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Volumn 76, Issue 2, 2010, Pages 107-115

Enlarging the scope of cell-penetrating prenylated peptides to include farnesylated 'CAAX' box sequences and diverse cell types

Author keywords

amino acid; carbohydrate; chemical biology; lipid; nucleic acid; peptide

Indexed keywords

6 CARBOXYFLUORESCEIN; CELL PENETRATING PEPTIDE; DISULFIDE; NUCLEIC ACID; PROTEIN FARNESYLTRANSFERASE; RAS PROTEIN; FARNESYL TRANS TRANSFERASE; FLUORESCENT DYE; PEPTIDE;

EID: 77954363076     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2010.00992.x     Document Type: Article
Times cited : (9)

References (40)
  • 2
    • 67649781671 scopus 로고    scopus 로고
    • Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients
    • Eckert G.P., Hooff G.P., Strandjord D.M., Igbavboa U., Volmer D.A., Muller W.E., Wood G.W. (2009) Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients. Neurobiol Dis 35 : 251 257.
    • (2009) Neurobiol Dis , vol.35 , pp. 251-257
    • Eckert, G.P.1    Hooff, G.P.2    Strandjord, D.M.3    Igbavboa, U.4    Volmer, D.A.5    Muller, W.E.6    Wood, G.W.7
  • 3
    • 52349087722 scopus 로고    scopus 로고
    • Isoprenoid quantitation in human brain tissue: A validated HPLC-fluorescence detection method for endogenous farnesyl- (FPP) and geranylgeranylpyrophosphate (GGPP)
    • Hooff G.P., Volmer D.A., Wood W.G., Mueller W.E., Eckert G.P. (2008) Isoprenoid quantitation in human brain tissue: a validated HPLC-fluorescence detection method for endogenous farnesyl- (FPP) and geranylgeranylpyrophosphate (GGPP). Anal Bioanal Chem 392 : 673 680.
    • (2008) Anal Bioanal Chem , vol.392 , pp. 673-680
    • Hooff, G.P.1    Volmer, D.A.2    Wood, W.G.3    Mueller, W.E.4    Eckert, G.P.5
  • 5
    • 0031970317 scopus 로고    scopus 로고
    • Membrane association and targeting of prenylated Ras-like GTPases
    • Seabra M.C. (1998) Membrane association and targeting of prenylated Ras-like GTPases. Cell Signal 10 : 167 172.
    • (1998) Cell Signal , vol.10 , pp. 167-172
    • Seabra, M.C.1
  • 6
    • 33750730629 scopus 로고    scopus 로고
    • Protein prenylation: An (almost) comprehensive overview on discovery history, enzymology, and significance in physiology and disease
    • Benetka W., Koranda M., Eisenhaber F. (2006) Protein prenylation: an (almost) comprehensive overview on discovery history, enzymology, and significance in physiology and disease. Monatsh Chem 137 : 1241 1281.
    • (2006) Monatsh Chem , vol.137 , pp. 1241-1281
    • Benetka, W.1    Koranda, M.2    Eisenhaber, F.3
  • 7
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey P.J. (1992) Biochemistry of protein prenylation. J Lipid Res 33 : 1731 1740.
    • (1992) J Lipid Res , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 8
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S. (1992) Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu Rev Biochem 61 : 355 386.
    • (1992) Annu Rev Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 9
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang F.L., Casey P.J. (1996) Protein prenylation: molecular mechanisms and functional consequences. Annu Rev Biochem 65 : 241 269.
    • (1996) Annu Rev Biochem , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 10
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann A.M., Casey P.J. (2005) Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 5 : 405 412.
    • (2005) Nat Rev Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 11
    • 33644815892 scopus 로고    scopus 로고
    • Tailoring Ras-pathway-Inhibitor combinations for cancer therapy
    • Blum R., Kloog Y. (2005) Tailoring Ras-pathway-Inhibitor combinations for cancer therapy. Drug Resist Updat 8 : 369 380.
    • (2005) Drug Resist Updat , vol.8 , pp. 369-380
    • Blum, R.1    Kloog, Y.2
  • 12
    • 34548815038 scopus 로고    scopus 로고
    • Development of farnesyltransferase inhibitors for clinical cancer therapy: Focus on hematologic malignancies
    • Karp J.E., Lancet J.E. (2007) Development of farnesyltransferase inhibitors for clinical cancer therapy: focus on hematologic malignancies. Cancer Invest 25 : 484 494.
    • (2007) Cancer Invest , vol.25 , pp. 484-494
    • Karp, J.E.1    Lancet, J.E.2
  • 13
    • 1642477902 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors as anticancer agents: Current status
    • Zhu K., Hamilton A.D., Sebti S.M. (2003) Farnesyltransferase inhibitors as anticancer agents: current status. Curr Opin Investig Drugs 4 : 1428 1435.
