Expression and Distribution of a Human Colon-Carcinoma-Associated Antigen in Normal and Diseased Liver Tissue

Abstract

Expression and distribution of 17-1 A, a human colon-carcinoma-associated antigen as defined by a monoclonal antibody (17-1A mAb), were evaluated in liver tissues from normal subjects and patients with inflammatory and noninflammatory liver diseases. The antigen recognized by 17-1A mAb is a 41-kD protein that does not belong to the proteins of the cytoskeleton. Using a streptavidin-biotin-peroxidase method on frozen sections of liver tissue, it was located in the cytoplasm of bile duct epithelial cells in normal livers, whereas the hepatocytes were completely unreactive. When diseased liver tissue was examined, a strong 17-1A Ag expression was demonstrable in the epithelium of typical and atypical bile ductules in portal areas. In addition, periportal or periseptal hepatocytes revealed variable staining for 17-1A Ag directly related to acute and chronic inflammatory changes. 17-1A Ag expression in hepatocytes reached the highest frequency in acute hepatitis (5/5) and chronic active hepatitis (17/19). These results indicate that periportal hepatocytes are capable of acquiring antigen expression common to bile ductular cells in inflammatory liver diseases, further supporting the view that these ductules represent transformed hepatocytes. Furthermore, two distinct pictures were found in primary liver malignancies. Neoplastic bile duct epithelium did not maintain 17-1A Ag expression in cholangiocarcinoma, whereas neoplastic liver cells acquired cytoplasmic 17-1A Ag expression in clustered areas in hepatocellular carcinoma and the intensity of staining and antigen distribution were inversely related to the grade of tumor differentiation.

Immunohistochemical study on phenotypical changes of hepatocytes in liver disease with reference to extracellular matrix composition

“…Expression of biliary antigens on hepatocytes has been shown by immunohistochemical staining for CEA (2 l), epithelial membrane antigen (21), and cytokeratins (10,22). A previous study, using a monoclonal antibody for colon-carcinoma-associated antigen, is in agreement with these results (23). However, EGP is not expressed on bile canaliculi and might be different from their molecule.…”

The Epithelial Cell Adhesion Molecule (Ep-CAM) as a Morphoregulatory Molecule Is a Tool in Surgical Pathology

“…Furthermore, Ep-CAM differentiated between HCC and metastatic adenocarcinoma from the colon, lung, breast, pancreas, small intestine, kidney, or ovary. 37,38 However, according to Sansonno and Dammacco, 36 neoplastic bile duct epithelium did not react for Ep-CAM (mAb17-1A) in cholangiocarcinoma, whereas neoplastic liver cells acquired cytoplasmic-positive staining in clustered areas in HCC. The intensity of staining and Ep-CAM distribution were inversely related to the grade of tumor differentiation.…”

“…Diseased liver tissue displayed a strong Ep-CAM expression (mAb 17-1A) in the epithelium of typical and atypical bile ducts. 36 In addition, periportal or periseptal hepatocytes revealed variable staining of Ep-CAM, which is directly related to acute and chronic inflammatory changes. The Ep-CAM expression in hepatocytes was most pronounced in acute and chronic active hepatitis, with Ep-CAM expression levels that are common to bile ductular cells.…”

Capturing Cancer: Emerging Microfluidic Technologies for the Capture and Characterization of Circulating Tumor Cells

“…Immunoaffi nity purifi cation has long been employed in the investigation of CTCs because of the specifi c binding between antibody and the antigen expressed on the surfaces of CTCs. [57][58][59][60][61][62][63][64][65][66][67][68][69] The most fascinating merit of using antibodies is that it increases the specifi city of the captured CTCs and improves the isolation purity. Basically, most positive isolation methods achieve CTC enrichment by utilizing the specifi c binding of CTCs to antibodies attached on microchannels or various microstructures in microfl uidic chips.…”

“…Immunoaffinity purification has long been employed in the investigation of CTCs because of the specific binding between antibody and the antigen expressed on the surfaces of CTCs . The most fascinating merit of using antibodies is that it increases the specificity of the captured CTCs and improves the isolation purity.…”