• 제목/요약/키워드: 30K protein

검색결과 3,894건 처리시간 0.034초

대장암과 선종 병변에서 mTOR 신호 단백질의 면역조직화학 염색성 평가 (Evaluation of the Immunohistochemical Staining Pattern of the mTOR Signaling Proteins in Colorectal Cancers and Adenoma Lesions)

  • 김진목;이현욱
    • 대한임상검사과학회지
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    • 제49권4호
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    • pp.470-476
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    • 2017
  • mTOR 신호전달 단백질의 변화는 다양한 종류의 암에서 관찰 되었다. 따라서 이들 단백질은 최근에 암 치료제에 대한 새롭고 흥미로운 표적이 되고 있다. 우리는 대장암과 선종 환자의 mTOR 세포신호의 활성도를 조사하였다. 면역조직화학적 방법으로 대장암과 선종의 세포신호 단백질 성분인 mTOR, p70-S6K, S6, 4EBP1 발현을 분석하였다. 이번 연구는 모두 100개의 예를 악성(Colorectal Adenocarcinoma, CRAC) 40건, 고등급 선종(Adenoma with High grade intraepithelial neoplasms, HIN) 30건, 저등급 선종(Adenoma with Low-grade intraepithelial neoplasms, LIN) 30건으로 분류하여 진행하였다. p-mTOR의 발현률은 LIN 7%, HIN 30%, CRAC 75%였고 p-S6의 발현률 또한 LIN 10%, HIN 27%, CRAC 55%였다. p-mTOR, p-S6의 발현과 선종-선암 연속성은 중요한 상관관계 있다는 것이 발견되었다. 그리고 흥미롭게도 p-S6 발현률은 진행암보다 초기암에서 더 높았다.

Opening of ATP-sensitive $K^+$ Channel by Pinacidil Requires Serine/Threonine Phosphorylation in Rat Ventricular Myocytes

  • Kwak, Yong-Geun;Chae, Soo-Wan
    • The Korean Journal of Physiology and Pharmacology
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    • 제3권3호
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    • pp.293-303
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    • 1999
  • The influences of specific protein phosphatase and protein kinase inhibitors on the ATP-sensitive $K^+\;(K_{ATP})$ channel-opening effect of pinacidil were investigated in single rat ventricular myocytes using patch clamp technique. In cell-attached patches, pinacidil $(100\;{\mu}M)$ induced the opening of the $K_{ATP}$ channel, which was blocked by the pretreatment with H-7 $(100\;{\mu}M)$ whereas enhanced by the pretreatment with genistein $(30\;{\mu}M)$ or tyrphostin A23 $(10\;{\mu}M)$. In inside-out patches, pinacidil $(10\;{\mu}M)$ activated the $K_{ATP}$ channels in the presence of ATP (0.3 mM) or AMP-PNP (0.3 mM) and in a partial rundown state. The effect of pinacidil $(10\;{\mu}M)$ was not affected by the pretreatment with protein tyrosine phosphatase 1B $(PTP1B,\;10\;{\mu}g\;ml^{-1}),$ but blocked by the pretreatment of protein phosphatase 2A $(PP2A,\;1\;U\;ml^{-1})$. In addition, pinacidil $(10\;{\mu}M)$ could not induce the opening of the reactivated $K_{ATP}$ channels in the presence of H-7 $(100\;{\mu}M)$ but enhanced it in the presence of ATP (1 mM) and genistein $(30\;{\mu}M).$ These results indicate that the $K_{ATP}$ channel-opening effect of pinacidil is not mediated via phosphorylation of $K_{ATP}$ channel protein or associated protein, although it still requires the phosphorylation of serine/threonine residues as a prerequisite condition.

