메뉴 건너뛰기




Volumn 288, Issue 38, 2013, Pages 27444-27455

Efficient use of exogenous isoprenols for protein isoprenylation by MDA-MB-231 cells is regulated independently of the mevalonate pathway

Author keywords

[No Author keywords available]

Indexed keywords

ANILINE; BIOSYNTHESIS; CELL CULTURE; DISEASES; DRUG PRODUCTS; LIPIDS; MAMMALS; MASS SPECTROMETRY; PROTEINS;

EID: 84884578809     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.482307     Document Type: Article
Times cited : (12)

References (25)
  • 1
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., and Brown, M. S. (1990) Regulation of the mevalonate pathway. Nature 343, 425-430
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 2
    • 77951592990 scopus 로고    scopus 로고
    • Functional characterization of the atypical integral membrane lipid phosphatase PDP1/PPAPDC2 identifies a pathway for interconversion of isoprenols and isoprenoid phosphates in mammalian cells
    • Miriyala, S., Subramanian, T., Panchatcharam, M., Ren, H., McDermott, M. I., Sunkara, M., Drennan, T., Smyth, S. S., Spielmann, H. P., and Morris, A. J. (2010) Functional characterization of the atypical integral membrane lipid phosphatase PDP1/PPAPDC2 identifies a pathway for interconversion of isoprenols and isoprenoid phosphates in mammalian cells. J. Biol. Chem. 285, 13918-13929
    • (2010) J. Biol. Chem. , vol.285 , pp. 13918-13929
    • Miriyala, S.1    Subramanian, T.2    Panchatcharam, M.3    Ren, H.4    McDermott, M.I.5    Sunkara, M.6    Drennan, T.7    Smyth, S.S.8    Spielmann, H.P.9    Morris, A.J.10
  • 4
    • 78651095782 scopus 로고    scopus 로고
    • Absence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin
    • Yang, S. H., Chang, S. Y., Ren, S., Wang, Y., Andres, D. A., Spielmann, H. P., Fong, L. G., and Young, S. G. (2011) Absence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin. Hum. Mol. Genet. 20, 436-444
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 436-444
    • Yang, S.H.1    Chang, S.Y.2    Ren, S.3    Wang, Y.4    Andres, D.A.5    Spielmann, H.P.6    Fong, L.G.7    Young, S.G.8
  • 5
    • 77950666952 scopus 로고    scopus 로고
    • A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting
    • Onono, F. O., Morgan, M. A., Spielmann, H. P., Andres, D. A., Subramanian, T., Ganser, A., and Reuter, C. W. (2010) A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting. Mol. Cell. Proteomics 9, 742-751
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 742-751
    • Onono, F.O.1    Morgan, M.A.2    Spielmann, H.P.3    Andres, D.A.4    Subramanian, T.5    Ganser, A.6    Reuter, C.W.7
  • 7
    • 0028991308 scopus 로고
    • Metabolism of [3H]farnesol to cholesterol and cholesterogenic intermediates in the living rat eye
    • Fliesler, S. J., and Keller, R. K. (1995) Metabolism of [3H]farnesol to cholesterol and cholesterogenic intermediates in the living rat eye. Biochem. Biophys. Res. Commun. 210, 695-702
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 695-702
    • Fliesler, S.J.1    Keller, R.K.2
  • 8
    • 0036198699 scopus 로고    scopus 로고
    • Farnesol and geranylgeraniol: Prevention and reversion of lovastatin-induced effects in NIH3T3 cells
    • Ownby, S. E., and Hohl, R. J. (2002) Farnesol and geranylgeraniol: prevention and reversion of lovastatin-induced effects in NIH3T3 cells. Lipids 37, 185-192
    • (2002) Lipids , vol.37 , pp. 185-192
    • Ownby, S.E.1    Hohl, R.J.2
  • 9
    • 0031800322 scopus 로고    scopus 로고
    • Geranylgeraniol overcomes the block of cell proliferation by lovastatin in C6 glioma cells
    • Crick, D. C., Andres, D. A., Danesi, R., Macchia, M., and Waechter, C. J. (1998) Geranylgeraniol overcomes the block of cell proliferation by lovastatin in C6 glioma cells. J. Neurochem. 70, 2397-2405
    • (1998) J. Neurochem. , vol.70 , pp. 2397-2405
    • Crick, D.C.1    Andres, D.A.2    Danesi, R.3    Macchia, M.4    Waechter, C.J.5
  • 10
    • 84863317657 scopus 로고    scopus 로고
    • Novel aspects of mevalonate pathway inhibitors as antitumor agents
    • Thurnher, M., Nussbaumer, O., and Gruenbacher, G. (2012) Novel aspects of mevalonate pathway inhibitors as antitumor agents. Clin. Cancer Res. 18, 3524-3531
    • (2012) Clin. Cancer Res. , vol.18 , pp. 3524-3531
    • Thurnher, M.1    Nussbaumer, O.2    Gruenbacher, G.3
  • 11
    • 77951709095 scopus 로고    scopus 로고
    • Pleiotropic effects of statins. Basic research and clinical perspectives
    • Zhou, Q., and Liao, J. K. (2010) Pleiotropic effects of statins. Basic research and clinical perspectives. Circ. J. 74, 818-826
