus 로고
    • Pharmacological modification of immunoregulatory T lymphocytes. I. Effect of adenosine, H1 and H2 histamine agonists upon T lymphocyte regulation of B lymphocyte differentiation in vitro
    • Birch, R. E., and S. H. Polmar. 1982. Pharmacological modification of immunoregulatory T lymphocytes. I. Effect of adenosine, H1 and H2 histamine agonists upon T lymphocyte regulation of B lymphocyte differentiation in vitro. Clin. Exp. Immunol. 48:218.
    • (1982) Clin. Exp. Immunol. , vol.48 , pp. 218
    • Birch, R.E.1    Polmar, S.H.2
  • 3
    • 0022652191 scopus 로고
    • Adenosine induced immunosuppression: The role of the adenosine receptor-adenylate cyclase interaction in the alteration of T-lymphocyte surface phenotype and immunoregulatory function
    • Birch, R. E., and S. H. Polmar. 1986. Adenosine induced immunosuppression: the role of the adenosine receptor-adenylate cyclase interaction in the alteration of T-lymphocyte surface phenotype and immunoregulatory function. Int. J. Immunopharmacol. 8:329.
    • (1986) Int. J. Immunopharmacol. , vol.8 , pp. 329
    • Birch, R.E.1    Polmar, S.H.2
  • 4
    • 84886638223 scopus 로고
    • Inhibition of lymphocyte-mediated cytolysis by adenosine analogs: Biochemical studies concerning mechanism of action
    • Wolberg, G., T. P. Zimmerman, G. S. Duncan, K. H. Singer, and G. B. Elion. 1978. Inhibition of lymphocyte-mediated cytolysis by adenosine analogs: biochemical studies concerning mechanism of action. Biochem. Pharmacol. 27:1487.
    • (1978) Biochem. Pharmacol. , vol.27 , pp. 1487
    • Wolberg, G.1    Zimmerman, T.P.2    Duncan, G.S.3    Singer, K.H.4    Elion, G.B.5
  • 6
    • 0022534865 scopus 로고
    • Analysis of isolated and combined effects of calcium ionophore and phorbol ester on T lymphocyte activation
    • Nobrega, A. F., M. S. Maldonado, and G. A. Dos Reis. 1986. Analysis of isolated and combined effects of calcium ionophore and phorbol ester on T lymphocyte activation. Clin. Exp. Immunol. 65:559.
    • (1986) Clin. Exp. Immunol. , vol.65 , pp. 559
    • Nobrega, A.F.1    Maldonado, M.S.2    Dos Reis, G.A.3
  • 7
    • 0022462367 scopus 로고
    • Role of adenylate cyclase in human T-lymphocyte surface antigen capping
    • Kammer, G. M., C. A. Boehm, and S. A. Rudolph. 1986. Role of adenylate cyclase in human T-lymphocyte surface antigen capping. Cell. Immunol. 101:251.
    • (1986) Cell. Immunol. , vol.101 , pp. 251
    • Kammer, G.M.1    Boehm, C.A.2    Rudolph, S.A.3
  • 8
    • 0021190155 scopus 로고
    • Adenosine A2 receptors on human monocytes modulate C2 production
    • Lappin, D., and K. Whaley. 1984. Adenosine A2 receptors on human monocytes modulate C2 production. Clin. Exp. Immunol. 57:454.
    • (1984) Clin. Exp. Immunol. , vol.57 , pp. 454
    • Lappin, D.1    Whaley, K.2
  • 9
    • 0022397930 scopus 로고
    • Adenosine, a physiologic modulator of superoxide anion generation by human neutrophils: Adenosine acts via an A2 receptor on human neutrophils
    • Cronstein, B. N., E. D. Rosenstein, S. B. Kramer, G. Weissman, and R. Hirschhorn. 1985. Adenosine, a physiologic modulator of superoxide anion generation by human neutrophils: adenosine acts via an A2 receptor on human neutrophils. J. Immunol. 135:1366.
    • (1985) J. Immunol. , vol.135 , pp. 1366
    • Cronstein, B.N.1    Rosenstein, E.D.2    Kramer, S.B.3    Weissman, G.4    Hirschhorn, R.5
  • 10
    • 0026709899 scopus 로고
    • Molecular mechanism of methotrexate action in inflammation
    • Cronstein, B. N. 1992. Molecular mechanism of methotrexate action in inflammation. Inflammation 16:411.