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Yam Extracts Increase Cell Proliferation and Bone Matrix Protein Collagen Synthesis of Murine Osteoblastic MC3T3-E1 Cells

  • Shin, Mee-Young;Alcantara, Ethel H.;Park, Youn-Moon;Kwon, Soon-Tae;Kwun, In-Sook
    • Preventive Nutrition and Food Science
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    • 제16권4호
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    • pp.291-298
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    • 2011
  • Yam extracts (Dioscorea batatas) have been reported to possess a variety of functions. However, studies on its osteogenic properties are limited. In this study, we investigated the effect of ethanol and water extracts on osteoblast proliferation and bone matrix protein synthesis, type I collagen and alkaline phosphatase (ALP), using osteoblastic MC3T3-E1 cell model. MC3T3-E1 cells were cultured with yam ethanol and water extracts (0~30 mg/L) within 39 days of osteoblast differentiation period. Cell proliferation was measured by MTT assay. Bone matrix proteins were assessed by the accumulation of type I collagen and ALP activity by staining the cell layers for matrix staining. Also, the secreted (media) matrix protein concentration (type I collagen) and enzyme activity (ALP) were measured colorimetrically. Yam ethanol and water extracts stimulated cell proliferation within the range of 15~30 mg/L at 15 day treatment. The accumulation of type I collagen in the extracellular matrix, as well as secreted collagen in the media, increased with increasing doses of yam ethanol (3~15 mg/L) and water (3~30 mg/L) extracts. ALP activity was not affected by yam ethanol extracts. Our results demonstrated that yam extracts stimulated osteoblast proliferation and enhanced the accumulation of the collagenous bone matrix protein type I collagen in the extracellular matrix. These results suggest that yam extracts may be a potential activator for bone formation by increasing osteoblast proliferation and increasing bone matrix protein type I collagen. Before confirming the osteogenic action of yam, further studies for clarifying how and whereby yam extracts can stimulate this ostegenesis action are required.

단백질 침착에 의한 소프트콘택트렌즈의 직경 및 곡률반경 변화 (The diameter and base curve changes of soft contact Lens by protein deposition)

  • 박미정;조규태;신성환;이흠숙;김대수
    • 한국안광학회지
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    • 제10권3호
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    • pp.165-171
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    • 2005
  • 본 연구는 단백질 침착에 의한 소프트콘택트렌즈의 직경 및 곡률반경의 변화를 밝히기 위해 수행되었다. 소프트콘택트렌즈를 인공누액 및 누액과 동일한 조성의 단백질 용액에서 2분, 10분, 30분, 1시간, 3시간, 6시간, 12시간, 24시간 담가둔 후, 고속촬영기(Fastcam ultima 1024)로 촬영하여 직경 및 곡률반경을 측정하였다. 인공누액에 오랫동안 담가둔 소프트콘택트렌즈일수록 소프트콘택트렌즈의 직경과 곡률반경의 변화가 컸다. 단백질만을 침착시킨 소프트콘택트렌즈의 경우도 유사한 양상이 나타나 직경 및 곡률반경이 감소하였다. 그러나 칼슘이온의 영향은 단백질에 비해 미약한 것으로 나타났다. 이상의 결과로 누액 단백질로 인하여 소프트콘택트렌즈의 직경 및 곡률반경이 감소되며, 이러한 결과는 렌즈 착용 후의 착용감저하와 관련이 있을 것으로 여겨진다.

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Production of Ready-to-Reconstitute Functional Beverages by Utilizing Whey Protein Hydrolysates and Probiotics

  • Kumar, Sabbini Kalyan;Jayaprakasha, Heddur Manjappa;Paik, Hyun-Dong;Kim, Soo-Ki;Han, Song-Ee;Jeong, A-Ram;Yoon, Yoh-Chang
    • 한국축산식품학회지
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    • 제30권4호
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    • pp.575-581
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    • 2010
  • This investigation was aimed at developing a ready-to-reconstitute beverage by utilizing probiotics and whey protein hydrolysates carrying bioactive peptides. Cheddar cheese whey was ultrafiltered. The 18% protein retentate was subjected to protein hydrolysis using Neutrase. The hydrolyzed retentate was further condensed to 35% total solids and spray-dried at $75^{\circ}C$ outlet air temperature. Different levels of sugar, citric acid and stabilizer were blended for spray-dried hydrolysates. Spray-dried hydrolysate was further inoculated with different levels of probiotics grown in a whey medium and dried in fluidized-bed drier at $40^{\circ}C$ to obtain a ready-to-reconstitute beverage. Hydrolysis was greatest at an enzyme:substrate ratio of 1:25 for 3 h. Spray-dried hydrolysate reconstituted to 1% protein and blended with 15% sugar, 0.2% citric acid and 0.15% xantham gum resulted in a superior product with no sedimentation. Accordingly, sugar, citric acid and xanthum gum were dry-blended with spray-dried hydrolysates. Bifidobacterium bifidum and Lactobacillus acidophilus that was grown separately in a whey medium, blended to produce 2% spray-dried hydrolysate and dried as described above resulted in a readyto-reconstitute beverage mix. The fluidized dried product typically exhibited a probiotic count of $10^8$colony forming units (CFU)/g. However, blending of probiotic to the retentate and direct spray-drying precipitously reduced the probiotic count to $10^4$ CFU/g of powder.

