O solve structure: SHELXS97 (Sheldrick, 2008); system(s) applied to refine structure
O solve structure: SHELXS97 (Sheldrick, 2008); program(s) applied to refine structure: SHELXL97 (Sheldrick, 2008); molecular graphics: ORTEP-3 for Windows (Farrugia, 2012)and PLATON (Spek, 2009); software employed to prepare material for publication: WinGX (Farrugia, 2012).Associated literatureFor the functionalization of camphor, see: Jennings Herschbach (1965); Pastran et al., (2011). For transition metal complexes of camphor, see: Spannenberg et al. (2002); Harrad et al. (2010); Ait Ali et al. (2006); Gaudo et al. (2011). For ringpuckering parameters, see: Cremer Pople (1975).The authors thank Professor Daniel Avignant for the X-ray measurements.Supplementary data and figures for this paper are offered from the IUCr electronic archives (Reference: BT6921).
Wang et al. BMC Cancer 2014, 14:442 http:biomedcentral1471-240714RESEARCH ARTICLEOpen AccessSrc-homology 2 domain-containing tyrosine phosphatase two promotes oral cancer invasion and metastasisHsueh-Chun Wang1,two, Wei-Fan Chiang3, Hsin-Hsiu Huang4, Ying-Ying Shen5 and Hung-Che Chiang4,6AbstractBackground: Tumor invasion and metastasis represent a significant unsolved dilemma in cancer pathogenesis. Current research have indicated the involvement of Src-homology 2 domain-containing tyrosine phosphatase two (SHP2) in numerous malignancies; nevertheless, the role of SHP2 in oral cancer progression has however to become elucidated. We propose that SHP2 is involved inside the progression of oral cancer toward metastasis. Techniques: SHP2 expression was evaluated in paired oral cancer tissues by using immunohistochemical staining and real-time reverse transcription polymerase chain reaction. Isogenic extremely invasive oral cancer cell lines from their respective low invasive parental lines had been established making use of a Boyden chamber assay, and changes within the hallmarks with the epithelial-mesenchymal transition (EMT) were assessed to evaluate SHP2 function. SHP2 activity in oral cancer cells was decreased making use of si-RNA knockdown or enforced expression of a catalytically deficient mutant to analyze migratory and invasive ability in vitro and metastasis toward the lung in mice in vivo. Benefits: We observed the important upregulation of SHP2 in oral cancer tissues and cell lines. Following SHP2 knockdown, the oral cancer cells markedly attenuated migratory and invasion potential. We observed related results in phosphatase-dead SHP2 C459S mutant expressing cells. Enhanced invasiveness was connected with considerable upregulation of E-cadherin, vimentin, SnailTwist1, and matrix metalloproteinase-2 inside the extremely invasive clones. Furthermore, we determined that SHP2 activity is necessary for the downregulation of phosphorylated ERK12, which modulates the downstream effectors, Snail and Twist1 at a transcript level. In lung tissue sections of mice, we observed that HSC3 tumors with SHP2 deletion exhibited drastically lowered metastatic capacity, compared with tumors administered handle si-RNA. Conclusions: Our information CYP2 review suggest that SHP2 promotes the invasion and metastasis of oral cancer cells. These final results supply a rationale for further investigating the effects of small-molecule SHP2 inhibitors around the progression of oral cancer, and indicate a previously unrecognized SHP2-ERK12-SnailTwist1 pathway that may be HDAC10 Storage & Stability likely to play a critical part in oral cancer invasion and metastasis. Keywords: Extracellular signal-related kinase, Invasion, Metastasis, Oral cancer, Src-homology 2 domain-containing tyrosine phosphatase Correspondence: hcchiangnhri.org.t.