• Asian-Australasian Journal of Animal Sciences
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• v.19 no.8
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• pp.1159-1163
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• 2006

This experiment was performed to examine the influences of high ambient temperature on milk production, nutrient digestibility, energy and protein sufficiency ratio, and plasma metabolites concentration in lactating cows. In a $2{\times}2$ crossover design, four multiparous lactating Holstein cows were maintained in a chamber under treatment of constant moderate ($18^{\circ}C$) ambient temperature (MT) or high ($28^{\circ}C$) ambient temperatures (HT). The DMI and milk protein yield were significantly lower in HT (p<0.05). The milk yield, milk lactose yield, and milk SNF yield tended to be lower in HT (p<0.10). No statistical differences for 4% fat-corrected milk and milk fat yield were observed. Rectal temperatures were significantly higher in HT than MT (p<0.05). The apparent DM, OM, ether extract, CF, and ash digestibility did not differ between treatments. On the other hand, the apparent CP digestibility was increased significantly (p<0.05) and nitrogen free extract tended to increase (p<0.10) in HT. The sufficiency ratio of ME and DCP intake for each requirement tended to be lower in HT than in MT (p<0.10). Concentrations of total protein (TP), albumin, and urea nitrogen in plasma did not differ between treatments. Plasma 3-methylhistidine (3MH) concentration as a marker of myofibrillar protein degradation tended to be higher in HT (p<0.15). In conclusion, high ambient temperature was associated with a lower energy and protein sufficiency ratio, and decreased milk protein production, even though the body protein mobilization tended to be higher.

• Journal of Microbiology
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• v.43 no.6
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• pp.529-536
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• 2005

Viral infection causes stress to the endoplasmic reticulum (ER). The response to endoplasmic reticulum stress, known as the unfolded protein response (UPR), is designed to eliminate misfolded proteins and allow the cell to recover. The role of hepatitis C virus (HCV) non-structural protein NS4B, a component of the HCV replicons that induce UPR, is incompletely understood. We demonstrate that HCV NS4B could induce activating transcription factor (ATF6) and inositol-requiring enzyme 1 (IRE1), to favor the HCV subreplicon and HCV viral replication. HCV NS4B activated the IRE1 pathway, as indicated by splicing of X box-binding protein (Xbp-1) mRNA. However, transcriptional activation of the XBP-1 target gene, EDEM (ER degradation-enhancing $\alpha-mannosidase-like$ protein, a protein degradation factor), was inhibited. These results imply that NS4B might induce UPR through ATF6 and IRE1-XBP1 pathways, but might also modify the outcome to benefit HCV or HCV subreplicon replication.

• Molecules and Cells
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• v.39 no.11
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• pp.821-826
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• 2016

The ${\beta}$-catenin functions as an adhesion molecule and a component of the Wnt signaling pathway. In the absence of the Wnt ligand, ${\beta}$-catenin is constantly phosphorylated, which designates it for degradation by the APC complex. This process is one of the key regulatory mechanisms of ${\beta}$-catenin. The level of ${\beta}$-catenin is also controlled by the E3 ubiquitin protein ligase SIAH-1 via a phosphorylation-independent degradation pathway. Similar to ${\beta}$-catenin, STAT3 is responsible for various cellular processes, such as survival, proliferation, and differentiation. However, little is known about how these molecules work together to regulate diverse cellular processes. In this study, we investigated the regulatory relationship between STAT3 and ${\beta}$-catenin in HEK293T cells. To our knowledge, this is the first study to report that ${\beta}$-catenin-TCF-4 transcriptional activity was suppressed by phosphorylated STAT3; furthermore, STAT3 inactivation abolished this effect and elevated activated ${\beta}$-catenin levels. STAT3 also showed a strong interaction with SIAH-1, a regulator of active ${\beta}$-catenin via degradation, which stabilized SIAH-1 and increased its interaction with ${\beta}$-catenin. These results suggest that activated STAT3 regulates active ${\beta}$-catenin protein levels via stabilization of SIAH-1 and the subsequent ubiquitin-dependent proteasomal degradation of ${\beta}$-catenin in HEK293T cells.