참깨와 들깨 단백질의 기능성에 관한 연구 (Studies on the Functional Properties of Sesame and Perilla Protein Isolate)

  • 박현숙;안빈;양차범
    • 한국식품과학회지
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    • 제22권3호
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    • pp.350-356
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    • 1990
  • 참깨와 들깨 단백질을 알칼리에서 추출시킨 후 참깨는 pH6.0, 들깨는 pH4.0에서 침전시켜 분리 단백질을 제조하여 그들의 기능성 즉, 용해도, 유화성, 기포성, 유지 및 수분 흡착력 등을 pH와 염농도를 달리하여 측정하였다. 단백질 용해도는 참깨 단백질이 pH6.0에서, 들깨와 대두 단백질은 pH4.0에서 가장 낮아 등전점을 보이었고, pH2.0과 pH8.0 이상에서는 크게 증가하였다. 0.1M NaCl 첨가시에는 참깨 단백질과 들깨 단백질의 경우 전 pH 범위에서 단백질 용해도가 증가하였다. 유화력은 각 시료 단백질의 등전점 부근에서 가장 낮았으며 0.1M NaCl 첨가시에는 모든 시료들의 유화력이 증가되었으나 0.5M NaCl 농도에서는 오히려 감소되는 경향이었다. 유화안정성은 유화력과 비슷한 크기로 나타나, $80^{\circ}C$에서 30분 가열에서도 이들 단백질이 열에 안정함을 보이었다. 기포 형성력은 참깨와 들깨 단백질이 대두 단백질에 비해 현저히 낮았으며, 0.1M NaCl과 0.5M NaCl 첨가시에는 모두 그 값이 증가되는 경향을 보이었다. 기포 안정성은 대두 단백질이 10분 이내에 크게 감소된 반면 참깨와 들깨 단백질은 30분까지 완만하게 감소하였다. 유지 흡착력은 들깨 단백질이 가장 높은 값을 보였고, 수분 흡착력은 시료간에 차이가 없었다.

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시판어묵의 식품학적 품질과 저장안정성 (Food Quality and Shelf-life of Korean Commercial Fried Kamaboko)

  • 류홍수;최남도;이소연
    • 한국수산과학회지
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    • 제47권3호
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    • pp.211-219
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    • 2014
  • To confirm the food quality and storage stability of commercial Korean kamaboko, we experimented with the composition and textural properties using various surimis and kamaboko products. We also investigated changes in protein digestibility and lipid oxidation of vacuum packed products under chilled storage at $4{\pm}1^{\circ}C$. Among the fish meatbased surimi, vegetable mixed surimi had the lowest protein content (23.73 %), as compared to other surimi (51.9-73.6%). Siginificant (P<0.05) differences in protein, lipid content and degree of fat oxidation were noted between the fried kamaboko products of three companies. Adhesiveness, springiness, cohesiveness, gumminess, chewiness and resilience were similar in all samples, but there were notable differences in hardness and fractuability between samples. In vitro protein digestibility and trypsin indigestible substrate (TIS) were not inversely proportional in fried kamaboko products. The protein digestibility (80.30%) of steamed vegetable mixed fried kamaboko was lower than that of other fried samples (84.9-86.2%). Computed protein efficiency ratio (C-PER) of companies A and C's fried kamaboko was 2.6 but company B's was 1.9. There was no noticeable change in thiobarbituric acid reactive substances (TBARs) or protein digestibility for any of the vacuum packed fried kamaboko during 30 days of chilled storage.