    • (1992) Inflammation , vol.16 , pp. 411
    • Cronstein, B.N.1
  • 12
    • 0025967399 scopus 로고
    • Methotrexate inhibits neutrophil function by stimulating adenosine release from connective tissue cells
    • Cronstein, B. N., M. A. Eberle, H. E. Gruben, and RI Levin. 1991. Methotrexate inhibits neutrophil function by stimulating adenosine release from connective tissue cells. Proc. Natl. Acad. Sci. USA 88:2441.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2441
    • Cronstein, B.N.1    Eberle, M.A.2    Gruben, H.E.3    Levin, R.I.4
  • 14
    • 0020055138 scopus 로고
    • Kinetic considerations for the regulation of adenosine and deoxyadenosine metabolism in mouse and human tissues based on a thymocyte model
    • Snyder, F. F., and T. Lukey. 1982. Kinetic considerations for the regulation of adenosine and deoxyadenosine metabolism in mouse and human tissues based on a thymocyte model. Biochim. Biophys. Acta 696:299.
    • (1982) Biochim. Biophys. Acta , vol.696 , pp. 299
    • Snyder, F.F.1    Lukey, T.2
  • 15
    • 0019908684 scopus 로고
    • Ecto-5′ nucleotidase and adenosine deaminase activities of lymphoid cells
    • Dornand, J., J. C. Bonnafous, J. Favero, and J. C. Mani. 1982. Ecto-5′ nucleotidase and adenosine deaminase activities of lymphoid cells. Biochem. Med. 28:144.
    • (1982) Biochem. Med. , vol.28 , pp. 144
    • Dornand, J.1    Bonnafous, J.C.2    Favero, J.3    Mani, J.C.4
  • 16
    • 0023733849 scopus 로고
    • Coordinate regulation of mRNA encoding adenosine deaminase, purine nucleoside phosphorylase, and terminal deoxynucleotidyltransferase by phorbol esters in human thymocytes
    • Martinez-Valdez, H., and A. Cohen. 1988. Coordinate regulation of mRNA encoding adenosine deaminase, purine nucleoside phosphorylase, and terminal deoxynucleotidyltransferase by phorbol esters in human thymocytes. Proc. Natl. Acad. Sci. USA 85:6900.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6900
    • Martinez-Valdez, H.1    Cohen, A.2
  • 17
    • 0025359477 scopus 로고
    • Phorbol esters induce changes in adenosine deaminase, purine nucleoside phosphorylase, and terminal deoxynucleotidyl transferase messenger RNA levels in human leukemic cell lines
    • Madrid-Marina, V., H. Martinez-Valdez, and A. Cohen. 1990. Phorbol esters induce changes in adenosine deaminase, purine nucleoside phosphorylase, and terminal deoxynucleotidyl transferase messenger RNA levels in human leukemic cell lines. Cancer Res. 50:2891.
    • (1990) Cancer Res. , vol.50 , pp. 2891
    • Madrid-Marina, V.1    Martinez-Valdez, H.2    Cohen, A.3
  • 18
    • 0002510268 scopus 로고
    • The role of purine metabolic enzymes and terminal deoxynucleotidyl transferase in intrathymic T-cell differentiation
    • Ma, D. D. F., T. Sylwestrowicz, G. Janossy, and A. V. Hoffbrand. 1983. The role of purine metabolic enzymes and terminal deoxynucleotidyl transferase in intrathymic T-cell differentiation. Immunol. Today 4:65.
    • (1983) Immunol. Today , vol.4 , pp. 65
    • Ma, D.D.F.1    Sylwestrowicz, T.2    Janossy, G.3    Hoffbrand, A.V.4
  • 19
    • 0021719254 scopus 로고
    • Isolation and characterization of a deoxycytidine kinase-deficient human promyelocytic leukemic cell line highly resistant to 1-β-D-arabinofuranosylcytosine
    • Bhalla, K., R. Nayak, and S. Grant. 1984. Isolation and characterization of a deoxycytidine kinase-deficient human promyelocytic leukemic cell line highly resistant to 1-β-D-arabinofuranosylcytosine. Cancer Res. 44:5029.
