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Volumn 1637, Issue 2, 2003, Pages 171-177

Polyethylene glycol-conjugated adenosine phosphorylase: Development of alternative enzyme therapy for adenosine deaminase deficiency

Author keywords

Adenosine phosphorylase; PEG AP; Polyethylene glycol; Purine nucleoside phosphorylase

Indexed keywords

ADENOSINE PHOSPHATE PHOSPHATASE; DEOXYADENOSINE; INOSINE; MACROGOL DERIVATIVE; POLYETHYLENEGLYCOL CONJUGATED ADENOSINE PHOSPHORYLASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; URIC ACID;

EID: 0037456687     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4439(03)00016-4     Document Type: Review
Times cited : (5)

References (33)
  • 1
    • 0033410175 scopus 로고    scopus 로고
    • Design of an adenosine phosphorylase by active-site modification of murine purine nucleoside phosphorylase. Enzyme kinetics and molecular dynamics simulation of Asn-243 and Lys-244 substitutions of purine nucleoside phosphorylase
    • Maynes J.T., Yam W.-S., Jenuth J.P., Yuan R.G., Litster S.A., Phipps B.M., Snyder F.F. Design of an adenosine phosphorylase by active-site modification of murine purine nucleoside phosphorylase. Enzyme kinetics and molecular dynamics simulation of Asn-243 and Lys-244 substitutions of purine nucleoside phosphorylase. Biochem. J. 344:1999;585-592.
    • (1999) Biochem. J. , vol.344 , pp. 585-592
    • Maynes, J.T.1    Yam, W.-S.2    Jenuth, J.P.3    Yuan, R.G.4    Litster, S.A.5    Phipps, B.M.6    Snyder, F.F.7
  • 2
    • 0029081965 scopus 로고
    • PEG-ADA replacement therapy for adenosine deaminase deficiency: An update after 8.5 years
    • Hershfield M.S. PEG-ADA replacement therapy for adenosine deaminase deficiency: an update after 8.5 years. Clin. Immunol. Immunopathol. 76:1995;S228-S232.
    • (1995) Clin. Immunol. Immunopathol. , vol.76
    • Hershfield, M.S.1
  • 3
    • 0031723552 scopus 로고    scopus 로고
    • Adenosine deaminase deficiency: Clinical expression, molecular basis, and therapy
    • Hershfield M.S. Adenosine deaminase deficiency: clinical expression, molecular basis, and therapy. Semin. Hematol. 35:1998;291-298.
    • (1998) Semin. Hematol. , vol.35 , pp. 291-298
    • Hershfield, M.S.1
  • 4
    • 0027232403 scopus 로고
    • Suppression of an antibody to adenosine-deaminase (ADA) in an ADA-deficient patient receiving polyethylene glycol modified adenosine deaminase
    • Chum J.D., Lee N., Kobayashi R.H., Chaffee S., Hershfield M.S., Stiehm E.R. Suppression of an antibody to adenosine-deaminase (ADA) in an ADA-deficient patient receiving polyethylene glycol modified adenosine deaminase. Ann. Allergy. 70:1993;462-466.
    • (1993) Ann. Allergy , vol.70 , pp. 462-466
    • Chum, J.D.1    Lee, N.2    Kobayashi, R.H.3    Chaffee, S.4    Hershfield, M.S.5    Stiehm, E.R.6
  • 5
    • 0034069531 scopus 로고    scopus 로고
    • Extreme thrombocytosis in response to PEG-ADA: Early therapeutic and risk indicator
    • Marwaha V.R., Italia D.H., Esper F., Hostoffer R.W. Extreme thrombocytosis in response to PEG-ADA: early therapeutic and risk indicator. Clin. Pediatr. 39:2000;183-186.
    • (2000) Clin. Pediatr. , vol.39 , pp. 183-186
    • Marwaha, V.R.1    Italia, D.H.2    Esper, F.3    Hostoffer, R.W.4
  • 6
    • 0031914978 scopus 로고    scopus 로고
