메뉴 건너뛰기




Volumn 240, Issue 2, 1998, Pages 282-292

Induction of apoptosis in leukemia U937 cells by 5'-deoxy-5'- methylthioadenosine, a potent inhibitor of protein carboxylmethyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE;

EID: 0031856088     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4000     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0014603440 scopus 로고
    • Phosphate-stimulated breakdown of 5′-methylthioadenosine by rat ventral prostate
    • Pegg A. E., Williams-Ashman H. G. Phosphate-stimulated breakdown of 5′-methylthioadenosine by rat ventral prostate. Biochem. J. 115:1969;241-247.
    • (1969) Biochem. J. , vol.115 , pp. 241-247
    • Pegg, A.E.1    Williams-Ashman, H.G.2
  • 2
    • 85029466009 scopus 로고
    • Purification and properties of 5′-deoxy-5′-methylthioadenosine phosphorylase from rat spleen
    • Lee S. H., Cho Y. D. Purification and properties of 5′-deoxy-5′-methylthioadenosine phosphorylase from rat spleen. Korean Biochem. J. 26:1993;440-444.
    • (1993) Korean Biochem. J. , vol.26 , pp. 440-444
    • Lee, S.H.1    Cho, Y.D.2
  • 3
    • 0018591912 scopus 로고
    • The role of 5′-methylthioadenosine phosphorylase in 5′-methylthioadenosine-mediated inhibition of lymphocyte transformation
    • Ferro A., Vandenbark A. A., Marchitto K. The role of 5′-methylthioadenosine phosphorylase in 5′-methylthioadenosine-mediated inhibition of lymphocyte transformation. Biochim. Biophys. Acta. 588:1979;294-301.
    • (1979) Biochim. Biophys. Acta , vol.588 , pp. 294-301
    • Ferro, A.1    Vandenbark, A.A.2    Marchitto, K.3
  • 4
    • 0019445317 scopus 로고
    • Effect of 5′-methylthioadenosine and its analogs on murine lymphoid cell proliferation
    • Wolford R. W., MacDonald M. R., Zehfus B., Rogers T. J., Ferro A. Effect of 5′-methylthioadenosine and its analogs on murine lymphoid cell proliferation. Cancer Res. 41:1981;3035-3039.
    • (1981) Cancer Res. , vol.41 , pp. 3035-3039
    • Wolford, R.W.1    MacDonald, M.R.2    Zehfus, B.3    Rogers, T.J.4    Ferro, A.5
  • 5
    • 0020594942 scopus 로고
    • 5′-deoxy-5′-methylthioadenosine inhibition of rat T lymphocyte phosphodiesterase: Correlation with inhibition of con A induced proliferation
    • Christa L., Thuillier L., Perignon J. 5′-deoxy-5′-methylthioadenosine inhibition of rat T lymphocyte phosphodiesterase: Correlation with inhibition of con A induced proliferation. Biochem. Biophys. Res. Commun. 113:1983;425-432.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 425-432
    • Christa, L.1    Thuillier, L.2    Perignon, J.3
  • 6
    • 0026541956 scopus 로고
    • Lipopolysaccharide-induced NF-kB activation in mouse 70Z/3 pre-B lymphocytes is inhibited by mevinolin and 5′-methylthioadenosine: Roles of protein isoprenylation and carboxyl methylation reactions
    • Law R. E., Stimmel J. B., Damore M. A., Carter C., Clarke S., Wall R. Lipopolysaccharide-induced NF-kB activation in mouse 70Z/3 pre-B lymphocytes is inhibited by mevinolin and 5′-methylthioadenosine: Roles of protein isoprenylation and carboxyl methylation reactions. Mol. Cell. Biol. 12:1992;103-111.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 103-111
    • Law, R.E.1    Stimmel, J.B.2    Damore, M.A.3    Carter, C.4    Clarke, S.5    Wall, R.6
  • 7
    • 0018603417 scopus 로고
    • Relationship between inhibition of protein methylase I and inhibition of Rous sarcoma virus-induced cell transformation
    • Enouf J., Lawrence F., Tempete C., Robert-Gero M., Lederer E. Relationship between inhibition of protein methylase I and inhibition of Rous sarcoma virus-induced cell transformation. Cancer Res. 39:1979;4497-4502.