    • (2010) Circ. J. , vol.74 , pp. 818-826
    • Zhou, Q.1    Liao, J.K.2
  • 12
    • 50149093463 scopus 로고    scopus 로고
    • Molecular basis for statin-induced muscle toxicity: Implications and possibilities
    • Buettner, C., and Lecker, S. H. (2008) Molecular basis for statin-induced muscle toxicity: implications and possibilities. Pharmacogenomics 9, 1133-1142
    • (2008) Pharmacogenomics , vol.9 , pp. 1133-1142
    • Buettner, C.1    Lecker, S.H.2
  • 18
    • 84880776374 scopus 로고    scopus 로고
    • Syntheses of deuterium labeled prenyldiphosphate and prenylcysteine analogues for in vivo mass spectrometric quantification
    • Subramanian, T., Subramanian, K. L., Sunkara, M., Onono, F. O., Morris, A. J., and Spielmann, H. P. (2013) Syntheses of deuterium labeled prenyldiphosphate and prenylcysteine analogues for in vivo mass spectrometric quantification. J. Labelled Comp. Radiopharm. 56, 370-375
    • (2013) J. Labelled Comp. Radiopharm. , vol.56 , pp. 370-375
    • Subramanian, T.1    Subramanian, K.L.2    Sunkara, M.3    Onono, F.O.4    Morris, A.J.5    Spielmann, H.P.6
  • 19
    • 9944233982 scopus 로고    scopus 로고
    • Simultaneous determination of farnesyl and geranylgeranyl pyrophosphate levels in cultured cells
    • Tong, H., Holstein, S. A., and Hohl, R. J. (2005) Simultaneous determination of farnesyl and geranylgeranyl pyrophosphate levels in cultured cells. Anal. Biochem. 336, 51-59
    • (2005) Anal. Biochem. , vol.336 , pp. 51-59
    • Tong, H.1    Holstein, S.A.2    Hohl, R.J.3
  • 20
    • 70449533661 scopus 로고    scopus 로고
    • Quantitative determination of geranyl diphosphate levels in cultured human cells
    • Holstein, S. A., Tong, H., Kuder, C. H., and Hohl, R. J. (2009) Quantitative determination of geranyl diphosphate levels in cultured human cells. Lipids 44, 1055-1062
    • (2009) Lipids , vol.44 , pp. 1055-1062
    • Holstein, S.A.1    Tong, H.2    Kuder, C.H.3    Hohl, R.J.4
  • 21
    • 0033539526 scopus 로고    scopus 로고
    • Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions
    • Thai, L., Rush, J. S., Maul, J. E., Devarenne, T., Rodgers, D. L., Chappell, J., and Waechter, C. J. (1999) Farnesol is utilized for isoprenoid biosynthesis in plant cells via farnesyl pyrophosphate formed by successive monophosphorylation reactions. Proc. Natl. Acad. Sci. U. S. A. 96, 13080-13085
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13080-13085
    • Thai, L.1    Rush, J.S.2    Maul, J.E.3    Devarenne, T.4    Rodgers, D.L.5    Chappell, J.6    Waechter, C.J.7
  • 22
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller, R. K., Zhao, Z., Chambers, C., and Ness, G. C. (1996) Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver. Arch. Biochem. Biophys. 328, 324-330
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.C.4
  • 23
    • 0037064133 scopus 로고    scopus 로고
    • Prenylcysteine lyase deficiency in mice results in the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver
    • Beigneux, A., Withycombe, S. K., Digits, J. A., Tschantz, W. R., Weinbaum, C. A., Griffey, S. M., Bergo, M., Casey, P. J., and Young, S. G. (2002) Prenylcysteine lyase deficiency in mice results in the accumulation of farnesylcysteine and geranylgeranylcysteine in brain and liver. J. Biol. Chem. 277, 38358-38363
    • (2002) J. Biol. Chem. , vol.277 , pp. 38358-38363
    • Beigneux, A.1    Withycombe, S.K.2    Digits, J.A.3    Tschantz, W.R.4    Weinbaum, C.A.5    Griffey, S.M.6    Bergo, M.7    Casey, P.J.8    Young, S.G.9
  • 24
    • 0033591216 scopus 로고    scopus 로고
    • The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae
    • Faulkner, A., Chen, X., Rush, J., Horazdovsky, B., Waechter, C. J., Carman, G. M., and Sternweis, P. C. (1999) The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. J. Biol. Chem. 274, 14831-14837
    • (1999) J. Biol. Chem. , vol.274 , pp. 14831-14837
    • Faulkner, A.1    Chen, X.2    Rush, J.3    Horazdovsky, B.4    Waechter, C.J.5    Carman, G.M.6    Sternweis, P.C.7
  • 25
    • 84864696245 scopus 로고    scopus 로고
    • The pleiotropic effects and therapeutic potential of the hydroxy-methyl-glutaryl-CoA reductase inhibitors in malignancies: A comprehensive review
    • Zeichner, S., Mihos, C. G., and Santana, O. (2012) The pleiotropic effects and therapeutic potential of the hydroxy-methyl-glutaryl-CoA reductase inhibitors in malignancies: a comprehensive review. J. Cancer Res. Ther. 8, 176-183
    • (2012) J. Cancer Res. Ther. , vol.8 , pp. 176-183
    • Zeichner, S.1    Mihos, C.G.2    Santana, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.