Explores the effects of fatty acid-binding protein-5 deficiency on cell motility in ocular cells, suggesting a novel regulatory pathway in wound healing.
Fatty acid binding protein-5 (FABP5) is a multifaceted protein involved in various cellular processes, such as fatty acid uptake, migration, invasion, cell growth, survival, and inflammation. However, the role of intracellular FABP5 in ocular cells remains limited. Therefore, this study explored the regulatory role of intracellular FABP5 in healing capacity of human corneal epithelial cells (HCEs) through in vitro experimental methods. Intracellular FABP5 was silenced in HCEs through lentivirus-based silencing system and puromycin selection, thereby obtaining stable FABP5-deficient cells. Cell viability was analyzed using CCK-8 reagent, and cell migration was monitored by real-time ASTEC migration system and analyzed by InForm software. The expression of genes and proteins was determined by next-generation sequencing (NGS) analysis and immunoblotting, respectively. The regulatory relationship among genes and proteins was analyzed by ingenuity pathway analysis (IPA) software. There was no difference in the morphology of mock and FABP5-silenced HCEs. According to NGS analysis, 317 of the FABP5 silencing-altered genes are associated with wound healing in general lesions. Silencing of intracellular FABP5 suppressed cell proliferation and cell migration in HCEs. In terms of protein changes, silencing FABP5 reduced the expression of Bcl-xL, Fibulin-1, MMP1, MMP9, p-NFκB, and p-RIP3. In contrast, silencing FABP5 increased the expression of Akt-1, Bcl-2, cleaved caspase-3, MKP-1, Smurf2, Sumo1, Sumo4, Survinin, p-FAK, p-p38, p-p53, p-PTEN, p-Rac1, and RIP3. The results indicated that intracellular FABP5 plays a negative regulatory role in corneal wound healing by disrupting the balance of multiple regulatory mechanisms. This abstract was presented at the American Physiology Summit 2026 and is only available in HTML format. There is no downloadable file or PDF version. The Physiology editorial board was not involved in the peer review process.
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