Effects of quercetin and sunphenon on responses of cancer cells to heat shock damage

Exp Mol Pathol. 1999 Apr;66(1):66-75. doi: 10.1006/exmp.1999.2247.


Quercetin is a flavonoid well known to inhibit growth and heat shock protein (HSP) synthesis of cancer cells. However, sunphenon has been scarcely reported concerning effects on cancer cells. We compared the effects of sunphenon with those of quercetin on the human cholangio-cellular carcinoma cell line (HuCC-T1). Both flavonoids inhibited HuCC-T1 growth in a concentration-dependent manner without reduction of HSP70 and HSP90 expression before heat shock damage. The heat shock reduced the cell viability of the quercetin-treated HuCC-T1, but not that of the sunphenon-treated cells. This inhibitory effect of quercetin on tolerance to heat shock is thought to be due to marked suppression of HSP72. Sunphenon conversely increased HSP72 expression after heat shock. Although neither flavonoid altered HSP90 protein levels before and after heat shock, quercetin delayed the reorganization of filamentous actin (F-actin) during the recovery period after heat shock. Since HSP90 could preserve F-actin structure during stresses, quercetin might affect the interaction between HSP90 and F-actin without influencing HSP90 expression. In conclusion, quercetin would be more useful than sunphenon in combined therapy with hyperthermia for cancer.

MeSH terms

  • Anticarcinogenic Agents / toxicity*
  • Bile Duct Neoplasms
  • Bile Ducts, Intrahepatic
  • Cell Division / drug effects
  • Cholangiocarcinoma
  • Dose-Response Relationship, Drug
  • Gene Expression Regulation, Neoplastic / drug effects*
  • HSP70 Heat-Shock Proteins / genetics*
  • HSP90 Heat-Shock Proteins / genetics*
  • Hot Temperature*
  • Humans
  • Kinetics
  • Phenols / toxicity*
  • Quercetin / toxicity*
  • Time Factors
  • Tumor Cells, Cultured


  • Anticarcinogenic Agents
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Phenols
  • Sunphenon
  • Quercetin