COL1A1 expression induced by overexpression of both a 15‑amino acid peptide from the fibrinogen domain of tenascin‑X and integrin α11 in LX‑2 cells.

Abstract

Extracellular matrix tenascin‑X (TNX) is the largest member of the tenascin family. Our previous study demonstrated that TNX was involved in hepatic dysfunction, including fibrosis, in mice that were administered a high‑fat and high‑cholesterol diet with high levels of phosphorus and calcium. The present study investigated whether overexpression of both the fibrinogen domain of TNX (TNX‑FG) and integrin α11, one of the TNX cell surface receptors, induces invitro fibrosis in LX‑2 human hepatic stellate cells. Overexpression of both a 15‑amino acid peptide (hTNX‑FGFFFF) derived from the TNX‑FG domain and integrin α11 induced the expression of typeI collagen α1 chain (COL1A1). Treatment with verteporfin [YAP (Yes‑associated protein) inhibitor] attenuated the elevated COL1A1 expression elicited by overexpression of both hTNX‑FGFFFF and integrin α11. In addition, small interfering RNA‑mediated knockdown of YAP1 resulted in a decrease in COL1A1 expression induced by overexpression of both hTNX‑FGFFFF and integrin α11. These results indicated that overexpression of both hTNX‑FGFFFF and integrin α11 induced COL1A1 expression via the YAP signaling pathway.