메뉴 건너뛰기




Volumn 5, Issue JUN, 2015, Pages

The human cathelicidin antimicrobial peptide LL-37 and mimics are potential anticancer drugs

Author keywords

Anticancer; Antimicrobial peptides; Carcinogenesis; Cathelicidin; Ll 37

Indexed keywords


EID: 84934269603     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2015.00144     Document Type: Review
Times cited : (130)

References (119)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature (2002) 415(6870):389-95. doi:10.1038/415389a.
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 2
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti M. The role of cathelicidins in the innate host defenses of mammals. Curr Issues Mol Biol (2005) 7(2):17, 9-96.
    • (2005) Curr Issues Mol Biol , vol.7 , Issue.2 , pp. 179-196
    • Zanetti, M.1
  • 3
    • 58149187882 scopus 로고    scopus 로고
    • APD2: the updated antimicrobial peptide database and its application in peptide design
    • Database Issue
    • Wang G, Li X, Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res (2009) 37(Database issue):D933-7. doi:10.1093/nar/gkn823.
    • (2009) Nucleic Acids Res , vol.37 , pp. D933-D937
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 4
    • 0042208088 scopus 로고    scopus 로고
    • Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina
    • Sorensen OE, Gram L, Johnsen AH, Andersson E, Bangsboll S, Tjabringa GS, et al. Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina. J Biol Chem (2003) 278(31):28540-6. doi:10.1074/jbc.M301608200.
    • (2003) J Biol Chem , vol.278 , Issue.31 , pp. 28540-28546
    • Sorensen, O.E.1    Gram, L.2    Johnsen, A.H.3    Andersson, E.4    Bangsboll, S.5    Tjabringa, G.S.6
  • 5
    • 33750139445 scopus 로고    scopus 로고
    • Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin
    • Yamasaki K, Schauber J, Coda A, Lin H, Dorschner RA, Schechter NM, et al. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. FASEB J (2006) 20(12):2068-80. doi:10.1096/fj.06-6075com.
    • (2006) FASEB J , vol.20 , Issue.12 , pp. 2068-2080
    • Yamasaki, K.1    Schauber, J.2    Coda, A.3    Lin, H.4    Dorschner, R.A.5    Schechter, N.M.6
  • 6
    • 0032488904 scopus 로고    scopus 로고
    • Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37
    • Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. J Biol Chem (1998) 273(6):3718-24. doi:10.1074/jbc.273.6.3718.
    • (1998) J Biol Chem , vol.273 , Issue.6 , pp. 3718-3724
    • Johansson, J.1    Gudmundsson, G.H.2    Rottenberg, M.E.3    Berndt, K.D.4    Agerberth, B.5
  • 7
    • 0028942078 scopus 로고
    • FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis
    • Agerberth B, Gunne H, Odeberg J, Kogner P, Boman HG, Gudmundsson GH. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc Natl Acad Sci U S A (1995) 92(1):195-9. doi:10.1073/pnas.92.1.195.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.1 , pp. 195-199
    • Agerberth, B.1    Gunne, H.2    Odeberg, J.3    Kogner, P.4    Boman, H.G.5    Gudmundsson, G.H.6
  • 8
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • De Y, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, et al. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J Exp Med (2000) 192(7):1069-74. doi:10.1084/jem.192.7.1069.
    • (2000) J Exp Med , vol.192 , Issue.7 , pp. 1069-1074
    • De, Y.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6
  • 9
    • 40749146805 scopus 로고    scopus 로고
    • Expression of cathelicidin LL-37 during Mycobacterium tuberculosis infection in human alveolar macrophages, monocytes, neutrophils, and epithelial cells
    • Rivas-Santiago B, Hernandez-Pando R, Carranza C, Juarez E, Contreras JL, Aguilar-Leon D, et al. Expression of cathelicidin LL-37 during Mycobacterium tuberculosis infection in human alveolar macrophages, monocytes, neutrophils, and epithelial cells. Infect Immun (2008) 76(3):935-41. doi:10.1128/IAI.01218-07.
    • (2008) Infect Immun , vol.76 , Issue.3 , pp. 935-941
    • Rivas-Santiago, B.1    Hernandez-Pando, R.2    Carranza, C.3    Juarez, E.4    Contreras, J.L.5    Aguilar-Leon, D.6
  • 10
    • 84903701599 scopus 로고    scopus 로고
    • High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments
    • Wang G, Mishra B, Epand RF, Epand RM. High-quality 3D structures shine light on antibacterial, anti-biofilm and antiviral activities of human cathelicidin LL-37 and its fragments. Biochim Biophys Acta (2014) 1838(9):2160-72. doi:10.1016/j.bbamem.2014.01.016.
    • (2014) Biochim Biophys Acta , vol.1838 , Issue.9 , pp. 2160-2172
    • Wang, G.1    Mishra, B.2    Epand, R.F.3    Epand, R.M.4
  • 11
    • 77956363683 scopus 로고    scopus 로고
    • Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications
    • Wu WK, Wang G, Coffelt SB, Betancourt AM, Lee CW, Fan D, et al. Emerging roles of the host defense peptide LL-37 in human cancer and its potential therapeutic applications. Int J Cancer (2010) 127(8):1741-7. doi:10.1002/ijc.25489.
    • (2010) Int J Cancer , vol.127 , Issue.8 , pp. 1741-1747
    • Wu, W.K.1    Wang, G.2    Coffelt, S.B.3    Betancourt, A.M.4    Lee, C.W.5    Fan, D.6
  • 12
    • 3242889844 scopus 로고    scopus 로고
    • C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells
    • Okumura K, Itoh A, Isogai E, Hirose K, Hosokawa Y, Abiko Y, et al. C-terminal domain of human CAP18 antimicrobial peptide induces apoptosis in oral squamous cell carcinoma SAS-H1 cells. Cancer Lett (2004) 212(2):185-94. doi:10.1016/j.canlet.2004.04.006.
    • (2004) Cancer Lett , vol.212 , Issue.2 , pp. 185-194
    • Okumura, K.1    Itoh, A.2    Isogai, E.3    Hirose, K.4    Hosokawa, Y.5    Abiko, Y.6
  • 13
    • 84865334555 scopus 로고    scopus 로고
    • Anti-proliferative effect of an analogue of the LL-37 peptide in the colon cancer derived cell line HCT116 p53+/+ and p53
    • Kuroda K, Fukuda T, Yoneyama H, Katayama M, Isogai H, Okumura K, et al. Anti-proliferative effect of an analogue of the LL-37 peptide in the colon cancer derived cell line HCT116 p53+/+ and p53. Oncol Rep (2012) 28(3):829-34. doi:10.3892/or.2012.1876.
    • (2012) Oncol Rep , vol.28 , Issue.3 , pp. 829-834
    • Kuroda, K.1    Fukuda, T.2    Yoneyama, H.3    Katayama, M.4    Isogai, H.5    Okumura, K.6
  • 14
    • 0030602220 scopus 로고    scopus 로고
    • Structural, functional analysis and localization of the human CAP18 gene
    • Larrick JW, Lee J, Ma S, Li X, Francke U, Wright SC, et al. Structural, functional analysis and localization of the human CAP18 gene. FEBS Lett (1996) 398(1):74-80. doi:10.1016/S0014-5793(96)01199-4.
    • (1996) FEBS Lett , vol.398 , Issue.1 , pp. 74-80
    • Larrick, J.W.1    Lee, J.2    Ma, S.3    Li, X.4    Francke, U.5    Wright, S.C.6
  • 15
    • 0029007198 scopus 로고
    • hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules
    • Cowland JB, Johnsen AH, Borregaard N. hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules. FEBS Lett (1995) 368(1):173-6. doi:10.1016/0014-5793(95)00634-L.
    • (1995) FEBS Lett , vol.368 , Issue.1 , pp. 173-176
    • Cowland, J.B.1    Johnsen, A.H.2    Borregaard, N.3
  • 16
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen O, Arnljots K, Cowland JB, Bainton DF, Borregaard N. The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood (1997) 90(7):2796-803.