    • (1979) Cancer Res. , vol.39 , pp. 4497-4502
    • Enouf, J.1    Lawrence, F.2    Tempete, C.3    Robert-Gero, M.4    Lederer, E.5
  • 8
    • 0018992213 scopus 로고
    • Studies on substrate specificity ofS-adenosylmethionine:protein-carboxyl methyltransferase from calf brain
    • Oliva A., Galletti P., Zappia V. Studies on substrate specificity ofS-adenosylmethionine:protein-carboxyl methyltransferase from calf brain. Eur. J. Biochem. 104:1980;595-602.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 595-602
    • Oliva, A.1    Galletti, P.2    Zappia, V.3
  • 9
    • 0018924841 scopus 로고
    • Inhibition of lymphocyte transformation by a naturally occurring metabolite: 5′-methylthioadenosine
    • Vandenbark A. A., Ferro A. J., Barney C. L. Inhibition of lymphocyte transformation by a naturally occurring metabolite: 5′-methylthioadenosine. Cell. Immunol. 49:1980;26-33.
    • (1980) Cell. Immunol. , vol.49 , pp. 26-33
    • Vandenbark, A.A.1    Ferro, A.J.2    Barney, C.L.3
  • 10
    • 0019017137 scopus 로고
    • Studies of inhibition of rat spermidine synthase and spermine synthase
    • Hibasami H., Borchardt R. T., Chen S. Y., Coward J. K., Pegg A. E. Studies of inhibition of rat spermidine synthase and spermine synthase. Biochem. J. 187:1980;419-428.
    • (1980) Biochem. J. , vol.187 , pp. 419-428
    • Hibasami, H.1    Borchardt, R.T.2    Chen, S.Y.3    Coward, J.K.4    Pegg, A.E.5
  • 11
    • 0019992484 scopus 로고
    • Inhibition of lymphocyte cyclic AMP phosphodiesterase and lymphocyte function by 5′-methyl-thioadenosine
    • Wolberg G., Zimmerman T. P., Schmitges C. J., Duncan G. S., Deeprose R. D. Inhibition of lymphocyte cyclic AMP phosphodiesterase and lymphocyte function by 5′-methyl-thioadenosine. Biochem. Pharmacol. 31:1982;2201-2203.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 2201-2203
    • Wolberg, G.1    Zimmerman, T.P.2    Schmitges, C.J.3    Duncan, G.S.4    Deeprose, R.D.5
  • 12
    • 0019890571 scopus 로고
    • Inactivation ofS-adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine
    • Ferro A. J., Vandenbark A. A., MacDonald M. R. Inactivation ofS-adenosylhomocysteine hydrolase by 5′-deoxy-5′-methylthioadenosine. Biochem. Biophys. Res. Commun. 100:1981;523-531.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 523-531
    • Ferro, A.J.1    Vandenbark, A.A.2    MacDonald, M.R.3
  • 13
    • 0022344633 scopus 로고
    • Nerve growth factor and epidermal growth factor and induce rapid transient changes in proto-oncogene transcription in PC12 cells
    • Greenberg M. E., Greene L. A., Ziff E. B. Nerve growth factor and epidermal growth factor and induce rapid transient changes in proto-oncogene transcription in PC12 cells. J. Biol.Chem. 260:1988;14101-14110.
    • (1988) J. Biol.Chem. , vol.260 , pp. 14101-14110
    • Greenberg, M.E.1    Greene, L.A.2    Ziff, E.B.3
  • 14
    • 0021357849 scopus 로고
    • Differential inhibition of nerve growth factor and epidermal growth factor effects on the PC12 pheochromocytoma line
    • Seeley P. A., Rukenstein A., Connolly J. L., Greene L. A. Differential inhibition of nerve growth factor and epidermal growth factor effects on the PC12 pheochromocytoma line. J. Cell Biol. 98:1984;417-426.
