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Volumn 388, Issue 4, 2009, Pages 736-741

Intracellular delivery of bovine lactoferricin's antimicrobial core (RRWQWR) kills T-leukemia cells

Author keywords

Antimicrobial peptide; Bovine lactoferricin; Cancer; Caspase; Cathepsin B; Fusogenic liposome

Indexed keywords

ACETYLCYSTEINE; ANTINEOPLASTIC AGENT; ARGINYLARGINYLTRYPTOPHYLGLUTAMINYLTRYPTOPHYLARGININE; CASPASE; CASPASE INHIBITOR; CATHEPSIN B; CATHEPSIN B INHIBITOR; CYTOCHROME C; DNA; GLUTATHIONE; LACTOFERRICIN B; LIPOSOME; PEPTIDE DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

EID: 69949150585     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.083     Document Type: Article
Times cited : (55)

References (32)
  • 2
    • 0014574791 scopus 로고
    • Lactoferrin, an iron-binding protein in neutrophilic leukocytes
    • Masson P.L., Heremans J.F., and Schonne E. Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130 (1969) 643-658
    • (1969) J. Exp. Med. , vol.130 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 4
    • 0027232811 scopus 로고
    • Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Wakabayashi H., Takase M., Kawase K., Shimamura S., and Tomita M. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol. 182 (1993) 97-105
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 97-105
    • Bellamy, W.1    Wakabayashi, H.2    Takase, M.3    Kawase, K.4    Shimamura, S.5    Tomita, M.6
  • 6
    • 0031589527 scopus 로고    scopus 로고
    • Apoptosis in human leukemic cells induced by lactoferricin, a bovine milk protein-derived peptide: involvement of reactive oxygen species
    • Yoo Y.C., Watanabe R., Koike Y., Mitobe M., Shimazaki K., Watanabe S., and Azuma I. Apoptosis in human leukemic cells induced by lactoferricin, a bovine milk protein-derived peptide: involvement of reactive oxygen species. Biochem. Biophys. Res. Commun. 237 (1997) 624-628
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 624-628
    • Yoo, Y.C.1    Watanabe, R.2    Koike, Y.3    Mitobe, M.4    Shimazaki, K.5    Watanabe, S.6    Azuma, I.7
  • 7
    • 18044397724 scopus 로고    scopus 로고
    • Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines
    • Mader J.S., Salsman J., Conrad D.M., and Hoskin D.W. Bovine lactoferricin selectively induces apoptosis in human leukemia and carcinoma cell lines. Mol. Cancer Ther. 4 (2005) 612-624
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 612-624
    • Mader, J.S.1    Salsman, J.2    Conrad, D.M.3    Hoskin, D.W.4
  • 10
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., and Vogel H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37 (1998) 4288-4298
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 11
    • 0036185339 scopus 로고    scopus 로고
    • Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides
    • Vogel H.J., Schibli D.J., Jing W., Lohmeier-Vogel E.M., Epand R.F., and Epand R.M. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochem. Cell Biol. 80 (2002) 49-63
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 49-63
    • Vogel, H.J.1    Schibli, D.J.2    Jing, W.3    Lohmeier-Vogel, E.M.4    Epand, R.F.5    Epand, R.M.6
  • 12
    • 0029860472 scopus 로고    scopus 로고
    • Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin
    • Kang J.H., Lee M.K., Kim K.L., and Hahm K.S. Structure-biological activity relationships of 11-residue highly basic peptide segment of bovine lactoferrin. Int. J. Pept. Protein Res. 48 (1996) 357-363
    • (1996) Int. J. Pept. Protein Res. , vol.48 , pp. 357-363
    • Kang, J.H.1    Lee, M.K.2    Kim, K.L.3    Hahm, K.S.4
  • 13
    • 0033787915 scopus 로고    scopus 로고
    • Antibacterial activity of 15-residue lactoferricin derivatives
    • Strom M.B., Rekdal O., and Svendsen J.S. Antibacterial activity of 15-residue lactoferricin derivatives. J. Pept. Res. 56 (2000) 265-274
    • (2000) J. Pept. Res. , vol.56 , pp. 265-274
    • Strom, M.B.1    Rekdal, O.2    Svendsen, J.S.3
  • 14
    • 0029175052 scopus 로고
    • Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids
    • Kachel K., Asuncion-Punzalan E., and London E. Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids. Biochemistry 34 (1995) 15475-15479
    • (1995) Biochemistry , vol.34 , pp. 15475-15479
    • Kachel, K.1    Asuncion-Punzalan, E.2    London, E.3
  • 16
    • 0035083899 scopus 로고    scopus 로고
    • A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils
