• Radiation Oncology Journal
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• v.38 no.2
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• pp.129-137
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• 2020

Purpose: To identify the clinical usefulness of serum M protein and to establish a rationale for regular follow-up with serum protein electrophoresis in solitary plasmacytoma. Materials and Methods: Sixty-nine patients with solitary plasmacytoma and solitary plasmacytoma with minimal marrow involvement according to the International Myeloma Working Group criteria were retrospectively reviewed. Results: At a median follow-up of 6.2 years, 5-year local control (LC), 5-year multiple myeloma-free survival (MMFS), 5-year failure-free survival (FFS), and 5-year overall survival (OS) were 82.6%, 44.1%, 41.8%, and 85.1%, respectively. Among the patients whose initial serum M protein was present or not evaluated, 37.3% of patients showed disappearance of serum M protein after various treatment. MMFS of these patients were comparable to non-secretory plasmacytoma with undetectable levels of M protein, and significantly better than patients with persistent M protein. Increase of serum M protein ≥0.1 g/dL was most predictive of treatment failure with area under the curve of 0.731. Conclusion: Patients who eventually showed persistence of serum M protein after treatment showed worse MMFS and FFS compared to those whose serum M protein disappeared or who had initially non-secretory disease. The increase of serum M protein level ≥0.1 g/dL from current nadir was predictive of treatment failure. Therefore, regular follow-up with serum M protein is highly recommended especially unless the patient had initially non-secretory disease.

• Plant Resources
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• v.1 no.2
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• pp.113-120
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• 1998

Soybean is an important crop because its seed has very high protein relative to others. The quality of soy protein is limited by the concentration of the sulfur-containing amino acids in the amino acid profile. Among the supply of various forms of 0.4mM sulfur as S nutrition during seed fill. only 0.4mM L-methionine can inhibit ${\beta}$-subunit synthesis completely and produce the highest glycinin-containing seeds. Compared to 0.4mM sulfate control, seeds supplied by 0.4mM L-methionine have lower ${\alpha}$-, no ${\beta}$-subunit, and highly increased glycinin without altering total protein concentration. Supply of 0.2mM cystine (0.4mM S) did not affect the accumulative pattern of seed storage protein (SSP) subunits. In the supply of L-methionine, 0.2mM treatment showed higher glycinin in seeds but 0.05mM resulted in lower glycinin than tile sulfate control. The relative abundance of ${\alpha}^`$-subunit was not altered by any N or S nutrition. Under 5mM nitrogen, protein concentration was increased about 3-5% by substituting ammonia for nitrate during seed fill independent of nutrition. The increase resulted in the only increase of 7S protein, mainly ${\beta}$-subunit. Our data suggest that the regulatory system of SSP genes responds to the balance between N and S assimilates supplied from mother plant. and controls the di fferential synthesis of their subunits for the maximum protein accumulation in developing soybean seed.

• Animal cells and systems
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• v.1 no.2
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• pp.317-321
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• 1997

Tau protein is one of the microtubule-associated proteins in the mammalian brain. In Alzheimer's disease, tau protein is immobilized in the somatodendritic compartment of certain nerve cells, where it forms a part of the paired helical filament (PHF). To understand the role of tau protein in the formation of PHF, a recombinant human tau protein expressed in Escherichia coli and five synthetic peptide fragments (peptide 1 to peptide 5), corresponding to the C-terminal region of tau protein, were prepared and their ability in self-assembly to form filamentous structures was examined. The recombinant human tau protein formed short rod-like structures in 0.1M MES buffer containing 1 mM $MgCI_2$, while a synthetic peptide fragment 1 containing 55 amino acid residues could assemble into a lot of long filamentous structures in water and particularly twisted helical structures in 0.1M MES buffer containing 1 mM $MgCI_2$. This suggests that the C-terminal region possesses a filament-forming ability and may be related to the formation of the helical structure by providing a powerful filament-forming driving force.

• Asian-Australasian Journal of Animal Sciences
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• v.4 no.4
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• pp.361-368
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• 1991

In two experiments 640 starcross replacement pullets between 25 and 154 days of age were fed ad libitum on either of 16 diets formed by the combination of $4CP{\times}4ME$ levels to study the interaction of CP and ME on growth performances. In both experiments, feed intake decreased, but protein intake, energy intake, live weight gain and feed conversion efficiency increased and sexual maturity hastened with the increase of dietary protein and/or energy level. The protein conversion efficiency decreased with the increase of dietary protein level. The energy conversion efficiency, however, did not show any relationship with dietary energy level. There was a greater improvement of growth performance due to simultaneous increase of dietary protein and energy level than that of increasing protein or energy alone.