    • (1997) Blood , vol.90 , Issue.7 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 17
    • 0030956070 scopus 로고    scopus 로고
    • The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders
    • Frohm M, Agerberth B, Ahangari G, Stahle-Backdahl M, Liden S, Wigzell H, et al. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J Biol Chem (1997) 272(24):15258-63. doi:10.1074/jbc.272.24.15258.
    • (1997) J Biol Chem , vol.272 , Issue.24 , pp. 15258-15263
    • Frohm, M.1    Agerberth, B.2    Ahangari, G.3    Stahle-Backdahl, M.4    Liden, S.5    Wigzell, H.6
  • 18
    • 0036891933 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva
    • Murakami M, Ohtake T, Dorschner RA, Gallo RL. Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. J Dent Res (2002) 81(12):845-50. doi:10.1177/154405910208101210.
    • (2002) J Dent Res , vol.81 , Issue.12 , pp. 845-850
    • Murakami, M.1    Ohtake, T.2    Dorschner, R.A.3    Gallo, R.L.4
  • 19
    • 64049103406 scopus 로고    scopus 로고
    • Treatment with LL-37 peptide enhances antitumor effects induced by CpG oligodeoxynucleotides against ovarian cancer
    • Chuang CM, Monie A, Wu A, Mao CP, Hung CF. Treatment with LL-37 peptide enhances antitumor effects induced by CpG oligodeoxynucleotides against ovarian cancer. Hum Gene Ther (2009) 20(4):303-13. doi:10.1089/hum.2008.124.
    • (2009) Hum Gene Ther , vol.20 , Issue.4 , pp. 303-313
    • Chuang, C.M.1    Monie, A.2    Wu, A.3    Mao, C.P.4    Hung, C.F.5
  • 20
    • 66349099109 scopus 로고    scopus 로고
    • The human host defense peptide LL-37 induces apoptosis in a calpain- and apoptosis-inducing factor-dependent manner involving Bax activity
    • Mader JS, Mookherjee N, Hancock RE, Bleackley RC. The human host defense peptide LL-37 induces apoptosis in a calpain- and apoptosis-inducing factor-dependent manner involving Bax activity. Mol Cancer Res (2009) 7(5):689-702. doi:10.1158/1541-7786.MCR-08-0274.
    • (2009) Mol Cancer Res , vol.7 , Issue.5 , pp. 689-702
    • Mader, J.S.1    Mookherjee, N.2    Hancock, R.E.3    Bleackley, R.C.4
  • 21
    • 1342282224 scopus 로고    scopus 로고
    • Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense
    • Murakami M, Lopez-Garcia B, Braff M, Dorschner RA, Gallo RL. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J Immunol (2004) 172(5):3070-7. doi:10.4049/jimmunol.172.5.3070.
    • (2004) J Immunol , vol.172 , Issue.5 , pp. 3070-3077
    • Murakami, M.1    Lopez-Garcia, B.2    Braff, M.3    Dorschner, R.A.4    Gallo, R.L.5
  • 22
    • 75749117540 scopus 로고    scopus 로고
    • The host defense peptide LL-37 activates the tumor-suppressing bone morphogenetic protein signaling via inhibition of proteasome in gastric cancer cells
    • Wu WK, Sung JJ, To KF, Yu L, Li HT, Li ZJ, et al. The host defense peptide LL-37 activates the tumor-suppressing bone morphogenetic protein signaling via inhibition of proteasome in gastric cancer cells. J Cell Physiol (2010) 223(1):178-86. doi:10.1002/jcp.22026.
    • (2010) J Cell Physiol , vol.223 , Issue.1 , pp. 178-186
    • Wu, W.K.1    Sung, J.J.2    To, K.F.3    Yu, L.4    Li, H.T.5    Li, Z.J.6
  • 23
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • Wang G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J Biol Chem (2008) 283(47):32637-43. doi:10.1074/jbc.M805533200.
    • (2008) J Biol Chem , vol.283 , Issue.47 , pp. 32637-32643
    • Wang, G.1
  • 24
    • 33746087225 scopus 로고    scopus 로고
    • Control of the innate epithelial antimicrobial response is cell-type specific and dependent on relevant microenvironmental stimuli
    • Schauber J, Dorschner RA, Yamasaki K, Brouha B, Gallo RL. Control of the innate epithelial antimicrobial response is cell-type specific and dependent on relevant microenvironmental stimuli. Immunology (2006) 118(4):509-19. doi:10.1111/j.1365-2567.2006.02399.x.
    • (2006) Immunology , vol.118 , Issue.4 , pp. 509-519
    • Schauber, J.1    Dorschner, R.A.2    Yamasaki, K.3    Brouha, B.4    Gallo, R.L.5
  • 26
    • 55549129604 scopus 로고    scopus 로고
    • Vitamin D3 induces pro-LL-37 expression in myeloid precursors from patients with severe congenital neutropenia
    • Karlsson J, Carlsson G, Larne O, Andersson M, Putsep K. Vitamin D3 induces pro-LL-37 expression in myeloid precursors from patients with severe congenital neutropenia. J Leukoc Biol (2008) 84(5):1279-86. doi:10.1189/jlb.0607437.
    • (2008) J Leukoc Biol , vol.84 , Issue.5 , pp. 1279-1286
    • Karlsson, J.1    Carlsson, G.2    Larne, O.3    Andersson, M.4    Putsep, K.5
  • 27
    • 34249780526 scopus 로고    scopus 로고
    • IFN-gamma- and TNF-independent vitamin D-inducible human suppression of mycobacteria: the role of cathelicidin LL-37
    • Martineau AR, Wilkinson KA, Newton SM, Floto RA, Norman AW, Skolimowska K, et al. IFN-gamma- and TNF-independent vitamin D-inducible human suppression of mycobacteria: the role of cathelicidin LL-37. J Immunol (2007) 178(11):7190-8. doi:10.4049/jimmunol.178.11.7190.
    • (2007) J Immunol , vol.178 , Issue.11 , pp. 7190-7198
    • Martineau, A.R.1    Wilkinson, K.A.2    Newton, S.M.3    Floto, R.A.4    Norman, A.W.5    Skolimowska, K.6
  • 28
    • 41049111043 scopus 로고    scopus 로고
    • Hypothesis - ultraviolet-B irradiance and vitamin D reduce the risk of viral infections and thus their sequelae, including autoimmune diseases and some cancers
    • Grant WB. Hypothesis - ultraviolet-B irradiance and vitamin D reduce the risk of viral infections and thus their sequelae, including autoimmune diseases and some cancers. Photochem Photobiol (2008) 84(2):356-65. doi:10.1111/j.1751-1097.2007.00266.x.
    • (2008) Photochem Photobiol , vol.84 , Issue.2 , pp. 356-365
    • Grant, W.B.1
  • 29
    • 84886744158 scopus 로고    scopus 로고
    • Differential regulation of human cathelicidin LL-37 by free fatty acids and their analogs
    • Jiang W, Sunkara LT, Zeng X, Deng Z, Myers SM, Zhang G. Differential regulation of human cathelicidin LL-37 by free fatty acids and their analogs. Peptides (2013) 50:129-38. doi:10.1016/j.peptides.2013.10.008.
    • (2013) Peptides , vol.50 , pp. 129-138
    • Jiang, W.1    Sunkara, L.T.2    Zeng, X.3    Deng, Z.4    Myers, S.M.5    Zhang, G.6
  • 30
    • 84883420258 scopus 로고    scopus 로고
    • Induction of porcine host defense peptide gene expression by short-chain fatty acids and their analogs
    • Zeng X, Sunkara LT, Jiang W, Bible M, Carter S, Ma X, et al. Induction of porcine host defense peptide gene expression by short-chain fatty acids and their analogs. PLoS One (2013) 8(8):e72922. doi:10.1371/journal.pone.0072922.