    • (1984) Cancer Res. , vol.44 , pp. 5029
    • Bhalla, K.1    Nayak, R.2    Grant, S.3
  • 20
    • 0018118318 scopus 로고
    • Purinogenic immunodeficiency diseases: Selective toxicity of deoxyribonucleosides for T cells
    • Mitchell, B. S., E. Mejias, P. E. Daddona, W. N. Kelley. 1978. Purinogenic immunodeficiency diseases: selective toxicity of deoxyribonucleosides for T cells. Proc. Natl. Acad. Sci. USA 75:5011.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5011
    • Mitchell, B.S.1    Mejias, E.2    Daddona, P.E.3    Kelley, W.N.4
  • 21
    • 0022580334 scopus 로고
    • Cytogenetic and immunophenotypic analysis of cell lines established from patients with T cell leukemia/lymphoma
    • Smith, S. D., R. Morgan, M. P. Link, P. McFall, and F. Hecht. 1986. Cytogenetic and immunophenotypic analysis of cell lines established from patients with T cell leukemia/lymphoma. Blood 67:650.
    • (1986) Blood , vol.67 , pp. 650
    • Smith, S.D.1    Morgan, R.2    Link, M.P.3    McFall, P.4    Hecht, F.5
  • 22
    • 0016649230 scopus 로고
    • An analytical system for rapid separation of tissue nucleotides at low pressures on conventional anion exchangers
    • Khym, J. X. 1975. An analytical system for rapid separation of tissue nucleotides at low pressures on conventional anion exchangers. Clin. Chem. 21:1245.
    • (1975) Clin. Chem. , vol.21 , pp. 1245
    • Khym, J.X.1
  • 23
    • 0025126844 scopus 로고
    • Selective adenosine release from human B but not T lymphoid cell line
    • Barankiewicz, J., G. Ronlov, R. Jimenez, and H. E. Gruber. 1990. Selective adenosine release from human B but not T lymphoid cell line. J. Biol. Chem. 265:15738.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15738
    • Barankiewicz, J.1    Ronlov, G.2    Jimenez, R.3    Gruber, H.E.4
  • 24
    • 0016249049 scopus 로고
    • Methods for the study of purine metabolism in human cells in vitro
    • Henderson, J. F., J. H. Fraser, and E. E. McCoy. 1974. Methods for the study of purine metabolism in human cells in vitro. Clin. Biochem. 7:339.
    • (1974) Clin. Biochem. , vol.7 , pp. 339
    • Henderson, J.F.1    Fraser, J.H.2    McCoy, E.E.3
  • 25
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156.
    • (1987) Anal. Biochem. , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 26
    • 0025709722 scopus 로고
    • Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form
    • Misumi, Y., S. Ogata, K. Ohkubo, S. Hirose, and Y. Ikehara. 1990. Primary structure of human placental 5′-nucleotidase and identification of the glycolipid anchor in the mature form. Eur. J. Biochem. 191:563.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 563
    • Misumi, Y.1    Ogata, S.2    Ohkubo, K.3    Hirose, S.4    Ikehara, Y.5
  • 28
    • 0027377459 scopus 로고
    • Hereditary overexpression of adenosine deaminase in erythrocytes-evidence for a cis-acting mutation
    • Chen, E. H., A. P. Tartaglia, and B. S. Mitchell. 1993. Hereditary overexpression of adenosine deaminase in erythrocytes-evidence for a cis-acting mutation. Am. J. Hum. Genet. 53:889.
    • (1993) Am. J. Hum. Genet. , vol.53 , pp. 889
    • Chen, E.H.1    Tartaglia, A.P.2    Mitchell, B.S.3
  • 29
    • 0020639120 scopus 로고
    • Evidence for a substrate cycle between AMP and adenosine in isolated hepatocytes
    • Bontemps, F., G. Van den Berghe, and H.-G. Hers. 1983. Evidence for a substrate cycle between AMP and adenosine in isolated hepatocytes. Proc. Natl. Acad. Sci. USA 80:2829.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2829
    • Bontemps, F.1    Van Den Berghe, G.2    Hers, H.-G.3
  • 30
    • 0023110998 scopus 로고
    • Adenine nucleotide metabilism in isolated chicken hepatocytes
    • Spychala, J., and G. Van den Berghe. 1987. Adenine nucleotide metabilism in isolated chicken hepatocytes. Biochem. J. 242:551.
    • (1987) Biochem. J. , vol.242 , pp. 551
    • Spychala, J.1    Van Den Berghe, G.2
  • 31
    • 0022522163 scopus 로고
    • Myocardial adenosine cycling rates during normoxia and under conditions of stimulated purine release
    • Achterberg, P. W., R. J. Stroeve, and J. W. de Jong. 1986. Myocardial adenosine cycling rates during normoxia and under conditions of stimulated purine release. Biochem. J. 235:13.
