title: Antitumor effects and cell selectivity of temporin-1CEa, an antimicrobial peptide from the skin secretions of the Chinese brown frog (Rana chensinensis).
abstract: Many antimicrobial peptides from amphibian exhibit additional anticancer properties due to a similar mechanism of action at both bacterial and cancer cells. We have previously reported the cDNA sequence of the antimicrobial peptide temporin-1CEa precursor cloned from the Chinese brown frog Rana chensinensis. In this study, we purified, synthesized and structurally characterized temporin-1CEa from the skin secretions of R. chensinensis. The cytotoxicity and cell selectivity of temporin-1CEa were further examined on twelve human carcinoma cell lines and on normal human umbilical vein smooth muscle cells (HUVSMCs). Our results indicated that temporin-1CEa has the amino acid sequence of FVDLKKIANIINSIF-NH(2), and exhibits 50-56% identity with temporin family peptides from other frog species. The CD spectra for temporin-1CEa adopted a well-defined α-helical structure in 50% TFE/water solution. The results of MTT assay showed that temporin-1CEa exhibits cytotoxicity to all tested cancer cell lines in a concentration-dependent manner, being MCF-7 cells the most sensitive. Moreover, temporin-1CEa had lower hemolytic effect to human erythrocytes and had no significant cytotoxicity to normal HUVSMCs at concentrations showed potent antitumor activity. In summary, temporin-1CEa, an amphiphilic α-helical cationic peptide, may represent a novel anticancer agent for breast cancer therapy, considering its cancer cell selectivity and relatively lower cytotoxicity to normal cells.
authors.affiliation: Liaoning Provincial Key Laboratory of Biotechnology and Drug Discovery, Liaoning Normal University, Dalian, Liaoning 116029, China.
authors.forename: Che
authors.initials: C
authors.lastname: Wang
authors.forename: Hui-Bing
authors.initials: HB
authors.lastname: Li
authors.forename: Song
authors.initials: S
authors.lastname: Li
authors.forename: Li-Li
authors.initials: LL
authors.lastname: Tian
authors.forename: De-Jing
authors.initials: DJ
authors.lastname: Shang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000138:chemical synthesis / Q000302:isolation & purification / Q000494:pharmacology*; D000970:Antineoplastic Agents / Q000138:chemical synthesis / Q000302:isolation & purification / Q000494:pharmacology*; D001943:Breast Neoplasms / Q000188:drug therapy* / Q000378:metabolism / Q000473:pathology; D002277:Carcinoma / Q000188:drug therapy* / Q000378:metabolism / Q000473:pathology; D045744:Cell Line, Tumor; D002470:Cell Survival / Q000187:drug effects; D002681:China; D018076:DNA, Complementary / Q000235:genetics; D004912:Erythrocytes / Q000187:drug effects; D005260:Female; D061307:Human Umbilical Vein Endothelial Cells; D006801:Humans; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000138:chemical synthesis / Q000302:isolation & purification / Q000494:pharmacology; D011506:Proteins / Q000138:chemical synthesis / Q000302:isolation & purification / Q000494:pharmacology*; D011898:Ranidae / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000378:metabolism*
chemical_list: D023181:Antimicrobial Cationic Peptides; D000970:Antineoplastic Agents; D018076:DNA, Complementary; D020033:Protein Isoforms; D011506:Proteins; C104501:temporin