• Microbiology and Biotechnology Letters
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• v.24 no.3
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• pp.290-298
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• 1996

In an effort to understand the role of the conserved domain and of the heterologous one-third part of the carboxy terminal domain of transglutaminase C (TGase II), attempts were made to express TGase II cDNA of human origin in yeast Saccharomyces cerevisiae as in a full-length form as well as in a form of C-terminal truncation. The 2$\mu$-based expression plasmids which contained the TGase II cDNA under the gal inducible promoter were introduced into yeast and the maintenance of the full-length and truncated form of the TGase II gene plasmids were confirmed by Southern blot. The expression of the TGase II gene was analysed by reverse transcription polymerase chain reaction (RT-PCR), and western blot analyses. As assayed by [1,4$^{14}$C]-putrescine incorporation into succinylated casein, the full-lenth as well as the truncated forms of recombinant TGase II showed some catalytic activity. These results indicate that the N-terminal homologous domain of human TGase II retains a catalytically active domain. The level of TGase II expressed in yeast, however, was far lower than satisfactory and other expression system should be sought further chracterization of the enzyme. The negative effect of TGase II on the growth of yeast is interesting with respect to the physiological effect of TGase II in cornification of epidermal keratinocytes.

• Biomolecules & Therapeutics
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• v.27 no.1
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• pp.34-40
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• 2019

Transglutaminase 2 (TGase 2) plays a key role in p53 regulation, depleting p53 tumor suppressor through autophagy in renal cell carcinoma. We found that microtubule-associated protein 1A/1B-light chain 3 (LC3), a hallmark of autophagy, were tightly associated with the level of TGase 2 in cancer cells. TGase 2 overexpression increased LC3 levels, and TGase 2 knockdown decreased LC3 levels in cancer cells. Transcript abundance of LC3 was inversely correlated with level of wild type p53. TGase 2 knockdown using siRNA, or TGase 2 inhibition using GK921 significantly reduced autophagy through reduction of LC3 transcription, which was followed by restoration of p53 levels in cancer cells. TGase 2 overexpression promoted the autophagy process by LC3 induction, which was correlated with p53 depletion in cancer cells. Rapamycin-resistant cancer cells also showed higher expression of LC3 compared to the rapamycin-sensitive cancer cells, which was tightly correlated with TGase 2 levels. TGase 2 knockdown or TGase 2 inhibition sensitized rapamycin-resistant cancer cells to drug treatment. In summary, TGase 2 induces drug resistance by potentiating autophagy through LC3 induction via p53 regulation in cancer.

• Food Science of Animal Resources
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• v.24 no.1
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• pp.23-28
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• 2004

The objective of this study was to reduce the tumbling time with improved binding capacity for the manufacture of restructured hams(RHs) using a transglutaminase(TGase). The RHs had 73.9∼75.7% moisture, 3.63∼4.18% fat, 16.6∼20.6% protein with pH values of 5.95∼6.10 and water activity of 0.95∼0.96. No differences in hunter color values or functional properties were observed with the addition of 0.3% TGase or increased tumbling time. However, RHs without TGase had lower(p<0.05) textural profile analysis(TPA) values than those with TGase, regardless of tumbling time. Improved shear values were also observed with increased tumbling time only in RHs without TGase or with the addition of 0.3% TGase as well. This study indicated that 1 hr tumbling with the addition of 0.3% TGase improved the textural characteristics, as compared to the control 1(1 hr tumbling without TGase), resulting in similar shear values of the treatment, which tumbled for 4 hrs without TGase.