    • (1984) J. Cell Biol. , vol.98 , pp. 417-426
    • Seeley, P.A.1    Rukenstein, A.2    Connolly, J.L.3    Greene, L.A.4
  • 15
    • 0642303588 scopus 로고
    • Nerve growth factor induces protein tyrosine phosphorylation
    • Maher P. A. Nerve growth factor induces protein tyrosine phosphorylation. Proc. Natl. Acad. Sci. USA. 85:1988;6788-6791.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6788-6791
    • Maher, P.A.1
  • 16
    • 0024411048 scopus 로고
    • Selective inhibition of nerve growth factor-stimulated protein kinases by K-252a and 5′-S-methyladenosine in PC12 cells
    • Smith D. S., King C. S., Pearson E., Gittinger C. K., Landreth G. E. Selective inhibition of nerve growth factor-stimulated protein kinases by K-252a and 5′-S-methyladenosine in PC12 cells. J. Neurochem. 53:1989;800-806.
    • (1989) J. Neurochem. , vol.53 , pp. 800-806
    • Smith, D.S.1    King, C.S.2    Pearson, E.3    Gittinger, C.K.4    Landreth, G.E.5
  • 18
  • 19
    • 0027363447 scopus 로고
    • Modification of eukaryotic signaling proteins by C-terminal methylation reactions
    • Hrycyna C. A., Clarke S. Modification of eukaryotic signaling proteins by C-terminal methylation reactions. Pharmacol. Ther. 59:1993;281-300.
    • (1993) Pharmacol. Ther. , vol.59 , pp. 281-300
    • Hrycyna, C.A.1    Clarke, S.2
  • 20
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem. 61:1992;355-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 21
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue
    • Cox A. D., Der C. J. Protein prenylation: More than just glue. Curr. Opin. Cell Biol. 4:1992;1008-1016.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 1008-1016
    • Cox, A.D.1    Der, C.J.2
  • 22
    • 0025845750 scopus 로고
    • The Caax motif is required for isoprenylation, carboxylmethylation, and nuclear membrane association of Lamin B2
    • Kitten G. T., Nigg E. A. The Caax motif is required for isoprenylation, carboxylmethylation, and nuclear membrane association of Lamin B2. J. Cell Biol. 113:1991;13-23.
    • (1991) J. Cell Biol. , vol.113 , pp. 13-23
    • Kitten, G.T.1    Nigg, E.A.2
  • 23
    • 0024519418 scopus 로고
    • Lamin B methylation and assembly into the nuclear envelope
    • Chelsky D., Sobotka C., O'Neill C. L. Lamin B methylation and assembly into the nuclear envelope. J. Biol. Chem. 264:1989;7637-7643.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7637-7643
    • Chelsky, D.1    Sobotka, C.2    O'Neill, C.L.3
  • 25
    • 0024470862 scopus 로고
    • Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin,and other cytotoxic anticancer drugs: A cautionary note
    • Kaufmann S. H. Induction of endonucleolytic DNA cleavage in human acute myelogenous leukemia cells by etoposide, camptothecin,and other cytotoxic anticancer drugs: A cautionary note. Cancer Res. 49:1989;5870-5878.
    • (1989) Cancer Res. , vol.49 , pp. 5870-5878
    • Kaufmann, S.H.1
  • 26
    • 0026672306 scopus 로고
    • Activation-driven T cell death. II. Quantitiative differences alone distinguish stimuli triggering nontransformed T cell proliferation or death
    • Ucker D. S., Meyers J., Obermiller P. S. Activation-driven T cell death. II. Quantitiative differences alone distinguish stimuli triggering nontransformed T cell proliferation or death. J. Immunol. 149:1992;1583-1592.
    • (1992) J. Immunol. , vol.149 , pp. 1583-1592
    • Ucker, D.S.1    Meyers, J.2    Obermiller, P.S.3
  • 27
    • 14844356354 scopus 로고
    • Degradation of lamin B1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei
    • Neamati N., A. Fernandez, S. Wright, Kiefer J., McConkey D. J. Degradation of lamin B1 precedes oligonucleosomal DNA fragmentation in apoptotic thymocytes and isolated thymocyte nuclei. J. Immunol. 154:1995;3788-3795.