    • Ueta E., Tanida T., and Osaki T. A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. J. Pept. Res. 57 (2001) 240-249
    • (2001) J. Pept. Res. , vol.57 , pp. 240-249
    • Ueta, E.1    Tanida, T.2    Osaki, T.3
  • 17
    • 0032997518 scopus 로고    scopus 로고
    • The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles
    • Schibli D.J., Hwang P.M., and Vogel H.J. The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles. FEBS Lett. 446 (1999) 213-217
    • (1999) FEBS Lett. , vol.446 , pp. 213-217
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 19
    • 0025792001 scopus 로고
    • The JAM test. A simple assay for DNA fragmentation and cell death
    • Matzinger P. The JAM test. A simple assay for DNA fragmentation and cell death. J. Immunol. Methods 145 (1991) 185-192
    • (1991) J. Immunol. Methods , vol.145 , pp. 185-192
    • Matzinger, P.1
  • 20
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65 (1983) 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 21
    • 0024483266 scopus 로고
    • Fluorescent labeling of mitochondria
    • Chen L.B. Fluorescent labeling of mitochondria. Methods Cell Biol. 29 (1989) 103-123
    • (1989) Methods Cell Biol. , vol.29 , pp. 103-123
    • Chen, L.B.1
  • 22
    • 34250883860 scopus 로고    scopus 로고
    • Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria
    • Mader J.S., Richardson A., Salsman J., Top D., de Antueno R., Duncan R., and Hoskin D.W. Bovine lactoferricin causes apoptosis in Jurkat T-leukemia cells by sequential permeabilization of the cell membrane and targeting of mitochondria. Exp. Cell Res. 313 (2007) 2634-2650
    • (2007) Exp. Cell Res. , vol.313 , pp. 2634-2650
    • Mader, J.S.1    Richardson, A.2    Salsman, J.3    Top, D.4    de Antueno, R.5    Duncan, R.6    Hoskin, D.W.7
  • 23
    • 0347766076 scopus 로고    scopus 로고
    • The effects of shortening lactoferrin derived peptides against tumour cells, bacteria and normal human cells
    • Yang N., Strom M.B., Mekonnen S.M., Svendsen J.S., and Rekdal O. The effects of shortening lactoferrin derived peptides against tumour cells, bacteria and normal human cells. J. Pept. Sci. 10 (2004) 37-46
    • (2004) J. Pept. Sci. , vol.10 , pp. 37-46
    • Yang, N.1    Strom, M.B.2    Mekonnen, S.M.3    Svendsen, J.S.4    Rekdal, O.5
  • 24
    • 69949164681 scopus 로고    scopus 로고
    • Novel peptide ligand directs liposomes toward EGF-R high-expressing cancer cells in vitro and in vivo
    • Song S., Liu D., Peng J., Deng H., Guo Y., Xu L.X., Miller A.D., and Xu Y. Novel peptide ligand directs liposomes toward EGF-R high-expressing cancer cells in vitro and in vivo. FASEB J. 23 (2009) 1396-1404
    • (2009) FASEB J. , vol.23 , pp. 1396-1404
    • Song, S.1    Liu, D.2    Peng, J.3    Deng, H.4    Guo, Y.5    Xu, L.X.6    Miller, A.D.7    Xu, Y.8
  • 25
    • 33748126226 scopus 로고    scopus 로고
    • Recent approaches to intracellular delivery of drugs and DNA and organelle targeting
    • Torchilin V.P. Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. Annu. Rev. Biomed. Eng. 8 (2006) 343-375
    • (2006) Annu. Rev. Biomed. Eng. , vol.8 , pp. 343-375
    • Torchilin, V.P.1
  • 26
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?
    • de Kroon A.I., Dolis D., Mayer A., Lill R., and de Kruijff B. Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?. Biochim. Biophys. Acta 1325 (1997) 108-116
    • (1997) Biochim. Biophys. Acta , vol.1325 , pp. 108-116
    • de Kroon, A.I.1    Dolis, D.2    Mayer, A.3    Lill, R.4    de Kruijff, B.5
  • 28
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates
    • 2+-dependent proteases in ischemic neuronal death: a conserved 'calpain-cathepsin cascade' from nematodes to primates. Cell Calcium 36 (2004) 285-293
    • (2004) Cell Calcium , vol.36 , pp. 285-293
    • Yamashima, T.1
  • 29
    • 34249978223 scopus 로고    scopus 로고
    • Lysosomal and mitochondrial pathways in miltefosine-induced apoptosis in U937 cells
    • Paris C., Bertiglio J., and Bréard J. Lysosomal and mitochondrial pathways in miltefosine-induced apoptosis in U937 cells. Apoptosis 12 (2007) 1257-1267
    • (2007) Apoptosis , vol.12 , pp. 1257-1267
    • Paris, C.1    Bertiglio, J.2    Bréard, J.3
  • 32
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • Hilpert K., Volkmer-Engert R., Walter T., and Hancock R.E. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23 (2005) 1008-1012
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.