    • Cell to cell contact is not required for bystander cell killing by Escherichia coli purine nucleoside phosphorylase
    • Hughes B.W., King S.A., Allan P.W., Parker W.B., Sorscher E.J. Cell to cell contact is not required for bystander cell killing by Escherichia coli purine nucleoside phosphorylase. J. Biol. Chem. 273:1998;2322-2328.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2322-2328
    • Hughes, B.W.1    King, S.A.2    Allan, P.W.3    Parker, W.B.4    Sorscher, E.J.5
  • 8
    • 0031572855 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli purine nucleoside phosphorylase: A comparison with the human enzyme reveals a conserved topology
    • Mao C., Cook W.J., Zhou M., Koszalka G.W., Krenitsky T.A., Ealick S.E. The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology. Structure. 5:1997;1373-1383.
    • (1997) Structure , vol.5 , pp. 1373-1383
    • Mao, C.1    Cook, W.J.2    Zhou, M.3    Koszalka, G.W.4    Krenitsky, T.A.5    Ealick, S.E.6
  • 9
    • 0025069455 scopus 로고
    • Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin
    • Bzowska A., Kulikowska E., Shugar D. Properties of purine nucleoside phosphorylase (PNP) of mammalian and bacterial origin. Z. Naturforsch., C. 45:1990;59-70.
    • (1990) Z. Naturforsch., C , vol.45 , pp. 59-70
    • Bzowska, A.1    Kulikowska, E.2    Shugar, D.3
  • 10
    • 0027497680 scopus 로고
    • Specific adenosine phosphorylase from hepatopancreas of gastropod Helix pomatia
    • Trembacz H., Jezewska M.M. Specific adenosine phosphorylase from hepatopancreas of gastropod Helix pomatia. Comp. Biochem. Physiol., B. 104:1993;481-487.
    • (1993) Comp. Biochem. Physiol., B , vol.104 , pp. 481-487
    • Trembacz, H.1    Jezewska, M.M.2
  • 11
    • 0037143547 scopus 로고    scopus 로고
    • PNP from Trichonomas vaginalis is a homologue of the bacterial enzyme
    • Munagala N., Wang C.C. PNP from Trichonomas vaginalis is a homologue of the bacterial enzyme. Biochemistry. 41:2002;10382-10389.
    • (2002) Biochemistry , vol.41 , pp. 10382-10389
    • Munagala, N.1    Wang, C.C.2
  • 12
    • 0036479331 scopus 로고    scopus 로고
    • Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum
    • Kicska G.A., Tyler P.C., Evans G.B., Furneaux R.H., Kim K., Schramm V.L. Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum. J. Biol. Chem. 277:2002;3219-3225.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3219-3225
    • Kicska, G.A.1    Tyler, P.C.2    Evans, G.B.3    Furneaux, R.H.4    Kim, K.5    Schramm, V.L.6
  • 13
    • 0030964925 scopus 로고    scopus 로고
    • Point mutations at the purine nucleoside phosphorylase locus impair thymocyte differentiation in the mouse
    • Snyder F.F., Jenuth J.P., Mably E.R., Mangat R.K. Point mutations at the purine nucleoside phosphorylase locus impair thymocyte differentiation in the mouse. Proc. Natl. Acad. Sci. U. S. A. 94:1997;2522-2527.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2522-2527
    • Snyder, F.F.1    Jenuth, J.P.2    Mably, E.R.3    Mangat, R.K.4
  • 15
    • 0028147268 scopus 로고
    • Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein
    • Watson E., Shah B., DePrince R., Hendren R.W., Nelson R. Matrix-assisted laser desorption mass spectrometric analysis of a pegylated recombinant protein. BioTechniques. 16:1994;278-281.
    • (1994) BioTechniques , vol.16 , pp. 278-281
