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Volumn 94, Issue 1, 1998, Pages 87-97

The effects of protein farnesyltransferase inhibitors on trypanosomatids: Inhibition of protein farnesylation and cell growth

Author keywords

Anti parasite therapeutics; Farnesylation; Geranylgeranylation; Isoprenylation; Leishmania mexicana; Mevalonic acid; Parasites; Prenylation; Protein farnesyltransferase; Simvastatin; Trypanosoma brucei; Trypanosoma cruzi; Trypanosomatidae

Indexed keywords

MEVALONIC ACID; PROTEIN FARNESYLTRANSFERASE INHIBITOR; SIMVASTATIN;

EID: 0032128169     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00053-X     Document Type: Article
Times cited : (88)

References (40)
  • 1
    • 0025277259 scopus 로고
    • Prenyl proteins in eukaryotic cells: A new type of membrane anchor
    • [1] Glomset JA, Gelb MH, Farnsworth CC. Prenyl proteins in eukaryotic cells: a new type of membrane anchor. Trends Biochem Sci 1990;15:139-42.
    • (1990) Trends Biochem Sci , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 2
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • [2] Zhang FL, Casey PJ. Protein prenylation: molecular mechanisms and functional consequences. Ann Rev Biochem 1996;65:241-69.
    • (1996) Ann Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 4
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxy-terminal cysteine residues
    • [4] Clarke S. Protein isoprenylation and methylation at carboxy-terminal cysteine residues. Annu Rev Biochem 1992;61:355-86.
    • (1992) Annu Rev Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 5
    • 0025375466 scopus 로고
    • Brain G protein γ subunits contain an all-trans-geranylgeranyl cysteine methyl ester a their carboxyl termini
    • [5] Yamane HK, Farnsworth CC, Xie H, et al. Brain G protein γ subunits contain an all-trans-geranylgeranyl cysteine methyl ester a their carboxyl termini. Proc Nat Acad Sci USA 1990;87:5868-72.
    • (1990) Proc Nat Acad Sci USA , vol.87 , pp. 5868-5872
    • Yamane, H.K.1    Farnsworth, C.C.2    Xie, H.3
  • 7
    • 0029965270 scopus 로고    scopus 로고
    • The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells
    • [7] Otto JC, Casey PJ. The hepatitis delta virus large antigen is farnesylated both in vitro and in animal cells. J Biol Chem 1996;271:4569-72.
    • (1996) J Biol Chem , vol.271 , pp. 4569-4572
    • Otto, J.C.1    Casey, P.J.2
  • 9
    • 0026806554 scopus 로고
    • Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements
    • [9] Moomaw JF, Casey PJ. Mammalian protein geranylgeranyltransferase. Subunit composition and metal requirements. J Biol Chem 1992;267:17438-43.
    • (1992) J Biol Chem , vol.267 , pp. 17438-17443
    • Moomaw, J.F.1    Casey, P.J.2
  • 10
    • 0027416643 scopus 로고
    • Purification of a mammalian protein geranylgeranyltransferase: Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex
    • [10] Yokoyama K, Gelb MH. Purification of a mammalian protein geranylgeranyltransferase: formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex. J Biol Chem 1993;268:4055-60.
    • (1993) J Biol Chem , vol.268 , pp. 4055-4060
    • Yokoyama, K.1    Gelb, M.H.2
  • 11
    • 0028135348 scopus 로고
    • Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases, Rab1A, Rab3A, and Rab5A
    • [11] Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA. Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases, Rab1A, Rab3A, and Rab5A. Proc Natl Acad Sci USA 1994;91:11963-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11963-11967
