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Cytocidal Effect of TALP-32 on Human Cervical Cancer Cell HeLa  

Park, Ji-Hoon (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Kim, Jong-Seok (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Yun, Eun-Jin (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Song, Kyoung-Sub (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Seo, Kang-Sik (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Kim, Hoon (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Jung, Yeon-Joo (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Yun, Wan-Hee (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Lim, Kyu (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Hwang, Byoung-Doo (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Park, Jong-Il (Dept. of Biochemistry, College of Medicine, Chungnam National University)
Publication Information
Toxicological Research / v.22, no.4, 2006 , pp. 315-322 More about this Journal
Abstract
TALP-32 is highly basic protein with a molecular weight of 32 kDa purified from human term placenta. Some basic proteins such as defensins and cecropins are known to induce cell death by increasing membrane permeability and some of them are under development as an anticancer drug especially targeting multi-drug resistant cancers. Therefore, we investigated cytotoxic effect and mechanism of TALP-32 When HeLa cell was incubated with TALP-32, cytotoxicity was increased in time and dose dependent manner. As time goes by, HeLa cells became round and plasma membrane was ruptured. Increase of plasma membrane permeability was determined with LDH release assay. Also in transmission electron microscopy, typical morphology of necrotic cell death, such as cell swelling and intracellular organelle disruption was observed, but DNA fragmentation and caspase activation was not. And necrotic cell death was determined with Annexin V/Pl staining. The cytotoxicity of TALP-32 was minimal and decreased or RBC and Hep3B respectively. These data suggests that TALP-32 induces necrosis on rapidly growing cells but not on slowly growing cells implicating the possibility of its development of anticancer peptide drug.
Keywords
Necrosis; Peptide drug;
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1 Choi, B.-H. and Hwang, B.-D. (1998): Purification and Characterization of Tubulin Polymerization Stimulating Protein-32 from Human Term Placenta
2 Fischer, D., Li, Y., Ahlemeyer, B., Krieglstein, J. and Kissel, T. (2003): In vitro cytotoxicity testing of polycations: influence of polymer structure on cell viability and hemolysis. Biomaterials, 24, 1121-1131   DOI   ScienceOn
3 Kerr, J.F., Wyllie, A.H. and Currie, A.R. (1972): Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. British Journal of Cancer, 26, 239-257   DOI
4 Papo, N., Braunstein, A., Eshhar, Z. and Shai, Y. (2004): Suppression of human prostate tumor growth in mice by a cytolytic D-, L-amino Acid Peptide: membrane lysis, increased necrosis, and inhibition of prostate-specific antigen secretion. Cancer Research, 64, 5779-5786   DOI   ScienceOn
5 Papo, N. and Shai, Y. (2003): New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. Biochemistry, 42, 9346-9354   DOI   ScienceOn
6 Takahashi, M., Kataoka, S., Kobayashi, E., Udagawa, Y., Aoki, D., Oie, S., Kozu, A. and Nozawa, S. (1999): Differences in apoptosis induced by anticancer drugs in sublines (SKG-3a, SKG-3b) from a human uterine cervical epidermoid carcinoma. Oncology Research, 11, 71-75
7 Kitanaka, C. and Kuchino, Y. (1999): Caspase-independent programmed cell death with necrotic morphology. Cell Death and Differentiation, 6, 508-515   DOI
8 Koopman, G., Reutelingsperger, C.P., Kuijten, G.A., Keehnen, R.M., Pals, S.T. and van Oers, M.H. (1994): Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood, 84, 1415-1420
9 Parkin, D.M., Pisani, P. and Ferlay, J. (1999): Global cancer statistics. CA: A Cancer Journal for Clinicians, 49, 33-64, 31   DOI   ScienceOn
10 Hwang, B.D., Kwak, S.T., Kweon, G.R. and Lim, K. (1995): Promotion of microtubule assembly in vitro by a novel 35-kDa protein purified from human term placenta. Biochemical and Biophysical Research Communications, 208, 1174-1180   DOI   ScienceOn
11 Korzeniewski, C. and Callewaert, D.M. (1983): An enzymerelease assay for natural cytotoxicity. Journal of Immunological Methods, 64, 313-320   DOI   ScienceOn
12 Nguyen, H.N. and Nordqvist, S.R. (1999): Chemotherapy of advanced and recurrent cervical carcinoma. Seminars in Surgical Oncology, 16, 247-250
13 Do, T.N., Rosal, R.V., Drew, L., Raffo, A.J., Michl, J., Pincus, M.R., Friedman, F.K., Petrylak, D.P., Cassai, N., Szmulewicz, J., Sidhu, G., Fine, R.L. and Brandt-Rauf, P.W. (2003): Preferential induction of necrosis in human breast cancer cells by a p53 peptide derived from the MDM2 binding site. Oncogene., 22, 1431-1444   DOI   ScienceOn
14 Edinger, A.L. and Thompson, C.B. (2004): Death by design: apoptosis, necrosis and autophagy. Current Opinion in Cell Biology, 16, 663-669   DOI   ScienceOn
15 Kim, S., Kim, S.S., Bang, Y.J., Kim, S.J. and Lee, B.J. (2003): In vitro activities of native and designed peptide antibiotics against drug sensitive and resistant tumor cell lines. Peptides, 24, 945-953   DOI   ScienceOn
16 Vaara, M. (1992): Agents that increase the permeability of the outer membrane. Microbiological Reviews, 56, 395-411
17 Fernandez, R.C. and Weiss, A.A. (1996): Susceptibilities of Bordetella pertussis strains to antimicrobial peptides. Antimicrobial Agents and Chemotherapy, 40, 1041-1043
18 Kanduc, D., Mittelman, A., Serpico, R., Sinigaglia, E., Sinha, A.A., Natale, C., Santacroce, R., Di Corcia, M.G., Lucchese, A., Dini, L., Pani, P., Santacroce, S., Simone, S., Bucci, R. and Farber, E. (2002): Cell death: apoptosis versus necrosis (review). International Journal of Oncology, 21, 165-170
19 Serkies, K. and Jassem, J. (2005): Chemotherapy in the primary treatment of cervical carcinoma. Critical Reviews in Oncology/Hematology, 54, 197-208   DOI   ScienceOn