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We recommend careful radiographic examination to evaluate PMF, especially in patients with distal tibial spiral fractures combined with proximal fibular fractures or intact fibulas.

When stainless steel is implanted in human bodies, the corrosion resistance and biocompatibility must be considered. In this study, first, a protective organic silicone film was coated on the surface of stainless steel by a plasma deposition technique with a precursor of hexamethyldisilazane (HMDSZ). Then, ultraviolet (UV) light-induced graft polymerization of N-isopropylacrylamide (NIPAAm) and acrylic acid (AAc) in different molar ratios were applied onto the organic silicone film in order to immobilize thermos-/pH-sensitive composite hydrogels on the surface. The thermo-/pH-sensitive composite hydrogels were tested at pH values of 4, 7.4 and 10 of a phosphate buffer saline (PBS) solution at a fixed temperature of 37 °C to observe the swelling ratio and drug delivery properties of caffeine which served as a drug delivery substance. According to the results of Fourier Transformation Infrared (FTIR) spectra and a potential polarization dynamic test, the silicone thin film formed by plasma deposition not only improved the adhesion ability between the substrate and hydrogels but also exhibited a high corrosion resistance. Furthermore, the composite hydrogels have an excellent release ratio of up to 90% of the absorbed amount after 8h at a pH of 10. In addition, the results of potential polarization dynamic tests showed that the corrosion resistance of stainless steel could be improved by the HMDSZ plasma deposition.

Phosphoglycerate kinase 1 (PGK-1) is a multifunctional protein that is involved in the glycolytic pathway and the generation of the angiogenesis inhibitor angiostatin. In a previous study, we showed that the overexpression of full-length PGK-1 in Lewis lung carcinoma (LLC-1) can reduce tumor growth in vivo by downregulation of COX-2 expression. Phosphoglycerate kinase 1 has two functional domains: a catalytic domain (CD); and a nucleotidebinding domain (NBD). To identify the functional domain of PGK-1 responsible for its antitumor effects, we evaluated the tumorigenicity of LLC-1 cells overexpressing full-length PGK-1 (LLC-1 ⁄ PGK), CD (LLC-1 ⁄ CD), and NBD (LLC-1 ⁄ NBD). Although no difference in tumor cell growth was observed in vitro, the tumor invasiveness was reduced in the LLC-1 ⁄ PGK, LLC-1 ⁄ CD, and LLC-1 ⁄ NBD cells compared to parental LLC-1 cells in vivo. In addition, in vivo tumor growth retardation by LLC-1 ⁄ CD and LLC-1 ⁄ NBD cells was observed, similar to that by LLC-1 ⁄ PGK cells. However, the reduced stability of COX-2 mRNA and downregulation of the COX-2 protein and its metabolite, prostaglandin E2, was only found in LLC-1 ⁄ PGK and LLC-1 ⁄ NBD cells. Low levels of COX-2 were also observed in the tumor mass formed by the modified cells when injected into mice. The results indicate that COX-2 suppression by PGK-1 is independent of its catalytic activity. COX-2 targeting by PGK-1 can be attributed to its NBD and is probably a result of the destabilization of COX-2 gene transcripts brought about by the mRNA-binding property of PGK-1. (Cancer Sci 2010; 101: 2411-2416 L ung cancer is the leading cause of carcinoma-related deaths worldwide, and non-small cell lung carcinoma (NSCLC) constitutes 85% of all lung cancers. Despite advances in lung cancer treatment, poor survival rates are commonly seen in patients with late-stage disease.(1) Therefore, early diagnosis and novel therapeutic approaches are urgently required. Previous studies indicated that the blocking of oncogenic signaling cascades that targeted the epidermal growth factor receptor-and COX-2-regulated pathways yielded promising results in specific subsets of lung cancers.(1,2)Phosphoglycerate kinase 1 (PGK-1), an enzyme comprising a common nucleotide-binding domain (NBD) and two unique catalytic domains (CDI and CDII), is an interesting multifunctional protein. (3,4,(5)(6)(7)(8)(9) In addition to being an essential enzyme in the glycolytic pathway, (3) PGK-1 is well known to play an inhibitory role in tumor angiogenesis by facilitating the formation of angiostatin from plasmin.(8) Moreover, PGK-1 can influence DNA replication and repair in the mammalian nucleus and stimulate viral mRNA synthesis in the cytosol.(5,6) The enzyme also serves as an mRNA-binding protein and is implicated in the negative regulation of the stability of urokinase-type plasminogen activator receptor (uPAR) mRNA.(7) The reduction in uPAR expression and cellular motility by overexpression of PGK-1 has been shown in human lung cancer cells.(7) Peptides of PGK-1 isol...

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