    • (2013) PLoS One , vol.8 , Issue.8
    • Zeng, X.1    Sunkara, L.T.2    Jiang, W.3    Bible, M.4    Carter, S.5    Ma, X.6
  • 31
    • 78651465611 scopus 로고    scopus 로고
    • Trace metal zinc stimulates secretion of antimicrobial peptide LL-37 from Caco-2 cells through ERK and p38 MAP kinase
    • Talukder P, Satho T, Irie K, Sharmin T, Hamady D, Nakashima Y, et al. Trace metal zinc stimulates secretion of antimicrobial peptide LL-37 from Caco-2 cells through ERK and p38 MAP kinase. Int Immunopharmacol (2011) 11(1):141-4. doi:10.1016/j.intimp.2010.10.010.
    • (2011) Int Immunopharmacol , vol.11 , Issue.1 , pp. 141-144
    • Talukder, P.1    Satho, T.2    Irie, K.3    Sharmin, T.4    Hamady, D.5    Nakashima, Y.6
  • 32
    • 3142592392 scopus 로고    scopus 로고
    • Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells
    • Schauber J, Iffland K, Frisch S, Kudlich T, Schmausser B, Eck M, et al. Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells. Mol Immunol (2004) 41(9):847-54. doi:10.1016/j.molimm.2004.05.005.
    • (2004) Mol Immunol , vol.41 , Issue.9 , pp. 847-854
    • Schauber, J.1    Iffland, K.2    Frisch, S.3    Kudlich, T.4    Schmausser, B.5    Eck, M.6
  • 33
    • 84934333177 scopus 로고    scopus 로고
    • Curcumin, inflammation, and chronic diseases: how are they linked?
    • He Y, Yue Y, Zheng X, Zhang K, Chen S, Du Z. Curcumin, inflammation, and chronic diseases: how are they linked? Molecules (2015) 20(5):9183-213. doi:10.3390/molecules20059183.
    • (2015) Molecules , vol.20 , Issue.5 , pp. 9183-9213
    • He, Y.1    Yue, Y.2    Zheng, X.3    Zhang, K.4    Chen, S.5    Du, Z.6
  • 34
    • 16844371915 scopus 로고    scopus 로고
    • Induction of apoptosis by curcumin and its implications for cancer therapy
    • Karunagaran D, Rashmi R, Kumar TR. Induction of apoptosis by curcumin and its implications for cancer therapy. Curr Cancer Drug Targets (2005) 5(2):117-29. doi:10.2174/1568009053202081.
    • (2005) Curr Cancer Drug Targets , vol.5 , Issue.2 , pp. 117-129
    • Karunagaran, D.1    Rashmi, R.2    Kumar, T.R.3
  • 35
    • 84876806459 scopus 로고    scopus 로고
    • Curcumin induces human cathelicidin antimicrobial peptide gene expression through a vitamin D receptor-independent pathway
    • Guo C, Rosoha E, Lowry MB, Borregaard N, Gombart AF. Curcumin induces human cathelicidin antimicrobial peptide gene expression through a vitamin D receptor-independent pathway. J Nutr Biochem (2013) 24(5):754-9. doi:10.1016/j.jnutbio.2012.04.002.
    • (2013) J Nutr Biochem , vol.24 , Issue.5 , pp. 754-759
    • Guo, C.1    Rosoha, E.2    Lowry, M.B.3    Borregaard, N.4    Gombart, A.F.5
  • 36
    • 77749314934 scopus 로고    scopus 로고
    • The effect of calcipotriol on the expression of human beta defensin-2 and LL-37 in cultured human keratinocytes
    • Kim BJ, Rho YK, Lee HI, Jeong MS, Li K, Seo SJ, et al. The effect of calcipotriol on the expression of human beta defensin-2 and LL-37 in cultured human keratinocytes. Clin Dev Immunol (2009) 2009:645898. doi:10.1155/2009/645898.
    • (2009) Clin Dev Immunol , vol.2009
    • Kim, B.J.1    Rho, Y.K.2    Lee, H.I.3    Jeong, M.S.4    Li, K.5    Seo, S.J.6
  • 37
    • 21744438757 scopus 로고    scopus 로고
    • Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3
    • Gombart AF, Borregaard N, Koeffler HP. Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up-regulated in myeloid cells by 1,25-dihydroxyvitamin D3. FASEB J (2005) 19(9):1067-77. doi:10.1096/fj.04-3284com.
    • (2005) FASEB J , vol.19 , Issue.9 , pp. 1067-1077
    • Gombart, A.F.1    Borregaard, N.2    Koeffler, H.P.3
  • 38
    • 74049133361 scopus 로고    scopus 로고
    • The global burden of cancer: priorities for prevention
    • Thun MJ, DeLancey JO, Center MM, Jemal A, Ward EM. The global burden of cancer: priorities for prevention. Carcinogenesis (2010) 31(1):100-10. doi:10.1093/carcin/bgp263.
    • (2010) Carcinogenesis , vol.31 , Issue.1 , pp. 100-110
    • Thun, M.J.1    DeLancey, J.O.2    Center, M.M.3    Jemal, A.4    Ward, E.M.5
  • 39
    • 84921763721 scopus 로고    scopus 로고
    • Drug radiotherapy combinations: review of previous failures and reasons for future optimism
    • Higgins GS, O'Cathail SM, Muschel RJ, McKenna WG. Drug radiotherapy combinations: review of previous failures and reasons for future optimism. Cancer Treat Rev (2015) 41(2):105-13. doi:10.1016/j.ctrv.2014.12.012.
    • (2015) Cancer Treat Rev , vol.41 , Issue.2 , pp. 105-113
    • Higgins, G.S.1    O'Cathail, S.M.2    Muschel, R.J.3    McKenna, W.G.4
  • 41
    • 84901986884 scopus 로고    scopus 로고
    • Targeting the PI3K/AKT/mTOR pathway in estrogen receptor-positive breast cancer
    • Ciruelos Gil EM. Targeting the PI3K/AKT/mTOR pathway in estrogen receptor-positive breast cancer. Cancer Treat Rev (2014) 40(7):862-71. doi:10.1016/j.ctrv.2014.03.004.
    • (2014) Cancer Treat Rev , vol.40 , Issue.7 , pp. 862-871
    • Ciruelos Gil, E.M.1
  • 43
    • 84929403724 scopus 로고    scopus 로고
    • Hepatotoxicity of molecular targeted therapy
    • Karczmarek-Borowska B, Salek-Zan A. Hepatotoxicity of molecular targeted therapy. Contemp Oncol (Pozn) (2015) 19(2):87-92. doi:10.5114/wo.2014.43495.
    • (2015) Contemp Oncol (Pozn) , vol.19 , Issue.2 , pp. 87-92
    • Karczmarek-Borowska, B.1    Salek-Zan, A.2
  • 44
    • 68049105076 scopus 로고    scopus 로고
    • Role of hypoxia in the hallmarks of human cancer
    • Ruan K, Song G, Ouyang G. Role of hypoxia in the hallmarks of human cancer. J Cell Biochem (2009) 107(6):1053-62. doi:10.1002/jcb.22214.
    • (2009) J Cell Biochem , vol.107 , Issue.6 , pp. 1053-1062
    • Ruan, K.1    Song, G.2    Ouyang, G.3
  • 45
    • 33646568511 scopus 로고    scopus 로고
    • Mechanisms and strategies to overcome multiple drug resistance in cancer
    • Ozben T. Mechanisms and strategies to overcome multiple drug resistance in cancer. FEBS Lett (2006) 580(12):2903-9. doi:10.1016/j.febslet.2006.02.020.
    • (2006) FEBS Lett , vol.580 , Issue.12 , pp. 2903-2909
    • Ozben, T.1
  • 46
    • 65649131520 scopus 로고    scopus 로고
    • Multidrug resistance through the spectacle of P-glycoprotein
    • Goda K, Bacso Z, Szabo G. Multidrug resistance through the spectacle of P-glycoprotein. Curr Cancer Drug Targets (2009) 9(3):281-97. doi:10.2174/156800909788166493.
