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Protein kinase C mediates the signal for interferon‐γ mRNA expression in cytotoxic T cells after their adhesion to laminin

A cytotoxic T‐cell line, CTLL‐2 cells, showed spreading after adhering to extracellular matrix proteins such as fibronectin (FN), laminin (LN) and hyarulonic acid (HA). The adhesion of CTLL‐2 cells to LN was mediated by very late activation antigen‐6 (VLA‐6). Expression of interferon‐γ (IFN‐γ) mRNA was enhanced in CTLL‐2 cells, also when they adhered to extracellular matrix proteins; and the enhanced IFN‐γ mRNA expression by adhering to LN was blocked by anti‐α6 antibody. Calphostin C, a protein kinase C (PKC) inhibitor, markedly inhibited the enhancement of IFN‐γ mRNA expression in a dose‐dependent manner, which suggested that PKC acted as a second messenger in the IFN‐γ mRNA expression mediated by the interaction of VLA‐6 with LN in CTLL‐2 cells. Furthermore, confocal laser‐microscopic analysis and Western blot analysis revealed that PKC‐α was activated after CTLL‐2 cells adhered to LN. PKC activity translocated from the cytosol fraction to the particulate fraction, after CTLL‐2 cells adhered to LN. Altogether, we suggest that PKC plays an important role in the signal transduction for IFN‐γ mRNA expression after cytotoxic T cells adhere to LN.