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Volumn 127, Issue 1-2, 2007, Pages 78-83

The interactions of aurein 1.2 with cancer cell membranes

Author keywords

Anionic lipid; Aurein 1.2; Lysine residues; Snorkelling; T98G cancer cell membranes

Indexed keywords

ANION; LIPID; MEMBRANE LIPID; PEPTIDE; PROTEIN AUREIN; UNCLASSIFIED DRUG;

EID: 33847175151     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.12.009     Document Type: Article
Times cited : (67)

References (39)
  • 1
    • 16244403039 scopus 로고    scopus 로고
    • Cancer incidence and mortality in Europe, 2004
    • Boyle P., and Ferlay J. Cancer incidence and mortality in Europe, 2004. Ann. Oncol. 16 (2005) 481-488
    • (2005) Ann. Oncol. , vol.16 , pp. 481-488
    • Boyle, P.1    Ferlay, J.2
  • 2
    • 4444244978 scopus 로고    scopus 로고
    • International variation
    • Parkin D.M. International variation. Oncogene 23 (2004) 6329-6340
    • (2004) Oncogene , vol.23 , pp. 6329-6340
    • Parkin, D.M.1
  • 3
    • 2942545893 scopus 로고    scopus 로고
    • Carcinogenesis: The more we seek to know the more we need to know - challenges in the post Genomic Era
    • Kovvali G., Shiff S., Telang N., Das K., Kohgo Y., Narayan S., and Li H. Carcinogenesis: The more we seek to know the more we need to know - challenges in the post Genomic Era. J. Carcinog. 2 (2003) 1-2
    • (2003) J. Carcinog. , vol.2 , pp. 1-2
    • Kovvali, G.1    Shiff, S.2    Telang, N.3    Das, K.4    Kohgo, Y.5    Narayan, S.6    Li, H.7
  • 4
    • 0345254979 scopus 로고    scopus 로고
    • An overview of the mechanisms of mutagenesis and carcinogenesis
    • Sarasin A. An overview of the mechanisms of mutagenesis and carcinogenesis. Mutat. Res. 544 (2003) 99-106
    • (2003) Mutat. Res. , vol.544 , pp. 99-106
    • Sarasin, A.1
  • 5
    • 14144249767 scopus 로고    scopus 로고
    • In vitro assays for anticancer drug discovery - a novel approach based on engineered mammalian cell lines
    • Gonzalez-Nicolini V., and Fussenegger M. In vitro assays for anticancer drug discovery - a novel approach based on engineered mammalian cell lines. Anticancer Drugs 16 (2005) 223-228
    • (2005) Anticancer Drugs , vol.16 , pp. 223-228
    • Gonzalez-Nicolini, V.1    Fussenegger, M.2
  • 6
    • 22844436226 scopus 로고    scopus 로고
    • Recent advances in tumor-targeting anticancer drug conjugates
    • Jaracz S., Chen J., Kuznetsova L.V., and Ojima I. Recent advances in tumor-targeting anticancer drug conjugates. Bioorg. Med. Chem. 13 (2005) 5043-5054
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 5043-5054
    • Jaracz, S.1    Chen, J.2    Kuznetsova, L.V.3    Ojima, I.4
  • 7
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense
    • Leslie E.M., Deeley R.G., and Cole S.P. Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense. Toxicol. Appl. Pharmacol. 204 (2005) 216-237
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.3
  • 8
    • 33644860579 scopus 로고    scopus 로고
    • An update on overcoming MDR1-mediated multidrug resistance in cancer chemotherapy
    • Takara K., Sakaeda T., and Okumura K. An update on overcoming MDR1-mediated multidrug resistance in cancer chemotherapy. Curr. Pharm. Des. 12 (2006) 273-286
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 273-286
    • Takara, K.1    Sakaeda, T.2    Okumura, K.3
  • 9
    • 23744438018 scopus 로고    scopus 로고
    • The molecular pathology of new anti-cancer agents
    • Cross S.S. The molecular pathology of new anti-cancer agents. Curr. Diagn. Pathol. 11 (2005) 329-339
    • (2005) Curr. Diagn. Pathol. , vol.11 , pp. 329-339
    • Cross, S.S.1
  • 10
    • 30344487254 scopus 로고    scopus 로고
    • Use of P-glycoprotein and BCRP inhibitors to improve oral bioavailability and CNS penetration of anticancer drugs
    • Breedveld P., Beijnen J.H., and Schellens J.H. Use of P-glycoprotein and BCRP inhibitors to improve oral bioavailability and CNS penetration of anticancer drugs. Trends Pharmacol. Sci. 27 (2006) 17-24
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 17-24
    • Breedveld, P.1    Beijnen, J.H.2    Schellens, J.H.3
  • 11
    • 33645393209 scopus 로고    scopus 로고
    • Recent advances in the research and development of human defensins
    • Chen H., Xu Z., Peng L., Fang X., Yin X., Xu N., and Cen P. Recent advances in the research and development of human defensins. Peptides 27 (2006) 931-940
    • (2006) Peptides , vol.27 , pp. 931-940
    • Chen, H.1    Xu, Z.2    Peng, L.3    Fang, X.4    Yin, X.5    Xu, N.6    Cen, P.7
  • 13