    • (2009) Curr Cancer Drug Targets , vol.9 , Issue.3 , pp. 281-297
    • Goda, K.1    Bacso, Z.2    Szabo, G.3
  • 47
    • 73449126570 scopus 로고    scopus 로고
    • Mechanisms of chemotherapeutic drug resistance in cancer therapy - a quick review
    • Liu FS. Mechanisms of chemotherapeutic drug resistance in cancer therapy - a quick review. Taiwan J Obstet Gynecol (2009) 48(3):239-44. doi:10.1016/S1028-4559(09)60296-5.
    • (2009) Taiwan J Obstet Gynecol , vol.48 , Issue.3 , pp. 239-244
    • Liu, F.S.1
  • 48
    • 0037358040 scopus 로고    scopus 로고
    • Overcoming multidrug resistance in cancer: an update on the clinical strategy of inhibiting p-glycoprotein
    • Thomas H, Coley HM. Overcoming multidrug resistance in cancer: an update on the clinical strategy of inhibiting p-glycoprotein. Cancer Control (2003) 10(2):159-65.
    • (2003) Cancer Control , vol.10 , Issue.2 , pp. 159-165
    • Thomas, H.1    Coley, H.M.2
  • 49
    • 71549171732 scopus 로고    scopus 로고
    • Opportunities in discovery and delivery of anticancer drugs targeting mitochondria and cancer cell metabolism
    • Pathania D, Millard M, Neamati N. Opportunities in discovery and delivery of anticancer drugs targeting mitochondria and cancer cell metabolism. Adv Drug Deliv Rev (2009) 61(14):1250-75. doi:10.1016/j.addr.2009.05.010.
    • (2009) Adv Drug Deliv Rev , vol.61 , Issue.14 , pp. 1250-1275
    • Pathania, D.1    Millard, M.2    Neamati, N.3
  • 50
    • 77950654528 scopus 로고    scopus 로고
    • Tubulin-targeting agents in hybrid drugs
    • Breen EC, Walsh JJ. Tubulin-targeting agents in hybrid drugs. Curr Med Chem (2010) 17(7):609-39. doi:10.2174/092986710790416254.
    • (2010) Curr Med Chem , vol.17 , Issue.7 , pp. 609-639
    • Breen, E.C.1    Walsh, J.J.2
  • 51
    • 72549089385 scopus 로고    scopus 로고
    • Angiogenesis as a strategic target for prostate cancer therapy
    • Li Y, Cozzi PJ. Angiogenesis as a strategic target for prostate cancer therapy. Med Res Rev (2010) 30(1):23-66. doi:10.1002/med.20161.
    • (2010) Med Res Rev , vol.30 , Issue.1 , pp. 23-66
    • Li, Y.1    Cozzi, P.J.2
  • 52
    • 52949127312 scopus 로고    scopus 로고
    • An integrated genomic analysis of human glioblastoma multiforme
    • Parsons DW, Jones S, Zhang X, Lin JC, Leary RJ, Angenendt P, et al. An integrated genomic analysis of human glioblastoma multiforme. Science (2008) 321(5897):1807-12. doi:10.1126/science.1164382.
    • (2008) Science , vol.321 , Issue.5897 , pp. 1807-1812
    • Parsons, D.W.1    Jones, S.2    Zhang, X.3    Lin, J.C.4    Leary, R.J.5    Angenendt, P.6
  • 53
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: production, processing, and potential health benefits
    • Udenigwe CC, Aluko RE. Food protein-derived bioactive peptides: production, processing, and potential health benefits. J Food Sci (2012) 77(1):R11-24. doi:10.1111/j.1750-3841.2011.02455.x.
    • (2012) J Food Sci , vol.77 , Issue.1 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 54
  • 56
    • 71749100398 scopus 로고    scopus 로고
    • Cationic amphiphilic peptides with cancer-selective toxicity
    • Schweizer F. Cationic amphiphilic peptides with cancer-selective toxicity. Eur J Pharmacol (2009) 625(1-3):190-4. doi:10.1016/j.ejphar.2009.08.043.
    • (2009) Eur J Pharmacol , vol.625 , Issue.1-3 , pp. 190-194
    • Schweizer, F.1
  • 57
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa GS, Aarbiou J, Ninaber DK, Drijfhout JW, Sorensen OE, Borregaard N, et al. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J Immunol (2003) 171(12):6690-6. doi:10.4049/jimmunol.171.12.6690.
    • (2003) J Immunol , vol.171 , Issue.12 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3    Drijfhout, J.W.4    Sorensen, O.E.5    Borregaard, N.6
  • 58
    • 25444468300 scopus 로고    scopus 로고
    • Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37
    • Tokumaru S, Sayama K, Shirakata Y, Komatsuzawa H, Ouhara K, Hanakawa Y, et al. Induction of keratinocyte migration via transactivation of the epidermal growth factor receptor by the antimicrobial peptide LL-37. J Immunol (2005) 175(7):4662-8. doi:10.4049/jimmunol.175.7.4662.
    • (2005) J Immunol , vol.175 , Issue.7 , pp. 4662-4668
    • Tokumaru, S.1    Sayama, K.2    Shirakata, Y.3    Komatsuzawa, H.4    Ouhara, K.5    Hanakawa, Y.6
  • 59
    • 33646586648 scopus 로고    scopus 로고
    • Human cathelicidin LL-37 is a chemoattractant for eosinophils and neutrophils that acts via formyl-peptide receptors
    • Tjabringa GS, Ninaber DK, Drijfhout JW, Rabe KF, Hiemstra PS. Human cathelicidin LL-37 is a chemoattractant for eosinophils and neutrophils that acts via formyl-peptide receptors. Int Arch Allergy Immunol (2006) 140(2):103-12. doi:10.1159/000092305.
    • (2006) Int Arch Allergy Immunol , vol.140 , Issue.2 , pp. 103-112
    • Tjabringa, G.S.1    Ninaber, D.K.2    Drijfhout, J.W.3    Rabe, K.F.4    Hiemstra, P.S.5
  • 60
    • 27144468929 scopus 로고    scopus 로고
    • Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure
    • Shaykhiev R, Beisswenger C, Kandler K, Senske J, Puchner A, Damm T, et al. Human endogenous antibiotic LL-37 stimulates airway epithelial cell proliferation and wound closure. Am J Physiol Lung Cell Mol Physiol (2005) 289(5):L842-8. doi:10.1152/ajplung.00286.2004.
    • (2005) Am J Physiol Lung Cell Mol Physiol , vol.289 , Issue.5 , pp. L842-L848
    • Shaykhiev, R.1    Beisswenger, C.2    Kandler, K.3    Senske, J.4    Puchner, A.5    Damm, T.6
  • 61
    • 14844311295 scopus 로고    scopus 로고
    • Antimicrobial protein hCAP18/LL-37 is highly expressed in breast cancer and is a putative growth factor for epithelial cells
    • Heilborn JD, Nilsson MF, Jimenez CI, Sandstedt B, Borregaard N, Tham E, et al. Antimicrobial protein hCAP18/LL-37 is highly expressed in breast cancer and is a putative growth factor for epithelial cells. Int J Cancer (2005) 114(5):713-9. doi:10.1002/ijc.20795.
    • (2005) Int J Cancer , vol.114 , Issue.5 , pp. 713-719
    • Heilborn, J.D.1    Nilsson, M.F.2    Jimenez, C.I.3    Sandstedt, B.4    Borregaard, N.5    Tham, E.6
  • 62
    • 0038142308 scopus 로고    scopus 로고
    • An angiogenic role for the human peptide antibiotic LL-37/hCAP-18
    • Koczulla R, von Degenfeld G, Kupatt C, Krotz F, Zahler S, Gloe T, et al. An angiogenic role for the human peptide antibiotic LL-37/hCAP-18. J Clin Invest (2003) 111(11):1665-72. doi:10.1172/JCI17545.
