• Asian Pacific Journal of Cancer Prevention
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• v.13 no.9
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• pp.4327-4330
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• 2012

The mouse double minute 2 (MDM2) gene plays a key role in the p53 pathway, and the SNP 309T/G single-nucleotide polymorphism in the promoter region of MDM2 has been shown to be associated with increased risk of cancer. However, no consistent results were found concerning the relationships between the polymorphism and prostate cancer risk. This meta-analysis, covering 4 independent case-control studies, was conducted to better understand the association between MDM2-SNP T309G and prostate cancer risk focusing on overall and subgroup aspects. The analysis revealed, no matter what kind of genetic model was used, no significant association between MDM2-SNP T309G and prostate cancer risk in overall analysis (GT/TT: OR = 0.84, 95%CI = 0.60-1.19; GG/TT: OR = 0.69, 95%CI = 0.43-1.11; dominant model: OR = 0.81, 95%CI= 0.58-1.13; recessive model: OR = 1.23, 95%CI = 0.95-1.59). In subgroup analysis, the polymorphism seemed more likely to be a protective factor in Europeans (GG/TT: OR = 0.52, 95%CI = 0.31-0.87; recessive model: OR = 0.58, 95%CI = 0.36-0.95) than in Asian populations, and a protective effect of the polymorphism was also seen in hospital-based studies in all models (GT/TT: OR = 0.74, 95%CI = 0.57-0.97; GG/TT: OR = 0.55, 95%CI = 0.38-0.79; dominant model: OR = 0.69, 95%CI = 0.54-0.89; recessive model: OR = 0.70, 95%CI = 0.51-0.97). However, more primary studies with a larger number of samples are required to confirm our findings.

• Korean Journal of Food Science and Technology
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• v.13 no.3
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• pp.171-175
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• 1981

Hand deboned and mechanically deboned chicken meat were produced from domestic broilers and spent layers. Meat yield, chemical composition, functional characteristics, storage stability and microbiogical properties were investigated. The results obtained were as follows: 1. 35% of carcass freight was recovered primarily as hand deboned chicken meat (HDM) and 45% secondarily as mechanically deboned chicken meat(MDM), total meat yield reaching 80% of carcass weight. 2. Moisture, protein, fat. ash and calcium content of MDM were 65, 12, 20, 1.7 and $0.2{\sim}0.4%$, respectively MDM was higher than HDM in fat, ash and calcium, but significantly lower in moisture and protein Total pigment content of MDM was 2.5 times higher than that of HDM, such high content being attributed to the increased inclusion of hemoglobin during the mechanical masceration of carcass in the deboning process. 3. The emulsifying capacity (ES) of MDM per g meat was only 70% that of HDM, but when ES was expressed on unit g of protein basis MDM showed even higher ES than HDM primarily due to the higher proportion of salt soluble protein fraction of MDM. 4. Since the TBA value of MDM increased rapidly after 4 weeks of frozen storage at $-20^{\circ}C$, the maximum possible storage period of MDM is estimated to be about 4 weeks. 5. Total microbial counts of MDM was approximately $1.8{\times}10\;cells/g$ showing no great difference from HDM or red meat.

• Biomolecules & Therapeutics
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• v.25 no.4
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• pp.396-403
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• 2017

Under normal, non-stressed conditions, intracellular p53 is continually ubiquitinated by MDM2 and targeted for degradation. However, in response to severe genotoxic stress, p53 protein levels are markedly increased and apoptotic cell death is triggered. Inhibiting the ubiquitination of p53 under conditions where DNA damage has occurred is therefore crucial for preventing the development of cancer, because if cells with severely damaged genomes are not removed from the population, uncontrolled growth can result. However, questions remain about the cellular mechanisms underlying the regulation of p53 stability. In this study, we show that p53-inducible gene 3 (PIG3), which is a transcriptional target of p53, regulates p53 stability. Overexpression of PIG3 stabilized both endogenous and transfected wild-type p53, whereas a knockdown of PIG3 lead to a reduction in both endogenous and UV-induced p53 levels in p53-proficient human cancer cells. Using both in vivo and in vitro ubiquitination assays, we found that PIG3 suppressed both ubiquitination- and MDM2-dependent proteasomal degradation of p53. Notably, we demonstrate that PIG3 interacts directly with MDM2 and promoted MDM2 ubiquitination. Moreover, elimination of endogenous PIG3 in p53-proficient HCT116 cells decreased p53 phosphorylation in response to UV irradiation. These results suggest an important role for PIG3 in regulating intracellular p53 levels through the inhibition of p53 ubiquitination.

