Objective To explore the a effects of integrin-β1 during the process of laminin (LN) promoting Schwann cells (SCs) to synthesis extracellular matrix （ECM）. Methods SCs were obtained from 10 SD rats and cultured EM>in vitro/EM>. After the treatment with ectogenic LN, double fluorescence immunocytochemical staining was performed to observe the expression of LN and integrin-β1 in SCs and the phosphorylation of focal adhesion kinase (FAK) was examined by Western blotting. The SCs surface receptor integrin-β1 was blocked by using Ha2/5 antibody and after the treatment with ectogenic LN, Western blotting was performed to observe the phosphorylation of FAK in SCs and the expression of components of ECM including LN, nidogen and type IV collagen were observed by fluorescence immunocytochemical staining. Results After the treatment with ectogenic LN, SCs had positive coexpression of LN and integrin-β1 and the phosphorylation of FAK was increased. After blocking the SCs surface receptor integrin-β1, phosphorylation of FAK was descended, but the positive expression of LN, nidogen and type IV collagen was not decreased. Conclusion LN can combine with SCs surface receptor integrin-β1 and in