    • (2003) J Clin Invest , vol.111 , Issue.11 , pp. 1665-1672
    • Koczulla, R.1    von Degenfeld, G.2    Kupatt, C.3    Krotz, F.4    Zahler, S.5    Gloe, T.6
  • 63
    • 67549084970 scopus 로고    scopus 로고
    • Human antimicrobial protein hCAP18/LL-37 promotes a metastatic phenotype in breast cancer
    • Weber G, Chamorro CI, Granath F, Liljegren A, Zreika S, Saidak Z, et al. Human antimicrobial protein hCAP18/LL-37 promotes a metastatic phenotype in breast cancer. Breast Cancer Res (2009) 11(1):R6. doi:10.1186/bcr2221.
    • (2009) Breast Cancer Res , vol.11 , Issue.1
    • Weber, G.1    Chamorro, C.I.2    Granath, F.3    Liljegren, A.4    Zreika, S.5    Saidak, Z.6
  • 64
    • 37549027589 scopus 로고    scopus 로고
    • The host defence peptide LL-37/hCAP-18 is a growth factor for lung cancer cells
    • von Haussen J, Koczulla R, Shaykhiev R, Herr C, Pinkenburg O, Reimer D, et al. The host defence peptide LL-37/hCAP-18 is a growth factor for lung cancer cells. Lung Cancer (2008) 59(1):12-23. doi:10.1016/j.lungcan.2007.07.014.
    • (2008) Lung Cancer , vol.59 , Issue.1 , pp. 12-23
    • von Haussen, J.1    Koczulla, R.2    Shaykhiev, R.3    Herr, C.4    Pinkenburg, O.5    Reimer, D.6
  • 65
    • 1842581655 scopus 로고    scopus 로고
    • A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release
    • Elssner A, Duncan M, Gavrilin M, Wewers MD. A novel P2X7 receptor activator, the human cathelicidin-derived peptide LL37, induces IL-1 beta processing and release. J Immunol (2004) 172(8):4987-94. doi:10.4049/jimmunol.172.8.4987.
    • (2004) J Immunol , vol.172 , Issue.8 , pp. 4987-4994
    • Elssner, A.1    Duncan, M.2    Gavrilin, M.3    Wewers, M.D.4
  • 66
    • 70149090684 scopus 로고    scopus 로고
    • Intracellular receptor for human host defense peptide LL-37 in monocytes
    • Mookherjee N, Lippert DN, Hamill P, Falsafi R, Nijnik A, Kindrachuk J, et al. Intracellular receptor for human host defense peptide LL-37 in monocytes. J Immunol (2009) 183(4):2688-96. doi:10.4049/jimmunol.0802586.
    • (2009) J Immunol , vol.183 , Issue.4 , pp. 2688-2696
    • Mookherjee, N.1    Lippert, D.N.2    Hamill, P.3    Falsafi, R.4    Nijnik, A.5    Kindrachuk, J.6
  • 67
    • 84875933870 scopus 로고    scopus 로고
    • Rapid cytotoxicity of antimicrobial peptide tempoprin-1CEa in breast cancer cells through membrane destruction and intracellular calcium mechanism
    • Wang C, Tian LL, Li S, Li HB, Zhou Y, Wang H, et al. Rapid cytotoxicity of antimicrobial peptide tempoprin-1CEa in breast cancer cells through membrane destruction and intracellular calcium mechanism. PLoS One (2013) 8(4):e60462. doi:10.1371/journal.pone.0060462.
    • (2013) PLoS One , vol.8 , Issue.4
    • Wang, C.1    Tian, L.L.2    Li, S.3    Li, H.B.4    Zhou, Y.5    Wang, H.6
  • 68
    • 80054828685 scopus 로고    scopus 로고
    • Pleurocidin-family cationic antimicrobial peptides are cytolytic for breast carcinoma cells and prevent growth of tumor xenografts
    • Hilchie AL, Doucette CD, Pinto DM, Patrzykat A, Douglas S, Hoskin DW. Pleurocidin-family cationic antimicrobial peptides are cytolytic for breast carcinoma cells and prevent growth of tumor xenografts. Breast Cancer Res (2011) 13(5):R102. doi:10.1186/bcr3043.
    • (2011) Breast Cancer Res , vol.13 , Issue.5
    • Hilchie, A.L.1    Doucette, C.D.2    Pinto, D.M.3    Patrzykat, A.4    Douglas, S.5    Hoskin, D.W.6
  • 69
    • 73049106277 scopus 로고    scopus 로고
    • Isolation, characterization and anti-cancer activity of SK84, a novel glycine-rich antimicrobial peptide from Drosophila virilis
    • Lu J, Chen ZW. Isolation, characterization and anti-cancer activity of SK84, a novel glycine-rich antimicrobial peptide from Drosophila virilis. Peptides (2010) 31(1):44-50. doi:10.1016/j.peptides.2009.09.028.
    • (2010) Peptides , vol.31 , Issue.1 , pp. 44-50
    • Lu, J.1    Chen, Z.W.2
  • 70
    • 27144462218 scopus 로고    scopus 로고
    • Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation
    • Xiao W, Hsu YP, Ishizaka A, Kirikae T, Moss RB. Sputum cathelicidin, urokinase plasminogen activation system components, and cytokines discriminate cystic fibrosis, COPD, and asthma inflammation. Chest (2005) 128(4):2316-26. doi:10.1378/chest.128.4.2316.
    • (2005) Chest , vol.128 , Issue.4 , pp. 2316-2326
    • Xiao, W.1    Hsu, Y.P.2    Ishizaka, A.3    Kirikae, T.4    Moss, R.B.5
  • 71
    • 0030942221 scopus 로고    scopus 로고
    • Purification and characterization of defensins from cystic fibrosis sputum
    • Soong LB, Ganz T, Ellison A, Caughey GH. Purification and characterization of defensins from cystic fibrosis sputum. Inflamm Res (1997) 46(3):98-102. doi:10.1007/s000110050114.
    • (1997) Inflamm Res , vol.46 , Issue.3 , pp. 98-102
    • Soong, L.B.1    Ganz, T.2    Ellison, A.3    Caughey, G.H.4
  • 72
    • 0036528903 scopus 로고    scopus 로고
    • Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection
    • Schaller-Bals S, Schulze A, Bals R. Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am J Respir Crit Care Med (2002) 165(7):992-5. doi:10.1164/ajrccm.165.7.200110-020.
    • (2002) Am J Respir Crit Care Med , vol.165 , Issue.7 , pp. 992-995
    • Schaller-Bals, S.1    Schulze, A.2    Bals, R.3
  • 73
    • 0000450744 scopus 로고    scopus 로고
    • Antibacterial components in bronchoalveolar lavage fluid from healthy individuals and sarcoidosis patients
    • Agerberth B, Grunewald J, Castanos-Velez E, Olsson B, Jornvall H, Wigzell H, et al. Antibacterial components in bronchoalveolar lavage fluid from healthy individuals and sarcoidosis patients. Am J Respir Crit Care Med (1999) 160(1):283-90. doi:10.1164/ajrccm.160.1.9807041.
    • (1999) Am J Respir Crit Care Med , vol.160 , Issue.1 , pp. 283-290
    • Agerberth, B.1    Grunewald, J.2    Castanos-Velez, E.3    Olsson, B.4    Jornvall, H.5    Wigzell, H.6
  • 74
    • 69249086981 scopus 로고    scopus 로고
    • COPD prevalence is increased in lung cancer, independent of age, sex and smoking history
    • Young RP, Hopkins RJ, Christmas T, Black PN, Metcalf P, Gamble GD. COPD prevalence is increased in lung cancer, independent of age, sex and smoking history. Eur Respir J (2009) 34(2):380-6. doi:10.1183/09031936.00144208.
    • (2009) Eur Respir J , vol.34 , Issue.2 , pp. 380-386
    • Young, R.P.1    Hopkins, R.J.2    Christmas, T.3    Black, P.N.4    Metcalf, P.5    Gamble, G.D.6
  • 75
    • 4043174733 scopus 로고    scopus 로고
    • COPD increases the risk of squamous histological subtype in smokers who develop non-small cell lung carcinoma
    • Papi A, Casoni G, Caramori G, Guzzinati I, Boschetto P, Ravenna F, et al. COPD increases the risk of squamous histological subtype in smokers who develop non-small cell lung carcinoma. Thorax (2004) 59(8):679-81. doi:10.1136/thx.2003.018291.
