• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.954-954
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• 2005

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.955-955
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• 2005

• Proceedings of the Zoological Society Korea Conference
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• 1997.10b
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• pp.225.1-225
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• 1997

No Abstract, See Full Text

• YAKHAK HOEJI
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• v.37 no.1
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• pp.36-40
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• 1993

The 4-(2'-(N-(l-methyl-3'-carbamylphenyl)-n-propyl))aminoethyl)-l- hydroxy-2-pyridone which has isoelectronic and isosteric structural similarity with dobutamine without having the Catechol-O- Methyltransferase(COMT) vulnerable m-hydroxy group was synthesized via 12 synthetic steps.

• Toxicological Research
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• v.6 no.1
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• pp.89-97
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• 1990

Neural regulation of phenylethanolamine N-meth-yltransferase (PNMT) was studied with reserpine as a neuronal agent in rat adrenal medulla. The enzyme activity assay and northern blot analysis were performed to determine whether the induction of PNMT activity after reserpine treatment was associated with elevation of mRNA coding for PNMT. The i.p. administration of reserpine (2.5 mg/kg) on alternate days fot 4 injections to rats brought about 30% increase of adrenal medullary PNMT activity and approximately 60% stimulation of the PNMT mRNA level in rat adrenal gland. A dose of 10 mg/kg of reserpine was chosen to perform optimum induction of PNMT activity in the rat adrenal gland based on the results of dose response curve of reserpine. Time course reserpine (10 mg/kg) effects on the rat adrenal medullary PNMT were as follows: 1. Peripheral PNMT activity reached maximum level after 7 days of drug treatment on alternate days. 2. Trans-synaptic stimulation by reserpine increased pretranslational activity of rat adrenal PNMT, but not translational activity. 3. Immunotitration of PNMT molecule after reserpine treatment indicated that reserpine produced an enzyme with greater antibody affinity than endogenous molecule in the rat adrenal gland.

• Preventive Nutrition and Food Science
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• v.3 no.3
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• pp.251-255
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• 1998

Rat testis known to contain all of the enzymes required for carnitine biosynthesis also contains high concentration of calmodulin, a protein which may or may not contain trimethyllysine, the major substrate in carnitine biosynthesis. The purpose of this study was to investigate the levels of carnitine and the state of calmodulin N-methylation in rat testes, and to discuss the possibility of the involvement of calmodulin incarnitine biosynthesis. Nonesterified carnitine , acid soluble acyl carnitine, and acid insoluble acyl carnitine of ra tests were 273 nmole, 62nmole, and 4 nmole/g tissue, respectively. Total carnitine level was 339 nmole/g testes tissue. Calmodulin purified from rat tests was assayed for methylation potential using N-methyltransferase from the rat testes. Rat testes calmodulin showed no 3H-methyl incorporation indicating that the calmodulin was trimethylated already by endogenous calmodulin N-methyltransferase. Amino acid composition analysis revealed that the rat testes calmodulin containd one mole of trimethyllysine per mole of calmodulin. These data suggest that testes calmodulin could provide the trimethyllysine needed for the synthesis of carnitine in the rat tests.

• Journal of Environmental Health Sciences
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• v.35 no.5
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• pp.343-354
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• 2009

Since Barker found associations between low birth weight and several chronic diseases later in life, the hypothesis of fetal origins of adult disease (aka, Barker Hypothesis) and epigenetics have been emerging as a new paradigm for geneenvironment interaction of chronic disease. Epigenetics is the study of heritable changes in gene silencing that occur without any change in DNA sequence. Gene expression can be regulated by several epigenetic mechanisms, including DNA methylation and histone modifications, which may be associated with chronic conditions, such as cancers, cardiovascular disease, and type-2 diabetes. One carbon metabolism which involves the transfer of a methyl group catalyzed by DNA methyltransferase is an important mechanism by which DNA methylation occurs in promoter regions and/or repetitive elements of the genome. Environmental factors may induce epigenetic modification through production of reactive oxygen species, alteration of methyltransferase activity, and/or interference with methyl donors. In this review, we introduce recent studies of epigenetic modification and environmental factors, such as heavy metals, environmental hormones, air pollution, diet and psychosocial stress. We also discuss epigenetic perspectives of early life environmental exposure and late life disease occurrence.

• Current Research on Agriculture and Life Sciences
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• v.28
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• pp.63-68
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• 2010

The epigenetic therapy of cancers is emerging as an effective and valuable approach to both chemotherapy and the chemoprevention of cancer. The utilization of epigenetic targets that include histone methyltransferase (HMTase), Histone deacetylatase, and DNA methyltransferase, are emerging as key therapeutic targets. SET containing proteins such as the HMTase Setd1b has been found significantly amplified in cancerous cells. In order to shed some light on the histone methyl transferase family, we cloned the Setd1b gene from Mus musculus and build a collection of vectors for recombinant protein expression in E.coli that will pave the way for further structural biology studies. We prospect the role of the Setd1b pathway in cancer therapy and detail its unique value for designing novel anti-cancer epigenetic-drugs.

• Journal of Microbiology and Biotechnology
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• v.19 no.9
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• pp.972-981
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• 2009

In this paper, a fed-batch cultivation process in recombinant Escherichia coli BL21(DE3) bacteria, for the production of human soluble catechol-O-methyltransferase (hSCOMT), is presented. For the first time, a straightforward model is applied in a recombinant hSCOMT expression system and distinguishes an initial cell growth phase from a protein production phase upon induction. Specifically, the kinetic model predicts biomass, substrate, and product concentrations in the culture over time and was identified from a series of fed-batch experiments designed by testing several feed profiles. The main advantage of this model is that its parameters can be identified more reliably from distinct fed-batch strategies, such as glycerol pulses and exponential followed by constant substrate additions. Interestingly, with the limited amount of data available, the proposed model accomplishes satisfactorily the experimental results obtained for the three state variables, and no exhaustive process knowledge is required. The comparison of the measurement data obtained in a validation experiment with the model predictions showed the great extrapolation capability of the model presented, which could provide new complementary information for the COMT production system.

• Korean Journal of Veterinary Research
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• v.48 no.3
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• pp.243-250
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• 2008

A calmodulin-dihydrofolate reductase (DHFR) sandwich fusion protein was generated by insertion of calmodulin into the $\beta$-bulge region of DHFR to observe the effects of structurally constraining the calmodulin structure. The calcium binding properties of the sandwich protein were almost identical to calmodulin. Similar to calmodulin ($10.7 {\mu}M$), the sandwich protein bound four equivalents of calcium, with half saturation ($K_{0.5}$) observed at a [$Ca^{2+}$] of $8{\mu}M$. However, nicotinamide adenine dinucleotide (NAD) kinase activation property of the sandwich protein was lower than that of calmodulin. The sandwich protein activated NAD kinase, but to only half of the level obtained with calmodulin. The K 0.5 for both calmodulin and the sandwich protein were approximately the same (1-2 nM). Methylation analyses of the sandwich protein show that insertion of calmodulin into DHFR results in a large decrease in methylation. The $V_{max}$ observed with the sandwich protein (95 nmole/min/ml) was only 22% of the value observed with calmodulin (436 nmol/min/ml) in the presence of calcium. Addition of trimethoprim to the reaction significantly inhibited the observed methylation rate. Overall, the data suggest that the insertion of calmodulin into the DHFR structure has little effect on calcium binding by the individual lobes of calmodulin, but may constrain the lobes in a manner that results in altered interaction with the calmodulin-dependent proteins, and severely perturbed the methyltransferase recognition site.