    • Watson, E.1    Shah, B.2    DePrince, R.3    Hendren, R.W.4    Nelson, R.5
  • 16
    • 0035284411 scopus 로고    scopus 로고
    • PEGylation: A review of problems and solutions
    • Veronese F.M. PEGylation: a review of problems and solutions. Biomaterials. 22:2001;405-417.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 17
    • 0020612685 scopus 로고
    • Specific toxicity of 2-chlorodeoxyadenosine toward resting and proliferating human lymphocytes
    • Carson D.A., Wasson D.B., Taetle R., Yu A. Specific toxicity of 2-chlorodeoxyadenosine toward resting and proliferating human lymphocytes. Blood. 62:1983;737-743.
    • (1983) Blood , vol.62 , pp. 737-743
    • Carson, D.A.1    Wasson, D.B.2    Taetle, R.3    Yu, A.4
  • 18
    • 0027740067 scopus 로고
    • 2-Chlorodeoxyadenosine: Hairy cell leukemia takes a surprising turn
    • Beutler E., Carson D.A. 2-Chlorodeoxyadenosine: hairy cell leukemia takes a surprising turn. Blood Cells. 19:1993;559-568.
    • (1993) Blood Cells , vol.19 , pp. 559-568
    • Beutler, E.1    Carson, D.A.2
  • 19
    • 0028046704 scopus 로고
    • Development of an assay method for purine catabolic enzymes in the mouse and its adaptation for use on an autoanalyzer
    • Le Tissier P.R., Peters J., Skidmore C.J. Development of an assay method for purine catabolic enzymes in the mouse and its adaptation for use on an autoanalyzer. Anal. Biochem. 222:1994;168-175.
    • (1994) Anal. Biochem. , vol.222 , pp. 168-175
    • Le Tissier, P.R.1    Peters, J.2    Skidmore, C.J.3
  • 20
    • 0028341221 scopus 로고
    • An HPLC-linked assay of phosphoribosylpyrophosphate synthetase activity in the erythrocytes of adults and children with neurological disorders
    • Micheli V., Rocchigiani M., Pompucci G. An HPLC-linked assay of phosphoribosylpyrophosphate synthetase activity in the erythrocytes of adults and children with neurological disorders. Clin. Chim. Acta. 227:1994;79-86.
    • (1994) Clin. Chim. Acta , vol.227 , pp. 79-86
    • Micheli, V.1    Rocchigiani, M.2    Pompucci, G.3
  • 21
    • 4243230052 scopus 로고
    • Secondary deficiency of deoxyguanosine kinase associated with purine nucleoside phosphorylase deficiency in the mouse
    • Mably E.R., Jenuth J.P., Fung E., Snyder F.F. Secondary deficiency of deoxyguanosine kinase associated with purine nucleoside phosphorylase deficiency in the mouse. Biochim. Biophys. Acta. 999:1994;333-444.
    • (1994) Biochim. Biophys. Acta , vol.999 , pp. 333-444
    • Mably, E.R.1    Jenuth, J.P.2    Fung, E.3    Snyder, F.F.4
  • 22
    • 0018194525 scopus 로고
    • Cytotoxic and metabolic effects of adenosine and adenine on human lymphoblasts
    • Snyder F.F., Hershfield M.S., Seegmiller J.E. Cytotoxic and metabolic effects of adenosine and adenine on human lymphoblasts. Cancer Res. 38:1978;2357-2362.
    • (1978) Cancer Res. , vol.38 , pp. 2357-2362
    • Snyder, F.F.1    Hershfield, M.S.2    Seegmiller, J.E.3
  • 23
    • 0032126845 scopus 로고    scopus 로고
    • PEGylation of cytokines and other therapeutic proteins and peptides: The importance of biological optimisation of coupling techniques
    • Francis G.E., Fisher D., Delgado C., Malik F., Gardiner A., Neale D. PEGylation of cytokines and other therapeutic proteins and peptides: the importance of biological optimisation of coupling techniques. Int. J. Hematol. 68:1998;1-18.