• Korean Journal of Plant Resources
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• v.31 no.3
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• pp.218-227
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• 2018

In this study, we investigated the effect of the extracts from Vaccinium oldhamii on cell proliferation and the regulatory mechanisms of cyclin D1 protein level in human cancer cells. The branch extracts from Vaccinium oldhamii (VOB) showed higher inhibitor effect against the cell growth than leave extracts (VOL) and fruit extracts (VOF) in human colorectal cancer, breast cancer, prostate cancer, non-small lung cancer, pancreatic cancer and liver cancer cells. In addition, VOB decreased cyclin D1 level at both protein and mRNA level. MG132 treatment attenuated VOB-mediated cyclin D1 downregulation. A point mutation of threonine-286 to alanine attenuated cyclin D1 degradation by VOB. In addition, the inhibition of nuclear export by leptomycin B (LMB) attenuated cyclin D1 degradation by VOB. But, the treatment of PD98059 (ERK1/2 inhibitor), SB203580 (p38 inhibitor), SP600125 (JNK inhibitor), LiCl ($GSK3{\beta}$ inhibitor), LY294002 (PI3K inhibitor) or BAY 11-7082 ($I{\kappa}K$ inhibitor) did not affect VOB-induced cyclin D1 degradation. In conclusion, VOB induced cyclin D1 degradation through redistribution of cyclin D1 from the nucleus to cytoplasm via T286 phosphorylation of cyclin D1, which resulted in the inhibition of cancer cell proliferation.

• Microbiology and Biotechnology Letters
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• v.33 no.4
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• pp.308-314
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• 2005

Both high glucose and glucose degradation products (GDP) have been implicated in alterations of peritoneal membrane structure and function during long-term peritoneal dialysis (PD). The present study examined the role of GDP including methylglyoxal (MGO), acetaldehyde, and 3,4-dideoxyglucosone (3,4-DGE) in HPMC activation with respect to membrane hyperpermeability or fibrosis. The role of reactive oxygen species (ROS) and activation of protein kinase C (PKC) in GDP-induced HPMC activation were also examined. Using M199 culture medium as control, growth arrested and synchronized HPMC were continuously stimulated by MGO, acetaldehyde, and 3,4-DGE for 48 hours. Vascular endothelial growth factor (VEGF) was quantified as a marker of peritoneal membrane hyperpermeability and fibronectin and heat shock protein 47 (hsp47) as markers of fibrosis. Involvement of ROS and PKC was examined by the inhibitory effect of N-acetylcystein (NAC) or calphostin C, respectively. MGO significantly increased VEGF (1.9-fold), fibronectin (1.5-fold), and hsp47 (1.3-fold) secretion compared with control M199. NAC and calphostin C effectively inhibited MGO-induced VEGF upregulation. Acetaldehyde stimulated and 3,4-DGE inhibited VEGF secretion. Fibronectin secretion and hsp47 expression in HPMC were not affected by acetaldehyde or 3,4-DGE In conclusion, MGO upregulated VEGF and fibronectin secretion and hsp47 expression in HPMC, and PKC as well as ROS mediate MGO-induced VEGF secretion by HPMC. This implies that PKC activation and ROS generation by GDP may constitute important signals for activation of HPMC leading to progressive membrane hyperpermeability and accumulation of extracellular matrix and eventual peritoneal fibrosis.

• Proceedings of the Microbiological Society of Korea Conference
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• 2006.05a
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• pp.39-41
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• 2006

• Korean Journal of Plant Resources
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• v.30 no.3
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• pp.265-271
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• 2017

In this study, we elucidated the molecular mechanism of silymarin by which silymarin may inhibits cell proliferation in human colorectal cancer cells in order to search the new potential anti-cancer target associated with the cell growth arrest. Silymarin reduced the level of c-Myc protein but not mRNA level indicating that silymarin-mediated downregulation of c-Myc may result from the proteasomal degradation. In the confirmation of silymarin-mediated c-Myc degradation, MG132 as a proteasome inhibitor attenuated c-Myc degradation by silymarin. In addition, silymarin phosphorylated the threonine-58 (Thr58) of c-Myc and the point mutation of Thr58 to alanine blocked its degradation by silymarin, which indicates that Thr58 phosphorylation may be an important modification for silymarin-mediated c-Myc degradation. We observed that the inhibition of ERK1/2, p38 and $GSK3{\beta}$ blocked the Thr58 phosphorylation and subsequent c-Myc degradation by silymarin. Finally, the point mutation of Thr58 to alanine attenuated silymarin-mediated inhibition of the cell growth. The results suggest that silymarin induces the cell growth arrest through c-Myc proteasomal degradation via ERK1/2, p38 and $GSK3{\beta}-dependent$ Thr58 phosphorylation.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.7
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• pp.979-982
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• 2003

