Publications by authors named "C Ngamkitidechakul"

Phyllanthus emblica Linn. (PE) is a medicinal fruit used in many Asian traditional medicine systems for the treatment of various diseases including cancer. The present study tested the potential anticancer effects of aqueous extract of PE in four ways: (1) against cancer cell lines, (2) in vitro apoptosis, (3) mouse skin tumourigenesis and (4) in vitro invasiveness.

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Aim: To examine the growth inhibitory effects of Phyllanthus emblica (P. emblica) and Terminalia bellerica (T. bellerica) extracts on human hepatocellular carcinoma (HepG2), and lung carcinoma (A549) cells and their synergistic effect with doxorubicin or cisplatin.

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A prominent feature of all cancers including oral carcinoma is an abnormality in cellular proliferation. Neural precursor cell-expressed developmentally down-regulated 8 (NEDD8) is a ubiquitin-like protein exerting its biological function through covalent ligation to a family of cullin proteins, which act as a component of the Skp1, cullin, and F-box protein complex that plays a critical role in the regulation of cell cycle. Using Western blot analysis, an increase in NEDD8 conjugation was observed in all highly proliferative cells, including immortalized normal oral keratinocyte (NOK), oral-derived carcinoma (KB, HSC4), and several types of human carcinoma cell lines as compared to normal human gingival fibroblast.

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Maspin, an ov-serpin, inhibits tumor invasion and induces cell adhesion to extracellular matrix molecules. Here, we use maspin/ovalbumin chimeric proteins and the maspin reactive site loop (RSL) peptide to characterize the role of the RSL in maspin-mediated functions. Replacement of the RSL plus the C-terminal region or the RSL alone of maspin with that of ovalbumin resulted in the loss of the stimulatory effect on adhesion of corneal stromal cells to type I collagen, fibronectin, and laminin and of mammary carcinoma MDA-MB-231 cells to fibronectin.

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Expression of recombinant proteins using a secretion system can minimize co-purification of contaminating host proteins. Production of His-tagged recombinant proteins in the yeast alpha-factor secretion system has previously required a fermenter system to control the growth conditions such as pH of the yeast culture. We describe an inexpensive non-fermenter system for the production of secreted recombinant His-tagged proteins in Saccharomyces cerevisiae that uses a buffered low peptone YP glycerol medium, which does not interfere with immobilized metal affinity chromatography.

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