메뉴 건너뛰기




Volumn 1713, Issue 2, 2005, Pages 73-82

Interaction of a pseudosubstrate peptide of protein kinase C and its myristoylated form with lipid vesicles: Only the myristoylated form translocates into the lipid bilayer

Author keywords

Fatty acylated peptide; Fluorescence spectroscopy; Lipid vesicle; Membrane binding; Membrane perturbation; Translocation across membrane

Indexed keywords

5(6) CARBOXYFLUORESCEIN LYSYL(EPSILON MERISTIC ACID) LYSYLSERYLISOLEUCYLTYROSYLARGINYLARGINYLGLYCYLALANYLARGINYLARGINYLTRYPTOPHYL ARGINYLLYSYLLEUCINE; 5(6) CARBOXYFLUORESCEIN LYSYLSERYLISOLEUCYLTYROSYLARGINYLARGINYLGLYCYLALANYLARGINYLARGINYLTRYPTOPHYL ARGINYLLYSYLLEUCINE; LIPID; LYSYLSERYLISOLEUCYLTYROSYLARGINYLARGINYLGLYCYLALANYLARGINYLARGINYL TRYPTOPHYLARGINYLLYSYLLEUCINE; PEPTIDE DERIVATIVE; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 21844479028     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2005.05.008     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0036636074 scopus 로고    scopus 로고
    • Nucleic-acid therapeutics: Basic principles and recent applications
    • J.B. Opalinska, and A.M. Gewirtz Nucleic-acid therapeutics: basic principles and recent applications Nat. Rev., Drug Discov. 1 2002 503 514
    • (2002) Nat. Rev., Drug Discov. , vol.1 , pp. 503-514
    • Opalinska, J.B.1    Gewirtz, A.M.2
  • 2
    • 0036489770 scopus 로고    scopus 로고
    • Recent developments in peptide-based cancer therapeutics
    • A. Sehgal Recent developments in peptide-based cancer therapeutics Curr. Opin. Drug Discov. Dev. 5 2002 245 250
    • (2002) Curr. Opin. Drug Discov. Dev. , vol.5 , pp. 245-250
    • Sehgal, A.1
  • 3
    • 0035976612 scopus 로고    scopus 로고
    • Delineation of mRNA export pathways by the use of cell-permeable peptides
    • I.E. Gallouzi, and J.A. Steitz Delineation of mRNA export pathways by the use of cell-permeable peptides Science 294 2001 1895 1901
    • (2001) Science , vol.294 , pp. 1895-1901
    • Gallouzi, I.E.1    Steitz, J.A.2
  • 6
    • 0034141430 scopus 로고    scopus 로고
    • In vivo protein transduction: Intracellular delivery of biologically active proteins, compounds and DNA
    • S.R. Schwarze, and S.F. Dowdy In vivo protein transduction: intracellular delivery of biologically active proteins, compounds and DNA Trends Pharmacol. Sci. 21 2000 45 48
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 45-48
    • Schwarze, S.R.1    Dowdy, S.F.2
  • 8
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • D. Derossi, G. Chassaing, and A. Prochiantz Trojan peptides: the penetratin system for intracellular delivery Trends Cell Biol. 8 1998 84 87
    • (1998) Trends Cell Biol. , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 10
    • 0345275894 scopus 로고    scopus 로고
    • Penetratin and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential
    • D. Terrone, S.L. Sang-Wai, L. Roudaia, and J.R. Silvius Penetratin and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential Biochemistry 42 2003 13787 13899
    • (2003) Biochemistry , vol.42 , pp. 13787-13899
    • Terrone, D.1    Sang-Wai, S.L.2    Roudaia, L.3    Silvius, J.R.4
  • 11
    • 1042288299 scopus 로고    scopus 로고
    • Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes
    • S. Deshayes, A. Heitz, M.C. Morris, P. Charnet, G. Divita, and F. Heitz Primary amphipathic cell-penetrating peptides: structural requirements and interactions with model membranes Biochemistry 43 2004 1449 1457
    • (2004) Biochemistry , vol.43 , pp. 1449-1457
    • Deshayes, S.1    Heitz, A.2    Morris, M.C.3    Charnet, P.4    Divita, G.5    Heitz, F.6
  • 13
    • 1642483442 scopus 로고    scopus 로고
    • Receptor/transporter-independent targeting of functional peptides across the plasma membrane
    • R.A. Veach, D. Liu, S. Yao, Y. Chen, X.Y. Liu, S. Downs, and J. Hawiger Receptor/transporter-independent targeting of functional peptides across the plasma membrane J. Biol. Chem. 279 2004 11425 11431
    • (2004) J. Biol. Chem. , vol.279 , pp. 11425-11431
    • Veach, R.A.1    Liu, D.2    Yao, S.3    Chen, Y.4    Liu, X.Y.5    Downs, S.6    Hawiger, J.7
  • 14
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 Tat requires cell surface heparan sulfate proteoglycans
    • M. Tyagi, M. Rusnati, M. Presta, and M. Giacca Internalization of HIV-1 Tat requires cell surface heparan sulfate proteoglycans J. Biol. Chem. 276 2001 3254 3261
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 16
    • 0025189331 scopus 로고
    • A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells
    • T. Eichholtz, J. Alblas, M. van Overveld, W. Moolenaar, and H. Ploegh A pseudosubstrate peptide inhibits protein kinase C-mediated phosphorylation in permeabilized Rat-1 cells FEBS Lett. 261 1990 147 150
    • (1990) FEBS Lett. , vol.261 , pp. 147-150
    • Eichholtz, T.1    Alblas, J.2    Van Overveld, M.3    Moolenaar, W.4    Ploegh, H.5
  • 17
    • 0032835198 scopus 로고    scopus 로고
    • Direct evidence of cytoplasmic delivery of PKC-alpha, -epsilon and -zeta pseudosubstrate lipopeptides: Study of their implication in the induction of apoptosis
    • K. Thiam, E. Loing, D. Zoukhri, C. Rommens, R. Hodges, D. Dartt, C. Verwaerde, C. Auriault, H. Gras-Masse, and C. Sergheraert Direct evidence of cytoplasmic delivery of PKC-alpha, -epsilon and -zeta pseudosubstrate lipopeptides: study of their implication in the induction of apoptosis FEBS Lett. 459 1999 285 290
    • (1999) FEBS Lett. , vol.459 , pp. 285-290
    • Thiam, K.1    Loing, E.2    Zoukhri, D.3    Rommens, C.4    Hodges, R.5    Dartt, D.6    Verwaerde, C.7    Auriault, C.8    Gras-Masse, H.9    Sergheraert, C.10
  • 18
    • 0033539052 scopus 로고    scopus 로고
    • IFN-gamma derived lipopeptides: Influence of the lipid modification on the conformation and on the ability to induce MHC class II expression in murine and human cells
    • K. Thiam, A. Delanoye, C. Verwaerde, C. Auriault, and H. Gras-Masse IFN-gamma derived lipopeptides: influence of the lipid modification on the conformation and on the ability to induce MHC class II expression in murine and human cells J. Med. Chem. 42 1999 3732 3736
    • (1999) J. Med. Chem. , vol.42 , pp. 3732-3736
    • Thiam, K.1    Delanoye, A.2    Verwaerde, C.3    Auriault, C.4    Gras-Masse, H.5
  • 21
  • 22
    • 0035254226 scopus 로고    scopus 로고
    • Synthesis by chemoselective ligation and biological evaluation of a novel cell-permeable PKC-zeta pseudosubstrate lipopeptide
    • D. Bonnet, K. Thiam, E. Loing, O. Melnyk, and H. Gras-Masse Synthesis by chemoselective ligation and biological evaluation of a novel cell-permeable PKC-zeta pseudosubstrate lipopeptide J. Med. Chem. 44 2001 468 471
    • (2001) J. Med. Chem. , vol.44 , pp. 468-471
    • Bonnet, D.1    Thiam, K.2    Loing, E.3    Melnyk, O.4    Gras-Masse, H.5
  • 23
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • M.D. Resh Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta 1451 1999 1 16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 24
    • 0036374077 scopus 로고    scopus 로고
    • A synthetic strategy for on-resin amino acid specific multiple fatty acid acylation of peptides
    • A. Harishchandran, B. Pallavi, and R. Nagaraj A synthetic strategy for on-resin amino acid specific multiple fatty acid acylation of peptides Prot. Pept. Letters 9 2002 411 417
    • (2002) Prot. Pept. Letters , vol.9 , pp. 411-417
    • Harishchandran, A.1    Pallavi, B.2    Nagaraj, R.3
  • 26
    • 0030711494 scopus 로고    scopus 로고
    • Trifluoroacetic acid cleavage and deprotection of resin-bound peptides following synthesis by Fmoc chemistry
    • C.A. Guy, and G.B. Fields Trifluoroacetic acid cleavage and deprotection of resin-bound peptides following synthesis by Fmoc chemistry Methods Enzymol. 289 1997 67 83
    • (1997) Methods Enzymol. , vol.289 , pp. 67-83
    • Guy, C.A.1    Fields, G.B.2
  • 28
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • A.I. De Kroon, M.W. Soekarjo, J. De Gier, and B. De Kruijff The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers Biochemistry 29 1990 8229 8240
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 29
    • 0028053759 scopus 로고
    • Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids
    • C.T. Sigal, W. Zhou, C.A. Buser, S. McLaughlin, and M.D. Resh Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids Proc. Natl. Acad. Sci. U. S. A. 91 1994 12253 12257
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12253-12257
    • Sigal, C.T.1    Zhou, W.2    Buser, C.A.3    McLaughlin, S.4    Resh, M.D.5
  • 30
    • 0029065501 scopus 로고
    • Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • K. Matsuzaki, O. Murase, N. Fujii, and K. Miyajima Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore Biochemistry 34 1995 6521 6526
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 31
    • 0030037217 scopus 로고    scopus 로고
    • Transbilayer transport of ions and lipids coupled with mastoparan X translocation
    • K. Matsuzaki, S. Yoneyama, O. Murase, and K. Miyajima Transbilayer transport of ions and lipids coupled with mastoparan X translocation Biochemistry 35 1996 8450 8456