    • (1986) Biochem. J. , vol.235 , pp. 13
    • Achterberg, P.W.1    Stroeve, R.J.2    De Jong, J.W.3
  • 32
    • 0024406156 scopus 로고
    • The rate of the AMP/Adenosine substrate cycle in concanavalin-A-stimulaled rat lymphocytes
    • Szondy, Z., and E. A. Newsholme. 1989. The rate of the AMP/Adenosine substrate cycle in concanavalin-A-stimulaled rat lymphocytes. Biochem. J. 261:739.
    • (1989) Biochem. J. , vol.261 , pp. 739
    • Szondy, Z.1    Newsholme, E.A.2
  • 33
    • 0019773856 scopus 로고
    • Adenosine production inside rat polymorphonuclear leucocytes
    • Newby, A. C., and C. A. Holmquist. 1981. Adenosine production inside rat polymorphonuclear leucocytes. Biochem. J. 200:399.
    • (1981) Biochem. J. , vol.200 , pp. 399
    • Newby, A.C.1    Holmquist, C.A.2
  • 34
    • 0016261604 scopus 로고
    • Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. I. Evidence for an ecto-adenosine monophosphatase, adenosine triphosphatase, and p-nitro-phenyl phosphatase
    • DePierre, J. W., and M. L. Karnovsky. 1974. Ecto-enzymes of the guinea pig polymorphonuclear leukocyte. I. Evidence for an ecto-adenosine monophosphatase, adenosine triphosphatase, and p-nitro-phenyl phosphatase. J. Biol. Chem. 249:7111.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7111
    • DePierre, J.W.1    Karnovsky, M.L.2
  • 37
    • 0022622216 scopus 로고
    • Human placental cytoplasmic 5′-nucleotidase. Kinetic properties and inhibition
    • Madrid-Marina, V., and I. H. Fox. 1986. Human placental cytoplasmic 5′-nucleotidase. Kinetic properties and inhibition. J. Biol. Chem. 261:444.
    • (1986) J. Biol. Chem. , vol.261 , pp. 444
    • Madrid-Marina, V.1    Fox, I.H.2
  • 38
    • 0014246030 scopus 로고
    • Properties of 5′-nucleotidase from hepatic tissue of higher animals
    • Itoh, R., A. Mitsui, and K. Tsushima. 1968. Properties of 5′-nucleotidase from hepatic tissue of higher animals. J. Biochem. 63:165.
    • (1968) J. Biochem. , vol.63 , pp. 165
    • Itoh, R.1    Mitsui, A.2    Tsushima, K.3
  • 39
    • 0017347905 scopus 로고
    • A kinetic study of the soluble 5′-nucleotidase of rat liver
    • Van den Berghe, G., C. Van Pottersberghe, and H.-G. Hers. 1977. A kinetic study of the soluble 5′-nucleotidase of rat liver. Biochem. J. 162:611.
    • (1977) Biochem. J. , vol.162 , pp. 611
    • Van Den Berghe, G.1    Van Pottersberghe, C.2    Hers, H.-G.3
  • 40
    • 0024165139 scopus 로고
    • High-Km soluble 5′-nucleotidase from human placenta: Properties and allosteric regulation by IMP and ATP
    • Spychala, J., V. Madrid-Marina, and I. H. Fox. 1988. High-Km soluble 5′-nucleotidase from human placenta: properties and allosteric regulation by IMP and ATP. J. Biol. Chem. 263:18759.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18759
    • Spychala, J.1    Madrid-Marina, V.2    Fox, I.H.3
  • 41
    • 0024506725 scopus 로고
    • AMP and IMP dephosphorylation by soluble high- and low-Km 5′-nucleotidases
    • Spychala, J., V. Madrid-Marina, P. J. Nowak, and I. H. Fox. 1989. AMP and IMP dephosphorylation by soluble high- and low-Km 5′-nucleotidases. Am. J. Physiol. 256:E386.
