Objective. To delineate the expression of transforming growth factor ␤-inducible gene h3 (␤IG-H3) in rheumatoid synovitis and to determine the regulatory role of ␤IG-H3 in the adhesion and migration of fibroblast-like synoviocytes (FLS).Methods. Synovial tissue was obtained from patients with rheumatoid arthritis (RA) during joint replacement surgery, and FLS were isolated using enzymatic treatment. Immunohistochemical staining was performed to show the expression of ␤IG-H3 within rheumatoid synovium. Synthesis of ␤IG-H3 from FLS was determined by semiquantitative reverse transcription-polymerase chain reaction, Western blot analysis, and enzyme-linked immunosorbent assay. Cell adhesion and migration assays were performed using the YH18 peptide in the fourth fas-1 domain of ␤IG-H3 and function-blocking antibodies to integrins.Results. Expression of ␤IG-H3 was up-regulated in RA synovial tissue compared with synovial tissue from patients with osteoarthritis. FLS isolated from RA synovial tissue constitutively produced ␤IG-H3, which was up-regulated by transforming growth factor ␤1, interleukin-1␤, and tumor necrosis factor ␣. Although FLS expressed a variety of integrins, ␤IG-H3 mediated adhesion and migration of FLS through interaction with ␣v␤3 integrin. Cytokines failed to affect the ␤IG-H3-mediated adhesion. However, migration of FLS guided by ␤IG-H3 was enhanced by interferon-␥ and plateletderived growth factor type BB. The YH18 peptide in the fourth fas-1 domain of ␤IG-H3 inhibited adhesion and migration in a dose-dependent manner. Conclusion.The results suggest that ␤IG-H3, which is abundantly expressed in RA synovial tissue, plays a regulatory role in chronic destructive inflammation through the modulation of the adhesion and migration of FLS. This finding indicates the relevance of ␤IG-H3 and ␣v␤3 integrin-interacting motifs as potential therapeutic targets in this disease.

EC: Endometrial cancer; 3'-UTR: 3'-untranslated regions; TPX2: target protein for Xenopus kinesin-like protein 2; TCGA: the Cancer Genome Atlas; UCEC: uterine corpus endometrial carcinoma; CCK-8: cell counting kit-8; OD: optical density; FCM: flow cytometry; EMT: epithelial-mesenchymal transition.

) is a multifunctional carbohydrate-binding protein associated with cell migration, cell proliferation, cell adhesion, and cell-cell interaction in tumor cells. It has been implied to be involved in the tumor progression and chemoresistance of epithelial ovarian cancer (EOC). However, it is unclear whether the Gal-3-mediated regulation on the EOC chemosensitivity is associated with hypoxia or mitochondrial dysfunction. In the present study, we examined the regulation by Gal-3 overexpression on cisplatin-sensitivity or cisplatin-resistance in EOC cells in vitro. We manipulated Gal-3 via plasmid transfection and RNA interference in the cisplatin-resistant EOC cells, and re-evaluated the sensitivity of the cisplatin-resistant EOC cells to cisplatin, with CCK-8 assay, colony forming assay, apoptosis analysis and mitochondrial function examination. Results demonstrated that galectin-3 overexpression downregulated the cisplatin sensitivity in EOC OVCAR-3 cell clone, resulting in an upregulated growth and a reduced apoptosis in the cisplatin-treated OVCAR-3 cells. On the other hand, the Gal-3 knockdown with Gal-3-specific siRNA transfection aggravated cisplatin-induced apoptosis in OVCAR-3 cells. In conclusion, Galectin-3 reduces the sensitivity of ovarian cancer cells to cisplatin via regulating cisplatin-induced mitochondrial dysfunction. Galectin-3 knockdown inhibits the chemo-resistance of EOC cells. It implies that Galectin-3 might be a potential target to overcome the chemo-resistance in EOC cells.

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