• The Journal of Korean Medicine
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• v.25 no.4
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• pp.188-199
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• 2004

Transglutaminase 2 (TGase 2) is an enzyme that is widely used in many biological systems for generic tissue stabilization purposes or immediate defenses for wounds. Many reports have showed that TGase 2 is aberrantly activated in tissues and cells and contributes to a variety of diseases, including neurodegenerative diseases and autoimmune diseases. In most cases, the TGase 2 appears to be a factor in the formation of inappropriate proteinaceous aggregates that may be cytotoxic. However, in other cases such as celiac disease, arthritis, lupus, amyotrophic lateral sclerosis, TGase 2 is involved in the generation of autoantibodies. This suggests the possibility that the inappropriate expression and/or presentation of TGase 2 to T cells might contribute to these diseases in genetically predisposed individuals. Others and we have found that TGase 2 expression is also increased in the inflammation process. We also demonstrated reverse of inflammation by TGase inhibition. Furthermore we discovered the genuine role of TGase 2 in immune cell activation. Increase of TGase activity induces or exacerbates inflammation via NF-κB activation without I-κBα kinase signalings. This review will examine a possibility of TGase inhibitors as therapeutic agents in a variety of inflammatory diseases.

• Food Science of Animal Resources
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• v.37 no.5
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• pp.635-645
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• 2017

In this study, effect of transglutaminase (TGase) addition on physical, water barrier, optical and mechanical properties of mechanically deboned chicken meat protein (MDCM-P) films was investigated. When TGase was added to the films, the thickness increased, but the solubility decreased. Films treated with TGase exhibited higher water vapor permeability than control film (p<0.05). When TGase concentration increased, the $L^*$ values of films decreased, but $a^*$ and $b^*$ values increased. All films showed very good barrier properties against UV light. The highest tensile strength was obtained in MDCM-P films containing 3% TGase (p<0.05). The elongation at break values increased with the TGase concentration increasing from 1 to 3%, but decreased at higher enzyme concentration (p<0.05). The addition of TGase altered molecular organization and intermolecular interaction in the film matrix. TGase treated films showed smoother and ordered surface structure and homogeneous and compact microstructure. The results indicated that TGase use can be an effective approach in improving the solubility and mechanical properties of MDCM-P films.

• The Korean Journal of Mycology
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• v.36 no.1
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• pp.93-97
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• 2008

A $Ca^{2+}-independent$ microbial transglutaminase (mTGase) from the actinomycete Streptomyces mobaraensis IFO13819 is a useful enzyme in the food industry. It is consists 406 amino acid residues, which comprised leader and pro region of 75 amino acid residues and the structure region of 331 amino acid residues. Pro and structure gene of TGase were cloned into the yeast shuttle vector pYAEG-TER and then used to transform Saccharomyces cerevisiae 2805. Expression of mTGase in recombinant was confirmed with Northern hybridization and the maximal activity of TGase was shown 26 mU/ml.

• Biomolecules & Therapeutics
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• v.21 no.3
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• pp.204-209
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• 2013

Osteoprotegerin (OPG) is a secreted glycoprotein and a member of the tumor necrosis factor receptor superfamily. It usually functions in bone remodeling, by inhibiting osteoclastogenesis through interaction with a receptor activator of the nuclear factor ${\kappa}B$ (RANKL). Transglutaminases-2 (Tgase-2) is a group of multifunctional enzymes that plays a role in cancer cell metastasis and bone formation. However, relationship between OPG and Tgase-2 is not studied. Therefore, we investigated the involvement of 12-O-Tetradecanoylphorbol 13-acetate in the expression of OPG in MG-63 osteosarcoma cells. Interleukin-$1{\beta}$ time-dependently induced OPG and Tgase-2 expression in cell lysates and media of the MG-63 cells by a Western blot. Additional 110 kda band was found in the media of MG-63 cells. 12-O-Tetradecanoylphorbol 13-acetate also induced OPG and Tgase-2 expression. However, an 110 kda band was not found in TPA-treated media of MG-63 cells. Cystamine, a Tgase-2 inhibitor, dose-dependently suppressed the expression of OPG in MG-63 cells. Gene silencing of Tgase-2 also significantly suppressed the expression of OPG in MG-63 cells. Next, we examined whether a band of 110 kda of OPG contains an isopeptide bond, an indication of Tgase-2 action, by monoclonal antibody specific for the isopeptide bond. However, we could not find the isopeptide bond at 110 kda but 77 kda, which is believed to be the band position of Tgase-2. This suggested that 110 kda is not the direct product of Tgase-2's action. All together, OPG and Tgase-2 is induced by IL-$1{\beta}$ or TPA in MG-63 cells and Tgase-2 is involved in OPG expression in MG-63 cells.