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 1428-1435
    • Zhu, K.1    Hamilton, A.D.2    Sebti, S.M.3
  • 15
    • 0037372488 scopus 로고    scopus 로고
    • Efficacy of the farnesyl transferase inhibitor R115777 in chronic myeloid leukemia and other hematologic malignancies
    • Cortes J., Albitar M., Thomas D., Giles F., Kurzrock R., Thibault A. et al. (2003) Efficacy of the farnesyl transferase inhibitor R115777 in chronic myeloid leukemia and other hematologic malignancies. Blood 101 : 1692 1697.
    • (2003) Blood , vol.101 , pp. 1692-1697
    • Cortes, J.1    Albitar, M.2    Thomas, D.3    Giles, F.4    Kurzrock, R.5    Thibault, A.6
  • 17
    • 47349089381 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: A detailed chemical view on an elusive biological problem
    • Sousa S.F., Fernandes P.A., Ramos M.J. (2008) Farnesyltransferase inhibitors: a detailed chemical view on an elusive biological problem. Curr Med Chem 15 : 1478 1492.
    • (2008) Curr Med Chem , vol.15 , pp. 1478-1492
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 18
    • 0029785706 scopus 로고    scopus 로고
    • G protein gamma subunits with altered prenylation sequences are properly modified when expressed in Sf9 cells
    • Lindorfer M.A., Sherman N.E., Woodfork K.A., Fletcher J.E., Hunt D.F., Garrison J.C. (1996) G protein gamma subunits with altered prenylation sequences are properly modified when expressed in Sf9 cells. J Biol Chem 271 : 18582 18587.
    • (1996) J Biol Chem , vol.271 , pp. 18582-18587
    • Lindorfer, M.A.1    Sherman, N.E.2    Woodfork, K.A.3    Fletcher, J.E.4    Hunt, D.F.5    Garrison, J.C.6
  • 19
    • 0036357938 scopus 로고    scopus 로고
    • Statin drugs and dietary isoprenoids downregulate protein prenylation in signal transduction and are antithrombotic and prothrombolytic agents
    • Fenton J.W. II., Jeske W.P., Catalfamo J.L., Brezniak D.V., Moon D.G., Shen G.X. (2002) Statin drugs and dietary isoprenoids downregulate protein prenylation in signal transduction and are antithrombotic and prothrombolytic agents. Biochemistry (Mosc) 67 : 85 91.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 85-91
    • Fenton II, J.W.1    Jeske, W.P.2    Catalfamo, J.L.3    Brezniak, D.V.4    Moon, D.G.5    Shen, G.X.6
  • 21
    • 0034682560 scopus 로고    scopus 로고
    • Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B
    • Roy M.-O., Leventis R., Silvius J.R. (2000) Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B. Biochemistry 39 : 8298 8307.
    • (2000) Biochemistry , vol.39 , pp. 8298-8307
    • Roy, M.-O.1    Leventis, R.2    Silvius, J.R.3
  • 22
    • 0030708812 scopus 로고    scopus 로고
    • Chemoenzymic synthesis of fluorescent N-Ras lipopeptides and their use in membrane localization studies in vivo
    • Waldmann H., Schelhaas M., Nagele E., Kuhlmann J., Wittinghofer A., Schroeder H. et al. (1997) Chemoenzymic synthesis of fluorescent N-Ras lipopeptides and their use in membrane localization studies in vivo. Angew Chem Int Ed Engl 36 : 2238 2241.
    • (1997) Angew Chem Int Ed Engl , vol.36 , pp. 2238-2241
    • Waldmann, H.1    Schelhaas, M.2    Nagele, E.3    Kuhlmann, J.4    Wittinghofer, A.5    Schroeder, H.6
  • 24
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene L.A., Tischler A.S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc Natl Acad Sci U S A 73 : 2424 2428.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tischler, A.S.2
  • 25
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King D.S., Fields C.G., Fields G.B. (1990) A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis. Int J Pept Protein Res 36 : 255 266.
    • (1990) Int J Pept Protein Res , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 26
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • Meriin A.B., Yaglom J.A., Gabai V.L., Zon L., Ganiatsas S., Mosser D.D. et al. (1999) Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol Cell Biol 19 : 2547 2555.
    • (1999) Mol Cell Biol , vol.19 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.A.2    Gabai, V.L.3    Zon, L.4    Ganiatsas, S.5    Mosser, D.D.6
  • 27
    • 0016690360 scopus 로고
    • Adhesion of cells to surfaces coated with polylysine. Applications to electron microscopy
    • Mazia D., Schatten G., Sale W. (1975) Adhesion of cells to surfaces coated with polylysine. Applications to electron microscopy. J Cell Biol 66 : 198 200.
    • (1975) J Cell Biol , vol.66 , pp. 198-200
