Aim Heat shock protein 47 （HSP47） is a highly conservative proteint. It is considered as the pro-collagen-specific chaperone protein and plays an important function in the process of collagen deposition and fibrosis. The thesis investigates the molecular mechanisms of structural ventricular remodeling in chronic heart failure （CHF）. Methods The serum and right atrial tissues samples were taken from 60 patients with cardiac surgery. They were divided into three groups: 20 samples were in NYHA Ⅰ group, 20 samples were in NYHA Ⅱ group, 20 samples were in NYHA Ⅲ group. The mRNA amounts of HSP47 were studied by real time quantitative polymerase chain reaction （RT-PCR） method, and the HSP47 and procollagen Ⅰ carboxy terminal propeptide （PⅠCP） in serum were measured by enzyme-linked immunosorbent assay （ELISA） method. Results （1）The HSP47 mRNA level significantly increased in both NYHA Ⅱ group and NYHA Ⅲ group compared with NYHA Ⅰ group （P<0.05）. Also the mRNA level of HSP47 significantly increased in the NYHA Ⅲ group compared with NYHA Ⅱ group （P<0.05）. （2）There were conspicuous and independent direct correlation between the expression of HSP47 and the HSP47, PⅠCP levels in serum （r＝0.704, P<0.05 r＝0.811, P<0.05）. Conclusion The HSP47 mRNA level increased in CHF, and it indicates that HSP47 gene may be involved in the ventricular remodeling.