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Volumn 49, Issue 10, 2006, Pages 2998-3002

Discovery of a potent, nonpolyglutamatable inhibitor of glycinamide ribonucleotide transformylase

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID; FOLIC ACID; LOMETREXOL; METHOTREXATE; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; POLYGLUTAMIC ACID; TETRAZOLE DERIVATIVE;

EID: 33646743834     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm0601147     Document Type: Article
Times cited : (10)

References (28)
  • 1
    • 33646750785 scopus 로고
    • 2-Amino-N-ribosylacetamide 5′-phosphate (glycinamide ribotide) transformylase
    • Warren, L.; Buchanan, J. M. 2-Amino-N-ribosylacetamide 5′-phosphate (glycinamide ribotide) transformylase. J. Biol. Chem. 1957, 229, 1979-1992.
    • (1957) J. Biol. Chem. , vol.229 , pp. 1979-1992
    • Warren, L.1    Buchanan, J.M.2
  • 2
    • 0017905124 scopus 로고
    • N10-Formyltetrahydrufolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli
    • Dev, I. K.; Harvey, R. J. N10-Formyltetrahydrufolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli. J. Biol. Chem. 1978, 253, 4242-4244.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4242-4244
    • Dev, I.K.1    Harvey, R.J.2
  • 3
    • 0012018743 scopus 로고
    • Selective killing of human malignant cell lines deficient in methylthioadenosine phosphorylase, a purine metabolic enzyme
    • (a) Kamatani, N.; Nelson-Rees, W. A.; Carson, D. A. Selective killing of human malignant cell lines deficient in methylthioadenosine phosphorylase, a purine metabolic enzyme. Proc. Natl. Acad. Sci. U.S.A. 1981, 78, 1219-1223.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 1219-1223
    • Kamatani, N.1    Nelson-Rees, W.A.2    Carson, D.A.3
  • 4
    • 0029774143 scopus 로고    scopus 로고
    • Methylthioadenosine phosphorylase cDNA transfection alters sensitivity to depletion of purine and methionine in A549 lung cancer cells
    • See also: (b) Hori, H.; Tran, P.; Carrera, C. J.; Hori, Y.; Rosenbach, M. D.; Carson, D. A.; Nobori, T. Methylthioadenosine phosphorylase cDNA transfection alters sensitivity to depletion of purine and methionine in A549 lung cancer cells. Cancer Res. 1996, 56, 5653-5658.
    • (1996) Cancer Res. , vol.56 , pp. 5653-5658
    • Hori, H.1    Tran, P.2    Carrera, C.J.3    Hori, Y.4    Rosenbach, M.D.5    Carson, D.A.6    Nobori, T.7
  • 5
    • 0023078927 scopus 로고
    • Synthesis of purines in human lymphoblast cells deficient in methylthioadenosine phosphorylase activity
    • Gordon, R. B.; Blackwell, K.; Emmerson, B. T. Synthesis of purines in human lymphoblast cells deficient in methylthioadenosine phosphorylase activity. Biochim. Biophys. Acta 1987, 927, 1-7.
    • (1987) Biochim. Biophys. Acta , vol.927 , pp. 1-7
    • Gordon, R.B.1    Blackwell, K.2    Emmerson, B.T.3
  • 6
    • 0036100974 scopus 로고    scopus 로고
    • Methylthioadenosine phosphorylase as target for chemoselective treatment of T-cell acute lymphoblastic leukemic cells
    • Efferth, T.; Miyachi, H.; Drexler, H. G.; Gebhart, E. Methylthioadenosine phosphorylase as target for chemoselective treatment of T-cell acute lymphoblastic leukemic cells. Blood Cells, Mol. Dis. 2002, 28, 47-56.
    • (2002) Blood Cells, Mol. Dis. , vol.28 , pp. 47-56
    • Efferth, T.1    Miyachi, H.2    Drexler, H.G.3    Gebhart, E.4
  • 7
    • 0030864215 scopus 로고    scopus 로고
    • - malignant cells: Restoration of methylthioadenosine phosphorylase-dependent salvage pathways and alterations of sensitivity to inhibitors of purine de novo synthesis
    • - malignant cells: restoration of methylthioadenosine phosphorylase-dependent salvage pathways and alterations of sensitivity to inhibitors of purine de novo synthesis. Mol. Pharmacol. 1997, 52, 903-911.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 903-911
    • Chen, Z.H.1    Olopade, O.I.2    Savarese, T.M.3
  • 9
