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1860797478660472832
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INTELEK Repository
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| collection |
Online Access
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https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072
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| date |
2016-03-22 15:35:58
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Restricted Document
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| id |
12895
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UniSZA
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| internalnotes |
Al-Benna S, Shai Y, Jacobsen F, Steinstraesser L. Oncolytic activities of host defense peptides. Int J Mol Sci, 2011;12(11):8027–51. Chang W-T, Pan C-Y, Rajanbabu V, Cheng C-W, Chen J-Y. Tilapia (Oreochromis mossambicus) antimicrobial peptide, Hepcidin 1-5, shows antitumor activity in cancer cells. Peptides, 201;32(2):342–52. Chen J-Y, Lin W-J, Lin T-L. A fish antimicrobial peptide, tilapia Hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells. Peptides, 2009;30(9):1636–42. 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. Duprez L, Wirawan E, Vanden Berghe T, Vandenabeele P. Major cell death pathways at a glance. Microbes Infect, 2009; 11(13): 1050–62. Hancock REW, Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr Drug Targets Infect Disord, 2002;2(1):79–83. Hassan MA, Mohd KS, Azemin W-A, Dharmaraj S. Cytotoxic effect of Hepcidin (TH1-5) on human breast cancer cellline MCF-7. Jurnal Teknologi, 2015; 77(3):73-79. Hassan MSU, Ansari J, Spooner D, Hussain SA. Chemotherapy for breast cancer (Review). Oncol Rep, 2010;24(5):1121–31. Hoskin DW, Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim Biophys Acta, 2008; 1778(2):357–75. Lamkanfi M, Kanneganti T-D. Caspase-7: a protease involved in apoptosis and inflammation. Int J Biocemistry Cell Biol, 2010; 42(1):21–24. Lavrik IN, Golks A, Krammer PH. Caspases: pharmacological manipulation of cell death. J Clin Invest, 2005;115(10):2665–72. Mader JS, Hoskin DW. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin Investig Drugs, 2006;15(8):933–46. McIlwain DR, Berger T, Mak TW. Caspase functions in cell death and disease. Cold Spring Harb Perspect Biol, 2013;5(4):a008656. Mohd KS, Azemin WA, Ali AM. Induction of apoptosis and G2/M phase cell cycle arrest by antimicrobial peptide HepTH1-5. In: International Conference on Natural Product 2015, 24-25 March 2015, Johor Bharu. Norbury CJ, Hickson ID. Cellular responses to DNA damage. Annu Rev Pharmacol Toxicol, 2001;4(1):367–401. Omar ZA, Tamin NSI. National Cancer Registry Report 2007.Malaysia Cancer Statistics-Data and Figure, Kuala Lumpur: National Cancer Registry, Ministry of Health Malaysia, 2011, 89. Papo N, Shai Y. Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci, 2005;62(7-8):784–90. Park MH, Choi MS, Kwak DH, Oh K-W, Yoon DY, Han SB, et al. Anti-cancer effect of bee venom in prostate cancer cells through activation of caspase pathway via inactivation of NF-κB. Prostate, 2011;71(8):801–12. Porter AG, Jänicke RU. Emerging roles of caspase-3 in apoptosis. Cell Death Differ, 1999;6(2):99–104. Rajanbabu V, Chen J-Y. Applications of antimicrobial peptides from fish and perspectives for the future. Peptides, 2011;32(2):415–20. Sankari SL, Masthan KMK, Babu NA, Bhattacharjee T, Elumalai M. Apoptosis in cancer - an update. Asian Pacific J Cancer Prev, 2012;13(10):4873–8. Shiozaki EN, Chai J, Shi Y. Oligomerization and activation of caspase-9, induced by Apaf-1 CARD. Proc Natl Acad Sci USA, 2002;99(7):4197–202. Steinstraesser L, Kraneburg UM, Hirsch T, Kesting M, Jacobsen F, Al-benna S. Host defense peptides as effector molecules of the innate immune response : asledgehammer for drug resistance ? Int J Mol Sci, 2009; 10(9):3951–70. Su X, Xu C, Li Y, Gao X, Lou Y. Antitumor activity of polysaccharides and saponin extracted from sea cucumber. J Clin Cell Immunol, 2011; 02(105). WHO. GLOBOCAN 2012: Estimated cancer incidence, mortality and prevalence worldwide in 2012. Lyon, Fr Int Agency Res Cancer, 2014. WHO. Breast cancer awareness in October. Avaialble at www.who.int/cancer/events/breast_cancer_month/en/ [Accessed 15 November 2015]. Wong RSY. Apoptosis in cancer: from pathogenesis to treatment. J Exp Clin Cancer Res, 2011;30(1):87. Xu H, Chen CX, Hu J, Zhou P, Zeng P, Cao CH, et al. Dual modes of antitumor action of an amphiphilic peptide A(9)K. Biomaterials, 2013;34(11):2731–7. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature, 2002;415(6870):389–95.
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7202-01-FH02-FP-16-05541.jpg
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norman
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oai_dc
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https://intelek.unisza.edu.my/intelek/pages/view.php?ref=12895
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12895 https://intelek.unisza.edu.my/intelek/pages/view.php?ref=12895 https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072 Restricted Document Article Journal image/jpeg inches 96 96 norman 1423 31 31 763 2016-03-22 15:35:58 1423x763 7202-01-FH02-FP-16-05541.jpg UniSZA Private Access Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells Journal of Applied Pharmaceutical Science Breast cancer is the most commonly diagnosed and leading cause of cancer deaths among women globally. In continuation of our investigation into the cytotoxicity of the antimicrobial peptide, Hepcidin TH1-5 on human breast adenocarcinoma cell line (MCF-7), we further affirm the apoptosis-inducing effect of the cysteine-rich peptide in the present study. Annexin V-fluorescein isothiocyanate and propidium iodide (annexin V-FITC/PI) apoptosis assay was performed after treatment of the cells. In the determination of caspase activity and pathway of apoptosis, luminescent assay was also performed where caspase-3/7, caspase-8 and caspase-9 were evaluated. Results of annexin V-FITC/PI staining showed proportion of early apoptotic cell were 73.67 ± 4.93%, 61.00 ± 5.57% and 44.33 ± 2.52% at 24, 48 and 72 hours respectively, while late apoptotic cell were 6.33 ± 1.53%, 23 ± 3.56% and 34 ± 3.51% within the same time interval. Based on the data from the luminescence test, Hepcidin TH1-5 activated caspases-3/7 and -9 which suggests that the apoptosis induced was due to the peptide treatment. Hepcidin TH1-5 induced apoptosis in MCF-7 via the activation of caspase-9 of the intrinsic pathway. These results support our previous findings of the cytotoxicity of Hepcidin TH1-5 and indicate that the peptide may be a potential agent for breast cancer therapy. 6 2 Open Science Publishers LLP Inc. Open Science Publishers LLP Inc. 081-086 Al-Benna S, Shai Y, Jacobsen F, Steinstraesser L. Oncolytic activities of host defense peptides. Int J Mol Sci, 2011;12(11):8027–51. Chang W-T, Pan C-Y, Rajanbabu V, Cheng C-W, Chen J-Y. Tilapia (Oreochromis mossambicus) antimicrobial peptide, Hepcidin 1-5, shows antitumor activity in cancer cells. Peptides, 201;32(2):342–52. Chen J-Y, Lin W-J, Lin T-L. A fish antimicrobial peptide, tilapia Hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells. Peptides, 2009;30(9):1636–42. 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. Duprez L, Wirawan E, Vanden Berghe T, Vandenabeele P. Major cell death pathways at a glance. Microbes Infect, 2009; 11(13): 1050–62. Hancock REW, Patrzykat A. Clinical development of cationic antimicrobial peptides: from natural to novel antibiotics. Curr Drug Targets Infect Disord, 2002;2(1):79–83. Hassan MA, Mohd KS, Azemin W-A, Dharmaraj S. Cytotoxic effect of Hepcidin (TH1-5) on human breast cancer cellline MCF-7. Jurnal Teknologi, 2015; 77(3):73-79. Hassan MSU, Ansari J, Spooner D, Hussain SA. Chemotherapy for breast cancer (Review). Oncol Rep, 2010;24(5):1121–31. Hoskin DW, Ramamoorthy A. Studies on anticancer activities of antimicrobial peptides. Biochim Biophys Acta, 2008; 1778(2):357–75. Lamkanfi M, Kanneganti T-D. Caspase-7: a protease involved in apoptosis and inflammation. Int J Biocemistry Cell Biol, 2010; 42(1):21–24. Lavrik IN, Golks A, Krammer PH. Caspases: pharmacological manipulation of cell death. J Clin Invest, 2005;115(10):2665–72. Mader JS, Hoskin DW. Cationic antimicrobial peptides as novel cytotoxic agents for cancer treatment. Expert Opin Investig Drugs, 2006;15(8):933–46. McIlwain DR, Berger T, Mak TW. Caspase functions in cell death and disease. Cold Spring Harb Perspect Biol, 2013;5(4):a008656. Mohd KS, Azemin WA, Ali AM. Induction of apoptosis and G2/M phase cell cycle arrest by antimicrobial peptide HepTH1-5. In: International Conference on Natural Product 