Osteopontin’s colocalization with the adhesion molecule CEACAM5 in cytoplasm of carcinoma of tongue and its correlation with the invasion of that diease

Paraffin were sections of 80 samples with squamous carcinoma of tongue and 40 samples with normal tissue of tongue for benign lesion having undergone surgery. Immunohistochemistry (IHC) was used to study the distribution of CEACAM5 and OPN, and double–labeling immunohistochemistry was used to observe the relationship between CEACAM5 and OPN expression.CEACAM5 and OPN are found in normal tissue of tongue, but with different expression pattern. CEACAM5 expression mainly with membranous staining is restricted on the superficial epithelium. However, OPN expression with mainly cytoplasmic staining is restricted on the deep epithelium. No colocalization of CEACAM5 and OPN have been observed in normal tissue of tongue. In squamous carcinoma of tongue, CEACAM5 expression with cytoplasmic staining is different from normal tongue tissue with membranous staining, and the transformation of CEACAM5 distribution from membrane to cytoplasm is an important incident for the invasion and differentiation of tumor. CEACAM5 and OPN are colocalized in cytoplasm, and a significant correlation was observed between the positive colocalization and the negative colocalization in the depth of invasion and the differentiation of the tumor.Homeostasis in normal tissue is regulated by a balance between proliferative activity and cell loss by apoptosis [1,2]. Attachment to correct extracellular matrix (ECM) is essential for survival and growth of normal adhering cells, whereas cancer cells are able to abrogate this requirement. Several growth factors and cytokines play pivotal roles in the regulation of growth and survival of neoplastic cells through affecting integrin-mediated adhesion to ECM.Cell adhesion molecules are important mediators of cellular contacts and cellular polarity that also modulate proliferation, differentiation, and invasion. Osteopontin (OPN) is a 70-kDa secreted extracellular matrix glycoprotein with an arginine-glycine aspartate-binding motif capable of interaction with int