    • (2004) Thorax , vol.59 , Issue.8 , pp. 679-681
    • Papi, A.1    Casoni, G.2    Caramori, G.3    Guzzinati, I.4    Boschetto, P.5    Ravenna, F.6
  • 76
    • 84901506299 scopus 로고    scopus 로고
    • Expression of the antimicrobial peptide cathelicidin in myeloid cells is required for lung tumor growth
    • Li D, Beisswenger C, Herr C, Schmid RM, Gallo RL, Han G, et al. Expression of the antimicrobial peptide cathelicidin in myeloid cells is required for lung tumor growth. Oncogene (2014) 33(21):2709-16. doi:10.1038/onc.2013.248.
    • (2014) Oncogene , vol.33 , Issue.21 , pp. 2709-2716
    • Li, D.1    Beisswenger, C.2    Herr, C.3    Schmid, R.M.4    Gallo, R.L.5    Han, G.6
  • 77
    • 79952396539 scopus 로고    scopus 로고
    • LL-37 as a therapeutic target for late stage prostate cancer
    • Hensel JA, Chanda D, Kumar S, Sawant A, Grizzle WE, Siegal GP, et al. LL-37 as a therapeutic target for late stage prostate cancer. Prostate (2011) 71(6):659-70. doi:10.1002/pros.21282.
    • (2011) Prostate , vol.71 , Issue.6 , pp. 659-670
    • Hensel, J.A.1    Chanda, D.2    Kumar, S.3    Sawant, A.4    Grizzle, W.E.5    Siegal, G.P.6
  • 78
    • 38749148077 scopus 로고    scopus 로고
    • Ovarian cancers overexpress the antimicrobial protein hCAP-18 and its derivative LL-37 increases ovarian cancer cell proliferation and invasion
    • Coffelt SB, Waterman RS, Florez L, Honer zu Bentrup K, Zwezdaryk KJ, Tomchuck SL, et al. Ovarian cancers overexpress the antimicrobial protein hCAP-18 and its derivative LL-37 increases ovarian cancer cell proliferation and invasion. Int J Cancer (2008) 122(5):1030-9. doi:10.1002/ijc.23186.
    • (2008) Int J Cancer , vol.122 , Issue.5 , pp. 1030-1039
    • Coffelt, S.B.1    Waterman, R.S.2    Florez, L.3    Honer zu Bentrup, K.4    Zwezdaryk, K.J.5    Tomchuck, S.L.6
  • 79
    • 67649610425 scopus 로고    scopus 로고
    • Leucine leucine-37 uses formyl peptide receptor-like 1 to activate signal transduction pathways, stimulate oncogenic gene expression, and enhance the invasiveness of ovarian cancer cells
    • Coffelt SB, Tomchuck SL, Zwezdaryk KJ, Danka ES, Scandurro AB. Leucine leucine-37 uses formyl peptide receptor-like 1 to activate signal transduction pathways, stimulate oncogenic gene expression, and enhance the invasiveness of ovarian cancer cells. Mol Cancer Res (2009) 7(6):907-15. doi:10.1158/1541-7786.MCR-08-0326.
    • (2009) Mol Cancer Res , vol.7 , Issue.6 , pp. 907-915
    • Coffelt, S.B.1    Tomchuck, S.L.2    Zwezdaryk, K.J.3    Danka, E.S.4    Scandurro, A.B.5
  • 80
    • 34948862264 scopus 로고    scopus 로고
    • Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide
    • Lande R, Gregorio J, Facchinetti V, Chatterjee B, Wang YH, Homey B, et al. Plasmacytoid dendritic cells sense self-DNA coupled with antimicrobial peptide. Nature (2007) 449(7162):564-9. doi:10.1038/nature06116.
    • (2007) Nature , vol.449 , Issue.7162 , pp. 564-569
    • Lande, R.1    Gregorio, J.2    Facchinetti, V.3    Chatterjee, B.4    Wang, Y.H.5    Homey, B.6
  • 81
    • 84876509176 scopus 로고    scopus 로고
    • P2X7 receptor function in bone-related cancer
    • Adinolfi E, Amoroso F, Giuliani AL. P2X7 receptor function in bone-related cancer. J Osteoporos (2012) 2012:637863. doi:10.1155/2012/637863.
    • (2012) J Osteoporos , vol.2012
    • Adinolfi, E.1    Amoroso, F.2    Giuliani, A.L.3
  • 83
    • 84943658021 scopus 로고    scopus 로고
    • The P2X7 receptor is a key modulator of the PI3K/GSK3beta/VEGF signaling network: evidence in experimental neuroblastoma
    • Amoroso F, Capece M, Rotondo A, Cangelosi D, Ferracin M, Franceschini A, et al. The P2X7 receptor is a key modulator of the PI3K/GSK3beta/VEGF signaling network: evidence in experimental neuroblastoma. Oncogene (2015). doi:10.1038/onc.2014.444.
    • (2015) Oncogene
    • Amoroso, F.1    Capece, M.2    Rotondo, A.3    Cangelosi, D.4    Ferracin, M.5    Franceschini, A.6
  • 84
    • 0041736471 scopus 로고    scopus 로고
    • Sensitivity of genera Porphyromonas and Prevotella to the bactericidal action of C-terminal domain of human CAP18 and its analogues
    • Isogai E, Isogai H, Matuo K, Hirose K, Kowashi Y, Okumuara K, et al. Sensitivity of genera Porphyromonas and Prevotella to the bactericidal action of C-terminal domain of human CAP18 and its analogues. Oral Microbiol Immunol (2003) 18(5):329-32. doi:10.1034/j.1399-302X.2003.00083.x.
    • (2003) Oral Microbiol Immunol , vol.18 , Issue.5 , pp. 329-332
    • Isogai, E.1    Isogai, H.2    Matuo, K.3    Hirose, K.4    Kowashi, Y.5    Okumuara, K.6
  • 85
    • 84877887193 scopus 로고    scopus 로고
    • FK-16 derived from the anticancer peptide LL-37 induces caspase-independent apoptosis and autophagic cell death in colon cancer cells
    • Ren SX, Shen J, Cheng AS, Lu L, Chan RL, Li ZJ, et al. FK-16 derived from the anticancer peptide LL-37 induces caspase-independent apoptosis and autophagic cell death in colon cancer cells. PLoS One (2013) 8(5):e63641. doi:10.1371/journal.pone.0063641.
    • (2013) PLoS One , vol.8 , Issue.5
    • Ren, S.X.1    Shen, J.2    Cheng, A.S.3    Lu, L.4    Chan, R.L.5    Li, Z.J.6
  • 86
    • 84923087132 scopus 로고    scopus 로고
    • Antimicrobial peptide FF/CAP18 induces apoptotic cell death in HCT116 colon cancer cells via changes in the metabolic profile
    • Kuroda K, Fukuda T, Isogai H, Okumura K, Krstic-Demonacos M, Isogai E. Antimicrobial peptide FF/CAP18 induces apoptotic cell death in HCT116 colon cancer cells via changes in the metabolic profile. Int J Oncol (2015) 46(4):1516-26. doi:10.3892/ijo.2015.2887.
    • (2015) Int J Oncol , vol.46 , Issue.4 , pp. 1516-1526
    • Kuroda, K.1    Fukuda, T.2    Isogai, H.3    Okumura, K.4    Krstic-Demonacos, M.5    Isogai, E.6
  • 87
    • 10744224946 scopus 로고    scopus 로고
    • Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori
    • Hase K, Murakami M, Iimura M, Cole SP, Horibe Y, Ohtake T, et al. Expression of LL-37 by human gastric epithelial cells as a potential host defense mechanism against Helicobacter pylori. Gastroenterology (2003) 125(6):1613-25. doi:10.1053/j.gastro.2003.08.028.