Subcellular Localization of Diacylglycerol-responsive Protein Kinase C Isoforms in HeLa Cells

  • Kazi, Julhash U.;Kim, Cho-Rong;Soh, Jae-Won
    • Bulletin of the Korean Chemical Society
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    • 제30권9호
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    • pp.1981-1984
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    • 2009
  • Subcellular localization of protein kinase often plays an important role in determining its activity and specificity. Protein kinase C (PKC), a family of multi-gene protein kinases has long been known to be translocated to the particular cellular compartments in response to DAG or its analog phorbol esters. We used C-terminal green fluorescent protein (GFP) fusion proteins of PKC isoforms to visualize the subcellular distribution of individual PKC isoforms. Intracellular localization of PKC-GFP proteins was monitored by fluorescence microscopy after transient transfection of PKC-GFP expression vectors in the HeLa cells. In unstimulated HeLa cells, all PKC isoforms were found to be distributed throughout the cytoplasm with a few exceptions. PKC$\theta$ was mostly localized to the Golgi, and PKC$\gamma$, PKC$\delta$ and PKC$\eta$ showed cytoplasmic distribution with Golgi localization. DAG analog TPA induced translocation of PKC-GFP to the plasma membrane. PKC$\alpha$, PKC$\eta$ and PKC$\theta$ were also localized to the Golgi in response to TPA. Only PKC$\delta$ was found to be associated with the nuclear membrane after transient TPA treatment. These results suggest that specific PKC isoforms are translocated to different intracellular sites and exhibit distinct biological effects.

한국전통식단의 영양가 분석 (Nutritional Evaluation of Korean Traditional Diet)

  • 이철호;류시생
    • 한국식생활문화학회지
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    • 제3권3호
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    • pp.275-280
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    • 1988
  • 김호직(1944)의 7첩반상 구성예와 방신영(1957)의 식단 참고예를 근거로 하여 전통표준식단의 영양가를 산출하고 이들을 최근의 영양권장량과 비교 평가하였다. 이들 분석된 전통표준식단의 영양가는 일일 2000-2500kcal의 열량과 80-90g의 단백질을 공급할 수 있었다. 열량 구성비는 탄수화물 73-77%, 단백질 15-18%, 지방 10-12% 범위였으며 총 단백질중의 동물성 단백질 비율은 20-30% 수준이었다. 이들 전통표준식단은 열량 섭취량이 2000kcal를 넘으면 다른 필수영양소(단백질, 무기물, 비타민)도 성인남자의 기준에서 충분한 양이 공급되는 균형식임을 확인할 수 있었다.

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건강지향의 저지방/저염 식육가공품을 위한 Microbial Transglutaminase와 기능성 소재 이용 기술 (Application of Microbial Transglutaminase and Functional Ingredients for the Healthier Low-Fat/Salt Meat Products: A Review)

  • 이홍철;진구복
    • 한국축산식품학회지
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    • 제30권6호
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    • pp.886-895
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    • 2010
  • The level of fat and salt can affect the product quality and storage stability of processed meats. Additionally, consumers' demands require dietary guidelines for developing low-fat/salt functional foods. Microbial transglutaminase (MTGase), which enhances textural properties by catalyzing protein-protein cross-linkages, was introduced to develop healthier lowfat/salt meat products. The potential possibilities of low-fat/salt processed meats were reviewed under optimal conditions for functional ingredients from several previous studies. The addition of non-meat protein (e.g. sodium caseinate and soy protein isolates), hydrocolloids (e. g. konjac flour, carrageenan, and alginates), and MTGase alone or in combination with other functional ingredients improved textural and sensory properties similar to those of regularly processed meats. When MTGase was combined with hydrocolloids (konjac flour or sodium alginate) or other functional ingredients, gelling properties of meat protein were improved even at a low salt level. Based on these reviews, functional ingredients combined with new processing technologies could be incorporated into processed meats to improve the functionality of various low-fat/salt meat products.