    • 0025817134 scopus 로고
    • Decreased folypolyglutamate synthase activity as a mechanism of methotrexate resistance in CCRF-CEM human leukemia sublines
    • McCloskey, D. E.; McGuire, J. J.; Russel, C. A.; Rowan, B. G.; Bertino, J. R.; Pizzorno, G.; Mini, E. J. Decreased folypolyglutamate synthase activity as a mechanism of methotrexate resistance in CCRF-CEM human leukemia sublines. J. Biol. Chem. 1991, 266, 6181-6187.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6181-6187
    • McCloskey, D.E.1    McGuire, J.J.2    Russel, C.A.3    Rowan, B.G.4    Bertino, J.R.5    Pizzorno, G.6    Mini, E.J.7
  • 10
    • 0037377560 scopus 로고    scopus 로고
    • Decreased expression of the reduced folate carrier and folypolyglutamate synthetase is the basis for acquired resistance to the pemetrexed antifolate (LY231514) in an L1210 murine leukemia cell line
    • Wang, Y.; Zhao, R.; Goldman, I. D. Decreased expression of the reduced folate carrier and folypolyglutamate synthetase is the basis for acquired resistance to the pemetrexed antifolate (LY231514) in an L1210 murine leukemia cell line. Biochem. Pharmacol. 2003, 65, 1163-1170.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1163-1170
    • Wang, Y.1    Zhao, R.2    Goldman, I.D.3
  • 12
    • 0020360963 scopus 로고
    • Characteristics of methotrexate polyglutamate formation in cultured hepatic cells
    • Balinska, M.; Nimec, Z.; Galivan, J. Characteristics of methotrexate polyglutamate formation in cultured hepatic cells. Arch. Biochem. Biophys. 1982, 216, 466-476.
    • (1982) Arch. Biochem. Biophys. , vol.216 , pp. 466-476
    • Balinska, M.1    Nimec, Z.2    Galivan, J.3
  • 13
  • 15
    • 0028960513 scopus 로고
    • Nonglutamate type pyrrolo[2,3-d]pyrimidine antifolates. I: Synthesis and biological properties of pyrrolo[2,3-d]pyrimidine antifolates containing tetrazole congeners of glutamic acid
    • Itoh, F.; Yukishige, K.; Wajima, M.; Ootsu, K.; Akimoto, H. Nonglutamate type pyrrolo[2,3-d]pyrimidine antifolates. I: Synthesis and biological properties of pyrrolo[2,3-d]pyrimidine antifolates containing tetrazole congeners of glutamic acid. Chem. Pharm. Bull. 1995, 43, 230-235.
    • (1995) Chem. Pharm. Bull. , vol.43 , pp. 230-235
    • Itoh, F.1    Yukishige, K.2    Wajima, M.3    Ootsu, K.4    Akimoto, H.5
  • 16
    • 0344708477 scopus 로고    scopus 로고
    • Deaza analogues of folic acid as antitumor agents
    • Kisliuk, R. L. Deaza analogues of folic acid as antitumor agents. Curr. Pharm. Des. 2003, 9, 2615-2625.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 2615-2625
    • Kisliuk, R.L.1
  • 17
    • 37049099338 scopus 로고
    • Synthesis of monoamides of methotrexate from L-glutamic acid monoamide tert-butyl esters
    • Antonjuk, D. J.; Boadle, D. K.; Cheung, H. T. A.; Tran, T. Q. Synthesis of monoamides of methotrexate from L-glutamic acid monoamide tert-butyl esters. J. Chem. Soc., Perkin Trans. 1 1984, 1989-2003.
    • (1984) J. Chem. Soc., Perkin Trans. 1 , pp. 1989-2003
    • Antonjuk, D.J.1    Boadle, D.K.2    Cheung, H.T.A.3    Tran, T.Q.4
  • 18
    • 0033539085 scopus 로고    scopus 로고
    • Moran, R. G. 5-Deazafolate analogues with a rotationally restricted glutamate or ornithine side chain: Synthesis and binding interaction with folypolyglutamate synthetase
    • Rosowsky, A.; Forsch, R. A.; Null, A.; Moran, R. G. 5-Deazafolate analogues with a rotationally restricted glutamate or ornithine side chain: synthesis and binding interaction with folypolyglutamate synthetase. J. Med. Chem. 1999, 42, 3510-3519.
    • (1999) J. Med. Chem. , vol.42 , pp. 3510-3519
    • Rosowsky, A.1    Forsch, R.A.2    Null, A.3
  • 20
    • 0037846072 scopus 로고    scopus 로고
    • Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-trifluoroacetyl-5,10-dideaza-acyclic-5,6,7,8- tetrahydrofolic acid