    • Mazia, D.1    Schatten, G.2    Sale, W.3
  • 28
    • 70349554126 scopus 로고    scopus 로고
    • Mitochondria-penetrating peptides: Sequence effects and model cargo transport
    • Yousif L.F., Stewart K.M., Horton K.L., Kelley S.O. (2009) Mitochondria-penetrating peptides: sequence effects and model cargo transport. Chembiochem 10 : 2081 2088.
    • (2009) Chembiochem , vol.10 , pp. 2081-2088
    • Yousif, L.F.1    Stewart, K.M.2    Horton, K.L.3    Kelley, S.O.4
  • 29
    • 0026554482 scopus 로고
    • Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst
    • Xue C.B., Becker J.M., Naider F. (1992) Efficient regioselective isoprenylation of peptides in acidic aqueous solution using zinc acetate as catalyst. Tetrahedron Lett 33 : 1435 1438.
    • (1992) Tetrahedron Lett , vol.33 , pp. 1435-1438
    • Xue, C.B.1    Becker, J.M.2    Naider, F.3
  • 31
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake
    • Richard J.P., Melikov K., Vives E., Ramos C., Verbeure B., Gait M.J. et al. (2003) Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake. J Biol Chem 278 : 585 590.
    • (2003) J Biol Chem , vol.278 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Vives, E.3    Ramos, C.4    Verbeure, B.5    Gait, M.J.6
  • 33
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine R.L., Moskovitz J., Stadtman E.R. (2000) Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 50 : 301 307.
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 34
    • 54449089676 scopus 로고    scopus 로고
    • In situ immunocytochemical detection of altered membrane composition induced by cell-cell contact in cultured mammalian cells
    • Du W., Cui Z., Tsui Z.C., Chen Q., Willingham M.C. (2008) In situ immunocytochemical detection of altered membrane composition induced by cell-cell contact in cultured mammalian cells. Microsc Res Tech 71 : 749 759.
    • (2008) Microsc Res Tech , vol.71 , pp. 749-759
    • Du, W.1    Cui, Z.2    Tsui, Z.C.3    Chen, Q.4    Willingham, M.C.5
  • 35
    • 27744525788 scopus 로고    scopus 로고
    • Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery
    • Massodi I., Bidwell G.L. III., Raucher D. (2005) Evaluation of cell penetrating peptides fused to elastin-like polypeptide for drug delivery. J Control Release 108 : 396 408.
    • (2005) J Control Release , vol.108 , pp. 396-408
    • Massodi, I.1    Bidwell III, G.L.2    Raucher, D.3
  • 36
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • Stewart E.J., Aslund F., Beckwith J. (1998) Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J 17 : 5543 5550.
    • (1998) EMBO J , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 37
    • 33646777423 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. CAAX modification and membrane targeting of Ras
    • Wright L.P., Philips M.R. (2006) Thematic review series: lipid posttranslational modifications. CAAX modification and membrane targeting of Ras. J Lipid Res 47 : 883 891.
    • (2006) J Lipid Res , vol.47 , pp. 883-891
    • Wright, L.P.1    Philips, M.R.2
  • 38
    • 13244283092 scopus 로고    scopus 로고
    • Chemical cytometry for monitoring metabolism of a Ras-mimicking substrate in single cells
    • Arkhipov S.N., Berezovski M., Jitkova J., Krylov S.N. (2005) Chemical cytometry for monitoring metabolism of a Ras-mimicking substrate in single cells. Cytometry A 63A : 41 47.
    • (2005) Cytometry A , vol.63 , pp. 41-47
    • Arkhipov, S.N.1    Berezovski, M.2    Jitkova, J.3    Krylov, S.N.4
  • 39
    • 0036709006 scopus 로고    scopus 로고
    • Measuring the activity of farnesyltransferase by capillary electrophoresis with laser-induced fluorescence detection
    • Berezovski M., Li W.-P., Poulter C.D., Krylov S.N. (2002) Measuring the activity of farnesyltransferase by capillary electrophoresis with laser-induced fluorescence detection. Electrophoresis 23 : 3398 3403.
    • (2002) Electrophoresis , vol.23 , pp. 3398-3403
    • Berezovski, M.1    Li, W.-P.2    Poulter, C.D.3    Krylov, S.N.4
  • 40
    • 4143084891 scopus 로고    scopus 로고
    • Monitoring the three enzymatic activities involved in posttranslational modifications of Ras proteins
    • Jitkova J., Carrigan C.N., Poulter C.D., Krylov S.N. (2004) Monitoring the three enzymatic activities involved in posttranslational modifications of Ras proteins. Anal Chim Acta 521 : 1 7.
    • (2004) Anal Chim Acta , vol.521 , pp. 1-7
    • Jitkova, J.1    Carrigan, C.N.2    Poulter, C.D.3    Krylov, S.N.4


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