Gelsolin (GSN), a Ca2+-regulated actin filament severing and capping protein, is a widespread, polyfunctional regulator of cell structure and metabolism (Li et al., 2012). GSN is a widely expressed actin regulator, and has been reported to be a multifunctional regulator of physiological and pathological cellular processes, and regulates cell migration, cell morphology, proliferation and apoptosis (Sun et al., 1999; Li et al., 2012). Previous research demonstrated that GSN was prevalently expressed in a variety of cells (Tanaka et al., 2006). A previous study revealed that the levels of GSN are decreased in various cancers, including breast, urinary bladder, colon, kidney, ovary, prostate, gastric and urinary system cancer (Tanaka et al., 2006). A study presented by Zhou et al. (2015) showed that upregulated GSN inhibits apoptosis, whereas downregulated GSN promotes apoptosis, which could be associated with the regulation of GSN in the apoptosis-associated pathways and the apoptosis factors caspase 3 and bcl-2. In addition, a study showed that GSN was observed in vitro to suppress the proliferation and invasion of 786-0 renal cell carcinoma cells (Zhu et al., 2015). A previous study found that GSN in colorectal tumor cell regulates cell invasion through its modulation of the urokinase (uPA)/urokinase receptor (uPAR) cascade, with possible vital roles in colorectal tumor dissemination to metastatic sites (Zhuo et al., 2012).