Activation of TRPV2 and BKCa channels by the LL-37 enantiomers stimulates calcium entry and migration of cancer cells

Oncotarget. 2016 Apr 26;7(17):23785-800. doi: 10.18632/oncotarget.8122.

Abstract

Expression of the antimicrobial peptide hCAP18/LL-37 is associated to malignancy in various cancer forms, stimulating cell migration and metastasis. We report that LL-37 induces migration of three cancer cell lines by activating the TRPV2 calcium-permeable channel and recruiting it to pseudopodia through activation of the PI3K/AKT pathway. Ca2+ entry through TRPV2 cooperated with a K+ efflux through the BKCa channel. In a panel of human breast tumors, the expression of TRPV2 and LL-37 was found to be positively correlated. The D-enantiomer of LL-37 showed identical effects as the L-peptide, suggesting that no binding to a specific receptor was involved. LL-37 attached to caveolae and pseudopodia membranes and decreased membrane fluidity, suggesting that a modification of the physical properties of the lipid membrane bilayer was the underlying mechanism of its effects.

Keywords: LL-37; breast cancer; calcium signaling; cell migration; membrane association.

MeSH terms

  • Antimicrobial Cationic Peptides / chemistry
  • Antimicrobial Cationic Peptides / pharmacology*
  • Apoptosis / drug effects
  • Biomarkers, Tumor / metabolism*
  • Breast Neoplasms / drug therapy
  • Breast Neoplasms / metabolism
  • Breast Neoplasms / pathology*
  • Calcium / metabolism*
  • Cathelicidins
  • Cell Movement / drug effects*
  • Cell Proliferation / drug effects
  • Female
  • Humans
  • Large-Conductance Calcium-Activated Potassium Channel alpha Subunits / metabolism*
  • TRPV Cation Channels / metabolism*
  • Tumor Cells, Cultured

Substances

  • Antimicrobial Cationic Peptides
  • Biomarkers, Tumor
  • KCNMA1 protein, human
  • Large-Conductance Calcium-Activated Potassium Channel alpha Subunits
  • TRPV Cation Channels
  • TRPV2 protein, human
  • Calcium
  • Cathelicidins