1. ¹Beijing Institute for Cancer Research, School of Oncology, Peking University No. 52, Fucheng Rd, Hai Dian District, Beijing 100036, PR China
2. ²Department of Surgery, Anyang Cancer Hospital, Anyang City, Henan Province 455000, PR China
3. ³Department of Cell Biology, Health Science Center, Peking University No. 38, Xueyuan Rd, Hai Dian District, Beijing 100083, PR China
4. ⁴Cancer Research Center, Health Science Center, Peking University No. 38, Xueyuan Rd, Hai Dian District, Beijing 100083, PR China

Correspondence: Dr Y Ke, E-mails: keyang@bjmu.edu.cn and karazhou@163.com

Received 9 January 2007; Revised 11 May 2007; Accepted 14 May 2007.

Abstract

HPV16 E6 interacts with and degrades tumour suppressor protein TSC2 leading to the phosphorylation of p70 S6 kinase. We studied the association of S6 kinase phosphorylation and HPV16 infection in cervical cancer and esophageal cancer. Immunohistochemistry was used to assess phosphorylated S6 kinase (Thr 389) and phosphorylated S6 (Ser235/236) in 140 cervical cancer and 161 esophageal cancer specimens. Immunohistochemical staining for pS6 kinase and pS6 was significantly more frequent in the HPV16-infected cervical cancer specimens than the HPV16-negative specimens. In contrast, the expression of S6 kinase was similar in both HPV16-positive and -negative samples. The phosphorylation of Akt, the key regulator of S6 kinase, was also detected. Our analysis showed that Akt phosphorylation was unaffected by HPV16 infection. These results together with our previous study suggest that HPV16 modifies S6 kinase activation via mechanism, which activates S6 kinase downstream of Akt function.