Expression of the cell adhesion molecule, epithelial nism. The transmembrane linker glycoprotein that cadherin (E-CD) and its binding proteins, a-and b-caten-mediates this adhesion is thought to be epithelial cadins, in normal liver, chronic liver diseases, and hepatoherin (E-CD), the homophilic interaction of which links cellular carcinomas (HCCs) was investigated immunoadjacent cells. 4 E-CD is a member of the cadherin famhistologically. In normal liver, weak immunostaining of ily that is involved in Ca 2/ -dependent cell-cell adhesion E-CD and catenins was observed at the lateral memin vertebrate tissues. 5 Regulated E-CD expression fabranes of the hepatocytes, whereas at the interlobular cilitates several epithelial morphogenetic events, inbile duct epithelia, they stained strongly. No immunorecluding cell migration, separation of different cell layactions were seen in sinusoidal Kupffer cells. Similar ers, formation of boundaries between cell layers, and results were observed in the majority of livers from differentiation of each cell layer into functionally dischronic hepatitis and cirrhosis sufferers; however, hepatocytes undergoing regeneration and rosette formation, tinct structures. In rat livers, it is suggested that Eas well as Hering canals and proliferating ductules, CD may be a fundamental factor in hepatocyte polarity showed markedly increased molecular expression. Analformation and in shaping hepatic plates during embryysis of 66 HCC lesions revealed that the majority (64.3onic development. 6 However, the physiological roles 96.6%) of thin trabecular-and pseudoglandular-type tuand distribution of E-CD in human liver are still poorly mors preserved or overexpressed E-CD and catenins, understood.
whereas thick trabecular-type HCCs frequently showed
Recent studies have shown that the full adhesive low E-CD and a-catenin expression (56.5-65.2% reducfunction of E-CD is expressed only when it is complexed tion), suggesting that the thick trabecular histology represented diffuse tumor cell growth. Likewise, the E-CD via a specific cytoplasmic binding domain with three and catenin expression levels correlated with the HCC cytosolic proteins, termed a-, b-, and g-catenins. 7,8 Cacell differentiation grades. These collective results inditenins mediate connection of E-CD to the actin filament cate that intercellular adhesion mediated by the E-CDnetwork and link E-CD to other transmembrane procatenin system plays a role in morphological changes in teins, such as Na / /K / adenosine triphosphatase, and nonmalignant and malignant hepatic diseases. (HEPAto peripheral cytoplasmic proteins, such as fodrin.