Analysis of interaction of tumor suppressor gene, Nm23, with molecular chaperon in an oral cancer cell
| Project/Area Number |
18592044
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional basic dentistry
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| Research Institution | Iwate Medical University |
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Principal Investigator |
KAMO Masaharu Iwate Medical University, School of Dentistry, Associate Professor (40214564)
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| Co-Investigator(Kenkyū-buntansha) |
CHOSA Naoyuki Iwate Medical University, School of Dentistry, Assistant Professor (80326694)
CHEN Ming-Chu Iwate Medical University, School of Dentistry, Research Worker (30438501)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥3,860,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥360,000)
Fiscal Year 2007: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2006: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | tumor suppressor gene / oral spuamous cell carcinoma / ribosomal protein / anoikis / galectin / Nm23 / metastasis / molecular chaperon |
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| Research Abstract |
It was known that a metastasis suppressor gene contributed to the carcinomatous metastaticity in an epidermic cell, but exhaustive analysis of proteins to interact was performed, because it was not understood enough functions of Nm23. In this study, we tried to understand the function of Nm23 by the proteomics approach.
Human cDNA containing Nm23-H1 and H2 were cloned into two types of expression vectors, respectively. The fusion vectors containing a tag of FLAG epitope were constructed. These tagged proteins were expressed into HEK293 cells or E. coli., and then were purified by affinity chromatography used with anti-FLAG affinity chromatography. The obtained proteins were separated by SDS-PAGE and identified by the peptide mass fingerprints method using LC-MS/MS spectrometer.
The large difference for kinds of identified proteins was not obtained in between Nm23-H1 and H2. In addition, among the proteins that constituted ribosome, 32 proteins (35%) were identified, and it was suggested that Nm23 was interacted with the whole ribosome. BolA-like protein 2 (BolAL2) that the conformation resembled ribosomal protein S3 (RPS3), but the function is unknown, was identified newly. We also observed that BolAL2 was interacted with Nm23-H1 when pull-down assay was performed after expressed BolAL2 highly in cells. BolAL2 was also interacted with ribosomal proteins. On the other hand, RPS3 that interacts with Nm23-H1 and NF-kappa B, and that contributes the invasion of tumor cells, is reported recently. Therefore, it was suggested that interaction of the Nm23-ribosomal proteins-BolAL2 contributed to a regulation of tumor metastasis.
We searched a factor participated in anoikis that is apoptosis induced by lack of attachment between cell and extracellular matrix to contribute to metastasis of epithelial origin tumor cells. As a result, it was suggested that galectin-1 mediated suppression of anoikis in oral squamous cell carcinoma cells.
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Report
(3 results)
Research Products
(47 results)