• Korean Journal of Exercise Nutrition
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• v.15 no.4
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• pp.153-161
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• 2011

The maintenance of skeletal muscle mass is very important for the prevention of life style-related diseases and the improvement of quality of life. It is well-known that resistance exercise and nutrition (especially amino acids) are the most effective interventions for maintaining skeletal muscle mass. It has been reported that many molecules are involved in the regulation of protein synthesis in response to resistance exercise and nutrition. Understanding the molecular mechanisms regulating muscle protein synthesis is crucial for the development of appropriate interventions. The role of intracellular signaling pathways through the mammalian target of rapamycin (mTOR), a serine/threonine protein kinase in the regulation of muscle protein synthesis, has been extensively investigated for these years. Control of protein synthesis by mTOR is mediated through phosphorylation of downstream targets that modulate translation initiation and elongation step. In contrast, upstream mediators regulating mTOR and protein synthesis in response to resistance exercise and amino acid still needed to be determined. In this brief review, we discuss the current progress of intracellular mechanisms for exercise- and amino acid-induced activation of mTOR pathways and protein synthesis in skeletal muscle.

• Archives of Pharmacal Research
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• v.22 no.2
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• pp.130-136
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• 1999

Mouse guanylate-binding protein 3 (mGBP3) is a 71-kDa GTPase which belongs to GTP-binding protein family. The present study showed that the expression of mGBP3 transcript was readily induced in a dose dependent fashion in the macrophage cell line RAW264.7 treated with either $interferon-{\gamma} (IFN-\gamma)$ or lipopolysaccaride (LPS). The expression of mGBP3 protein was also apparent by 4 and 6 h after the treatment of cells with IFN-\gamma (100 U/ml) or LPS ($1{\mu}g/ml$) , and remained at palteau for at least 24 h. Cycloheximide ($10{\mu}g/ml$) had no effect on the $IFN-\gamma-$ or LPS-induced mGBP3 expression, suggesting that the mGBP3 induction did not require further protein synthesis. Interestingly, a protein kinase C (PKC) inhibitor staurosporine (50 nM) abolished the induction of mGBP3 expression by LPS, but not by $IFN-{\gamma}$. These findings suggest that mGBP3 may be involved in the macrophage activation process and both IFN-\gamma and LS induce the mGBP3 expression through distinct signal transduction pathways.

• Korean Journal of Environmental Agriculture
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• v.17 no.4
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• pp.296-300
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• 1998

The analysis of biochemical changes in tobacco plant as increase of NaCl concentraion was conducted. Total protein content and soluble protein content were decreased as NaCl concentration was increased, in that steady decreased until 120mM NaCl and largely decreased at 150mM NaCl. The expression of 74Kd subunit was increased until 60mM NaCl. However, the amount of 74Kd protein was decreased from 90mM NaCl. There was no difference for expression of other protein subunits. Chlorophyll a content was significantly decrease as NaCl concentration was increased, but chlorophyll b content was not much decreased. The slow increase up to 120mM NaCl and large increase at 150mM NaCl for ATPase and peroxidase activities indicated that 120mM NaCl could be a limiting concentration for salt injury.

• Journal of the Korean Society of Food Culture
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• v.5 no.4
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• pp.443-448
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• 1990