    • (2003) Gastroenterology , vol.125 , Issue.6 , pp. 1613-1625
    • Hase, K.1    Murakami, M.2    Iimura, M.3    Cole, S.P.4    Horibe, Y.5    Ohtake, T.6
  • 88
    • 0038353372 scopus 로고    scopus 로고
    • Expression of LL-37/hCAP-18 gene in human leukemia cells
    • Yang YH, Zheng GG, Li G, Zhang B, Song YH, Wu KF. Expression of LL-37/hCAP-18 gene in human leukemia cells. Leuk Res (2003) 27(10):947-50. doi:10.1016/S0145-2126(03)00020-1.
    • (2003) Leuk Res , vol.27 , Issue.10 , pp. 947-950
    • Yang, Y.H.1    Zheng, G.G.2    Li, G.3    Zhang, B.4    Song, Y.H.5    Wu, K.F.6
  • 89
    • 84871188238 scopus 로고    scopus 로고
    • Host immune defense peptide LL-37 activates caspase-independent apoptosis and suppresses colon cancer
    • Ren SX, Cheng AS, To KF, Tong JH, Li MS, Shen J, et al. Host immune defense peptide LL-37 activates caspase-independent apoptosis and suppresses colon cancer. Cancer Res (2012) 72(24):6512-23. doi:10.1158/0008-5472.CAN-12-2359.
    • (2012) Cancer Res , vol.72 , Issue.24 , pp. 6512-6523
    • Ren, S.X.1    Cheng, A.S.2    To, K.F.3    Tong, J.H.4    Li, M.S.5    Shen, J.6
  • 90
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity
    • Oren Z, Lerman JC, Gudmundsson GH, Agerberth B, Shai Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem J (1999) 341(Pt 3):501-13. doi:10.1042/0264-6021:3410501.
    • (1999) Biochem J , vol.341 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 91
    • 33845373254 scopus 로고    scopus 로고
    • Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes
    • Dennison SR, Whittaker M, Harris F, Phoenix DA. Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumour cell membranes. Curr Protein Pept Sci (2006) 7(6):487-99. doi:10.2174/138920306779025611.
    • (2006) Curr Protein Pept Sci , vol.7 , Issue.6 , pp. 487-499
    • Dennison, S.R.1    Whittaker, M.2    Harris, F.3    Phoenix, D.A.4
  • 92
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem (2005) 280(13):12316-29. doi:10.1074/jbc.M413406200.
    • (2005) J Biol Chem , vol.280 , Issue.13 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 93
    • 79955748813 scopus 로고    scopus 로고
    • Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework
    • Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Mol Cancer Ther (2011) 10(3):416-26. doi:10.1158/1535-7163.MCT-10-0811.
    • (2011) Mol Cancer Ther , vol.10 , Issue.3 , pp. 416-426
    • Huang, Y.B.1    Wang, X.F.2    Wang, H.Y.3    Liu, Y.4    Chen, Y.5
  • 94
    • 80054987739 scopus 로고    scopus 로고
    • Revisiting peptide amphiphilicity for membrane pore formation
    • Lorin A, Noel M, Provencher ME, Turcotte V, Masson C, Cardinal S, et al. Revisiting peptide amphiphilicity for membrane pore formation. Biochemistry (2011) 50(43):9409-20. doi:10.1021/bi201335t.
    • (2011) Biochemistry , vol.50 , Issue.43 , pp. 9409-9420
    • Lorin, A.1    Noel, M.2    Provencher, M.E.3    Turcotte, V.4    Masson, C.5    Cardinal, S.6
  • 95
    • 82255189885 scopus 로고    scopus 로고
    • Oncolytic activities of host defense peptides
    • Al-Benna S, Shai Y, Jacobsen F, Steinstraesser L. Oncolytic activities of host defense peptides. Int J Mol Sci (2011) 12(11):8027-51. doi:10.3390/ijms12118027.
    • (2011) Int J Mol Sci , vol.12 , Issue.11 , pp. 8027-8051
    • Al-Benna, S.1    Shai, Y.2    Jacobsen, F.3    Steinstraesser, L.4
  • 96
    • 80053440806 scopus 로고    scopus 로고
    • Membrane-active host defense peptides - challenges and perspectives for the development of novel anticancer drugs
    • Riedl S, Zweytick D, Lohner K. Membrane-active host defense peptides - challenges and perspectives for the development of novel anticancer drugs. Chem Phys Lipids (2011) 164(8):766-81. doi:10.1016/j.chemphyslip.2011.09.004.
    • (2011) Chem Phys Lipids , vol.164 , Issue.8 , pp. 766-781
    • Riedl, S.1    Zweytick, D.2    Lohner, K.3
  • 97
    • 0344838675 scopus 로고    scopus 로고
    • Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure
    • Yang ST, Shin SY, Lee CW, Kim YC, Hahm KS, Kim JI. Selective cytotoxicity following Arg-to-Lys substitution in tritrpticin adopting a unique amphipathic turn structure. FEBS Lett (2003) 540(1-3):229-33. doi:10.1016/S0014-5793(03)00266-7.
    • (2003) FEBS Lett , vol.540 , Issue.1-3 , pp. 229-233
    • Yang, S.T.1    Shin, S.Y.2    Lee, C.W.3    Kim, Y.C.4    Hahm, K.S.5    Kim, J.I.6
  • 98
    • 73449124394 scopus 로고    scopus 로고
    • A theoretical analysis of secondary structural characteristics of anticancer peptides
    • Dennison SR, Harris F, Bhatt T, Singh J, Phoenix DA. A theoretical analysis of secondary structural characteristics of anticancer peptides. Mol Cell Biochem (2010) 333(1-2):129-35. doi:10.1007/s11010-009-0213-3.
    • (2010) Mol Cell Biochem , vol.333 , Issue.1-2 , pp. 129-135
    • Dennison, S.R.1    Harris, F.2    Bhatt, T.3    Singh, J.4    Phoenix, D.A.5
  • 99
    • 84871050291 scopus 로고    scopus 로고
    • On the selectivity and efficacy of defense peptides with respect to cancer cells
    • Harris F, Dennison SR, Singh J, Phoenix DA. On the selectivity and efficacy of defense peptides with respect to cancer cells. Med Res Rev (2013) 33(1):190-234. doi:10.1002/med.20252.
    • (2013) Med Res Rev , vol.33 , Issue.1 , pp. 190-234
    • Harris, F.1    Dennison, S.R.2    Singh, J.3    Phoenix, D.A.4
  • 100
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K, Ikonen E. How cells handle cholesterol. Science (2000) 290(5497):1721-6. doi:10.1126/science.290.5497.1721.
    • (2000) Science , vol.290 , Issue.5497 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 101
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • Matsuzaki K, Sugishita K, Fujii N, Miyajima K. Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. Biochemistry (1995) 34(10):3423-9. doi:10.1021/bi00010a034.
    • (1995) Biochemistry , vol.34 , Issue.10 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 103
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects
    • Steiner H, Andreu D, Merrifield RB. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim Biophys Acta (1988) 939(2):260-6. doi:10.1016/0005-2736(88)90069-7.
    • (1988) Biochim Biophys Acta , vol.939 , Issue.2 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 104
    • 33645457007 scopus 로고    scopus 로고
    • Elevated levels of cholesterol-rich lipid rafts in cancer cells are correlated with apoptosis sensitivity induced by cholesterol-depleting agents
    • Li YC, Park MJ, Ye SK, Kim CW, Kim YN. Elevated levels of cholesterol-rich lipid rafts in cancer cells are correlated with apoptosis sensitivity induced by cholesterol-depleting agents. Am J Pathol (2006) 168(4):1107-18. doi:10.2353/ajpath.2006.050959.
    • (2006) Am J Pathol , vol.168 , Issue.4 , pp. 1107-1118
    • Li, Y.C.1    Park, M.J.2    Ye, S.K.3    Kim, C.W.4    Kim, Y.N.5
  • 105
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • Varki A. Sialic acids in human health and disease. Trends Mol Med (2008) 14(8):351-60. doi:10.1016/j.molmed.2008.06.002.
