메뉴 건너뛰기




Volumn 76, Issue 8, 1997, Pages 1001-1010

Manumycin and gliotoxin derivative KT7595 block Ras farnesylation and cell growth but do not disturb lamin farnesylation and localization in human tumour cells

Author keywords

Cell growth; Farnesyl protein transferase; Gliotoxin derivative; Manumycin; Nuclear lamin; Ras

Indexed keywords

CELL DNA; GLIOTOXIN; KT 7595; LAMIN; MANUMYCIN; PROTEIN FARNESYLTRANSFERASE; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 9844247549     PISSN: 00070920     EISSN: None     Source Type: Journal    
DOI: 10.1038/bjc.1997.499     Document Type: Article
Times cited : (39)

References (43)
  • 2
    • 0024094640 scopus 로고
    • Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei
    • Beck LA, Hosick TJ and Sinensky M (1988) Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei. J Cell Biol 107: 1307-1316
    • (1988) J Cell Biol , vol.107 , pp. 1307-1316
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 3
    • 0022977187 scopus 로고
    • Involvement of nuclear lamins in postmitotic reorganization of chromatin as demonstrated by microinjection of lamin antibodies
    • Benavente R and Krohne G (1986) Involvement of nuclear lamins in postmitotic reorganization of chromatin as demonstrated by microinjection of lamin antibodies. J Cell Biol 103: 1847-1854
    • (1986) J Cell Biol , vol.103 , pp. 1847-1854
    • Benavente, R.1    Krohne, G.2
  • 4
    • 0027732538 scopus 로고
    • Protein regulating Ras and its relatives
    • Boguski MS and McCormick F (1993) Protein regulating Ras and its relatives. Nature 366: 643-654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 5
    • 0026667497 scopus 로고
    • Tetrapeptide inhibitors of protein farnesyltransferase: Amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation
    • Brown MS, Goldstein JL, Paris KJ, Burnier JP and Marsters JR (1992) Tetrapeptide inhibitors of protein farnesyltransferase: amino-terminal substitution in phenylalanine-containing tetrapeptides restores farnesylation. Proc Natl Acad Sci USA 89: 8313-8316
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8313-8316
    • Brown, M.S.1    Goldstein, J.L.2    Paris, K.J.3    Burnier, J.P.4    Marsters, J.R.5
  • 6
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end mitosis
    • Burke B and Gerace L (1986) A cell free system to study reassembly of the nuclear envelope at the end mitosis. Cell 44: 639-652
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 7
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue?
    • Cox AD and Der CJ (1992) Protein prenylation: more than just glue? Curr Opin Cell Biol 4: 1008-1016
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 1008-1016
    • Cox, A.D.1    Der, C.J.2
  • 9
    • 0025940718 scopus 로고
    • Isoprenoid modification and plasma membrane association: Critical factors for ras oncogenicity
    • Der CJ and Cox AD (1991) Isoprenoid modification and plasma membrane association: critical factors for ras oncogenicity. Cancer Cells 3: 331-337
    • (1991) Cancer Cells , vol.3 , pp. 331-337
    • Der, C.J.1    Cox, A.D.2
  • 10
  • 11
    • 0027320616 scopus 로고
    • Peptidomimetic inhibitors of Ras farnesylation and function in whole cells
    • Garcia AM, Rowell C, Ackermann K, Kowalczyk JJ and Lewis MD (1993) Peptidomimetic inhibitors of Ras farnesylation and function in whole cells. J Biol Chem 268: 18415-18418
    • (1993) J Biol Chem , vol.268 , pp. 18415-18418
    • Garcia, A.M.1    Rowell, C.2    Ackermann, K.3    Kowalczyk, J.J.4    Lewis, M.D.5
  • 12
    • 0000506532 scopus 로고
