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The fibroblast activation protein (FAP) is a cell surface serine proteasewhich has emerged as a specific marker of tumor-associated fibroblasts (TAFs).FAP has been shown to have both in vitro dipeptidyl peptidase and collagenaseactivity. However, the biological function of FAP in the tumor microenvironmentis largely unknown. In this study, we first show that TAFs isolated from ovariancancer samples have the characteristics of stem cells. To explore the functionalrole of FAP, the protein was silenced by siRNA lentiviral vector transfection.FAP silencing inhibited the growth of TAFs in vitro, accompanied with cell cyclearrest at the G2 and S phase in TAFs. FAP silencing also reduced the stem cellmarker gene expression in TAFs. SKOV3 cells do not express FAP. Although FAP-silencedSKOV3 cells induced ovarian tumors, the rate of tumor growth was significantlydecreased, as shown in the xenograft mouse model. TAF phenotypes in the xenografttumor tissues were further assayed by immunohistochemistry. The expression ofTAF markers, including fibroblast-specific protein, FAP, smooth muscle actin,desmin, vascular endothelial growth factor and fibroblast growth factor was decreasedin the tumor stroma induced by FAP-silenced SKOV3 cells. In conclusion, FAP isan important regulator of the microenvironment in tumor formation and targetingFAP is a potential therapeutic strategy to combat ovarian cancer.

Fibroblast activation protein regulates tumor-associated fibroblasts and epithelial ovarian cancer cells