• Korean Journal of Food Science and Technology
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• v.37 no.3
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• pp.345-351
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• 2005

Physicochemical properties and functionalities of sodium caseinate, whey protein, skim milk, and whole milk with or without transglutaminase (TGase, 200 : 1) at $38^{\circ}C$ were determined. After crosslinking by TGase, whey protein was effective in improving heat stability compared to native protein at over $70^{\circ}C$. Whole milk was stable with lower turbidity compared to native solution. Whey protein showed low hydrolysis degree, fewer than sodium caseinate, during early activation time and increased slightly thereafter Emulsifying activities of sodium caseinate at pH 2 and 8, and whey protein at pH 7 and 8 improved. Emulsion stability of sodium caseinate improved at entire pH range studied. Foam expansion and foam stability of samples improved with TGase-treatment. Viscosities of TGase-treated samples were higher than those of untreated ones.

• Journal of Korean Dental Science
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• v.6 no.1
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• pp.22-26
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• 2013

Purpose: Transglutaminase 2 (TGase 2) is expressed by tumor necrosis factor-${\alpha}$ in various carcinoma. The role of TGase 2 expression in salivary gland tumors is not clear yet. Established slaivary gland tumor (SGT)cell line has been used to study the pathogenesis of salivary gland adenocarcinoma on a cellular level in vitro. The pupose of this study were to examine mRNA expression of TGase 2 in SGT cell line compared to other tumor cell lines, and to apply these results to the pathogenesis of salivary gland tumor. Materials and Methods: After SGT, SCC-15, HN 4, and HeLa tumor cell lines were cultured under preconfl uency, and 3 days after postconfl uency, the cells were harvested for total RNA extraction and cDNA preparation. Result: Reverse transcription polymerase chain reaction for semiquantitative mRNA analysis was done. TGase 2 mRNA expression was not induced by confl uency in all the cell lines. TGase 2 mRNA expression was variable but markedly enhanced in SGT cell line. Conclusion: mRNA expression of TGase 2 should play an important role in the pathogenesis of SGT cell line originated from ductal cell.

• Korean journal of food and cookery science
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• v.33 no.2
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• pp.198-208
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• 2017

Purpose: To improve the quality of basic gluten-free rice bread composed of white rice flour, salt, sugar, yeast, skim milk powder, olive oil, and water, the effects of transglutaminase (TGase), whey protein (WP), propylene glycol alginate (PGA), and hydroxypropylmethylcelluose (HPMC) were investigated. Methods: TGase, WP, PGA, and HPMC were added to rice flour cumulatively. The pasting properties of rice flour blends as well as volume, shape, color value, textural properties and sensory evaluation of basic rice bread (RB1) RB1+TGase (RB2), RB1+TGase+WP (RB3), RB1+TGase+WP+PGA (RB4), and RB1+TGase+WP+PGA+HPMC (RB5) were compared. Results: Consistency of rice batter increased upon addition of TGase, WP and PGA, and RB3 and RB4 had higher specific volumes than others. PGA improved volume, crumb air cell uniformity, and resilience but lowered elasticity and moistness of RB. HPMC increased, hardness, moistness and softness, and slightly reduced volume. Conclusion: Therefore, it is suggested that hydrocolloids, PGA and HPMC may be necessary to improve volume, crumb structure, textural properties and overall eating quality of gluten-free rice bread.