    • (1995) J. Immunol. , vol.154 , pp. 3788-3795
    • Neamati, N.1    Fernandez, A.2    Wright, S.3    Kiefer, J.4    McConkey, D.J.5
  • 28
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao L., Perez D., White E. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135:1996;1441-1455.
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 29
    • 0023664184 scopus 로고
    • Cell cycle-dependent methyl esterification of lamin B
    • Chelsky D., Olson J. F., Koshland D. E. Jr. Cell cycle-dependent methyl esterification of lamin B. J. Biol. Chem. 262:1987;4303-4309.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4303-4309
    • Chelsky, D.1    Olson, J.F.2    Koshland D.E., Jr.3
  • 31
    • 0023840521 scopus 로고
    • Inhibition of phosphoinositide metabolism in human polymorphonuclear leukocytes by S-adenosylhomocysteine
    • Pike M. C., DeMeester C. A. Inhibition of phosphoinositide metabolism in human polymorphonuclear leukocytes by S-adenosylhomocysteine. J. Biol. Chem. 263:1988;3592-3599.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3592-3599
    • Pike, M.C.1    Demeester, C.A.2
  • 32
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxylmethyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein S., Berkower C., Michaelis S. Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxylmethyltransferase, and demonstration of its essential role in a-factor export. Mol. Cell Biol. 14:1994;1438-1449.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1438-1449
    • Sapperstein, S.1    Berkower, C.2    Michaelis, S.3
  • 33
    • 0024519418 scopus 로고
    • Lamin B methylation and assembly into the nuclear envelope
    • Chelsky D., Sobotka C., O'Neill C. L. Lamin B methylation and assembly into the nuclear envelope. J. Biol. Chem. 264:1989;7637-7643.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7637-7643
    • Chelsky, D.1    Sobotka, C.2    O'Neill, C.L.3
  • 34
    • 0029012269 scopus 로고
    • Evidence that Rap1 carboxylmethylation is involved in regulated insulin secretion
    • Leiser M., Efrat S., Fleisher N. Evidence that Rap1 carboxylmethylation is involved in regulated insulin secretion. Endocrinology. 136:1995;2521-2530.
    • (1995) Endocrinology , vol.136 , pp. 2521-2530
    • Leiser, M.1    Efrat, S.2    Fleisher, N.3
  • 35
    • 0029887332 scopus 로고    scopus 로고
    • Carboxylmethylation of the catalytic subunit of protein phosphatase 2A in insulin-secreting cells: Evidence for functional consequences on enzyme activity and insulin scretion
    • Kowluru A., Seavey S. E., Rabaglia M. E., Nesher R., Metz S. A. Carboxylmethylation of the catalytic subunit of protein phosphatase 2A in insulin-secreting cells: Evidence for functional consequences on enzyme activity and insulin scretion. Endocrinology. 137:1996;2315-2323.
    • (1996) Endocrinology , vol.137 , pp. 2315-2323
    • Kowluru, A.1    Seavey, S.E.2    Rabaglia, M.E.3    Nesher, R.4    Metz, S.A.5
  • 36
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie A. H. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature. 284:1980;555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 37
    • 0021367846 scopus 로고
    • Glucocorticoid activation of a calcium-dependent endonuclease in thymocyte nuclei leads to cell death
    • Cohen J. J., Duke R. C. Glucocorticoid activation of a calcium-dependent endonuclease in thymocyte nuclei leads to cell death. J. Immunol. 132:1984;38-42.
    • (1984) J. Immunol. , vol.132 , pp. 38-42
    • Cohen, J.J.1    Duke, R.C.2
  • 38
    • 0027479977 scopus 로고
    • Apoptosis: The biochemistry and molecular biology of programmed cell death
    • Schwartzman R. A., Cidlowski J. A. Apoptosis: The biochemistry and molecular biology of programmed cell death. Endocr. Rev. 14:1993;133-151.