    • Zhang, Y.; Desharnais, J.; Marsilje, T. H.; Li, C.; Hedrick, M. P.; Gooljarsingh, L. T.; Tavassoli, A.; Benkovic, S. J.; Olson, A. J.; Boger, D. L.; Wilson, I. A. Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-trifluoroacetyl-5,10-dideaza-acyclic- 5,6,7,8-tetrahydrofolic acid. Biochemistry 2003, 42, 6043-6056.
    • (2003) Biochemistry , vol.42 , pp. 6043-6056
    • Zhang, Y.1    Desharnais, J.2    Marsilje, T.H.3    Li, C.4    Hedrick, M.P.5    Gooljarsingh, L.T.6    Tavassoli, A.7    Benkovic, S.J.8    Olson, A.J.9    Boger, D.L.10    Wilson, I.A.11
  • 23
    • 0038042134 scopus 로고    scopus 로고
    • An expedient route to the tetrazole analogues of α-amino acids
    • Demko, Z.; Sharpless, K. B. An expedient route to the tetrazole analogues of α-amino acids. Org. Lett. 2002, 4, 2525-2527.
    • (2002) Org. Lett. , vol.4 , pp. 2525-2527
    • Demko, Z.1    Sharpless, K.B.2
  • 24
    • 0026632377 scopus 로고
    • Synthesis and biological activity of open-chain analogues of 5,6,7,8-tetrahydrofolic acid-potential antitumor agents
    • Bigham, E. C.; Hodson, S. J.; Mallory, W. R.; Wilson, D.; Duch, D. S.; Smith, G. K.; Ferone, R. Synthesis and biological activity of open-chain analogues of 5,6,7,8-tetrahydrofolic acid-potential antitumor agents. J. Med Chem. 1992, 35, 1399-1410.
    • (1992) J. Med Chem. , vol.35 , pp. 1399-1410
    • Bigham, E.C.1    Hodson, S.J.2    Mallory, W.R.3    Wilson, D.4    Duch, D.S.5    Smith, G.K.6    Ferone, R.7
  • 26
    • 0028267011 scopus 로고
    • A novel class of monoglutamated antifolates exhibits tight-binding inhibition of human glycinamide ribonucleotide formyltransferase and potent activity against solid tumors
    • Habeck, L. L.; Leitner, T. A.; Shackelford, K. A.; Gossett, L. S.; Schultz, R. M.; Andis, S. L.; Shih, C.; Grindey, G. B.; Mendelsohn, L. G. A novel class of monoglutamated antifolates exhibits tight-binding inhibition of human glycinamide ribonucleotide formyltransferase and potent activity against solid tumors. Cancer Res. 1994, 54, 1021-1026.
    • (1994) Cancer Res. , vol.54 , pp. 1021-1026
    • Habeck, L.L.1    Leitner, T.A.2    Shackelford, K.A.3    Gossett, L.S.4    Schultz, R.M.5    Andis, S.L.6    Shih, C.7    Grindey, G.B.8    Mendelsohn, L.G.9
  • 27
    • 0025318636 scopus 로고
    • Biochemical and growth inhibition studies with methotrexate and aminopterin analogues containing a tetrazole ring in place of the γ-carboxyl group
    • This assay, as is standard, was conducted with 72 h of continuous exposure to the candidate inhibitors. It has been reported that nonpolyglutamatable antifolates may exhibit lower potency under short exposure (6 h) conditions due to rapid efflux from the cells. This was not examined with 10-12 herein. See: (a) McGuire, J. J.; Russell, C. A.; Bolanowska, W. E.; Freitag, C. M.; Jones, C. S.; Kalman, T. I. Biochemical and growth inhibition studies with methotrexate and aminopterin analogues containing a tetrazole ring in place of the γ-carboxyl group. Cancer Res. 1990, 50, 1726-1731.
    • (1990) Cancer Res. , vol.50 , pp. 1726-1731
    • McGuire, J.J.1    Russell, C.A.2    Bolanowska, W.E.3    Freitag, C.M.4    Jones, C.S.5    Kalman, T.I.6
  • 28
    • 0030988738 scopus 로고    scopus 로고
    • Cellular pharmacology and in vivo activity of a new anticancer agent ZD9331: A water soluble, nonpolyglutamatable, quinazoline-based inhibitor of thymidylate synthase
    • (b) Jackman, A. L.; Kimbell, R.; Aherne, G. W.; Brunton, L.; Jansen, G.; Stephens, T. C.; Smith, M. N.; Wardleworth, J. M.; Boyle, F. T. Cellular pharmacology and in vivo activity of a new anticancer agent ZD9331: a water soluble, nonpolyglutamatable, quinazoline-based inhibitor of thymidylate synthase. Clin. Cancer Res. 1997, 3, 911-921.
    • (1997) Clin. Cancer Res. , vol.3 , pp. 911-921
    • Jackman, A.L.1    Kimbell, R.2    Aherne, G.W.3    Brunton, L.4    Jansen, G.5    Stephens, T.C.6    Smith, M.N.7    Wardleworth, J.M.8    Boyle, F.T.9


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