Author/Authors :
Okumura، نويسنده , , Kazuhiko and Itoh، نويسنده , , Akifumi and Isogai، نويسنده , , Emiko and Hirose، نويسنده , , Kimiharu and Hosokawa، نويسنده , , Yoichiro and Abiko، نويسنده , , Yoshihiro and Shibata، نويسنده , , Takatoshi and Hirata، نويسنده , , Michimasa and Isogai، نويسنده , , Hiroshi، نويسنده ,
Abstract :
Mammalian myeloid and epithelial cells express many antimicrobiotic peptides that contribute to innate host defense against invading microbes. In the present study, a 27-mer peptide of the C-terminal domain (hCAP18109–135) and analogs of the antimicrobial peptide human cathelicidin LL-37/human cationic antimicrobial protein 18 (hCAP18) were examined for tumoricidal activity. In vitro results showed that hCAP18109–135 induced apoptosis in human oral squamous cell carcinoma (OSCC), SAS-H1 cells. The hCAP18109–135 induced mitochondrial depolarization and apoptosis in SAS-H1 cells, but not in healthy human gingival fibroblasts (HGF) and human keratinocyte line HaCaT cells. Caspases were not activated during hCAP18109–135-induced apoptosis in SAS-H1 cells. The results indicate that hCAP18109–135 may induce caspase-independent apoptosis in OSCC but not in normal cells. hCAP18109–135 can therefore be a useful anti-tumor therapeutic agent in the treatment of OSCC.
Keywords :
Human oral squamos cell carcinoma cells , C-terminal domain of hCAP18 peptides , apoptosis , Hydrophobicity , mitochondrial membrane potential