PMA synergistically enhances apicularen A-induced cytotoxicity by disrupting microtubule networks in HeLa cells

BMC Cancer. 2014 Jan 22:14:36. doi: 10.1186/1471-2407-14-36.

Abstract

Background: Combination therapy is key to improving cancer treatment efficacy. Phorbol 12-myristate 13-acetate (PMA), a well-known PKC activator, increases the cytotoxicity of several anticancer drugs. Apicularen A induces cytotoxicity in tumor cells through disrupting microtubule networks by tubulin down-regulation. In this study, we examined whether PMA increases apicularen A-induced cytotoxicity in HeLa cells.

Methods: Cell viability was examined by thiazolyl blue tetrazolium (MTT) assays. To investigate apoptotic potential of apicularen A, DNA fragmentation assays were performed followed by extracting genomic DNA, and caspase-3 activity assays were performed by fluorescence assays using fluorogenic substrate. The cell cycle distribution induced by combination with PMA and apicularen A was examined by flow cytometry after staining with propidium iodide (PI). The expression levels of target proteins were measured by Western blotting analysis using specific antibodies, and α-tubulin mRNA levels were assessed by reverse transcription polymerase chain reaction (RT-PCR). To examine the effect of combination of PMA and apicularen A on the microtubule architecture, α-tubulin protein and nuclei were visualized by immunofluorescence staining using an anti-α-tubulin antibody and PI, respectively.

Results: We found that apicularen A induced caspase-dependent apoptosis in HeLa cells. PMA synergistically increased cytotoxicity and apoptotic sub-G1 population induced by apicularen A. These effects were completely blocked by the PKC inhibitors Ro31-8220 and Go6983, while caspase inhibition by Z-VAD-fmk did not prevent cytotoxicity. RNA interference using siRNA against PKCα, but not PKCβ and PKCγ, inhibited cytotoxicity induced by combination PMA and apicularen A. PMA increased the apicularen A-induced disruption of microtubule networks by further decreasing α- and β-tubulin protein levels in a PKC-dependent manner.

Conclusions: These results suggest that the synergy between PMA and apicularen A is involved by PKCα activation and microtubule disruption, and that may inform the development of novel approaches to treat cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Combined Chemotherapy Protocols / pharmacology*
  • Apoptosis / drug effects
  • Bridged Bicyclo Compounds, Heterocyclic / pharmacology
  • Caspase 3 / metabolism
  • Cell Cycle Checkpoints
  • Cell Survival / drug effects
  • Drug Synergism
  • Female
  • HeLa Cells
  • Humans
  • Microtubules / drug effects*
  • Microtubules / genetics
  • Microtubules / metabolism
  • Microtubules / pathology
  • Protein Kinase C-alpha / antagonists & inhibitors
  • Protein Kinase C-alpha / genetics
  • Protein Kinase C-alpha / metabolism
  • Protein Kinase Inhibitors / pharmacology
  • RNA Interference
  • Tetradecanoylphorbol Acetate / pharmacology
  • Time Factors
  • Transfection
  • Tubulin / genetics
  • Tubulin / metabolism
  • Tubulin Modulators / pharmacology
  • Uterine Cervical Neoplasms / genetics
  • Uterine Cervical Neoplasms / metabolism*
  • Uterine Cervical Neoplasms / pathology

Substances

  • Bridged Bicyclo Compounds, Heterocyclic
  • Protein Kinase Inhibitors
  • Tubulin
  • Tubulin Modulators
  • apicularen A
  • PRKCA protein, human
  • Protein Kinase C-alpha
  • CASP3 protein, human
  • Caspase 3
  • Tetradecanoylphorbol Acetate