    • 3042737827 scopus 로고    scopus 로고
    • Membrane disrupting lytic peptides for cancer treatments
    • Leuschner C., and Hansel W. Membrane disrupting lytic peptides for cancer treatments. Curr. Pharm. Des. 10 (2004) 2299-2310
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 2299-2310
    • Leuschner, C.1    Hansel, W.2
  • 14
    • 18544366816 scopus 로고    scopus 로고
    • Host defense peptides as new weapons in cancer treatment
    • Papo N., and Shai Y. Host defense peptides as new weapons in cancer treatment. Cell. Mol. Life Sci. 62 (2005) 784-790
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 784-790
    • Papo, N.1    Shai, Y.2
  • 15
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown K.L., and Hancock R.E. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18 (2006) 24-30
    • (2006) Curr. Opin. Immunol. , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 16
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., and Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198 (2004) 169-184
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 17
    • 11244333158 scopus 로고    scopus 로고
    • Amphiphilic alpha-helical antimicrobial peptides and their structure/function relationships
    • Dennison S.R., Wallace J., Harris F., and Phoenix D.A. Amphiphilic alpha-helical antimicrobial peptides and their structure/function relationships. Protein Pept. Lett. 12 (2005) 31-39
    • (2005) Protein Pept. Lett. , vol.12 , pp. 31-39
    • Dennison, S.R.1    Wallace, J.2    Harris, F.3    Phoenix, D.A.4
  • 18
    • 0142183723 scopus 로고    scopus 로고
    • Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications
    • Papagianni M. Ribosomally synthesized peptides with antimicrobial properties: biosynthesis, structure, function, and applications. Biotechnol. Adv. 21 (2003) 465-499
    • (2003) Biotechnol. Adv. , vol.21 , pp. 465-499
    • Papagianni, M.1
  • 19
    • 33845373254 scopus 로고    scopus 로고
    • Anticancer α-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes
    • Dennison S.R., Whittaker M., Harris F., and Phoenix D.A. Anticancer α-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes. Curr. Protein Pept. Sci. 7 (2006) 487-500
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 487-500
    • Dennison, S.R.1    Whittaker, M.2    Harris, F.3    Phoenix, D.A.4
  • 21
    • 0036151139 scopus 로고    scopus 로고
    • Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation of lesuerin from the skin secretion of the Australian Stony Creek frog Litoria lesueuri
    • Doyle J., Llewellyn L.E., Brinkworth C.S., Bowie J.H., Wegener K.L., Rozek T., Wabnitz P.A., Wallace J.C., and Tyler M.J. Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation of lesuerin from the skin secretion of the Australian Stony Creek frog Litoria lesueuri. Eur. J. Biochem. 269 (2002) 100-109
    • (2002) Eur. J. Biochem. , vol.269 , pp. 100-109
    • Doyle, J.1    Llewellyn, L.E.2    Brinkworth, C.S.3    Bowie, J.H.4    Wegener, K.L.5    Rozek, T.6    Wabnitz, P.A.7    Wallace, J.C.8    Tyler, M.J.9
  • 23
    • 0033787423 scopus 로고    scopus 로고
    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. Part 2. Sequence determination using electrospray mass spectrometry
    • Rozek T., Bowie J.H., Wallace J.C., and Tyler M.J. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis. Part 2. Sequence determination using electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 14 (2000) 2002-2011
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 2002-2011
    • Rozek, T.1    Bowie, J.H.2    Wallace, J.C.3    Tyler, M.J.4
  • 24
    • 0033859322 scopus 로고    scopus 로고
    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2
    • Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C., and Tyler M.J. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. Eur. J. Biochem. 267 (2000) 5330-5341
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5330-5341
    • Rozek, T.1    Wegener, K.L.2    Bowie, J.H.3    Olver, I.N.4    Carver, J.A.5    Wallace, J.C.6    Tyler, M.J.7
  • 25
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Med. Sci. 37 (1959) 911-917
    • (1959) Can. J. Med. Sci. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 27
    • 0036436859 scopus 로고    scopus 로고
    • Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid
    • Brandenburg K., Harris F., Dennison S., Seydel U., and Phoenix D. Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid. Eur. J. Biochem. 269 (2002) 5414-5422
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5414-5422