    • (1998) Int. J. Hematol. , vol.68 , pp. 1-18
    • Francis, G.E.1    Fisher, D.2    Delgado, C.3    Malik, F.4    Gardiner, A.5    Neale, D.6
  • 24
    • 0031733869 scopus 로고    scopus 로고
    • Attachment of degradable poly(ethylene glycol) to proteins has the potential to increase therapeutic efficacy
    • Roberts M.J., Harris J.M. Attachment of degradable poly(ethylene glycol) to proteins has the potential to increase therapeutic efficacy. J. Pharm. Sci. 87:1998;1440-1445.
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1440-1445
    • Roberts, M.J.1    Harris, J.M.2
  • 26
    • 0025784230 scopus 로고
    • Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol
    • Hershfield M.S., Chaffee S., Koro-Johnson L., Mary A., Smith A.A., Short S.A. Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl. Acad. Sci. U. S. A. 88:1991;7185-7189.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7185-7189
    • Hershfield, M.S.1    Chaffee, S.2    Koro-Johnson, L.3    Mary, A.4    Smith, A.A.5    Short, S.A.6
  • 28
    • 0035281760 scopus 로고    scopus 로고
    • Phase I trial of 40-kd branched pegylated interferon alfa-2a for patients with advanced renal cell carcinoma
    • Motzer R.J., Rakhit A., Ginsberg M., Rittweger K., Vuky J., Yu R., Fettner S., Hooftman L. Phase I trial of 40-kd branched pegylated interferon alfa-2a for patients with advanced renal cell carcinoma. J. Clin. Oncol. 19:2001;1312-1319.
    • (2001) J. Clin. Oncol. , vol.19 , pp. 1312-1319
    • Motzer, R.J.1    Rakhit, A.2    Ginsberg, M.3    Rittweger, K.4    Vuky, J.5    Yu, R.6    Fettner, S.7    Hooftman, L.8
  • 30
    • 0037124508 scopus 로고    scopus 로고
    • Use of peginterferon alfa-2a (40 KD) (Pegasys) for the treatment of hepatitis C
    • Rajender R.K., Modi M.W., Pedder S. Use of peginterferon alfa-2a (40 KD) (Pegasys) for the treatment of hepatitis C. Adv. Drug Deliv. Rev. 54:2002;571-586.
    • (2002) Adv. Drug Deliv. Rev. , vol.54 , pp. 571-586
    • Rajender, R.K.1    Modi, M.W.2    Pedder, S.3
  • 31
    • 85088329785 scopus 로고
    • Marked hypouricemia in purine nucleoside phosphorylase deficiency-serendipitous finding on screen
    • Timms P.M., Simmonds H.A., Bold A.M. Marked hypouricemia in purine nucleoside phosphorylase deficiency-serendipitous finding on screen. Clin. Chem. 42:1966;985.
    • (1966) Clin. Chem. , vol.42 , pp. 985
    • Timms, P.M.1    Simmonds, H.A.2    Bold, A.M.3
  • 32
    • 0024950676 scopus 로고
    • Genetic deficiency of purine nucleoside phosphorylase in the mouse. Characterization of partially and severely enzyme deficient mutants
    • Mably E.R., Fung E., Snyder F.F. Genetic deficiency of purine nucleoside phosphorylase in the mouse. Characterization of partially and severely enzyme deficient mutants. Genome. 32:1989;1026-1032.
    • (1989) Genome , vol.32 , pp. 1026-1032
    • Mably, E.R.1    Fung, E.2    Snyder, F.F.3
  • 33
    • 0018233086 scopus 로고
    • Uric acid metabolism in homozygous and heterozygous muscular dystrophic mice
    • Dju M.Y., Yu T.-F. Uric acid metabolism in homozygous and heterozygous muscular dystrophic mice. Am. J. Physiol. 234:1978;E421-E425.
    • (1978) Am. J. Physiol. , vol.234
    • Dju, M.Y.1    Yu, T.-F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.