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Tumor Biology |
2 Chain Monomer in Invading Gastric Carcinoma Cells1
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Yokohama 244-0813 [N. K., K. Mo., H. T., H. M., K. Mi.]; Department of Pathology, Yokohama City University School of Medicine, Yokohama 236-0004 [Y. N.]; and Clinical Research Institute, Kanagawa Cancer Center, Yokohama 241-0815 [S. Y.], Japan
Laminin (LN)-5, a heterotrimer of 
3, 
3, and 
2 chains, has been suggested to be involved in tumor cell invasion. The present immunohistochemical study investigated the distribution of the LN 2 chain in 48 different human gastric adenocarcinomas. The immunohistochemical analysis showed two distinct patterns of LN 2 chain expression: (a) extracellular deposition; and (b) cytoplasmic accumulation. The extracellular deposition of the LN 2 chain was typically observed at neoplastic basement membranes of well-differentiated adenocarcinomas. The immunoreactivity was continuous along tumor basement membranes in these tumors but was irregular and diffuse in poorly differentiated carcinomas. These tumor cells coexpressed the LN 3 and 3 chains, suggesting that the LN 2 chain was deposited as the LN-5 complex. In contrast, tumor cells at the invading fronts showed strong cytoplasmic staining for the LN 2 chain without any detectable signal for the LN 3 or 3 chain in both well- and poorly differentiated carcinomas. On the other hand, in vitro analysis by two-dimensional SDS-PAGE demonstrated that human gastric carcinoma cells secrete a high level of LN 2 chain monomer in addition to the LN-5 complex into culture medium. These results indicate that the LN 2 chain can be secreted as a single subunit and might be involved in tumor cell invasion.
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