메뉴 건너뛰기




Volumn 454, Issue 2, 2013, Pages 738-747

The NFL-TBS.40-63 anti-glioblastoma peptide enters selectively in glioma cells by endocytosis

Author keywords

Endocytosis; Glioblastoma; Peptide; Tyrosine kinase receptor; Uptake

Indexed keywords

CELL PENETRATING PEPTIDE; GLYCOSAMINOGLYCAN; NFL TBS 40 63 PEPTIDE; PEPTIDE; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

EID: 84884164384     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2013.04.004     Document Type: Article
Times cited : (26)

References (52)
  • 1
    • 77958154973 scopus 로고    scopus 로고
    • Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells
    • Alves, I.D., Jiao, C.Y., Aubry, S., Aussedat, B., Burlina, F., Chassaing, G., Sagan, S., 2010. Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells. Biochim. Biophys. Acta 1798, 2231-2239.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2231-2239
    • Alves, I.D.1    Jiao, C.Y.2    Aubry, S.3    Aussedat, B.4    Burlina, F.5    Chassaing, G.6    Sagan, S.7
  • 2
    • 79955814107 scopus 로고    scopus 로고
    • Binding of cell-penetrating penetratin peptides to plasma membrane vesicles correlates directly with cellular uptake
    • Amand, H.L., Bostrom, C.L., Lincoln, P., Norden, B., Esbjorner, E.K., 2011. Binding of cell-penetrating penetratin peptides to plasma membrane vesicles correlates directly with cellular uptake. Biochim. Biophys. Acta 1808, 1860-1867.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1860-1867
    • Amand, H.L.1    Bostrom, C.L.2    Lincoln, P.3    Norden, B.4    Esbjorner, E.K.5
  • 3
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H.A., Chen, Y., Norkin, L.C., 1996. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae. Mol. Biol. Cell 7, 1825-1834. (Pubitemid 26386733)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.11 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 4
    • 84855768645 scopus 로고    scopus 로고
    • The vimentin-tubulin binding site peptide (Vim-TBS.58-81) crosses the plasma membrane and enters the nuclei of human glioma cells
    • Balzeau, J., Peterson, A., Eyer, J., 2012. The vimentin-tubulin binding site peptide (Vim-TBS.58-81) crosses the plasma membrane and enters the nuclei of human glioma cells. Int. J. Pharm. 423, 77-83.
    • (2012) Int. J. Pharm. , vol.423 , pp. 77-83
    • Balzeau, J.1    Peterson, A.2    Eyer, J.3
  • 5
    • 84874259731 scopus 로고    scopus 로고
    • The NFL-TBS. 40-63 peptide improves the in vitro and in vivo targeted uptake of lipid nanocapsules by glioblastoma cells
    • Balzeau, J., Pinier, M., Berges, R., Saulnier, P., Benoit, J.-P., Eyer, J., 2013. The NFL-TBS. 40-63 peptide improves the in vitro and in vivo targeted uptake of lipid nanocapsules by glioblastoma cells. Biomaterials 34, 3381-3389.
    • (2013) Biomaterials , vol.34 , pp. 3381-3389
    • Balzeau, J.1    Pinier, M.2    Berges, R.3    Saulnier, P.4    Benoit, J.-P.5    Eyer, J.6
  • 7
    • 84863426056 scopus 로고    scopus 로고
    • A tubulin binding peptide targets glioma cells disrupting their microtubules, blocking migration, and inducing apoptosis
    • Berges, R., Balzeau, J., Peterson, A.C., Eyer, J., 2012a. A tubulin binding peptide targets glioma cells disrupting their microtubules, blocking migration, and inducing apoptosis. Mol. Ther. 20, 1367-1377.
    • (2012) Mol. Ther. , vol.20 , pp. 1367-1377
    • Berges, R.1    Balzeau, J.2    Peterson, A.C.3    Eyer, J.4
  • 8
    • 84869017332 scopus 로고    scopus 로고
    • Structure-function analysis of the glioma targeting NFL-TBS.40-63 peptide corresponding to the tubulin-binding site on the light neurofilament subunit
    • Berges, R., Balzeau, J., Takahashi, M., Prevost, C., Eyer, J., 2012b. Structure-function analysis of the glioma targeting NFL-TBS.40-63 peptide corresponding to the tubulin-binding site on the light neurofilament subunit. PLoS ONE 7, e49436.