Two rapeseed meal samples (Sample A, hybrid 5900 and sample B, double low rapeseed No.4) obtained from China and one Canola meal sample obtained from a local crushing plant in Canada were used to investigate the amino acid degradability of rapeseed/Canola meal in rumen and amino acid digestibility of ruminal incubation residues by precision-fed rooster bioassay. Results show that in ruminal incubation the degradation rate of non amino acid nitrogen in crude protein is higher than that for amino acid nitrogen in crude protein, the results also suggest that the degradation rate of amino acid nitrogen in Chinese rapeseed meal sample B was lower than that for Canadian Canola, but that in Chinese rapeseed meal sample A is much close to that for Canadian canola meal. For all amino acids the digestibility of the bypass or residual protein as measured by the precision-fed rooster bioassay tended to be lower for Chinese rapeseed meal sample A than for sample B or Canadian canola meal which had similar digestibility values. However following a calculation of total amino acid availability, involving the digestibility of amino acids in the rumen and rooster bioassay the results are less contradictory. Results indicated that in traditional roasting-expelling process, heat treatment, especially dry heat treatmeat could decrease amino acids degradability in rumen of rapeseed/canola meal, but also may decrease total availability of amino acids of rapeseed/canola meal.

• YAKHAK HOEJI
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• v.4 no.1
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• pp.14-16
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• 1959

In order to confirm the biochemical process of the fermentation from soybean to maiju and of the fermentation from maiju to kanjang and dainjang, the introgen distributions of soybean, maiju, kanjang, and dainjang are studied on protein nitrogen, peptide nitrogen, amino nitrogen and volatile nitrogen. And the contents of amino nitrogen, peptide nitrogen, and true protein nitrogen to the total nitroge of soybean, maiju, kanjang, and dainjang are shown in table 1 and the ratios are shown in table 2 and the figure. According to the results indicated in the tables and figure, the following conclusions are summerized. 1. The main biochemical process at the fermentation from soybean to maiju would be the degradation from protein in soybean to peptide compounds in maiju. 2. The main biochemical process at the fermentation from maiju to kanjang and dainjand would be the degradation from peptide compounds in maiju to amino nitrogen compounds in kanjang and dainjang. 3. However bacause the protein nitrogen indicated as the ratio of protein nitrogen to total nitrogen is contained still higher content in dainjang. It is assumed that there might be two kinds of proteins in soybean one is the protein which could be converted to peptides at the maiju fermentation and to amino nitrogen compounds lastly at the kanjang fermentation. The other is the protein which would not be effected at these fermentation at all remaining as the protein nitrogen in dainjang. One of the finished products. 4. It can be indicated that the process from maiju to kanjang and dainjang would be due to the fermentation as indicated by HAW and CHOI.

• Journal of Microbiology
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• v.44 no.6
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• pp.641-648
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• 2006

We previously reported that Skp1, a component of the Skp1-Cullin-F-box protein (SCF) complex essential for the timely degradation of cell cycle proteins by ubiquitination, physically interacts with Bfa1, which is a key negative regulator of the mitotic exit network (MEN) in response to diverse checkpoint-activating stresses in budding yeast. In this study, we initially investigated whether the interaction of Skp1 and Bfa1 is involved in the regulation of the Bfa1 protein level during the cell cycle, especially by mediating its degradation. However, the profile of the Bfa1 protein did not change during the cell cycle in skp1-11, which is a SKP1 mutant allele in which the function of Skp1 as a part of SCF is completely impaired, thus indicating that Skp1 does not affect the degradation of Bfa1. On the other hand, we found that the skp1-12 mutant allele, previously reported to block G2-M transition, showed defects in mitotic exit and cytokinesis. The skp1-12 mutant allele also revealed a specific genetic interaction with ${\Delta}bfa1$. Bfa1 interacted with Skp1 via its 184 C-terminal residues (Bfa1-D8) that are responsible for its function in mitotic exit. In addition, the interaction between Bfa1 and the Skp1-12 mutant protein was stronger than that of Bfa1 and the wild type Skp1. We suggest a novel function of Skp1 in mitotic exit and cytokinesis, independent of its function as a part of the SCF complex. The interaction of Skp1 and Bfa1 may contribute to the function of Skp1 in the mitotic exit.