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Volumn 21, Issue 2, 2004, Pages 187-195

Enzyme activities controlling adenosine levels in normal and neoplastic tissues

Author keywords

Adenosine; Colorectal cancer; Neoplasia; Purine metabolism; Tumors

Indexed keywords

5' NUCLEOTIDASE; ADENOSINE; ADENOSINE DEAMINASE; ADENOSINE DIPHOSPHATE; ADENOSINE KINASE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; ADENYLATE KINASE; INOSINE; NUCLEOSIDE PHOSPHORYLASE; PURINE; PURINE NUCLEOSIDE PHOSPHORYLASE;

EID: 4243060411     PISSN: 13570560     EISSN: None     Source Type: Journal    
DOI: 10.1385/MO:21:2:187     Document Type: Article
Times cited : (36)

References (33)
  • 1
    • 0018121433 scopus 로고
    • Activities and some properties of 5′-nucleotidase, adenosine kinase and adenosine deaminase in tissues from vertebrates and invertebrates in relation to the control of the concentration and the physiological role of adenosine
    • Arch JR, Newsholme E.A. Activities and some properties of 5′-nucleotidase, adenosine kinase and adenosine deaminase in tissues from vertebrates and invertebrates in relation to the control of the concentration and the physiological role of adenosine. Biochem J 1978; 174:965-977.
    • (1978) Biochem J , vol.174 , pp. 965-977
    • Arch, J.R.1    Newsholme, E.A.2
  • 2
    • 0031570040 scopus 로고    scopus 로고
    • Adenosine metabolism during phorbol myristate acetate-mediated induction of HL-60 cell differentiation
    • Spychala J, Mitchell BS, Barankiewicz J. Adenosine metabolism during phorbol myristate acetate-mediated induction of HL-60 cell differentiation. J Immunol 1997; 158:4947-4952.
    • (1997) J Immunol , vol.158 , pp. 4947-4952
    • Spychala, J.1    Mitchell, B.S.2    Barankiewicz, J.3
  • 3
    • 0033796779 scopus 로고    scopus 로고
    • Tumour-promoting function of adenosine
    • Spychala J. Tumour-promoting function of adenosine. Pharmacol Therapy 2000; 87:161-173.
    • (2000) Pharmacol Therapy , vol.87 , pp. 161-173
    • Spychala, J.1
  • 4
    • 0027412657 scopus 로고
    • Mechanism of elevation of adenosine levels in anoxic hepatocytes
    • Bontemps F, Vincent MF, Van den Berghe G. Mechanism of elevation of adenosine levels in anoxic hepatocytes. Biochem J 1993, 290:671-677.
    • (1993) Biochem J , vol.290 , pp. 671-677
    • Bontemps, F.1    Vincent, M.F.2    Van Den Berghe, G.3
  • 5
    • 0023955880 scopus 로고
    • Absolute rates of adenosine formation during ischaemia in rat and pigeon hearts
    • Meghji P, Middleton KM, Newby AC. Absolute rates of adenosine formation during ischaemia in rat and pigeon hearts. Biochem J 1988; 249:695-703.
    • (1988) Biochem J , vol.249 , pp. 695-703
    • Meghji, P.1    Middleton, K.M.2    Newby, A.C.3
  • 6
    • 0035925098 scopus 로고    scopus 로고
    • Tumour hypoxia: Definitions and current clinical, biologic and molecular aspects
    • Hockel M, Vaupel P. Tumour hypoxia: definitions and current clinical, biologic and molecular aspects. J Natl Cancer Inst 2001, 93:266-276.
    • (2001) J Natl Cancer Inst , vol.93 , pp. 266-276
    • Hockel, M.1    Vaupel, P.2
  • 7
    • 0032851248 scopus 로고    scopus 로고
    • Enzymes involved in purine metabolism: A review of histochemical localization and functional implications
    • Moriwaki Y, Yamamoto T, Higashino K. Enzymes involved in purine metabolism: a review of histochemical localization and functional implications. Histol Histopathol 1999; 14:1321-1340.
    • (1999) Histol Histopathol , vol.14 , pp. 1321-1340
    • Moriwaki, Y.1    Yamamoto, T.2    Higashino, K.3
  • 8
    • 0344443811 scopus 로고    scopus 로고
    • Mammalian 5′-nucleotidase
    • Bianchi V, Spychala J. Mammalian 5′-nucleotidase. J Biol Chem 2003; 278:46195-46198.
    • (2003) J Biol Chem , vol.278 , pp. 46195-46198
    • Bianchi, V.1    Spychala, J.2
  • 9
    • 0032524568 scopus 로고    scopus 로고
    • Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′ nucleotidase by phospholipase C: Catalytic activation and modulation by the lipid bilayer
    • Lehto MT, Sharom FJ. Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5′ nucleotidase by phospholipase C: catalytic activation and modulation by the lipid bilayer. Biochem J 1998; 332:101-109.