    • (1993) Endocr. Rev. , vol.14 , pp. 133-151
    • Schwartzman, R.A.1    Cidlowski, J.A.2
  • 39
    • 0027217084 scopus 로고
    • Apoptotic death in epithelial cells: Cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation
    • Oberhammer F., Wilson J. W., Dive C., Morris I. D., Hickman J. A., Wakeling A. E., Walker P. R., Sikorska M. Apoptotic death in epithelial cells: Cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation. EMBO J. 12:1993;3679-3684.
    • (1993) EMBO J. , vol.12 , pp. 3679-3684
    • Oberhammer, F.1    Wilson, J.W.2    Dive, C.3    Morris, I.D.4    Hickman, J.A.5    Wakeling, A.E.6    Walker, P.R.7    Sikorska, M.8
  • 40
    • 0028290311 scopus 로고
    • Formation of large molecular weight fragments of DNA is a key committed step of apoptosis in thymocytes
    • Cohen G. M., Sun X. M., Fearnhead H., MacFarlane M., Brown D. G., Snowden R. T., Dinsdale D. Formation of large molecular weight fragments of DNA is a key committed step of apoptosis in thymocytes. J. Immunol. 153:1994;507-516.
    • (1994) J. Immunol. , vol.153 , pp. 507-516
    • Cohen, G.M.1    Sun, X.M.2    Fearnhead, H.3    MacFarlane, M.4    Brown, D.G.5    Snowden, R.T.6    Dinsdale, D.7
  • 42
    • 0029923176 scopus 로고    scopus 로고
    • Multiple pathways for apoptotic nuclear fragmentation
    • Dini L., Coppola S., Ruzittu M. T., Ghibelli L. Multiple pathways for apoptotic nuclear fragmentation. Exp. Cell Res. 223:1996;340-347.
    • (1996) Exp. Cell Res. , vol.223 , pp. 340-347
    • Dini, L.1    Coppola, S.2    Ruzittu, M.T.3    Ghibelli, L.4
  • 43
    • 0029831619 scopus 로고    scopus 로고
    • Calcium-dependent, interleukin 1 converting enzyme inhibitor-insensitive degradation of lamin B1 and DNA fragmentation in isolated thymocyte nuclei
    • McConkey D. J. Calcium-dependent, interleukin 1 converting enzyme inhibitor-insensitive degradation of lamin B1 and DNA fragmentation in isolated thymocyte nuclei. J. Biol. Chem. 271:1996;22398-22406.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22398-22406
    • McConkey, D.J.1
  • 44
    • 0028990125 scopus 로고
    • Yama a mammalian homolog of Ced-3, is a Crm A-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L., O'Rourke K., Desnoyers S., Zeng Z., Beidler D. R., Poirier G. G., Salvesen G. S., Dixit V. M. Yama a mammalian homolog of Ced-3, is a Crm A-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 45
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of stend regulatory element binding proteins (SREBPs) by cpp32 during apoptosis
    • Wang X., Zelenski N. G., Yang J., Sakai J., Brown M. S., Goldstein J. L. Cleavage of stend regulatory element binding proteins (SREBPs) by cpp32 during apoptosis. EMBO J. 15:1996;1012-1020.
    • (1996) EMBO J. , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 49
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser A., Evan G. A license to kill. Cell. 85:1996;781-784.
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 50
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts
    • Martin J. S., Green R. D. Protease activation during apoptosis: Death by a thousand cuts. Cell. 82:1995;349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, J.S.1    Green, R.D.2
  • 51
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 52
    • 0031586330 scopus 로고    scopus 로고
    • Antiapoptotic action of 1,25-dihydroxyvitamin D3 is associated with increased mitochondrial MCL-1 and RAF-1 proteins and reduced release of cytochrome C
    • Wang X., Studzinski G. P. Antiapoptotic action of 1,25-dihydroxyvitamin D3 is associated with increased mitochondrial MCL-1 and RAF-1 proteins and reduced release of cytochrome C. Exp.Cell Res. 235:1997;210-217.
    • (1997) Exp.Cell Res. , vol.235 , pp. 210-217
    • Wang, X.1    Studzinski, G.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.