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

TALP-32의 인체자궁암 세포주 HeLa에 대한 세포독성

  • 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)
  • 박지훈 (충남대학교 생화학교실) ;
  • 김종석 (충남대학교 생화학교실) ;
  • 윤은진 (충남대학교 생화학교실) ;
  • 송경섭 (충남대학교 생화학교실) ;
  • 서강식 (충남대학교 생화학교실) ;
  • 김훈 (충남대학교 생화학교실) ;
  • 정연주 (충남대학교 생화학교실) ;
  • 윤완희 (충남대학교 생화학교실) ;
  • 임규 (충남대학교 생화학교실) ;
  • 황병두 (충남대학교 생화학교실) ;
  • 박종일 (충남대학교 생화학교실)
  • Published : 2006.12.30

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

References

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