Focal adhesion kinase (FAK), a non-receptor tyrosine kinase protein, acts as an early modulator of integrin signaling cascade, regulating basic cellular functions. In transformed cells, unopposed FAK signaling has been considered to promote tumor growth, progression and metastasis. The aim of this study was to assess the role of FAK in human gastric carcinoma cells. SGC-7901 cells were transfected with PGPU6/GFP/shNC (shNC), PGPU6/GFP/FAK-299 (shRNA-299), respectively. Expression of FAK was detected by real-time PCR and Western blots. MTT assay was used to examine changes in cell proliferation. Cell apoptosis was analyzed by flow cytometry. The expression of caspase-3, -9 was measured by Western blots. The expression of FAK in SGC-7901 cells significantly decreased in shRNA-299 group contrast to the control group (P < 0.01). Cells proliferation was inhibited by shRNA-299 and shRNA-299 + cisplatin, and the effects were clearly enhanced when cells treated with the anticancer agents. The level of cell apoptosis in shRNA-299 and shRNA-299 + cisplatin group was higher than in the control group (P < 0.01). The current data support evidence that down-regulation of FAK could induce human gastric carcinoma cells (SGC-7901) apoptosis through the caspase-dependent cell death pathway. Inhibition of the kinases may be important for therapies designed to enhance the apoptosis in gastric carcinoma.