    • Brandenburg, K.1    Harris, F.2    Dennison, S.3    Seydel, U.4    Phoenix, D.5
  • 28
    • 0016369116 scopus 로고
    • Model membrane monolayers-description of use and interaction
    • Demel R.A. Model membrane monolayers-description of use and interaction. Methods Enzymol. 32 (1974) 539-545
    • (1974) Methods Enzymol. , vol.32 , pp. 539-545
    • Demel, R.A.1
  • 29
    • 24144461618 scopus 로고    scopus 로고
    • Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein
    • Ambroggio E.E., Separovic F., Bowie J.H., Fidelio G.D., and Bagatolli L.A. Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin, and aurein. Biophys. J. 89 (2005) 1874-1881
    • (2005) Biophys. J. , vol.89 , pp. 1874-1881
    • Ambroggio, E.E.1    Separovic, F.2    Bowie, J.H.3    Fidelio, G.D.4    Bagatolli, L.A.5
  • 30
    • 3342906298 scopus 로고    scopus 로고
    • Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes
    • Balla M.S., Bowie J.H., and Separovic F. Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes. Eur. Biophys J. 33 (2004) 109-116
    • (2004) Eur. Biophys J. , vol.33 , pp. 109-116
    • Balla, M.S.1    Bowie, J.H.2    Separovic, F.3
  • 31
    • 11244352103 scopus 로고    scopus 로고
    • Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?
    • Dennison S.R., Harris F., and Phoenix D.A. Are oblique orientated alpha-helices used by antimicrobial peptides for membrane invasion?. Protein Pept. Lett. 12 (2005) 27-29
    • (2005) Protein Pept. Lett. , vol.12 , pp. 27-29
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 32
    • 18744393069 scopus 로고    scopus 로고
    • Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction
    • Harris F., Brandenburg K., Seydel U., and Phoenix D. Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction. Eur. J. Biochem. 269 (2002) 5821-5829
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5821-5829
    • Harris, F.1    Brandenburg, K.2    Seydel, U.3    Phoenix, D.4
  • 33
    • 0032449948 scopus 로고    scopus 로고
    • An investigation into the lipid interactions of peptides corresponding to the C-terminal anchoring domains of Escherichia coli penicillin-binding proteins 4, 5 and 6
    • Harris F., Demel R., de Kruijff B., and Phoenix D.A. An investigation into the lipid interactions of peptides corresponding to the C-terminal anchoring domains of Escherichia coli penicillin-binding proteins 4, 5 and 6. Biochim. Biophys. Acta 1415 (1998) 10-22
    • (1998) Biochim. Biophys. Acta , vol.1415 , pp. 10-22
    • Harris, F.1    Demel, R.2    de Kruijff, B.3    Phoenix, D.A.4
  • 34
    • 18144369721 scopus 로고    scopus 로고
    • Mode of action of lipid II-targeting lantibiotics
    • Bauer R., and Dicks L.M. Mode of action of lipid II-targeting lantibiotics. Int. J. Food Microbiol. 101 (2005) 201-216
    • (2005) Int. J. Food Microbiol. , vol.101 , pp. 201-216
    • Bauer, R.1    Dicks, L.M.2
  • 35
    • 15744401646 scopus 로고    scopus 로고
    • The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • Johnsen L., Fimland G., and Nissen-Meyer J. The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. J. Biol. Chem. 280 (2005) 9243-9250
    • (2005) J. Biol. Chem. , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 36
    • 0036829110 scopus 로고    scopus 로고
    • Increased exposure of anionic phospholipids on the surface of tumor blood vessels
    • Ran S., Downes A., and Thorpe P.E. Increased exposure of anionic phospholipids on the surface of tumor blood vessels. Cancer Res. 62 (2002) 6132-6140
    • (2002) Cancer Res. , vol.62 , pp. 6132-6140
    • Ran, S.1    Downes, A.2    Thorpe, P.E.3
  • 37
    • 0025743796 scopus 로고
    • Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes
    • Utsugi T., Schroit A.J., Connor J., Bucana C.D., and Fidler I.J. Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes. Cancer Res. 51 (1991) 3062-3066
    • (1991) Cancer Res. , vol.51 , pp. 3062-3066
    • Utsugi, T.1    Schroit, A.J.2    Connor, J.3    Bucana, C.D.4    Fidler, I.J.5
  • 39
    • 0023154974 scopus 로고
    • Membrane phospholipid composition and membrane fluidity of human brain tumour: a spin label study
    • Hattori T., Andoh T., Sakai N., Yamada H., Kameyama Y., Ohki K., and Nozawa Y. Membrane phospholipid composition and membrane fluidity of human brain tumour: a spin label study. Neurol. Res. 9 (1987) 38-43
    • (1987) Neurol. Res. , vol.9 , pp. 38-43
    • Hattori, T.1    Andoh, T.2    Sakai, N.3    Yamada, H.4    Kameyama, Y.5    Ohki, K.6    Nozawa, Y.7


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