The protein was also found in the hepatocytes and cholangiocytes of infected Balb/c mice, possibly implying CsGRN could be internalised by various mammalian cells via an endocytotic mechanism [27–29]. Moreover, the surprising finding provided a clue about the protein pertaining to its function on interaction with host cells as an ingredient of CsESPs. According to some reports, granulin plays a central role in the carcinogenesis of a range of malignancies . For instance, PGRN is highly expressed in ovarian tumours , breast cancer , glioblastomas , and gastric cancer . Moreover, as an important mediator of tumorigenesis and wound repair, it is associated with aggressive and invasive tumour phenotypes by stimulating invasion, protecting against anoikis, and supporting tumour expansion in the unfavourable interstitial environment [34, 35]. Based on these aspects, the overexpressed-CsGRN stable cell lines named as PLC-GRN and RBE-GRN cells were successfully constructed, and the wound-healing assay and transwell assay were performed to observe the ability of the migration and invasion of CCA and HCC in vitro. The results displayed that they could stimulate cancer cell migration, which was similar to the action exerted by other recombinant proteins [36, 37]. Compared with cells co-cultured with protein, PLC-GRN and RBE-GRN cells were more approximate to the real situation that the internalised protein of this parasite might interfere with signalling and displayed the carcinogenic nature of biliary epithelial cells and hepatocytes. Likewise, Helicobacter pylori CagA protein targets PAR1/MARK kinase after delivery into gastric epithelial cells and disrupts cell polarity, resulting in disorganisation of the gastric epithelial architecture, inflammation and carcinogenesis . Furthermore, similar to lipoprotein, internalisation induced by activating the fuel-sensing enzyme adenosine monophosphate-activated protein kinase (AMPK) is crucial to maintaining glioblastoma cell growth .