    • (1998) Biochem J , vol.332 , pp. 101-109
    • Lehto, M.T.1    Sharom, F.J.2
  • 11
    • 0019316691 scopus 로고
    • Purification and properties of adenosine kinase from rat brain
    • Yamada Y, Goto H, Ogasawara N. Purification and properties of adenosine kinase from rat brain. Biochim Biophys Acta 1980; 616:199-207.
    • (1980) Biochim Biophys Acta , vol.616 , pp. 199-207
    • Yamada, Y.1    Goto, H.2    Ogasawara, N.3
  • 12
    • 0028292990 scopus 로고
    • An asp8-to-asm substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA2 allozyme): Occurrence in different chromosomal backgrounds and apparent intragenic crossover
    • Hirschhorn R, Yang DR, Israni A. An asp8-to-asm substitution results in the adenosine deaminase (ADA) genetic polymorphism (ADA2 allozyme): occurrence in different chromosomal backgrounds and apparent intragenic crossover. Ann Hum Genet 1994; 58:1-9.
    • (1994) Ann Hum Genet , vol.58 , pp. 1-9
    • Hirschhorn, R.1    Yang, D.R.2    Israni, A.3
  • 13
    • 0019287673 scopus 로고
    • Localization of purine and pyrimidine nucleoside phosphorylases in heart, kidney and liver
    • Rubio R, Berne RM. Localization of purine and pyrimidine nucleoside phosphorylases in heart, kidney and liver. Am J Physiol 1980; 239:H721-730.
    • (1980) Am J Physiol , vol.239
    • Rubio, R.1    Berne, R.M.2
  • 14
    • 0025319861 scopus 로고
    • Purine nucleoside phosphorylase: A new marker for free oxygen radical injury to the endothelial cell
    • Rao PN, et al. Purine nucleoside phosphorylase: a new marker for free oxygen radical injury to the endothelial cell. Hepatology 1990; 11:193-198.
    • (1990) Hepatology , vol.11 , pp. 193-198
    • Rao, P.N.1
  • 15
    • 0029126775 scopus 로고
    • Determination of plasma activities of purine phosphorylase by high-performance liquid chromatography: Estimates of non parenchyma cell injury after porcine liver transplantation
    • Minor TH, et al. Determination of plasma activities of purine phosphorylase by high-performance liquid chromatography: estimates of non parenchyma cell injury after porcine liver transplantation. J Chromatogr B 1995; 670:332-336.
    • (1995) J Chromatogr B , vol.670 , pp. 332-336
    • Minor, T.H.1
  • 16
    • 0025191301 scopus 로고
    • Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle
    • Zeleznikar RJ, et al. Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle J Biol Chem 1990; 265:300-311.
    • (1990) J Biol Chem , vol.265 , pp. 300-311
    • Zeleznikar, R.J.1
  • 17
    • 0024390429 scopus 로고
    • Human adenylate kinase deficiency associated with hemolytic anemia
    • Matsuura S, et al. Human adenylate kinase deficiency associated with hemolytic anemia. J Biol Chem 1989; 264:10148-10152.
    • (1989) J Biol Chem , vol.264 , pp. 10148-10152
    • Matsuura, S.1
  • 18
    • 0033768458 scopus 로고    scopus 로고
    • Activities of adenosine deaminase and 5′-nucleotidase in cancerous and noncancerous human colorectal tissues
    • Eroglu A, et al. Activities of adenosine deaminase and 5′-nucleotidase in cancerous and noncancerous human colorectal tissues. Med Oncol 2000, 17:319-324.
    • (2000) Med Oncol , vol.17 , pp. 319-324
    • Eroglu, A.1
  • 19
    • 0021332182 scopus 로고
    • Purine metabolizing enzymes in lymphocytes from patients with solid tumours
    • Majer J, Horbov S, Nygaard P. Purine metabolizing enzymes in lymphocytes from patients with solid tumours. Acta Med Scand 1984; 215:5-11.
    • (1984) Acta Med Scand , vol.215 , pp. 5-11
    • Majer, J.1    Horbov, S.2    Nygaard, P.3
  • 20
    • 0030068379 scopus 로고    scopus 로고
    • Activities of adenosine deaminase, 5′-nucleotidase, guanase and cytidine deaminase enzymes in cancerous and non-cancerous human breast tissues
    • Canbolat O, et al. Activities of adenosine deaminase, 5′-nucleotidase, guanase and cytidine deaminase enzymes in cancerous and non-cancerous human breast tissues. Breast Canc Res Treat 1996; 37:189-193.
    • (1996) Breast Canc Res Treat , vol.37 , pp. 189-193
    • Canbolat, O.1
  • 21
    • 0031003240 scopus 로고    scopus 로고
