The search for and exploitation of efficient catalytic systems for selective conversion of furfural into various high value-added chemicals remains a huge challenge for green synthesis in the chemical industry. Here, novel Pt nanoparticles supported on bamboo shoot-derived porous heteroatom doped carbon materials were designed as highly active catalysts for controlled hydrogenation of furfural in aqueous media. The porous heteroatom doped carbon supported Pt catalysts were endowed with a large surface area with a hierarchical porous structure, a high content of nitrogen and oxygen functionalities, a high dispersion of the Pt nanoparticles, good water dispersibility and reaction stability. Benefiting from these features, the novel Pt catalysts displayed a high activity and controlled tunable selectivity for furfural hydrogenation to produce furfuryl alcohol and cyclopentanone in water. The product selectivity could be easily modulated by controlling the carbonization temperature of the porous heteroatom doped carbon support and the reaction conditions (temperature and H pressure). Under mild conditions (100 °C, 1 MPa H), furfuryl alcohol was obtained in water with complete conversion of the furfural and an impressive furfuryl alcohol selectivity of >99% in the presence of Pt/NC-BS-500. A higher reaction temperature, in water, favored rearrangement of the furfural (FFA) with Pt/NC-BS-800 as the catalyst, which resulted in a high cyclopentanone yield of >76% at 150 °C and 3 MPa H. The surface properties and pore structure of the heteroatom doped carbon support, adjusted using the carbonization temperature, might determine the interactions between the Pt nanoparticles, carbon support and catalytic reactants in water, which in turn could have led to a good selectivity control. The effect of different reaction temperatures and reaction times on the product selectivity was also explored. Combined with exploration of the distribution of the reaction products, a reaction mechanism for furfural reduction has been proposed.

d-Catenin is the only member of the p120 catenin (p120ctn) subfamily that its primary expression is restricted to the brain. Since d-catenin is upregulated in human lung cancer, the effects of d-catenin overexpression in lung cancer still need to be clarified. Immunohistochemistry was performed to investigate the expression of d-catenin and Kaiso, a d-catenin-binding transcription factor, in 151 lung cancer specimens. A correlation between cytoplasmic d-catenin and Kaiso expression was also associated with high TNM stage, lymph node metastases and poor prognosis. Co-immunoprecipitation assay confirmed the interactions of d-catenin and Kaiso in lung cancer cells. In addition, gene transfection and RNAi technology were used to demonstrate that increased d-catenin expression was promoted, whereas its knockdown suppressed its lung cancer invasive ability. In addition, methylation-specific PCR and ChIP assay demonstrated that d-catenin could regulate MTA2 via Kaiso in a methylation-dependent manner, while it could regulate cyclin D1 and MMP7 expression through Kaiso in a sequence-specific manner. In conclusion, a d-catenin ⁄ Kaiso pathway exists in lung cancer cells. Increased d-catenin expression is critical for maintenance of the malignant phenotype of lung cancer, making d-catenin a candidate target protein for future cancer therapeutics. (Cancer Sci 2011; 102: 95-103) p 120 catenin (p120ctn) plays an important role in tumor progression and metastasis of non-small-cell lung cancer (NSCLC).(1,2) It is an Armadillo protein, which was first identified as a tyrosine kinase substrate implicated in cell transformation by Src.(3) It can bind to the juxtamembrane domain (JMD) of E-cadherin (4,5) where it modulates cell-cell adhesion by regulating cadherin turnover and stability at the cell surface.(6-8) In addition, p120ctn can bind directly with Kaiso, a transcription factor, (9) implicating a role for p120ctn in the regulation of transcriptional activity in addition to its cell-cell adhesion function.As a binding factor of p120ctn, Kaiso is a member of the BTB ⁄ POZ (Broad complex, Tramtrak, Bric à brac ⁄ Pox virus and zinc finger) subfamily of zinc finger proteins. It has the characteristic POZ domain at its amino-terminus where it facilitates Kaiso homodimerization and heterodimerization with diverse proteins, (10) while the zinc finger domain at the carboxyl terminal of Kaiso is responsible for DNA association.(11) Unlike any of the previously characterized POZ proteins, Kaiso could recognize both sequence-specific DNA consensus (KBS, TCCTGCNA) and methylated CpG-dinucleotides.(12,13) As a transcription repressor, (14) the majority of candidate Kaiso target genes identified thus far, that is, CDH1 (E-cadherin), MMP7, MTA2 and Wnt11, have been linked with development and ⁄ or cancer. (15) d-Catenin is an adhesive junction associated protein, (16,17) which is the only member of the p120ctn subfamily and its primary expression is restricted to the brain. Initially, it was widely accepted that d-catenin is the only m...

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