    • (1989) Am. J. Physiol. , vol.256
    • Spychala, J.1    Madrid-Marina, V.2    Nowak, P.J.3    Fox, I.H.4
  • 42
    • 0023188210 scopus 로고
    • Adenosine deaminase mRNA expression is regulated posttranscriptionally during differentiation of HL-60 cells
    • Berkvens, T. M., F. Schoute, H. van Ormondt, P. Meera Khan, and A. J. van der Eb. 1987. Adenosine deaminase mRNA expression is regulated posttranscriptionally during differentiation of HL-60 cells. Nucleic Acids Res. 15:6575.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 6575
    • Berkvens, T.M.1    Schoute, F.2    Van Ormondt, H.3    Meera Khan, P.4    Van Der Eb, A.J.5
  • 43
    • 0021951528 scopus 로고
    • Isoenzyme studies in human leukemia-lymphoma cell lines. 1. Carboxylic esterase
    • Drexler, H. G., G. Gaedicke, and J. Minowada. 1985. Isoenzyme studies in human leukemia-lymphoma cell lines. 1. Carboxylic esterase. Leuk. Res. 9:209.
    • (1985) Leuk. Res. , vol.9 , pp. 209
    • Drexler, H.G.1    Gaedicke, G.2    Minowada, J.3
  • 44
    • 0030033229 scopus 로고    scopus 로고
    • Role of activation of protein kinase C in the infarct size-limiting effect of ischemic preconditioning through activation of ecto-5′-nucleotidase
    • Kitakaze, M., K. Node, T. Minamino, K. Komamura, H. Funaya, Y. Shinozaki, M. Chujo, H. Mori, M. Inoue, M. Hori, and T. Kamada. 1996. Role of activation of protein kinase C in the infarct size-limiting effect of ischemic preconditioning through activation of ecto-5′-nucleotidase. Circulation 93:781.
    • (1996) Circulation , vol.93 , pp. 781
    • Kitakaze, M.1    Node, K.2    Minamino, T.3    Komamura, K.4    Funaya, H.5    Shinozaki, Y.6    Chujo, M.7    Mori, H.8    Inoue, M.9    Hori, M.10    Kamada, T.11
  • 46
    • 0028798796 scopus 로고
    • Parathyroid hormone stimulates ecto-5′-nucleotidase activity in renal epithelial cells: Role of protein kinase-C
    • Siegfried, G., F. Vrtovsnik, D. Prie, C. Amiel, and G. Freidlander. 1995. Parathyroid hormone stimulates ecto-5′-nucleotidase activity in renal epithelial cells: role of protein kinase-C. Endocrinology 136:1267.
    • (1995) Endocrinology , vol.136 , pp. 1267
    • Siegfried, G.1    Vrtovsnik, F.2    Prie, D.3    Amiel, C.4    Freidlander, G.5
  • 47
    • 0020214226 scopus 로고
    • Regulation of purine metabolism by plasma membrane and cytoplasmic 5′-nucleotidases
    • Edwards, N. L., D. Recker, J. Manfredi, R. Rembecki, and I. H. Fox. 1982. Regulation of purine metabolism by plasma membrane and cytoplasmic 5′-nucleotidases. Am. J. Physiol. 243:C270.
    • (1982) Am. J. Physiol. , vol.243
    • Edwards, N.L.1    Recker, D.2    Manfredi, J.3    Rembecki, R.4    Fox, I.H.5
  • 48
    • 0026060811 scopus 로고
    • The soluble low-Km 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase
    • Piec, G., and M. Lehir, 1991. The soluble low-Km 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase. Biochem. J. 273:409.
    • (1991) Biochem. J. , vol.273 , pp. 409
    • Piec, G.1    Lehir, M.2
  • 49
    • 0023772276 scopus 로고
    • Immunocytochemical localization of cytosol 5′-nucleotidase in chicken liver
    • Yokota, S., J. Oka, H. Ozasa, and R. Itoh. 1988. Immunocytochemical localization of cytosol 5′-nucleotidase in chicken liver. J. Histochem. Cytochem. 36:983.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 983
    • Yokota, S.1    Oka, J.2    Ozasa, H.3    Itoh, R.4
  • 50
    • 0023784260 scopus 로고
    • The pigeon heart 5′-nucleotidase responsible for ischemia-induced adenosine formation
    • Newby, A. C. 1988. The pigeon heart 5′-nucleotidase responsible for ischemia-induced adenosine formation. Biochem. J. 253:123.