    • (2012) PLoS ONE , vol.7
    • Berges, R.1    Balzeau, J.2    Takahashi, M.3    Prevost, C.4    Eyer, J.5
  • 10
    • 33847673078 scopus 로고    scopus 로고
    • Altered endocytosis of epidermal growth factor receptor in androgen receptor positve prostate cancer cell lines
    • DOI 10.1677/jme.1.02155
    • Bonaccorsi, L., Nosi, D., Muratori, M., Formigli, L., Forti, G., Baldi, E., 2007. Altered endocytosis of epidermal growth factor receptor in androgen receptor positive prostate cancer cell lines. J. Mol. Endocrinol. 38, 51-66. (Pubitemid 46351592)
    • (2007) Journal of Molecular Endocrinology , vol.38 , Issue.1-2 , pp. 51-66
    • Bonaccorsi, L.1    Nosi, D.2    Muratori, M.3    Formigli, L.4    Forti, G.5    Baldi, E.6
  • 11
    • 57449104947 scopus 로고    scopus 로고
    • PI3K signalling in glioma - animal models and therapeutic challenges
    • Cheng, C.K., Fan, Q.W., Weiss, W.A., 2009. PI3K signalling in glioma - animal models and therapeutic challenges. Brain Pathol. 19, 112-120.
    • (2009) Brain Pathol. , vol.19 , pp. 112-120
    • Cheng, C.K.1    Fan, Q.W.2    Weiss, W.A.3
  • 12
    • 0034677631 scopus 로고    scopus 로고
    • PIP2 and PIP3: Complex roles at the cell surface
    • Czech, M.P., 2000. PIP2 and PIP3: complex roles at the cell surface. Cell 100, 603-606.
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 14
    • 78751485498 scopus 로고    scopus 로고
    • The effects of anti-VEGFR and anti-EGFR agents on glioma cell migration through implication of growth factors with integrins
    • Dimitropoulos, K., Giannopoulou, E., Argyriou, A.A., Zolota, V., Petsas, T., Tsiata, E., Kalofonos, H.P., 2010. The effects of anti-VEGFR and anti-EGFR agents on glioma cell migration through implication of growth factors with integrins. Anticancer Res. 30, 4987-4992.
    • (2010) Anticancer Res. , vol.30 , pp. 4987-4992
    • Dimitropoulos, K.1    Giannopoulou, E.2    Argyriou, A.A.3    Zolota, V.4    Petsas, T.5    Tsiata, E.6    Kalofonos, H.P.7
  • 16
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • DOI 10.1111/j.1600-0854.2007.00572.x
    • Duchardt, F., Fotin-Mleczek, M., Schwarz, H., Fischer, R., Brock, R., 2007. A comprehensive model for the cellular uptake of cationic cell-penetrating peptides. Traffic 8, 848-866. (Pubitemid 46971632)
    • (2007) Traffic , vol.8 , Issue.7 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 17
    • 78149333191 scopus 로고    scopus 로고
    • The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells
    • Eierhoff, T., Hrincius, E.R., Rescher, U., Ludwig, S., Ehrhardt, C., 2010. The epidermal growth factor receptor (EGFR) promotes uptake of influenza A viruses (IAV) into host cells. PLoS Pathog. 6, e1001099.
    • (2010) PLoS Pathog. , vol.6
    • Eierhoff, T.1    Hrincius, E.R.2    Rescher, U.3    Ludwig, S.4    Ehrhardt, C.5
  • 18
    • 79952111297 scopus 로고    scopus 로고
    • Targeting the RTK-PI3K-mTOR axis in malignant glioma: Overcoming resistance
    • Fan, Q.W., Weiss, W.A., 2010. Targeting the RTK-PI3K-mTOR axis in malignant glioma: overcoming resistance. Curr. Top. Microbiol. Immunol. 347, 279-296.
    • (2010) Curr. Top. Microbiol. Immunol. , vol.347 , pp. 279-296
    • Fan, Q.W.1    Weiss, W.A.2
  • 19
    • 0034013621 scopus 로고    scopus 로고
    • A peptide of the alpha 3(IV) chain of type IV collagen modulates stimulated neutrophil function via activation of cAMP-dependent protein kinase and Ser/Thr protein phosphatase
    • DOI 10.1016/S0898-6568(00)00074-7, PII S0898656800000747
    • Fawzi, A., Robinet, A., Monboisse, J.C., Ziaie, Z., Kefalides, N.A., Bellon, G., 2000. A peptide of the alpha 3(IV) chain of type IV collagen modulates stimulated neutrophil function via activation of cAMP-dependent protein kinase and Ser/Thr protein phosphatase. Cell Signal. 12, 327-335. (Pubitemid 30261548)