    • Farnsworth, C.C.1    Seabra, M.C.2    Ericsson, L.H.3    Gelb, M.H.4    Glomset, J.A.5
  • 13
    • 0027154011 scopus 로고
    • Characterization of mevalonate-labeled lipids isolated from parasite proteins in Schistosoma mansoni
    • [13] Chen G-Z, Bennett JL. Characterization of mevalonate-labeled lipids isolated from parasite proteins in Schistosoma mansoni. Mol Biochem Parasitol 1993;59:287-92.
    • (1993) Mol Biochem Parasitol , vol.59 , pp. 287-292
    • Chen, G.-Z.1    Bennett, J.L.2
  • 14
    • 0030581643 scopus 로고    scopus 로고
    • Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei
    • [14] Field H, Blench I, Croft S, Field MC. Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei. Mol Biochem Parasitol 1996;82:67-80.
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 67-80
    • Field, H.1    Blench, I.2    Croft, S.3    Field, M.C.4
  • 16
    • 0028361906 scopus 로고
    • Evidence for guanosine triphosphate-binding proteins in Trypanosoma cruzi
    • [16] Oz HS, Huang H, Wittner M, et al. Evidence for guanosine triphosphate-binding proteins in Trypanosoma cruzi. Am J Trop Med Hyg 1994;50:620-31.
    • (1994) Am J Trop Med Hyg , vol.50 , pp. 620-631
    • Oz, H.S.1    Huang, H.2    Wittner, M.3
  • 17
    • 0026673477 scopus 로고
    • Characterization of a Gi-protein from Trypanosoma cruzi epimastigote membranes
    • [17] Coso OA, D'iaz AA, Martinetto H, et al. Characterization of a Gi-protein from Trypanosoma cruzi epimastigote membranes. Biochem J 1992;287:443-6.
    • (1992) Biochem J , vol.287 , pp. 443-446
    • Coso, O.A.1    D'iaz, A.A.2    Martinetto, H.3
  • 18
    • 0027290932 scopus 로고
    • Signal transduction in Trypanosoma cruzi: Opposite effects of adenylcyclase and phospholipase C systems in growth control
    • [18] Oliveira MM, Rocha ED, Rondinelli E, Arnholdt AV, Scharfstein J. Signal transduction in Trypanosoma cruzi: opposite effects of adenylcyclase and phospholipase C systems in growth control. Mol Cell Biochem 1993;124:91-9.
    • (1993) Mol Cell Biochem , vol.124 , pp. 91-99
    • Oliveira, M.M.1    Rocha, E.D.2    Rondinelli, E.3    Arnholdt, A.V.4    Scharfstein, J.5
  • 19
    • 0023785233 scopus 로고
    • Cyclic AMP and adenylate cyclase activators stimulate Trypanosoma cruzi differentiation
    • [19] Gonzales PM, Romero P, Goldenberg S. Cyclic AMP and adenylate cyclase activators stimulate Trypanosoma cruzi differentiation. Exp Parasitol 1988;66:205-12.
    • (1988) Exp Parasitol , vol.66 , pp. 205-212
    • Gonzales, P.M.1    Romero, P.2    Goldenberg, S.3
  • 20
    • 0027892198 scopus 로고
    • Identification of guanine nucleotide binding proteins from Trypanosoma cruzi
    • [20] Bubis J, Millan EJ, Martinez R. Identification of guanine nucleotide binding proteins from Trypanosoma cruzi. Biol Res 1993;26:177-88.
    • (1993) Biol Res , vol.26 , pp. 177-188
    • Bubis, J.1    Millan, E.J.2    Martinez, R.3
  • 21
    • 0022558265 scopus 로고
    • Evidence for the existence of an Ns-type regulatory protein in Trypanosoma cruzi membranes
    • [21] Eisenschlos CD, Paladini AA, Molina YVL, Torres HN, Flawi'a MM. Evidence for the existence of an Ns-type regulatory protein in Trypanosoma cruzi membranes. Biochem J 1986;237:913-7.
    • (1986) Biochem J , vol.237 , pp. 913-917
    • Eisenschlos, C.D.1    Paladini, A.A.2    Molina, Y.V.L.3    Torres, H.N.4    Flawi'a, M.M.5
  • 22
    • 0028944011 scopus 로고
    • Trypanosoma brucei: Characterisation of a life cycle stage-specific G-protein
    • [22] Coulter LJ, Hide G. Trypanosoma brucei: characterisation of a life cycle stage-specific G-protein. Exp Parasitol 1995;80:308-18.
