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Volumn 71, Issue 6, 2011, Pages 659-670

LL-37 as a therapeutic target for late stage prostate cancer

Author keywords

androgen independent; angiogenesis; CRAMP; metastasis; proliferation

Indexed keywords

CASPASE 3; CATHELICIDIN ANTIMICROBIAL PEPTIDE; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; CD31 ANTIGEN; COLLAGENASE; GELATINASE B; KI 67 ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PEPTIDE DERIVATIVE; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 79952396539     PISSN: 02704137     EISSN: 10970045     Source Type: Journal    
DOI: 10.1002/pros.21282     Document Type: Article
Times cited : (47)

References (41)
  • 1
  • 2
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou M, Gallo RL,. Cathelicidins, essential gene-encoded mammalian antibiotics. J Mol Med 2002; 80 (9): 549-561.
    • (2002) J Mol Med , vol.80 , Issue.9 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 4
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti M, Gennaro R, Romeo D,. Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett 1995; 374 (1): 1-5.
    • (1995) FEBS Lett , vol.374 , Issue.1 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 6
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.03.030, PII S000527360600126X
    • Durr UH, Sudheendra US, Ramamoorthy A,. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 2006; 1758 (9): 1408-1425. (Pubitemid 44436081)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 9
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • DOI 10.1046/j.1523-1747.2003.12069.x
    • Heilborn JD, Nilsson MF, Kratz G, Weber G, Sorensen O, Borregaard N,. The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J Invest Dermatol 2003; 120 (3): 379-389. (Pubitemid 36298423)
    • (2003) Journal of Investigative Dermatology , vol.120 , Issue.3 , pp. 379-389
    • Heilborn, J.D.1    Frohm Nilsson, M.2    Kratz, G.3    Weber, G.4    Sorensen, O.5    Borregaard, N.6    Stahle-Backdahl, M.7
  • 12
    • 63149198810 scopus 로고    scopus 로고
    • The human antimocrobial peptide LL-37 suppresses apoptosis in keratinocytes
    • Chamorro CI, Weber G, Gronberg A, Pivarci A, Stahle M,. The human antimocrobial peptide LL-37 suppresses apoptosis in keratinocytes. J Invest Derm 2009; 129: 937-944.
    • (2009) J Invest Derm , vol.129 , pp. 937-944
    • Chamorro, C.I.1    Weber, G.2    Gronberg, A.3    Pivarci, A.4    Stahle, M.5
  • 13
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA,. The hallmarks of cancer. Cell 2000; 100 (1): 57-70. (Pubitemid 30046295)
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 18
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18 is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sørensen OE, Follin P, Johnsen AH, Calafat J, Tjabringa GS, Hiemstra PS, Borregaard N,. Human cathelicidin, hCAP-18 is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 2001; 97 (12): 3951-3959.
    • (2001) Blood , vol.97 , Issue.12 , pp. 3951-3959
    • Sørensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 19
    • 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
    • Yang D, Chen Q, Schmidt AP, Anderson GM, Wang JM, Wooters J, Oppenheim JJ, Chertov O,. 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): 1069-1074.
    • (2000) J Exp Med , vol.192 , Issue.7 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 21
    • 18644363054 scopus 로고    scopus 로고
    • Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant
    • Kurosaka K, Chen Q, Yarovinsky F, Oppenheim JJ, Yang D,. Mouse cathelin-related antimicrobial peptide chemoattracts leukocytes using formyl peptide receptor-like 1/mouse formyl peptide receptor-like 2 as the receptor and acts as an immune adjuvant. J Immunol 2005; 174 (10): 6257-6265. (Pubitemid 40663818)
    • (2005) Journal of Immunology , vol.174 , Issue.10 , pp. 6257-6265
    • Kurosaka, K.1    Chen, Q.2    Yarovinsky, F.3    Oppenheim, J.J.4    Yang, D.5
  • 23
    • 0031009432 scopus 로고    scopus 로고
    • Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse
    • DOI 10.1074/jbc.272.20.13088
    • Gallo RL, Kim KJ, Bernfield M, Kozak CA, Zanetti M, Merluzzi L, Gennaro R,. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J Biol Chem 1997; 272 (20): 13088-13093. (Pubitemid 27216731)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.20 , pp. 13088-13093
    • Galloo, R.L.1    Kim, K.J.2    Bernfield, M.3    Kozak, C.A.4    Zanetti, M.5    Merluzzi, L.6    Gennaro, R.7
  • 24
    • 0034832028 scopus 로고    scopus 로고
    • Processing site and gene structure for the murine antimicrobial peptide CRAMP
    • DOI 10.1016/S0196-9781(01)00499-5, PII S0196978101004995
    • Pestonjamasp VK, Huttner KH, Gallo RL,. Processing site and gene structure for the murine antimicrobial peptide CRAMP. Peptides 2001; 22 (10): 1643-1650. (Pubitemid 32918243)
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1643-1650
    • Pestonjamasp, V.K.1    Huttner, K.H.2    Gallo, R.L.3
  • 25
    • 0036092782 scopus 로고    scopus 로고
    • Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy
    • DOI 10.1034/j.1399-3011.2002.01968.x
    • Yu K, Park K, Kim Y, Kang SW, Shin SY, Hahm KS,. Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy. J Pept Res 2002; 60: 1-9. (Pubitemid 34680828)
    • (2002) Journal of Peptide Research , vol.60 , Issue.1 , pp. 1-9
    • Yu, K.1    Park, K.2    Kim, Y.3    Kang, S.-W.4    Shin, S.Y.5    Hahm, K.-S.6
  • 26
    • 70449346550 scopus 로고    scopus 로고
    • Current perspectives on the Gleason grading of prostate cancer
    • Shah RB,. Current perspectives on the Gleason grading of prostate cancer. Arch Pathol Lab Med 2009; 133 (11): 1810-1816.
    • (2009) Arch Pathol Lab Med , vol.133 , Issue.11 , pp. 1810-1816
    • Shah, R.B.1
  • 30
    • 0030860498 scopus 로고    scopus 로고
    • Characterization of prostatic epithelial cell lines derived from transgenic adenocarcinoma of the mouse prostate (TRAMP) model
    • Foster BA, Gingrich JR, Kwon ED, Madias C, Greenberg NM,. Characterization of prostatic epithelial cell lines derived from transgenic adenocarcinoma of the mouse prostate (TRAMP) model. Cancer Res 1997; 57 (16): 3325-3330. (Pubitemid 27355467)
    • (1997) Cancer Research , vol.57 , Issue.16 , pp. 3325-3330
    • Foster, B.A.1    Gingrich, J.R.2    Kwon, E.D.3    Madias, C.4    Greenberg, N.M.5
  • 32
    • 2342520028 scopus 로고    scopus 로고
    • The Human Antimicrobial Peptide LL-37 Transfers Extracellular DNA Plasmid to the Nuclear Compartment of Mammalian Cells via Lipid Rafts and Proteoglycan-dependent Endocytosis
    • DOI 10.1074/jbc.M311440200
    • Sandgren S, Wittrup A, Cheng F, Jönsson M, Eklund E, Busch S, Belting M,. The human antimicrobial peptide LL-37 transfers extracellular DNA plasmid to the nuclear compartment of mamamalian cells via lipid rafts and proteoglycan-dependent endocytosis. J Biol Chem 2004; 279 (17): 17951-17956. (Pubitemid 38568102)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17951-17956
    • Sandgren, S.1    Wittrup, A.2    Cheng, F.3    Jonsson, M.4    Eklund, E.5    Busch, S.6    Belting, M.7
  • 33
    • 75949107937 scopus 로고    scopus 로고
    • VEGF inhibitors and prostate cancer therapy
    • Aragon-Ching JB, Dahut WL,. VEGF inhibitors and prostate cancer therapy. Curr Mol Pharmacol 2009; 2 (2): 161-168.
    • (2009) Curr Mol Pharmacol , vol.2 , Issue.2 , pp. 161-168
    • Aragon-Ching, J.B.1    Dahut, W.L.2
  • 34
    • 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): 907-915.
    • (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
  • 35
    • 1542724426 scopus 로고    scopus 로고
    • The Human Cationic Peptide LL-37 Induces Activation of the Extracellular Signal-Regulated Kinase and p38 Kinase Pathways in Primary Human Monocytes
    • Bowdish DM, Davidson DJ, Speert DP, Hancock RE,. The human cationic peptide LL-37 induces activation of the extracellular signal-regulated kinase and p38 kinase pathways in primary human monocytes. J Immunol 2004; 172 (6): 3758-3765. (Pubitemid 38337960)
    • (2004) Journal of Immunology , vol.172 , Issue.6 , pp. 3758-3765