    • Activity of the enzymes participating in purine metabolism of cancerous and non-cancerous human kidney tissues
    • Durak I, et al. Activity of the enzymes participating in purine metabolism of cancerous and non-cancerous human kidney tissues. Cancer Invest 1997; 15:212-216.
    • (1997) Cancer Invest , vol.15 , pp. 212-216
    • Durak, I.1
  • 22
    • 0344326338 scopus 로고    scopus 로고
    • Activities of DNA turnover and free radical metabolizing enzymes in cancerous human prostate tissue
    • Biri H, et al. Activities of DNA turnover and free radical metabolizing enzymes in cancerous human prostate tissue. Cancer Invest 1999; 17:314-319.
    • (1999) Cancer Invest , vol.17 , pp. 314-319
    • Biri, H.1
  • 23
    • 0021136347 scopus 로고
    • Enzymic capacities of purine de novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues
    • Natsumeda Y, Prajda N, Donohue JP; Glover JL, Weber G. Enzymic capacities of purine de novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues. Cancer Res 1984; 44:2475-2479.
    • (1984) Cancer Res , vol.44 , pp. 2475-2479
    • Natsumeda, Y.1    Prajda, N.2    Donohue, J.P.3    Glover, J.L.4    Weber, G.5
  • 24
    • 0021808226 scopus 로고
    • Purine enzymology of human colon carcinomas
    • Natsumeda Y, et al. Purine enzymology of human colon carcinomas. Cancer Res 1985; 45:2556-2559.
    • (1985) Cancer Res , vol.45 , pp. 2556-2559
    • Natsumeda, Y.1
  • 25
    • 0032817469 scopus 로고    scopus 로고
    • Purine metabolism in two human melanoma cell lines: Relation to proliferation and differentiation
    • Wei S, et al. Purine metabolism in two human melanoma cell lines: relation to proliferation and differentiation. Melanoma Res 1999; 9:351-359.
    • (1999) Melanoma Res , vol.9 , pp. 351-359
    • Wei, S.1
  • 26
    • 0020610710 scopus 로고
    • Adenosine deaminase and purine nucleoside phosphorylase activities in peripheral blood cells of patients with neoplastic diseases in bronchogenic carcinoma
    • Rendekova V, et al. Adenosine deaminase and purine nucleoside phosphorylase activities in peripheral blood cells of patients with neoplastic diseases in bronchogenic carcinoma. Neoplasma 1983; 30:233-238.
    • (1983) Neoplasma , vol.30 , pp. 233-238
    • Rendekova, V.1
  • 27
    • 0028064764 scopus 로고
    • A revised European-American classification of lymphoid neoplasms: A proposal from the international Lymphoma Study Group
    • Harris NL, et al. A revised European-American classification of lymphoid neoplasms: a proposal from the international Lymphoma Study Group. Blood 1994; 84:1361-1392.
    • (1994) Blood , vol.84 , pp. 1361-1392
    • Harris, N.L.1
  • 28
    • 0020640494 scopus 로고
    • Enzymes of purine metabolism in cancer
    • Weber G. Enzymes of purine metabolism in cancer. Clin Biochem 1983; 16:57-73.
    • (1983) Clin Biochem , vol.16 , pp. 57-73
    • Weber, G.1
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0025463108 scopus 로고
    • Purine salvage enzyme activities in normal and neoplastic human tissues
    • Camici M, et al. Purine salvage enzyme activities in normal and neoplastic human tissues. Cancer Biochem Biophys 1990; 11:201-209.
    • (1990) Cancer Biochem Biophys , vol.11 , pp. 201-209
    • Camici, M.1
  • 32
    • 0028409695 scopus 로고
    • Relationship between the levels of purine salvage pathway enzymes and clinical biological aggressiveness of human colon carcinoma
    • Sanfilippo O, et al. Relationship between the levels of purine salvage pathway enzymes and clinical biological aggressiveness of human colon carcinoma. Cancer Biochem Biophys 1994; 14:57-66.
    • (1994) Cancer Biochem Biophys , vol.14 , pp. 57-66
    • Sanfilippo, O.1
  • 33
    • 0030981587 scopus 로고    scopus 로고
    • Purine nucleotide metabolism: Specific aspects in chronic lymphocytic leucemia lymphocytes
    • Carlucci F, et al. Purine nucleotide metabolism: specific aspects in chronic lymphocytic leucemia lymphocytes. Biochim Biophys Acta 1997; 1360:203-210.
    • (1997) Biochim Biophys Acta , vol.1360 , pp. 203-210
    • Carlucci, F.1


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