    • (1995) Exp Parasitol , vol.80 , pp. 308-318
    • Coulter, L.J.1    Hide, G.2
  • 23
    • 0026162878 scopus 로고
    • Leishmania donovani: Characterization of a 38-kDa membrane protein that cross-reacts with the mammalian G-protein transducin
    • [23] Cassel D, Shoubi S, Glusman G, Cukierman E, Rotman M, Zilberstein D. Leishmania donovani: characterization of a 38-kDa membrane protein that cross-reacts with the mammalian G-protein transducin. Exp Parasitol 1991;72:411-7.
    • (1991) Exp Parasitol , vol.72 , pp. 411-417
    • Cassel, D.1    Shoubi, S.2    Glusman, G.3    Cukierman, E.4    Rotman, M.5    Zilberstein, D.6
  • 24
    • 0028853816 scopus 로고
    • cDNA expressed sequence tags of Trypanosoma brucei rhodesiense provide new insights into the biology of the parasite
    • [24] El-Sayed NM, Alarcon CM, Beck JC, Sheffield VC, Donelson JE. cDNA expressed sequence tags of Trypanosoma brucei rhodesiense provide new insights into the biology of the parasite. Mol Biochem Parasitol 1995;73:75-90.
    • (1995) Mol Biochem Parasitol , vol.73 , pp. 75-90
    • El-Sayed, N.M.1    Alarcon, C.M.2    Beck, J.C.3    Sheffield, V.C.4    Donelson, J.E.5
  • 25
    • 0030933192 scopus 로고    scopus 로고
    • Tandem duplication of rab genes followed by sequence divergence and acquisition of distinct functions in Trypanosoma brucei
    • [25] Field H, Field MC. Tandem duplication of rab genes followed by sequence divergence and acquisition of distinct functions in Trypanosoma brucei. J Biol Chem 1997;272:10498-505.
    • (1997) J Biol Chem , vol.272 , pp. 10498-10505
    • Field, H.1    Field, M.C.2
  • 26
    • 0029557676 scopus 로고
    • Trypanosoma brucei: Molecular cloning of homologues of small GTP-binding proteins involved in vesicle trafficking
    • [26] Field MC, Boothroyd JC. Trypanosoma brucei: molecular cloning of homologues of small GTP-binding proteins involved in vesicle trafficking. Exp Parasitol 1995;81:313-20.
    • (1995) Exp Parasitol , vol.81 , pp. 313-320
    • Field, M.C.1    Boothroyd, J.C.2
  • 27
    • 0027378869 scopus 로고
    • Cloning and characterization of a Golgi-associated GTP-binding protein homologue from Leishmania major
    • [27] Cappai R, Osborn AH, Gleeson PA, Handman E. Cloning and characterization of a Golgi-associated GTP-binding protein homologue from Leishmania major. Mol Biochem Parasitol 1993;62:73-82.
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 73-82
    • Cappai, R.1    Osborn, A.H.2    Gleeson, P.A.3    Handman, E.4
  • 28
    • 0027818524 scopus 로고
    • Identification of GTPase genes in the protozoa parasites Trypanosoma cruzi and Leishmania amazonensis
    • [28] Mendonca SM, Campos CB, Gueiros FFJ, Lopes UG. Identification of GTPase genes in the protozoa parasites Trypanosoma cruzi and Leishmania amazonensis. Biol Res 1993;26:3-9.
    • (1993) Biol Res , vol.26 , pp. 3-9
    • Mendonca, S.M.1    Campos, C.B.2    Gueiros, F.F.J.3    Lopes, U.G.4
  • 29
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • [29] Yokoyama K, Goodwin GW, Ghomashchi F, Glomset JA, Gelb MH. A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity. Proc Natl Acad Sci USA 1991;88:5302-6.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 30
    • 0028848171 scopus 로고
    • The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase
    • [30] McGeady P, Kuroda S, Shimizu K, Takai Y, Gelb MH. The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase. J Biol Chem 1995;270:26347-51.
    • (1995) J Biol Chem , vol.270 , pp. 26347-26351