The object of this study was to investigate the characteristics of pectinesterase(PE), polygalacturonase(PG) and Peroxidase(POD) in Kimchi materials. The results were as follows : 1. The specific activities of PEs in Korean cabbage, Korean raddish, garlic and ginger were 200 unit/mg protein, 23.1 unit/mg protein, 0.8 unit/mg protein and 32 unit/mg protein, respectively. The optimum pHs of PEs in all materials were between 7 to 8. The concentrations of NaCl, $CaCl_2$ which showed the highest activities of PEs were $0.2{\sim}0.3M$ NaCl, 50 mM $CaCl_2$ in Korean cabbage and raddish, 0.05 M NaCl, 20 mM $CaCl_2$ in garlic and 0.2 M NaCl, 20 mM $CaCl_2$ in ginger. 2. The specific activities and the optimum pHs of PGs were 1.5 unit/mg protein and pH 4.5 in Korean cabbage, 1.6 unit/mg protein and $pH\;4.5{\sim}5.5M$ in Korean raddish, 0.06 unit/mg protein and $pH\;3.0{\sim}3.5M$ in garlic, and 0.06 unit/mg protein and $CaCl_2$ in ginger. The concentrations of NaCl, $CaCl_2$ which showed the highest activities of PGs were $0.1{\sim}0.2M$ NaCl and $0.15{\sim}0.2mM$ mM $CaCl_2$ in all materials. 3. The specific activities and the optimum pHs of PODs in Korean cabbage, Korean raddish, garlic and ginger were 71.3 unit/mg protein ; pH 6.0. 769 unit/mg protein ; pH 5.5, 1.09 unit/mg protein ; pH 4.5 and 12.7 unit/mg protein ; $pH\;5.0{\sim}5.5M$, respectively. POD activities were not decreased in Korean cabbage, but decreased in Korean raddish by the increase of NaCl, $CaCl_2$ concentrations. In garlic and ginger, POD activities were a little slightly affected by the increase of NaCl, $CaCl_2$ concentrations.

• Journal of Animal Science and Technology
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• v.63 no.5
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• pp.1126-1141
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• 2021

Recent evidence has shown that methionine (Met) supplementation can improve milk protein synthesis under hyperthermia (which reduces milk production). To explore the mechanism by which milk protein synthesis is affected by Met supplementation under hyperthermia, mammary alveolar (MAC-T) cells were incubated at a hyperthermic temperature of 42℃ for 6 h in media with different concentrations of Met. While the control group (CON) contained a normal amino acid concentration profile (60 ㎍/mL of Met), the three treatment groups were supplemented with Met at concentrations of 10 ㎍/mL (MET70, 70 ㎍/mL of Met), 20 ㎍/mL (MET80, 80 ㎍/mL of Met), and 30 ㎍/mL (MET90,90 ㎍/mL of Met). Our results show that additional Met supplementation increases the mRNA and protein levels of BCL2 (B-cell lymphoma-2, an anti-apoptosis agent), and decreases the mRNA and protein levels of BAX (Bcl-2-associated X protein, a pro-apoptosis agent), especially at an additional supplementary concentration of 20 ㎍/mL (group Met80). Supplementation with higher concentrations of Met decreased the mRNA levels of Caspase-3 and Caspase-9, and increased protein levels of heat shock protein (HSP70). The total protein levels of the mechanistic target of rapamycin (mTOR) and the mTOR signalling pathway-related proteins, AKT, ribosomal protein S6 kinase B1 (RPS6KB1), and ribosomal protein S6 (RPS6), increased with increasing Met supplementation, and peaked at 80 ㎍/mL Met (group Met80). In addition, we also found that additional Met supplementation upregulated the gene expression of αS1-casein (CSN1S1), β-casein (CSN2), and the amino acid transporter genes SLC38A2, SLC38A3 which are known to be mTOR targets. Additional Met supplementation, however, had no effect on the gene expression of κ-casein (CSN3) and solute carrier family 34 member 2 (SLC34A2). Our results suggest that additional Met supplementation with 20 ㎍/mL may promote the synthesis of milk proteins in bovine mammary epithelial cells under hyperthermia by inhibiting apoptosis, activating the AKT-mTOR-RPS6KB1 signalling pathway, and regulating the entry of amino acids into these cells.

• Journal of Plant Biology
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• v.36 no.2
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• pp.171-176
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• 1993

Protein kinase C, a protein related in PI cascade, was partially purified from the cytosol protein of etiolated plants of Glycine max by DEAE-52 cellulose chromatography and phenylsepharose chromatography. When the DEAE column was eluted with 0-0.8 M linear gradient KCl, tow fractions were found that increased the phosphorylation of histon H1 about five and nine-fold in the presence of 5 $\mu\textrm{g}$/mL phosphatidylserine and 0.5 $\mu\textrm{g}$/mL diolein, respectively. These fractions were used as DEAE pool. The reaction eluted with relatively high concentration of KCl was loaded on phyenylsepharose column with 5 mM CaCl2 and eluted with 1 mM EGTA. A fraction contained the protein kinase C, which increased the phosphorylation of the histon H1 was fractionated. To determine the molecular weight of PKC, the fraction eluted from phenylsepharose column was analyzed by 5~15% polyacrylamide gel electrophoresis after concentrated with the Amicon membrane (YM10). That revealed two bands corresponding to 60 and 65 kGy by silver staining of the gel, respectively.