RT Journal Article
SR Electronic
T1 An Immunohistochemical Evaluation of Phosphorylated Akt at Threonine 308 [pAkt(Thr308)] in Invasive Breast Cancer
JF In Vivo
JO In Vivo
FD International Institute of Anticancer Research
SP 967
OP 972
VO 21
IS 6
A1 C. MAGKOU
A1 E. MYLONA
A1 I. THEOHARI
A1 I. GIANNOPOULOU
A1 E. PAPANIKOLAOU
A1 S. MARKAKI
A1 L. NAKOPOULOU
YR 2007
UL http://iv.iiarjournals.org/content/21/6/967.abstract
AB Background: Akt is a serine/threonine kinase which is fully activated when phosphorylated (pAkt). The aim of this study was to investigate the expression pattern of phosphorylated Akt at Threonine 308 [pAkt(Thr308)] in association with clinicopathological parameters and various biological markers. Materials and Methods: Immunohistochemistry was performed on paraffin-embedded tissue specimens from 152 invasive breast carcinomas to detect the expression of the proteins pAkt(Thr308), estrogen (ER) and progesterone (PR) receptors, p53, Ki-67 and c-erbB-2. Results: pAkt(Thr308) protein was immunodetected in the cytoplasm and the nuclei of the malignant cells. pAkt was found to be positively associated with the lobular histological type, while it was found to exert no impact on patients' survival. pAkt(Thr308) immunopositivity was inversely related to Ki-67 and p53 (p=0.013 and p=0.020, respectively), while being positively associated with cerbB2 expression (p=0.005). Conclusion: This is the first study to show a frequent detection of pAkt(Thr308) in lobular breast carcinomas and an association of its expression with indices of proliferation (c-erbB2, Ki-67) and apoptosis (p53). Copyright © 2007 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved