• 제목/요약/키워드: TGase

검색결과 59건 처리시간 0.022초

효모시스템에서 Human Transglutaminase C(TGase II)의 발현에 관한 연구 : C-말단부위의 결손효과

  • 우상규;정선미;이상기;안병윤;김희철
    • 한국미생물·생명공학회지
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    • 제24권3호
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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.

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Transglutaminase 2 Promotes Autophagy by LC3 Induction through p53 Depletion in Cancer Cell

  • Kang, Joon Hee;Lee, Seon-Hyeong;Cheong, Heesun;Lee, Chang Hoon;Kim, Soo-Youl
    • Biomolecules & Therapeutics
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    • 제27권1호
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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.

재구성 햄 제조 시 Transglutaminase 첨가에 의한 텀블링 시간의 단축과 전단력 증진 효과 (Reduction of Tumbling Time and Improvement of Shear Value for the Manufacture of Restructured Hams using Transglutaminase)

  • 이홍철;진구복
    • 한국축산식품학회지
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    • 제24권1호
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    • pp.23-28
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    • 2004
  • 본 연구는 TGase를 사용함으로써 재구성육 햄의 결착력과 텀블링시간에 미치는 영향을 조사하기 위하여 실시하였다. 재구성 햄은 73.9∼75.7% 수분, 3.63∼4.18% 지방, 16.6∼20.6% 단백질로 구성되었고, pH는 5.95∼6.10 그리고 0.95∼0.96의 수분 활성도를 보였다. 텀블링시간의 증가나 TGase 첨가에 의한 발색과 기능성에는 유의차를 보이지 않았으나 TGase 무첨가구는 첨가구에 비해 텀블링시간에 관계없이 조직학적 성상이 낮게 나타났다. 전단력은 재구성육 햄에서 TGase를 첨가하지 않은 경우 텀블링시간을 길게 하거나 또는 TGase의 첨가시 전단력이 향상되었다. 즉, TGase의 첨가는 1시간으로 텀블링시간을 줄인 대조구가 텀블링시간이 4시간인 대조구에 비해 조직학적 성상이나 전단력이 유의적 차이를 보여 저하된 것에 반하여, 유의차 없는 조직학적 성상과 전단력을 보여줌으로써 텀블링시간의 감소에 대한 보완적 효과를 나타내었고, 반면에 TGase를 첨가하고 4시간동안 텀블링하였던 처리구 TRT 4는 4시간 동안 텀블링만을 한 CTL 4와 조직학적 성상과 전단력의 향상을 보여주지 못하였다. 즉, TGase 첨가에 의한 효과와 텀블링 시간의 증가로 인한 효과는 각각 나타났으나, 두 요인의 복합에 의한 상승효과는 나타나지 않았다. 결론적으로 재구성육 햄의 제조에 있어서 0.3% TGase의 첨가는 전단력을 증가시킴으로써 상대적으로 텀블링 시간을 줄이는 효과를 나타냈고, 대조구(CTL 1)에 대해서는 조직감과 전단력의 보완적 효과를 보여준 것으로 사료되어진다.

Novel Therapeutic Approach toward Inflammatory Diseases: Targeting Transglutaminase 2

  • Kim Soo-Youl;Kim Hong-Yeoul;Lee Jae-Dong
    • 대한한의학회지
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    • 제25권4호
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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.

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Edible Packaging Film Derived from Mechanically Deboned Chicken Meat Proteins: Effect of Transglutaminase on Physicochemical Properties

  • Yayli, Damla;Turhan, Sadettin;Saricaoglu, Furkan Turker
    • 한국축산식품학회지
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    • 제37권5호
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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.

세균 유래 단백질연결효소 Transglutaminase의 클로닝과 효모에서의 발현 (Expression and Cloning of Microbial Transglutaminase in S. cerevisiae)

  • 김현영;오동순;김종화
    • 한국균학회지
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    • 제36권1호
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    • pp.93-97
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    • 2008
  • 방선균 Streptomyces mobaraensis IFO13819 유래 transglutaminase(mTGase)는 칼슘 비의존성으로 식품산업에서 유용하게 이용되고 있는 효소이다. mTGase는 406개의 아미노산으로 구성되어 있는데 leader와 pro 부위는 75개, 구조 부위는 331개의 아미노산으로 구성되어있다. mTGase의 pro와 구조 유전지를 pYAEG-TER 벡터에 클로닝하고 Saccharomyces cerevisiae 2805에 형질전환하였다. 형질전환체에서 mTGase의 발현을 Northern hybridization을 통해 확인하였으며, 최대 26 mU/ml의 mTGase의 활성을 측정할 수 있었다.

Transglutaminase-2 Is Involved in Expression of Osteoprotegerin in MG-63 Osteosarcoma Cells

  • Lee, Hye Ja;Lee, Chang Hoon
    • Biomolecules & Therapeutics
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    • 제21권3호
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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.

Transglutaminase를 처리한 분말 유제품의 특성 (Properties of Transglutaminase Treated Milk Product Powders)

  • 정지은;홍윤호
    • 한국식품과학회지
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    • 제37권3호
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    • pp.345-351
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    • 2005
  • 본 연구에서는 시판되고 있는 카제인 나트륨, 유청 단백질, 탈지분유 및 전지분유에 TGase를 첨가하여 이화학적 특성 및 식품첨가물 소재로서의 기능적 특성 등을 조사하였다. 카제인 나트륨의 경우 TGase효소 반응 후 pH 2, pH 4와 알칼리 범위에서, 유청 단백질은 pH 4에서 용해성이 향상되었고 탈지분유에서는 pH 4와 전지분유에서는 모든 pH 범위에서 용해성이 향상되었다. TGase를 첨가한 우유 단백질과 우유 분말 제품이 무첨가군에 비하여 pH 의존적으로 용해성, 유화활성 및 거품형성 등에 기능적 특성이 부분적으로 우수함을 알 수 있었다. 또한 TGase 첨가에 따라 일반성분의 변화가 없었으며 인체내 소화효소에 의해 가수분해가 용이하였고 점도의 증가가 관찰되었다. TGase를 첨가한 제품은 이화학적, pH 및 반응시간 등의 특징에 의하여 영향을 받으므로 식품에 응용할 경우 기능성들이 합리적으로 조절되도록 함이 바람직하다.

Transglutaminase 2 mRNA Expression in Salivary Gland Tumor Cell Line

  • Chun, Yoon Kwon;Lee, Chong Heon
    • Journal of Korean Dental Science
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    • 제6권1호
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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.

단백질과 트란스글루타미나제 첨가 글루텐 프리 쌀빵의 품질에 대한 친수콜로이드의 효과 (Effects of Hydrocolloids on the Quality of Protein and Transglutaminase Added Gluten-free Rice Bread)

  • 황순옥;김지명;신말식
    • 한국식품조리과학회지
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    • 제33권2호
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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.