• Journal of Life Science
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• v.28 no.4
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• pp.488-495
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• 2018

The p53 gene plays a critical role in the transcriptional regulation of cellular response to stress, DNA damage, hypoxia, and tumor development. Keeping in mind the recently discovered manifold physiological functions of p53, its involvement in the regulation of cancer is not surprising. In about 50% of all human cancers, inactivation of p53's protein function occurs either through mutations in the gene itself or defects in the mechanisms that activate it. This disorder plays a crucial role in tumor evolution by allowing the evasion of a p53-dependent response. Many recent studies have focused on directly targeting p53 mutants by identifying selective, small molecular compounds to deplete them or to restore their tumor-suppressive function. These small molecules should effectively regulate various interactions while maintaining good drug-like properties. Among them, the discovery of the key p53-negative regulator, MDM2, has led to the design of new small molecule inhibitors that block the interaction between p53 and MDM2. Some of these small molecule compounds have now moved from proof-of-concept studies into clinical trials, with prospects for further, more personalized anti-carcinogenic medicines. Here, we review the structural and functional consequences of wild type and mutant p53 as well as the development of therapeutic agents that directly target this gene, and compounds that inhibit the interaction between it and MDM2.

• Journal of Digital Convergence
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• v.8 no.4
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• pp.73-82
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• 2010

Auto-industry is very difficult to standardize item code generation rule, because it has more than 20,000 parts in this industry. As finished good companies have already used the ERP system such as SAP, they have a good Master Data Management(MDM) system. However, since many supplier companies have poor MDM system, they have a lot of barriers on system implementation like ERP, MES. PDM systems. This study surveys various benchmarking sites and investigates the standardization of item code of the auto-parts manufacturing companies. Finally, this study proposes the implementation guide (IMG) of auto-industry MDM standardization.

• Journal of Life Science
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• v.12 no.1
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• pp.8-15
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• 2002

In this paper we dealt with processing of sausage using duck mechanically deboned meat(duck-MDM). The results may be summarized as follows : 1) after semi-thawing of freezing duck-MDM at $25^{\circ}C$ for 3 hours and cutting as thin, 2) alkali washing at low temperature for 4 hours by 0.2% NaHCO$_3$and 0.15% NaCl, 3) curing at low temperature for 4 hours, 4) after washing and dehydrating(moisture 80%), 5) grinding at low temperature for 55 minutes by silent cutter such as 1st grinding for 10 minutes added only dehydrated meat, 2rd grinding for 30 minutes added salt in 1st grinded meat and 3rd grinding for 15 minutes added other additives, 6) after quick casing in PVDC film and heating at 9$0^{\circ}C$ for 80 minutes, 7) cooling to below room temperature. The additives added at 3rd grinding process were Polymix-CA(0.3%), Polymix-CS(0.3%), polyphosphate(0.3%), sugar(4.2%), potato starch(8.0%), pyre-phosphates(0.3%), isolated soy protein(7.0%), MSG(0.2%), onion powder(0.5%), garlic powder(0.1%), nutmeg (1.5%), potassium sorbate(<0.1%), food red no.40(0.0075%), egg albumin(7.0%) and gluten(3.0%).

• Journal of the Korean Association of Oral and Maxillofacial Surgeons
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• v.27 no.5
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• pp.373-384
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• 2001

Cellular proliferation is an intricately regulated process mediated by the coordinated interactions of critical growth control genes. Two of these factors in mammalian cells are the p53 and mdm-2 genes. A protein product of the mem-2 oncogene has been recently shown to associate with the protein encoded by the tumor suppressor gene p53. The p53 tumor suppressor protein is stabilized in response to DNA damage and other stress signals and causes the cell to undergo growth arrest or apoptosis, thus preventing the establishment of mutations in future cellular generations. Mutation or loss of p53 is a very common event in tumor progression. It occurs in about 50% of all tumors analysed including of colon, lung, breast and liver. The cellular mdm-2 gene, which has potential transforming activity that can be activated by overexpression, is amplified in a significant percentage of human sarcoma and in other mammalian tumors. Proteins encoded by the mdm-2 gene are able to bind to the p53 protein and, when overexpressed, can inhibit p53's transcriptional activation function, thus mdm-2 can act as a negative regulator of p53 function. Experimental study was performed to observe the relationship between p53 gene mutation and mdm-2 protein expression and apply the results to the clinical activity. 36 golden syrian hamster each weighing $60{\sim}80g$ were used and painted with 0.5% DMBA by 3 times weekly on the right buccal cheek(experimental side) for 6, 8, 10, 12, 14 and 16 weeks. Left buccal cheek(control side) was treated with mineral oil as the same manner to the right side. The hamsters were sacrificed on the 6, 8, 10, 12, 14 & 16 weeks. Normal and tumor tissues from paraffin block were examined for histology and immunohistochemistry observation, and were completely dissected by microdissection and DNA from both tissue were isolated by proteins K/phenol/chloroform extraction. Segments of the hamster p53 exons 5, 6, 7 and 8 were amplified by PCR using the oligonucleotide primers, and then confirmational change was observed by SSCP respectively. The results were as follows : 1. Dysplasia at 6 weeks, carcinoma in situ at 8 weeks and invasive carcinoma from 10 weeks could be observed in experimental groups. 2. p53 mutations were detected in 10 of the 36(28%) and the exons 6(6 of the 10 : 60%) was the most hot spot area among the highy conserved region(exons 5, 6, 7 & 8). 3. Immunohistochemical study confirmed 22 of the 36(61%) of p53 expression involving 10 of p53 mutations. 4. mdm-2 expression of was showed in 3 of the 36(8%) involving 1 of the 22 of p53 expression and 2 of the 14 of p53 non-expression. From the above results, mutation of p53 gene or expression of p53 protein may have the influence of the DMBA induced carcinoma of hamster buccal pouch but the expression of mdm-2 protein may not have relationship with tumorigenesis.