    • The organization of chromatin loops: Characterization of a scaffold attachment site
    • Gasser SM and Laemmli UK (1986) The organization of chromatin loops: characterization of a scaffold attachment site. EMBO J 5: 511-518
    • (1986) EMBO J , vol.5 , pp. 511-518
    • Gasser, S.M.1    Laemmli, U.K.2
  • 13
    • 0020354530 scopus 로고
    • Nuclear lamina and the structure organization of the nuclear envelope
    • Gerace L and Blobel G (1982) Nuclear lamina and the structure organization of the nuclear envelope. Cold Spring Harbor Symp Quant Biol 46: 967-978
    • (1982) Cold Spring Harbor Symp Quant Biol , vol.46 , pp. 967-978
    • Gerace, L.1    Blobel, G.2
  • 14
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L and Burke B (1988) Functional organization of the nuclear envelope. Annu Rev Cell Biol 4: 335-374
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 15
    • 0025877861 scopus 로고
    • Ras C-terminal processing enzymes - New drug targets?
    • Gibbs JB (1991) Ras C-terminal processing enzymes - new drug targets? Cell 65: 1-4
    • (1991) Cell , vol.65 , pp. 1-4
    • Gibbs, J.B.1
  • 17
    • 0028331587 scopus 로고
    • Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic
    • Gibbs JB, Oliff A and Kohl NE (1994) Farnesyltransferase inhibitors: Ras research yields a potential cancer therapeutic. Cell 77: 175-178
    • (1994) Cell , vol.77 , pp. 175-178
    • Gibbs, J.B.1    Oliff, A.2    Kohl, N.E.3
  • 19
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock JF, Magee AI, Childs JE and Marshall CJ (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57: 1167-1177
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 21
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes H and Nigg EA (1994) The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J Cell Sci 107: 1019-1029
    • (1994) J Cell Sci , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 25
    • 0024444733 scopus 로고
    • The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope
    • Krohne G, Waizenegger J and Höger TH (1989) The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope. J Cell Biol 109: 2003-2011
    • (1989) J Cell Biol , vol.109 , pp. 2003-2011
    • Krohne, G.1    Waizenegger, J.2    Höger, T.H.3
  • 27
  • 28
    • 0026559677 scopus 로고
    • Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin A assembly into the nuclear lamina
    • Lutz RJ, Trujillo MA, Denham KS, Wenger L and Sinensky M (1992) Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc Natl Acad Sci USA 89: 3000-3004
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3000-3004
    • Lutz, R.J.1    Trujillo, M.A.2    Denham, K.S.3    Wenger, L.4    Sinensky, M.5
  • 29
    • 0025649688 scopus 로고
    • Posttranslational modification of proteins by isoprenoids in mammalian cells
    • Maltese WA (1990) Posttranslational modification of proteins by isoprenoids in mammalian cells. FASEB J 4: 3319-3328
    • (1990) FASEB J , vol.4 , pp. 3319-3328
    • Maltese, W.A.1
  • 31
    • 0029940817 scopus 로고    scopus 로고
    • Inhibition of cell growth of human hepatoma cell line (Hep G2) by a farnesyl protein transferase inhibitor: A preferential suppression of ras farnesylation
    • Nagase T, Kawata S, Tamura S, Matsuda Y, Inui Y, Yamasaki E, Ishiguro H, Ito T and Matsuzawa Y (1996) Inhibition of cell growth of human hepatoma cell line (Hep G2) by a farnesyl protein transferase inhibitor: a preferential suppression of ras farnesylation. Int J Cancer 65: 620-626
    • (1996) Int J Cancer , vol.65 , pp. 620-626
    • Nagase, T.1    Kawata, S.2    Tamura, S.3    Matsuda, Y.4    Inui, Y.5    Yamasaki, E.6    Ishiguro, H.7    Ito, T.8    Matsuzawa, Y.9
  • 32
    • 0028869067 scopus 로고
    • Inhibition of human tumour xenograft growth by treatment with the farnesyl transferase inhibitor B956
    • Nagasu T, Yoshimatsu K, Rowell C, Lewis MD and Garcia AM (1995) Inhibition of human tumour xenograft growth by treatment with the farnesyl transferase inhibitor B956. Cancer Res 55: 5310-5314
    • (1995) Cancer Res , vol.55 , pp. 5310-5314
    • Nagasu, T.1    Yoshimatsu, K.2    Rowell, C.3    Lewis, M.D.4    Garcia, A.M.5
  • 33
    • 0027475678 scopus 로고
    • Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. I. Producing strain, fermentation, isolation and biological activity
    • Omura S, Van Der Pyl D, Inokoshi J, Takahashi Y and Takeshima H (1993) Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. I. Producing strain, fermentation, isolation and biological activity. J Antibiot 46: 222-228
    • (1993) J Antibiot , vol.46 , pp. 222-228
    • Omura, S.1    Van Der Pyl, D.2    Inokoshi, J.3    Takahashi, Y.4    Takeshima, H.5
  • 36
    • 0028835253 scopus 로고
    • A peptidomimetic inhibitor of farnesyl: Protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines
    • Sepp-Lorenzino L, Ma Z, Rands E, Kohl NE, Gibbs JB, Oliff A and Rosen N (1995) A peptidomimetic inhibitor of farnesyl: protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines. Cancer Res 55: 5302-5309
    • (1995) Cancer Res , vol.55 , pp. 5302-5309
    • Sepp-Lorenzino, L.1    Ma, Z.2    Rands, E.3    Kohl, N.E.4    Gibbs, J.B.5    Oliff, A.6    Rosen, N.7
  • 37
    • 0025202968 scopus 로고
    • Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis
    • Sinensky M, Beck LA, Leonard S and Evans R (1990) Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis. J Biol Chem 265: 19937-19941
    • (1990) J Biol Chem , vol.265 , pp. 19937-19941
    • Sinensky, M.1    Beck, L.A.2    Leonard, S.3    Evans, R.4
  • 38
    • 9844263191 scopus 로고
    • Nuclear localization of prenylation dependent maturation of pre-lamin A
    • Sinensky M, Trujillo MA and Lutz R (1991) Nuclear localization of prenylation dependent maturation of pre-lamin A (abstract). FASEB J 5: 1181
    • (1991) FASEB J , vol.5 , pp. 1181
    • Sinensky, M.1    Trujillo, M.A.2    Lutz, R.3
  • 39
    • 0028016261 scopus 로고
    • Expression of prelamin a but not mature lamin a confers sensitivity of DNA biosynthesis to lovastatin in F9 teratocarcinoma cells
    • Sinensky M, McLain TM and Fantle K (1994a) Expression of prelamin A but not mature lamin A confers sensitivity of DNA biosynthesis to lovastatin in F9 teratocarcinoma cells. J Cell Sci 107: 2215-2218
    • (1994) J Cell Sci , vol.107 , pp. 2215-2218
    • Sinensky, M.1    McLain, T.M.2    Fantle, K.3
  • 41
    • 0019947177 scopus 로고
    • Immunological localization of the major architectural protein associated with the nuclear envelope of the Xenopus laevis oocyte
    • Stick R and Krohne G (1982) Immunological localization of the major architectural protein associated with the nuclear envelope of the Xenopus laevis oocyte. Exp Cell Res 138: 319-330
    • (1982) Exp Cell Res , vol.138 , pp. 319-330
    • Stick, R.1    Krohne, G.2
  • 43
    • 0023917971 scopus 로고
    • Evidence for modification of lamin B by a product of mevalonic acid
    • Wolda S and Glomset JA (1988) Evidence for modification of lamin B by a product of mevalonic acid. J Biol Chem 263: 5997-6000
    • (1988) J Biol Chem , vol.263 , pp. 5997-6000
    • Wolda, S.1    Glomset, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.