    • (1988) Biochem. J. , vol.253 , pp. 123
    • Newby, A.C.1
  • 51
    • 0023748724 scopus 로고
    • 5′-Nucleotidase in rat heart: Evidence for the occurrence of two soluble enzymes with different substrate specificities
    • Truong, V. L., A. R. Collinson, and J. M. Lowenstein. 1988. 5′-Nucleotidase in rat heart: evidence for the occurrence of two soluble enzymes with different substrate specificities. Biochem. J. 253:117.
    • (1988) Biochem. J. , vol.253 , pp. 117
    • Truong, V.L.1    Collinson, A.R.2    Lowenstein, J.M.3
  • 52
    • 0023126858 scopus 로고
    • Chromatographic analysis of human erythrocyte pyrimidine 5′-nucleotidase from five patients with pyrimidine 5′-nucleotidase deficiency
    • Hirono, A., H. Fujii, H. Natori, I. Kurokawa, and S. Miwa. 1987. Chromatographic analysis of human erythrocyte pyrimidine 5′-nucleotidase from five patients with pyrimidine 5′-nucleotidase deficiency. Br. J. Haematol. 65:35.
    • (1987) Br. J. Haematol. , vol.65 , pp. 35
    • Hirono, A.1    Fujii, H.2    Natori, H.3    Kurokawa, I.4    Miwa, S.5
  • 53
    • 0025563804 scopus 로고
    • Extracellular ATP metabolism in B and T lymphocytes
    • Barankiewicz, J., and A. Cohen. 1990. Extracellular ATP metabolism in B and T lymphocytes. Ann. NY Acad. Sci. 603:380.
    • (1990) Ann. NY Acad. Sci. , vol.603 , pp. 380
    • Barankiewicz, J.1    Cohen, A.2
  • 54
    • 0023926827 scopus 로고
    • Extracellular nucleotide catabolism in human B and T lymphocytes: The source of adenosine production
    • Barankiewicz, J., H. M. Dosch, and A. Cohen. 1988. Extracellular nucleotide catabolism in human B and T lymphocytes: the source of adenosine production. J. Biol. Chem. 263:7094.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7094
    • Barankiewicz, J.1    Dosch, H.M.2    Cohen, A.3
  • 55
    • 0025974576 scopus 로고
    • Purine catabolism in polymorphonuclear neutrophils-phorbol myristate acetate-induced accumulation of adenosine owing to inactivation of extracellularly released adenosine deaminase
    • Van Waeg, G., and G. Van den Berghe. 1991. Purine catabolism in polymorphonuclear neutrophils-phorbol myristate acetate-induced accumulation of adenosine owing to inactivation of extracellularly released adenosine deaminase. J. Clin. Invest. 87:305.
    • (1991) J. Clin. Invest. , vol.87 , pp. 305
    • Van Waeg, G.1    Van Den Berghe, G.2
  • 56
    • 0026061115 scopus 로고
    • Cell-mediated cytotoxicity-ATP as an effector and the role of target cells
    • Steinberg, T. H., and F. Divirgilio. 1991. Cell-mediated cytotoxicity-ATP as an effector and the role of target cells. Curr. Opin. Immunol. 3:71.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 71
    • Steinberg, T.H.1    Divirgilio, F.2
  • 57
    • 0017703067 scopus 로고
    • Differences in surface membrane ecto-ATPase and ecto-AMPase in normal and malignant cells. I. Decrease in ecto-ATPase in myeloid leukemic cells and the independent regulation of ecto-ATPase and ecto-AMPase
    • Weiss, B., and L. Sachs. 1977. Differences in surface membrane ecto-ATPase and ecto-AMPase in normal and malignant cells. I. Decrease in ecto-ATPase in myeloid leukemic cells and the independent regulation of ecto-ATPase and ecto-AMPase. J. Cell. Physiol. 93:183.
    • (1977) J. Cell. Physiol. , vol.93 , pp. 183
    • Weiss, B.1    Sachs, L.2
  • 58
    • 0025177280 scopus 로고
    • Ecto-ATPase activity in cytolytic lymphocytes-T-protection from the cytolytic effects of extracellular ATP
    • Filippini, A., R. E. Taffs, T. Agui, and M. V. Sitkovsky. 1990. Ecto-ATPase activity in cytolytic lymphocytes-T-protection from the cytolytic effects of extracellular ATP. J. Biol. Chem. 265:334.
    • (1990) J. Biol. Chem. , vol.265 , pp. 334
    • Filippini, A.1    Taffs, R.E.2    Agui, T.3    Sitkovsky, M.V.4


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