    • McGeady, P.1    Kuroda, S.2    Shimizu, K.3    Takai, Y.4    Gelb, M.H.5
  • 32
    • 0024948840 scopus 로고
    • Continuous cultivation of T. brucei bloodstream forms containing a low concentration of serum protein without feeder cell layers
    • [32] Hirumi H, Hirumi K. Continuous cultivation of T. brucei bloodstream forms containing a low concentration of serum protein without feeder cell layers. J Parasitol 1989;75:985-9.
    • (1989) J Parasitol , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 33
    • 0029861640 scopus 로고    scopus 로고
    • Efficient technique for screening drugs for activity against Trypanosoma cruzi using parasites expressing β-galactosidase
    • [33] Buckner FS, Verlinde CLM, La Flamme AC, Van Voorhis WC. Efficient technique for screening drugs for activity against Trypanosoma cruzi using parasites expressing β-galactosidase. Antimicrob Agents Chemother 1996;40:2592-7.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 2592-2597
    • Buckner, F.S.1    Verlinde, C.L.M.2    La Flamme, A.C.3    Van Voorhis, W.C.4
  • 34
    • 0024520825 scopus 로고
    • F1-160: A surface antigen of Trypanosomal cruzi that mimics mammalian nervous tissue
    • [34] Van Voorhis WC, Eisen H. F1-160: A Surface Antigen of Trypanosomal cruzi that mimics mammalian nervous tissue. J Exp Med 1989;169:641-52.
    • (1989) J Exp Med , vol.169 , pp. 641-652
    • Van Voorhis, W.C.1    Eisen, H.2
  • 35
    • 0030612442 scopus 로고    scopus 로고
    • Farnesyltransferase as a target for anticancer drug design
    • [35] Qian Y, Sebti SM, Hamilton AD. Farnesyltransferase as a target for anticancer drug design. Biopolymers 1997;43:25-41.
    • (1997) Biopolymers , vol.43 , pp. 25-41
    • Qian, Y.1    Sebti, S.M.2    Hamilton, A.D.3
  • 36
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • [36] Casey PJ, Seabra MC. Protein prenyltransferases. J Biol Chem 1996;271:5289-92.
    • (1996) J Biol Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 37
    • 0029857638 scopus 로고    scopus 로고
    • Protein geranylgeranylation, not farnesylation, is required for the G1 to S phase transition in mouse fibroblasts
    • [37] Vogt A, Qian Y, McGuire TF, Hamilton AD, Sebti SM. Protein geranylgeranylation, not farnesylation, is required for the G1 to S phase transition in mouse fibroblasts. Oncogene 1996;13:1991-9.
    • (1996) Oncogene , vol.13 , pp. 1991-1999
    • Vogt, A.1    Qian, Y.2    McGuire, T.F.3    Hamilton, A.D.4    Sebti, S.M.5
  • 38
    • 0030923192 scopus 로고    scopus 로고
    • K-and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors
    • [38] Whyte DB, Kirschmeier P, Hockenberry TN, et al. K-and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors. J Biol Chem 1997;272:14459-64.
    • (1997) J Biol Chem , vol.272 , pp. 14459-14464
    • Whyte, D.B.1    Kirschmeier, P.2    Hockenberry, T.N.3
  • 39
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • [39] Rowell CA, Kowalczyk JJ, Lewis MD, Garcia AM. Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J Biol Chem 1997;272:14093-7.
    • (1997) J Biol Chem , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 40
    • 0031993476 scopus 로고
    • Protein prenylation: From discovery to prospects for cancer treatment
    • [40] Gelb MH, Scholten JD, Sebolt-Leopold JS. Protein prenylation: from discovery to prospects for cancer treatment. Curr Opin Chem Biol 1992;2:40-8.
    • (1992) Curr Opin Chem Biol , vol.2 , pp. 40-48
    • Gelb, M.H.1    Scholten, J.D.2    Sebolt-Leopold, J.S.3


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