Integrin-linked kinase (ILK) has been implicated in the development and progression of several human
malignancies. Previous in vitro studies also implicate ILK in the activation of Akt and
beta-catenin as well as in the regulation of
E-cadherin expression. However, the role of ILK in human
laryngeal cancer and its possible in vivo downstream effectors in the disease are currently unknown. We examined by immunohistochemistry the
protein expression of ILK, phosphorylated-Akt (p-Akt),
E-cadherin, and
beta-catenin in 97 invasive squamous laryngeal
carcinomas. Increased cytoplasmic and nuclear expression of ILK and p-Akt decreased membranous expression of
E-cadherin and nuclear accumulation of
beta-catenin was found in 87.6%, 85.6%, 71.1%, and 43.3% of cases, respectively. Our results suggest that ILK expression may be implicated in human laryngeal
carcinoma and its localization in the nucleus possibly proposes novel nuclear functions of this molecule. In addition, enhanced ILK expression correlates with activation of Akt but not with downregulation of
E-cadherin and activation of
beta-catenin. Finally, in our material while activated Akt seems to characterize well-differentiated
tumors, loss of
E-cadherin and activation of
beta-catenin correlated with high grade
carcinomas.