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The laminin γ2 chain, a subunit of laminin‐332 (α3β3γ2), is a molecular marker for invasive cancer cells, but its pathological roles in tumor progression remain to be clarified. It was recently found that the most N‐terminal, domain V ( dV ) of γ2 chain has activities to bind  CD 44 and stimulate tumor cell migration and vascular permeability. In the present study, we prepared a  mA b recognizing γ2  dV . Immunoblotting with this antibody, for the first time, showed that proteolytic fragments containing  dV  in a range of 15–80  kD a were highly produced in various human cancer cell lines and lung cancer tissues. In immunohistochemistry of adenocarcinomas and squamous cell carcinomas of the lung, this antibody immunostained the cytoplasm of invasive tumor cells and adjacent stroma much more strongly than a widely used antibody recognizing the C‐terminal core part of the processed γ2 chain. This suggests that the  dV  fragments are highly accumulated in tumor cells and stroma compared to the processed γ2 protein. The strong tumor cell staining with the  dV  antibody correlated with the tumor malignancy grade. We also found that the laminin β3 and α3 chains were frequently overexpressed in tumor cells and tumor stroma, respectively. The cytoplasmic  dV  detection was especially prominent in tumor cells infiltrating stroma, but low in the cells surrounded by basement membranes, suggesting that the active tumor–stroma interaction is critical for the aberrant γ2 expression. The present study suggests important roles of laminin γ2 N‐terminal fragments in tumor progression.

Highly sensitive detection of invasive lung cancer cells by novel antibody against amino‐terminal domain of laminin γ2 chain