PSTAT1 and subsequent antigen processing machinery componentmediated immune escape in head and neck cancer cells [24], suggesting that SHP2 is often targeted to enhance Tcellbased cancer immunotherapy. All round, these findings emphasize the possible use of SHP2 as a remedy target for oral cancer.Conclusions In this study, we report that SHP2 is a possible target for oral cancer remedy. We overexpressed SHP2 in oral cancer cells, and attenuated SHP2 to observe reduced invasion and metastasis. Our result indicated that the downregulatory effects of SHP2 on ERK1/2 may regulate Snail/Twist1 mRNA expression and play a critical function in oral cancer invasion and metastasis. These findings supply a rationale for future investigation in to the effects of smallmolecule SHP2 inhibitors on oral cancer progression, and may facilitate the improvement of novel treatments for human oral cancer. Extra filesAdditional file 1: Suplemetary supplies and Solutions. Further file two: Figure S1. SHP1 transcriptional level will not be associated with very invasive capacity in oral cancer cells. No significant distinction in SHP1 transcript was observed among parent and highly invasive clones derived from HSC3 cells. The expression of SHP1 for HSC3Inv4 and HSC3Inv8 was normalized to HSC3 parental cells. Information are representative of 3 independent experiments. Additional file 3: Figure S2. SHP2 catalyticdefective expressing cells showed enhanced tyrosine phosphorylation of protein. The cells expressing SHP2 wild variety or C/S mutant have been lysed, and subjected toWang et al.374791-02-3 Order BMC Cancer 2014, 14:442 http://www.4-Aminomethylbenzylalcohol supplier biomedcentral.PMID:23903683 com/14712407/14/Page 12 ofimmunoblotting with antiphosphotyrosine. Information are representative of 3 independent experiments. Extra file four: Figure S3. Profile of SHP2 activity in oral cancer cell lines (OC3, OECM1, HSC3, and SCC4). Experiments have been done in triplicate no less than, and values are indicated as imply SD. HOK, regular cells. Extra file 5: Figure S4. SHP2 negatively regulates EGFR activity in oral cancer cells. Total cell lysates were prepared, and SHP2 was immunoprecipitated from HSC3 cells expressing EGFPtagged SHP2 wild form or catalyticdefective SHP2 (SHP2C/S). SHP2 in association with active EGFR in these cells was detected by SDSPAGE and immunoblotting with antiphosphoEGFR, EGFR, and SHP2. GAPDH as loading manage. Information are representative of 3 independent experiments. Abbreviations ERK: extracellular signalrelated kinase; PARP: Poly ADPribose polymerase; SHP2: Srchomology two domaincontaining tyrosine phosphatase 2. Competing interests No potential conflicts of interest have been disclosed. Authors’ contributions HCW designed the study, conducted experiments, analyzed and interpreted information and wrote the manuscript. WFC ensured protocol integrity and collected data. HHH performed experiments and collected information. YYS analyzed and interpreted information. HCC reviewed the manuscript. All authors read and approved the final manuscript. Acknowledgements This work was supported by a grant from National Health Analysis Institutes, Taiwan (00A1EOPP11014). We are grateful for the Taiwan Mouse Clinic (NSC 1022325B001042) which can be funded by the National Study System for Biopharmaceuticals (NRPB) in the National Science Council (NSC) of Taiwan for technical assistance in capturing tissue images. We thank Dr. LuHai Wang’s laboratory for the technical assistance, and Dr. ShauKu Huang and Dr. AihCheun Lee for their critically reading this manuscri.