• The Bulletin of The Korean Astronomical Society
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• v.42 no.1
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• pp.50.2-50.2
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• 2017

We have been carrying out the long-term (3-5 years) AGN monitoring project since October 2015 to investigate the variability and measure the H beta line time lag of 69 nearby (0.06 < z < 0.47) AGNs based on the reverberation mapping method. Our targets have B band magnitudes of 14.4-18.6, luminosities of log L5100 = 45.6-48.1 erg/s, and the expected time lags of 28-597 light days. BVR band images are being taken with ~20-day cadence using MDM 1.3m, LOAO 1m and MDM 2.4m telescopes. Recently, Nickel 1m at Lick and DOAO 1m at Deokheung observatory are joined with photometric observations. Follow-up spectroscopic observations are on-going using the Lick 3m and MDM 2.4m telescopes. In this poster, we will describe our project including sample selection and the observational strategy, and present the preliminary results based on the 1st year photometry.

• Toxicological Research
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• v.20 no.1
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• pp.71-82
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• 2004

Changes in cell cycle control in the lungs and liver of the B6C3F1 mice (20 males per each group) exposed to ozone (0.5 ppm), 4-(N-methyl-N-nitrosamino)-1-(3-pyridyl)-1-butanone (NNK, 1.0 mg/kg), and dibutyl phthalate (DBP, 5,000 ppm) after 52 weeks were examined through Western, Northern blot, and immunohistochemistry based on alterations in protein expression levels of G1/S checkpoints (cyclin D1, cyclin E, and PCNA), G2/M checkpoints (cyclin B1, cyclin G, and cyclin A), negative regulators (p53, p21, GADD45, and p27), and positive regulator (mdm2). Expression levels of cyclins D1, E, G, PCNA, mutant p53, and mdm2 proteins were higher in the lungs and livers treated with combination of toxicants than in those treated with ozone only. Expression levels of the wild-type and mutant p53, p21, GADD45, p27, and mdm2 proteins and mRNAs were higher in toxicant-treated groups than those of the control. Immunohistochemical analysis revealed staining intensities of the PCNA, cyclin D1, c-myc and mdm2 protein- treated lungs and livers were stronger than those of the control group. Our results showed that combined treatment of ozone with NNK/DBP altered the cell cycle control through instability of the wild-type p53 gene. Such pivotal p53-mediated cell cycle alterations may be responsible for the toxicity observed under our experimental condition. These results may be applied to risk assessment of mixture-induced toxicity.

• BMB Reports
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• v.49 no.11
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• pp.598-606
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• 2016

ARF is an alternative reading frame product of the INK4a/ARF locus, inactivated in numerous human cancers. ARF is a key regulator of cellular senescence, an irreversible cell growth arrest that suppresses tumor cell growth. It functions by sequestering MDM2 (a p53 E3 ligase) in the nucleolus, thus activating p53. Besides MDM2, ARF has numerous other interacting partners that induce either cellular senescence or apoptosis in a p53-independent manner. This further complicates the dynamics of the ARF network. Expression of ARF is frequently disrupted in human cancers, mainly due to epigenetic and transcriptional regulation. Vigorous studies on various transcription factors that either positively or negatively regulate ARF transcription have been carried out. However, recent focus on posttranslational modifications, particularly ubiquitination, indicates wider dynamic controls of ARF than previously known. In this review, we discuss the role and dynamic regulation of ARF in senescence and cancer.