    • Bowdish, D.M.E.1    Davidson, D.J.2    Speert, D.P.3    Hancock, R.E.W.4
  • 36
    • 0033965483 scopus 로고    scopus 로고
    • Akt takes center stage in angiogenesis signaling
    • Dimmeler S, Zeiher AM,. Akt takes center stage in angiogenesis signaling. Circ Res 2000; 86: 4-5. (Pubitemid 30044160)
    • (2000) Circulation Research , vol.86 , Issue.1 , pp. 4-5
    • Dimmeler, S.1    Zeiher, A.M.2
  • 37
    • 0034681392 scopus 로고    scopus 로고
    • Utilization of distinct signaling pathways by receptors for vascular endothelial cell growth factor and other mitogens in the induction of endothelial cell proliferation
    • DOI 10.1074/jbc.275.7.5096
    • Wu LW, Mayo LD, Dunbar JD, Kessler KM, Baerwald MR, Jaffe EA, Wang D, Warren RS, Donner DB,. Utilization of distinct signaling pathways by receptors for vascular endothelial cell growth factor and other mitogens in the induction of endothelial cell proliferation. J Biol Chem 2000; 275 (7): 5096-5103. (Pubitemid 30108910)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 5096-5103
    • Wu, L.-W.1    Mayo, L.D.2    Dunbar, J.D.3    Kessler, K.M.4    Baerwald, M.R.5    Jaffe, E.A.6    Wang, D.7    Warren, R.S.8    Donner, D.B.9
  • 38
    • 34548651801 scopus 로고    scopus 로고
    • Water extract of Korean red ginseng stimulates angiogenesis by activating the PI3K/Akt-dependent ERK1/2 and eNOS pathways in human umbilical vein endothelial cells
    • DOI 10.1248/bpb.30.1674
    • Kim YM, Namkoong S, Yun YG, Hong HD, Lee YC, Ha KS, Lee H, Kwon HJ, Kwon YG, Kim YM,. Water extract of Korean red ginseng stimulates angiogenesis by activating the PI3K/Akt-dependent ERK1/2 and eNOS pathways in human umbilical vein endothelial cells. Biol Pharm Bull 2007; 30 (9): 1674-1679. (Pubitemid 47403243)
    • (2007) Biological and Pharmaceutical Bulletin , vol.30 , Issue.9 , pp. 1674-1679
    • Kim, Y.-M.1    Namkoong, S.2    Yun, Y.-G.3    Hong, H.-D.4    Lee, Y.-C.5    Ha, K.-S.6    Lee, H.7    Kwon, H.J.8    Kwon, Y.-G.9    Kim, Y.-M.10
  • 39
    • 50349102480 scopus 로고    scopus 로고
    • Prostate-specific kallikreins-2 and -4 enhance the proliferation of DU-145 prostate cancer cells through protease-activated receptors-1 and -2
    • Mize GJ, Wang W, Takayama TK,. Prostate-specific kallikreins-2 and -4 enhance the proliferation of DU-145 prostate cancer cells through protease-activated receptors-1 and -2. Mol Cancer Res 2008; 6 (6): 1043-1051.
    • (2008) Mol Cancer Res , vol.6 , Issue.6 , pp. 1043-1051
    • Mize, G.J.1    Wang, W.2    Takayama, T.K.3
  • 40
    • 0034194326 scopus 로고    scopus 로고
    • The Ras-mitogen-activated protein kinase pathway is critical for the activation of matrix metalloproteinase secretion and the invasiveness in v- crk-transformed 3Y1
    • Liu E, Thant AA, Kikkawa F, Kurata H, Tanaka S, Nawa A, Mizutani S, Matsuda S, Hanafusa H, Hamaguchi M,. The ras-mitogen-activated protein kinase pathway is critical for the activation of matrix metalloproteinase secretion and the invasiveness in v-crk-transformed 3Y1. Cancer Res 2000; 60: 2361-2364. (Pubitemid 30262422)
    • (2000) Cancer Research , vol.60 , Issue.9 , pp. 2361-2364
    • Liu, E.1    Thant, A.A.2    Kikkawa, F.3    Kurata, H.4    Tanaka, S.5    Nawa, A.6    Mizutani, S.7    Matsuda, S.8    Hanafusa, H.9    Hamaguchi, M.10
  • 41
    • 1642410959 scopus 로고    scopus 로고
    • Treatment of Epigallocatechin-3-Gallate Inhibits Matrix Metalloproteinases-2 and -9 via Inhibition of Activation of Mitogen-Activated Protein Kinases, c-jun and NF-κB in Human Prostate Carcinoma DU-145 Cells
    • DOI 10.1002/pros.10352
    • Vayalil PK, Katiyar SK,. Treatment of epigallocatechin-3-gallate inhibits matrix metalloproteinases-2 and -9 via inhibition of activation of mitogen-activated protein kinases, c-jun and NF-kB in human prostate carcinoma DU-145 cells. Prostate 2004; 59: 33-42. (Pubitemid 38387841)
    • (2004) Prostate , vol.59 , Issue.1 , pp. 33-42
    • Vayalil, P.K.1    Katiyar, S.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.