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  • 1
    Publication Date: 2013-07-10
    Description: p27 Kip1 is a key cell cycle regulator whose level is primarily regulated by the ubiquitin-proteasome degradation pathway. Its β1 subunit is one of seven β subunits that form the β-ring of the 20S proteasome, which is responsible for degradation of ubiquitinated proteins. We report here that the β1 subunit is up-regulated in esophageal cancer tissues and some ovarian cancer cell lines. It promotes cell growth and migration, as well as colony formation. β1 binds and degrades p27 Kip1 directly. Interestingly, the lack of phosphorylation at S158 of the β1 subunit promotes degradation of p27 Kip1 . We therefore propose that the β1 subunit plays a novel role in tumorigenesis by degrading p27 Kip1 .
    Print ISSN: 0144-8463
    Electronic ISSN: 1573-4935
    Topics: Biology , Chemistry and Pharmacology
    Published by Portland Press
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  • 2
    Publication Date: 2014-10-09
    Description: Peptide-N4-( N -acetyl-α-glucosaminyl) asparagine amidases (PNGases, N -glycanases, EC 3.5.1.52) are essential tools in the release of N -glycans from glycoproteins. We hereby report the discovery and characterization of a novel bacterial N -glycanase from Terriglobus roseus with an extremely low pH optimum of 2.6, and annotated it therefore as PNGase H + . The gene of PNGase H + was cloned and the recombinant protein was successfully expressed in E. coli. The recombinant PNGase H + could liberate high mannose-, hybrid-, and complex- type N -glycans including core α1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. In addition, PNGase H + exhibited better release efficiency over N -glycans without core α1,3-fucose compared to PNGase A. The facile expression, non-glycosylated nature, unusual pH optimum and broad substrate specificity of this novel type of N -glycanase makes recombinant PNGase H + a versatile tool in N -glycan analysis.
    Print ISSN: 0144-8463
    Electronic ISSN: 1573-4935
    Topics: Biology , Chemistry and Pharmacology
    Published by Portland Press
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  • 3
    Publication Date: 2013-03-15
    Description: Mesenchymal stem cells (MSCs) are a stem cell source that can be easily obtained from bone marrow. Despite the increasing importance of the pig as a large animal model, little is known about foetal porcine mesenchymal stem cells (pMSCs). In this study, we observed the gene expression of pluripotent markers in foetal pMSCs and the capacity of pMSCs to differentiate into adipocytes, osteocytes and neural-like cells using quantitative reverse transcription polymerase chain reaction (RT-PCR), normal histological staining and immunohistochemistry. Foetal pMSCs have either a spindle or a flattened shape, and flow cytometry revealed the expression of the MSC related proteins CD44 and CD105 (endoglin) but not CD34 and CD45. pMSCs express pluripotent markers such as octamer-binding transcription factor 4 (Oct4) and Nanog at the protein and mRNA levels. qRT-PCR analyses revealed that pMSCs expressed nestin (for neural stem cells, NSCs). Immunocytochemical and RT-PCR data showed that 29% and 23% of pMSCs expressed microtubule-associated protein 2 (MAP2 for neurons) and beta tubulin III (Tuj1 for immature neurons), respectively, after induction of neural differentiation. These findings demonstrate the plasticity of pMSCs and their potential for use in cellular replacement therapy for neural diseases.
    Print ISSN: 0144-8463
    Electronic ISSN: 1573-4935
    Topics: Biology , Chemistry and Pharmacology
    Published by Portland Press
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