    • (2008) Trends Mol Med , vol.14 , Issue.8 , pp. 351-360
    • Varki, A.1
  • 106
    • 0037945204 scopus 로고    scopus 로고
    • Gangliosides as therapeutic targets for cancer
    • Fredman P, Hedberg K, Brezicka T. Gangliosides as therapeutic targets for cancer. BioDrugs (2003) 17(3):155-67. doi:10.2165/00063030-200317030-00002.
    • (2003) BioDrugs , vol.17 , Issue.3 , pp. 155-167
    • Fredman, P.1    Hedberg, K.2    Brezicka, T.3
  • 107
    • 49749127215 scopus 로고    scopus 로고
    • Glycosylation in bladder cancer
    • Ohyama C. Glycosylation in bladder cancer. Int J Clin Oncol (2008) 13(4):308-13. doi:10.1007/s10147-008-0809-8.
    • (2008) Int J Clin Oncol , vol.13 , Issue.4 , pp. 308-313
    • Ohyama, C.1
  • 108
    • 72449147268 scopus 로고    scopus 로고
    • Proteoglycans: from structural compounds to signaling molecules
    • Schaefer L, Schaefer RM. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res (2010) 339(1):237-46. doi:10.1007/s00441-009-0821-y.
    • (2010) Cell Tissue Res , vol.339 , Issue.1 , pp. 237-246
    • Schaefer, L.1    Schaefer, R.M.2
  • 109
    • 79957605232 scopus 로고    scopus 로고
    • Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
    • Iozzo RV, Sanderson RD. Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med (2011) 15(5):1013-31. doi:10.1111/j.1582-4934.2010.01236.x.
    • (2011) J Cell Mol Med , vol.15 , Issue.5 , pp. 1013-1031
    • Iozzo, R.V.1    Sanderson, R.D.2
  • 110
    • 45949083498 scopus 로고    scopus 로고
    • The biological role of chondroitin sulfate in cancer and chondroitin-based anticancer agents
    • Asimakopoulou AP, Theocharis AD, Tzanakakis GN, Karamanos NK. The biological role of chondroitin sulfate in cancer and chondroitin-based anticancer agents. In vivo (2008) 22(3):385-9.
    • (2008) In vivo , vol.22 , Issue.3 , pp. 385-389
    • Asimakopoulou, A.P.1    Theocharis, A.D.2    Tzanakakis, G.N.3    Karamanos, N.K.4
  • 111
    • 58049215512 scopus 로고    scopus 로고
    • Targeting heparan sulfate proteoglycans in breast cancer treatment
    • Koo CY, Sen YP, Bay BH, Yip GW. Targeting heparan sulfate proteoglycans in breast cancer treatment. Recent Pat Anticancer Drug Discov (2008) 3(3):151-8. doi:10.2174/157489208786242278.
    • (2008) Recent Pat Anticancer Drug Discov , vol.3 , Issue.3 , pp. 151-158
    • Koo, C.Y.1    Sen, Y.P.2    Bay, B.H.3    Yip, G.W.4
  • 112
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • Zwaal RF, Comfurius P, Bevers EM. Surface exposure of phosphatidylserine in pathological cells. Cell Mol Life Sci (2005) 62(9):971-88. doi:10.1007/s00018-005-4527-3.
    • (2005) Cell Mol Life Sci , vol.62 , Issue.9 , pp. 971-988
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 113
    • 26844567701 scopus 로고    scopus 로고
    • Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli
    • Chen X, Niyonsaba F, Ushio H, Okuda D, Nagaoka I, Ikeda S, et al. Synergistic effect of antibacterial agents human beta-defensins, cathelicidin LL-37 and lysozyme against Staphylococcus aureus and Escherichia coli. J Dermatol Sci (2005) 40(2):123-32. doi:10.1016/j.jdermsci.2005.03.014.
    • (2005) J Dermatol Sci , vol.40 , Issue.2 , pp. 123-132
    • Chen, X.1    Niyonsaba, F.2    Ushio, H.3    Okuda, D.4    Nagaoka, I.5    Ikeda, S.6
  • 114
    • 0033995146 scopus 로고    scopus 로고
    • Synergistic actions of antibacterial neutrophil defensins and cathelicidins
    • Nagaoka I, Hirota S, Yomogida S, Ohwada A, Hirata M. Synergistic actions of antibacterial neutrophil defensins and cathelicidins. Inflamm Res (2000) 49(2):73-9. doi:10.1007/s000110050561.
    • (2000) Inflamm Res , vol.49 , Issue.2 , pp. 73-79
    • Nagaoka, I.1    Hirota, S.2    Yomogida, S.3    Ohwada, A.4    Hirata, M.5
  • 115
    • 0037973517 scopus 로고    scopus 로고
    • Staphylococcus aureus susceptibility to innate antimicrobial peptides, beta-defensins and CAP18, expressed by human keratinocytes
    • Midorikawa K, Ouhara K, Komatsuzawa H, Kawai T, Yamada S, Fujiwara T, et al. Staphylococcus aureus susceptibility to innate antimicrobial peptides, beta-defensins and CAP18, expressed by human keratinocytes. Infect Immun (2003) 71(7):3730-9. doi:10.1128/IAI.71.7.3730-3739.2003.
    • (2003) Infect Immun , vol.71 , Issue.7 , pp. 3730-3739
    • Midorikawa, K.1    Ouhara, K.2    Komatsuzawa, H.3    Kawai, T.4    Yamada, S.5    Fujiwara, T.6
  • 116
    • 10744230290 scopus 로고    scopus 로고
    • Activity of human beta-defensin 3 alone or combined with other antimicrobial agents against oral bacteria
    • Maisetta G, Batoni G, Esin S, Luperini F, Pardini M, Bottai D, et al. Activity of human beta-defensin 3 alone or combined with other antimicrobial agents against oral bacteria. Antimicrob Agents Chemother (2003) 47(10):3349-51. doi:10.1128/AAC.47.10.3349-3351.2003.
    • (2003) Antimicrob Agents Chemother , vol.47 , Issue.10 , pp. 3349-3351
    • Maisetta, G.1    Batoni, G.2    Esin, S.3    Luperini, F.4    Pardini, M.5    Bottai, D.6
  • 117
    • 79954520410 scopus 로고    scopus 로고
    • Recent advances in ophthalmic drug delivery
    • Kompella UB, Kadam RS, Lee VH. Recent advances in ophthalmic drug delivery. Ther Deliv (2010) 1(3):435-56. doi:10.4155/tde.10.40.
    • (2010) Ther Deliv , vol.1 , Issue.3 , pp. 435-456
    • Kompella, U.B.1    Kadam, R.S.2    Lee, V.H.3
  • 118
    • 84934284446 scopus 로고    scopus 로고
    • Enhanced antitumor efficacy of 5-fluorouracil loaded methoxy poly(ethylene glycol)-poly(lactide) nanoparticles for efficient therapy against breast cancer
    • Yuan Z, Qu X, Wang Y, Zhang DY, Luo JC, Jia N, et al. Enhanced antitumor efficacy of 5-fluorouracil loaded methoxy poly(ethylene glycol)-poly(lactide) nanoparticles for efficient therapy against breast cancer. Colloids Surf B Biointerfaces (2015) 128:489-97. doi:10.1016/j.colsurfb.2015.02.048.
    • (2015) Colloids Surf B Biointerfaces , vol.128 , pp. 489-497
    • Yuan, Z.1    Qu, X.2    Wang, Y.3    Zhang, D.Y.4    Luo, J.C.5    Jia, N.6
  • 119
    • 84925018113 scopus 로고    scopus 로고
    • A magnetic anti-cancer compound for magnet-guided delivery and magnetic resonance imaging
    • Eguchi H, Umemura M, Kurotani R, Fukumura H, Sato I, Kim JH, et al. A magnetic anti-cancer compound for magnet-guided delivery and magnetic resonance imaging. Sci Rep (2015) 5:9194. doi:10.1038/srep09194.
    • (2015) Sci Rep , vol.5 , pp. 9194
    • Eguchi, H.1    Umemura, M.2    Kurotani, R.3    Fukumura, H.4    Sato, I.5    Kim, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.