2015, 24-25 March 2015, Johor Bharu. Norbury CJ, Hickson ID. Cellular responses to DNA damage. Annu Rev Pharmacol Toxicol, 2001;4(1):367–401. Omar ZA, Tamin NSI. National Cancer Registry Report 2007.Malaysia Cancer Statistics-Data and Figure, Kuala Lumpur: National Cancer Registry, Ministry of Health Malaysia, 2011, 89. Papo N, Shai Y. Host defense peptides as new weapons in cancer treatment. Cell Mol Life Sci, 2005;62(7-8):784–90. Park MH, Choi MS, Kwak DH, Oh K-W, Yoon DY, Han SB, et al. Anti-cancer effect of bee venom in prostate cancer cells through activation of caspase pathway via inactivation of NF-κB. Prostate, 2011;71(8):801–12. Porter AG, Jänicke RU. Emerging roles of caspase-3 in apoptosis. Cell Death Differ, 1999;6(2):99–104. Rajanbabu V, Chen J-Y. Applications of antimicrobial peptides from fish and perspectives for the future. Peptides, 2011;32(2):415–20. Sankari SL, Masthan KMK, Babu NA, Bhattacharjee T, Elumalai M. Apoptosis in cancer - an update. Asian Pacific J Cancer Prev, 2012;13(10):4873–8. Shiozaki EN, Chai J, Shi Y. Oligomerization and activation of caspase-9, induced by Apaf-1 CARD. Proc Natl Acad Sci USA, 2002;99(7):4197–202. Steinstraesser L, Kraneburg UM, Hirsch T, Kesting M, Jacobsen F, Al-benna S. Host defense peptides as effector molecules of the innate immune response : asledgehammer for drug resistance ? Int J Mol Sci, 2009; 10(9):3951–70. Su X, Xu C, Li Y, Gao X, Lou Y. Antitumor activity of polysaccharides and saponin extracted from sea cucumber. J Clin Cell Immunol, 2011; 02(105). WHO. GLOBOCAN 2012: Estimated cancer incidence, mortality and prevalence worldwide in 2012. Lyon, Fr Int Agency Res Cancer, 2014. WHO. Breast cancer awareness in October. Avaialble at www.who.int/cancer/events/breast_cancer_month/en/ [Accessed 15 November 2015]. Wong RSY. Apoptosis in cancer: from pathogenesis to treatment. J Exp Clin Cancer Res, 2011;30(1):87. Xu H, Chen CX, Hu J, Zhou P, Zeng P, Cao CH, et al. Dual modes of antitumor action of an amphiphilic peptide A(9)K. Biomaterials, 2013;34(11):2731–7. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature, 2002;415(6870):389–95.
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| spellingShingle |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
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| summary |
Breast cancer is the most commonly diagnosed and leading cause of cancer deaths among women globally. In continuation of our investigation into the cytotoxicity of the antimicrobial peptide, Hepcidin TH1-5 on human breast adenocarcinoma cell line (MCF-7), we further affirm the apoptosis-inducing effect of the cysteine-rich peptide in the present study. Annexin V-fluorescein isothiocyanate and propidium iodide (annexin V-FITC/PI) apoptosis assay was performed after treatment of the cells. In the determination of caspase activity and pathway of apoptosis, luminescent assay was also performed where caspase-3/7, caspase-8 and caspase-9 were evaluated. Results of annexin V-FITC/PI staining showed proportion of early apoptotic cell were 73.67 ± 4.93%, 61.00 ± 5.57% and 44.33 ± 2.52% at 24, 48 and 72 hours respectively, while late apoptotic cell were 6.33 ± 1.53%, 23 ± 3.56% and 34 ± 3.51% within the same time interval. Based on the data from the luminescence test, Hepcidin TH1-5 activated caspases-3/7 and -9 which suggests that the apoptosis induced was due to the peptide treatment. Hepcidin TH1-5 induced apoptosis in MCF-7 via the activation of caspase-9 of the intrinsic pathway. These results support our previous findings of the cytotoxicity of Hepcidin TH1-5 and indicate that the peptide may be a potential agent for breast cancer therapy.
|
| title |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
|
| title_full |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
|
| title_fullStr |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
|
| title_full_unstemmed |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
|
| title_short |
Hepcidin TH1-5 induces apoptosis and activate caspase-9 in MCF-7 cells
|
| title_sort |
hepcidin th1-5 induces apoptosis and activate caspase-9 in mcf-7 cells
|