    • (1996) Biochemistry , vol.35 , pp. 8450-8456
    • Matsuzaki, K.1    Yoneyama, S.2    Murase, O.3    Miyajima, K.4
  • 33
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • M. Kojima, H. Hosoda, Y. Date, M. Nakazato, H. Matsuo, and K. Kangawa Ghrelin is a growth-hormone-releasing acylated peptide from stomach Nature 402 1999 656 660
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 37
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetrain when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • M. Magzoub, L.E. Goran Eriksson, and A. Graslund Conformational states of the cell-penetrating peptide penetrain when interacting with phospholipid vesicles: effects of surface charge and peptide concentration Biochim. Biophys. Acta 1563 2002 53 63
    • (2002) Biochim. Biophys. Acta , vol.1563 , pp. 53-63
    • Magzoub, M.1    Goran Eriksson, L.E.2    Graslund, A.3
  • 38
    • 0037466075 scopus 로고    scopus 로고
    • Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles
    • M. Magzoub, L.E. Goran Eriksson, and A. Graslund Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles Biophys. Chemist. 103 2003 271 288
    • (2003) Biophys. Chemist. , vol.103 , pp. 271-288
    • Magzoub, M.1    Goran Eriksson, L.E.2    Graslund, A.3
  • 39
    • 0037457905 scopus 로고    scopus 로고
    • Application of a novel analysis to measure the binding of the membrane-translocating peptide penetratin to negatively charged liposomes
    • D. Persson, Per E.G. Thoren, M. Herner, P. Lincoln, and B. Norden Application of a novel analysis to measure the binding of the membrane-translocating peptide penetratin to negatively charged liposomes Biochemistry 42 2003 421 429
    • (2003) Biochemistry , vol.42 , pp. 421-429
    • Persson, D.1    Thoren Per, E.G.2    Herner, M.3    Lincoln, P.4    Norden, B.5
  • 40
    • 4644224822 scopus 로고    scopus 로고
    • Vesicle membrane interactions of penetratin analogues
    • D. Persson, Per E.G. Thoren, P. Lincoln, and B. Norden Vesicle membrane interactions of penetratin analogues Biochemistry 43 2004 11045 11055
    • (2004) Biochemistry , vol.43 , pp. 11045-11055
    • Persson, D.1    Thoren Per, E.G.2    Lincoln, P.3    Norden, B.4
  • 41
    • 1042288299 scopus 로고    scopus 로고
    • Insight into the mechanism of internalization of the cell-penetrating carrier peptide Pep-1 through conformational analysis
    • S. Deshayes, A. Heitz, M.C. Moris, P. Charnet, G. Divita, and F. Heitz Insight into the mechanism of internalization of the cell-penetrating carrier peptide Pep-1 through conformational analysis Biochemistry 43 2004 1449 1457
    • (2004) Biochemistry , vol.43 , pp. 1449-1457
    • Deshayes, S.1    Heitz, A.2    Moris, M.C.3    Charnet, P.4    Divita, G.5    Heitz, F.6
  • 42
    • 3343017389 scopus 로고    scopus 로고
    • Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide Pep-1 in lipidic vesicles
    • S.T. Henriques, and M.A.R.B. Castanho Consequences of nonlytic membrane perturbation to the translocation of the cell penetrating peptide Pep-1 in lipidic vesicles Biochemistry 43 2004 9716 9724
    • (2004) Biochemistry , vol.43 , pp. 9716-9724
    • Henriques, S.T.1    Castanho, M.A.R.B.2
  • 43
    • 2942715203 scopus 로고    scopus 로고
    • Primary amphipathic cell-penetrating peptides: Structural requirements and interactions with model membranes
    • S. Deshayes, T. Plenat, G. Aldrian-Herrada, G. Divita, C.L. Grimellec, and F. Heitz Primary amphipathic cell-penetrating peptides: structural requirements and interactions with model membranes Biochemistry 43 2004 7698 7706
    • (2004) Biochemistry , vol.43 , pp. 7698-7706
    • Deshayes, S.1    Plenat, T.2    Aldrian-Herrada, G.3    Divita, G.4    Grimellec, C.L.5    Heitz, F.6
  • 45
    • 0028178786 scopus 로고
    • Hedgehog is a signaling protein with a key role in patterning Drosophila imaginal discs
    • T. Tabata, and T.B. Kornberg Hedgehog is a signaling protein with a key role in patterning Drosophila imaginal discs Cell 76 1994 89 102
    • (1994) Cell , vol.76 , pp. 89-102
    • Tabata, T.1    Kornberg, T.B.2
  • 46
    • 12544254673 scopus 로고    scopus 로고
    • The N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane
    • T. Utsumi, H. Ohta, Y. Kayano, N. Sakurai, and Y. Ozoe The N-terminus of B96Bom, a Bombyx mori G-protein-coupled receptor, is N-myristoylated and translocated across the membrane FEBS J. 272 2005 472
    • (2005) FEBS J. , vol.272 , pp. 472
    • Utsumi, T.1    Ohta, H.2    Kayano, Y.3    Sakurai, N.4    Ozoe, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.