title: Anticancer mechanisms of temporin-1CEa, an amphipathic α-helical antimicrobial peptide, in Bcap-37 human breast cancer cells.
abstract: OBJECTIVE
  Temporin-1CEa, a 17-residue antimicrobial peptide, is known to exert broad-spectrum anticancer activity that acts preferentially on cancer cells instead of normal cells. However, the mechanism of cancer cell death induced by temporin-1CEa is weakly understood.
  
  
  METHODS
  Here, we investigated the cytotoxic and membrane-disrupting effects of temporin-1CEa on human breast cancer cell line Bcap-37, using MTT assay, electronic microscope observation, fluorescence imaging and flow cytometry analysis.
  
  
  RESULTS
  The MTT assay indicated that one-hour temporin-1CEa treatment led to rapid cell death in either caspase-dependent or -independent manner. The electronic microscope observation suggested that temporin-1CEa exposure resulted in profound morphological changes in Bcap-37 cells. The fluorescence imaging and flow cytometry analysis demonstrated that temporin-1CEa exhibited membrane-disrupting property characterized by induction of cell-surface phosphatidylserine exposure, elevation of plasma membrane permeability, and rapid transmembrane potential depolarization. Moreover, temporin-1CEa might also induce rapid cell death through mitochondria-involved mechanisms, including rapid intracellular Ca(2+) leakage, collapse of mitochondrial membrane potential (Δφm) and over-generation of reactive oxygen species (ROS).
  
  
  CONCLUSIONS
  In summary, the present study indicates that temporin-1CEa triggers a rapid cytotoxicity in Bcap-37 cells through membrane-destruction and intracellular mechanisms involving mitochondria. These intracellular mechanisms and direct membrane-destruction effect were evaluated helping to understand the detail action of antimicrobial peptides in mammalian cancer cells.
authors.affiliation: Liaoning Provincial Key Laboratory of Biotechnology and Drug Discovery, Liaoning Normal University, Dalian 116029, China.
authors.forename: Che
authors.initials: C
authors.lastname: Wang
authors.forename: Yang
authors.initials: Y
authors.lastname: Zhou
authors.forename: Song
authors.initials: S
authors.lastname: Li
authors.forename: HuiBing
authors.initials: H
authors.lastname: Li
authors.forename: LiLi
authors.initials: L
authors.lastname: Tian
authors.forename: He
authors.initials: H
authors.lastname: Wang
authors.forename: DeJing
authors.initials: D
authors.lastname: Shang
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000494:pharmacology*; D000970:Antineoplastic Agents / Q000494:pharmacology*; D001943:Breast Neoplasms / Q000378:metabolism / Q000473:pathology*; D002118:Calcium / Q000378:metabolism; D045744:Cell Line, Tumor; D002463:Cell Membrane Permeability / Q000187:drug effects; D005260:Female; D005434:Flow Cytometry; D006801:Humans; D053078:Membrane Potential, Mitochondrial; D008854:Microscopy, Electron; D010455:Peptides / Q000494:pharmacology*; D017382:Reactive Oxygen Species / Q000378:metabolism
chemical_list: D023181:Antimicrobial Cationic Peptides; D000970:Antineoplastic Agents; D010455:Peptides; D017382:Reactive Oxygen Species; C582109:temporin-1CEa, Rana chensinensis; D002118:Calcium