    • (2000) Cellular Signalling , vol.12 , Issue.5 , pp. 327-335
    • Fawzi, A.1    Robinet, A.2    Monboisse, J.C.3    Ziaie, Z.4    Kefalides, N.A.5    Bellon, G.6
  • 20
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides: An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki, S., Suzuki, T., Ohashi, W., Yagami, T., Tanaka, S., Ueda, K., Sugiura, Y., 2001. Arginine-rich peptides: an abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276, 5836-5840.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 21
    • 0026334978 scopus 로고
    • Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells
    • Gladson, C.L., Cheresh, D.A., 1991. Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells. J. Clin. Invest. 88, 1924-1932.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1924-1932
    • Gladson, C.L.1    Cheresh, D.A.2
  • 22
  • 23
    • 74049160383 scopus 로고    scopus 로고
    • Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction
    • Gump, J.M., June, R.K., Dowdy, S.F., 2010. Revised role of glycosaminoglycans in TAT protein transduction domain-mediated cellular transduction. J. Biol. Chem. 285, 1500-1507.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1500-1507
    • Gump, J.M.1    June, R.K.2    Dowdy, S.F.3
  • 25
    • 0020626609 scopus 로고
    • Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts
    • Larkin, J.M., Brown, M.S., Goldstein, J.L., Anderson, R.G., 1983. Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts. Cell 33, 273-285. (Pubitemid 13096456)
    • (1983) Cell , vol.33 , Issue.1 , pp. 273-285
    • Larkin, J.M.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.W.4
  • 26
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • DOI 10.1038/nrm1571
    • Le Roy, C., Wrana, J.L., 2005. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell Biol. 6, 112-126. (Pubitemid 40215807)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.2 , pp. 112-126
    • Le, R.C.1    Wrana, J.L.2
  • 29
    • 79959365312 scopus 로고    scopus 로고
    • Mechanisms of cellular uptake of cell-penetrating peptides
    • Madani, F., Lindberg, S., Langel, U., Futaki, S., Graslund, A., 2011. Mechanisms of cellular uptake of cell-penetrating peptides. J. Biophys. 2011, 414729.
    • (2011) J. Biophys. , vol.2011 , pp. 414729
    • Madani, F.1    Lindberg, S.2    Langel, U.3    Futaki, S.4    Graslund, A.5
  • 30
    • 58149099412 scopus 로고    scopus 로고
    • Comparison of cellular uptake using 22 CPPs in 4 different cell lines
    • Mueller, J., Kretzschmar, I., Volkmer, R., Boisguerin, P., 2008. Comparison of cellular uptake using 22 CPPs in 4 different cell lines. Bioconjug. Chem. 19, 2363-2374.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 2363-2374
    • Mueller, J.1    Kretzschmar, I.2    Volkmer, R.3    Boisguerin, P.4
  • 34
    • 84860467135 scopus 로고    scopus 로고
    • Insights into the uptake mechanism of NrTP, a cell-penetrating peptide preferentially targeting the nucleolus of tumour cells
    • Radis-Baptista, G., de la Torre, B.G., Andreu, D., 2012. Insights into the uptake mechanism of NrTP, a cell-penetrating peptide preferentially targeting the nucleolus of tumour cells. Chem. Biol. Drug Des. 79, 907-915.
    • (2012) Chem. Biol. Drug Des. , vol.79 , pp. 907-915
    • Radis-Baptista, G.1    De La Torre, B.G.2    Andreu, D.3
  • 35
    • 84878766832 scopus 로고    scopus 로고
    • Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic
    • Raiborg, C., Schink, K.O., Stenmark, H., 2013. Class III phosphatidylinositol 3-kinase and its catalytic product PtdIns3P in regulation of endocytic membrane traffic. FEBS J., http://dx.doi.org/10.1111/febs.12116.
    • (2013) FEBS J.
    • Raiborg, C.1    Schink, K.O.2    Stenmark, H.3
  • 36
    • 17644386231 scopus 로고    scopus 로고
    • Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors
    • Richard, J.P., Melikov, K., Brooks, H., Prevot, P., Lebleu, B., Chernomordik, L.V., Cellular uptake of unconjugated TAT peptide involves clathrin-dependent endocytosis and heparan sulfate receptors. J. Biol. Chem. 280, 15300-15306.
    • J. Biol. Chem. , vol.280 , pp. 15300-15306
    • Richard, J.P.1    Melikov, K.2    Brooks, H.3    Prevot, P.4    Lebleu, B.5    Chernomordik, L.V.6
  • 38
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal, S.K., Skretting, G., Garred, O., Vilhardt, F., van Deurs, B., Sandvig, K., 1999. Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol. Biol. Cell 10, 961-974.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, O.3    Vilhardt, F.4    Van Deurs, B.5    Sandvig, K.6
  • 39
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles
    • Saalik, P., Niinep, A., Pae, J., Hansen, M., Lubenets, D., Langel, U., Pooga, M., 2011. Penetration without cells: membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles. J. Control. Release 153, 117-125.
    • (2011) J. Control. Release , vol.153 , pp. 117-125
    • Saalik, P.1    Niinep, A.2    Pae, J.3    Hansen, M.4    Lubenets, D.5    Langel, U.6    Pooga, M.7
  • 43
    • 0029011218 scopus 로고
    • The MAPK signalling cascade
    • Seger, R., Krebs, E.G., 1995. The MAPK signalling cascade. FASEB J. 9, 726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 44
    • 84862088439 scopus 로고    scopus 로고
    • Evaluation of in-labelled cyclic RGD peptides: Effects of peptide and linker multiplicity on their tumour uptake, excretion kinetics and metabolic stability
    • Shi, J., Zhou, Y., Chakraborty, S., Kim, Y.S., Jia, B., Wang, F., Liu, S., 2011. Evaluation of in-labelled cyclic RGD peptides: effects of peptide and linker multiplicity on their tumour uptake, excretion kinetics and metabolic stability. Theranostics 1, 322-340.
    • (2011) Theranostics , vol.1 , pp. 322-340
    • Shi, J.1    Zhou, Y.2    Chakraborty, S.3    Kim, Y.S.4    Jia, B.5    Wang, F.6    Liu, S.7
  • 47
    • 84858704212 scopus 로고    scopus 로고
    • Tat(48-60) peptide amino acid sequence is not unique in its cell penetrating properties and cell-surface glycosaminoglycans inhibit its cellular uptake
    • Subrizi, A., Tuominen, E., Bunker, A., Rog, T., Antopolsky, M., Urtti, A., 2011. Tat(48-60) peptide amino acid sequence is not unique in its cell penetrating properties and cell-surface glycosaminoglycans inhibit its cellular uptake. J. Control. Release 158, 277-285.
    • (2011) J. Control. Release , vol.158 , pp. 277-285
    • Subrizi, A.1    Tuominen, E.2    Bunker, A.3    Rog, T.4    Antopolsky, M.5    Urtti, A.6
  • 49
    • 54549108740 scopus 로고    scopus 로고
    • Comprehensive genomic characterization defines human glioblastoma genes and core pathways
    • The Cancer Genome Atlas Research Network
    • The Cancer Genome Atlas Research Network, 2008. Comprehensive genomic characterization defines human glioblastoma genes and core pathways. Nature 455, 1061-1068.
    • (2008) Nature , vol.455 , pp. 1061-1068
  • 50
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • Vives, E., Brodin, P., Lebleu, B., 1997. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272, 16010-16017. (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 51
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • DOI 10.1038/nm996
    • Wadia, J.S., Stan, R.V., Dowdy, S.F., 2004. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat. Med. 10, 310-315. (Pubitemid 38667624)
    • (2004) Nature Medicine , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.