• 제목/요약/키워드: PTP

검색결과 251건 처리시간 0.027초

Effects of PTP1B Inhibitors and Taurine on Blood Lipid Profiles in Adolescents Obesity Model Rats

  • Cheong, Sun-Hee;Hyeongjin Cho;Chang, Kyung-Ja
    • 대한지역사회영양학회:학술대회논문집
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    • 대한지역사회영양학회 2004년도 춘계학술대회
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    • pp.437.1-437
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    • 2004
  • The protein, called PTP1B (protein tyrosine phosphatase 1B), joins a list of enzymes that mice are associated with obesity. The purpose of this study was to investigate the effects of PTP1B inhibitors and taurine on blood lipid profiles in adolescents obesity model rats. Three week-old thirty-six male Sprague-Dawley rats were randomly assigned to six groups (high fat diet group; HFD group, high fat diet + taurine group; HF+TR group, high fat diet+PTP1B inhibitor A group; HF+A group, high fat diet+PTP1B inhibitor B; HF+B group, high fat diet+PTP1B inhibitor A+taurine group; HF+A+TR group, high fat diet + PTP1B inhibitor B+taurine group; HF+B+TR group).(omitted)

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PTP(Press-Through-Pack)에 의한 식도이물 3례 (Three Cases of A Press-Through-Pack in the Esophagus)

  • 국중호;임상철;조재식
    • 대한기관식도과학회지
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    • 제6권2호
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    • pp.201-203
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    • 2000
  • The PTP (Press-Through-Pack) has been widely used as a packing material for tablets and capsules. But esophageal foreign bodies attributed to the PTP may cause injury to esophageal mucous membrane, potentially inducing severe complications such as hemorrhage, perforation, etc. We report three cases of PTP foreign bodies in esophagus with reference to recent literature.

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유자와 탱자 과피 추출물의 항산화 및 면역 활성 효과 (Effect of Ethanol Extract from Peel of Citrus junos and Poncirus trifoliata on Antioxidant and Immune Activity.)

  • 박준희;강병원;김지은;서민정;이영춘;이재헌;주우홍;최영현;임학섭;정영기;이복규
    • 생명과학회지
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    • 제18권3호
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    • pp.403-408
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    • 2008
  • 본 연구는 탱자(Poncirus trifoliata) 과피의 80% 에탄올 추출물(PTP)에 대한 항산화 활성과 면역 활성을 유자(Citrus junos) 과피 추출물(CJP)과 비교하였다. 총 phenol 함량과 총 flavonoids 함량은 PTP가 각각 $60.75{\pm}1.15$ mg/100 g과 $33.75{\pm}0.15$ mg/100 g이었으며, 이는 CJP에 비해 다소 낮았다. PTP의 항산화 활성은 농도 의존적으로 증가하였으며 CJP의 항산화 활성과 비슷하게 나타났다. 면역반응 중 대식 세포가 생성하는 NO 생성량을 측정한 결과 CJP와 PTP를 단독으로 처리한 경우와 LPS와 혼합하여 처리한 경우 모두 1 mg/ml까지는 대조구와 비교하여 농도 의존적으로 증가하였으나 고농도에서는 감소하는 경향을 나타내었다. 비장세포를 이용한 면역세포 증식능에서 CJP와 PTP를 첨가한 경우, 1 mg/ml까지는 대조구와 비교하여 농도 의존적으로 증가하였으나 고농도에서는 감소하였다.

Docking Study of Biflavonoids, Allosteric Inhibitors of Protein Tyrosine Phosphatase 1B

  • Lee, Jee-Young;Jung, Ki-Woong;Woo, Eun-Rhan;Kim, Yang-Mee
    • Bulletin of the Korean Chemical Society
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    • 제29권8호
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    • pp.1479-1484
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    • 2008
  • Protein tyrosine phosphatase (PTP) 1B is the superfamily of PTPs and a negative regulator of multiple receptor tyrosine kinases (RTKs). Inhibition of protein tyrosine phosphatase 1B (PTP1B) has been proposed as a strategy for the treatment of type 2 diabetes and obesity. Recently, it has been reported that amentoflavone, a biflavonoid extracted from Selaginella tamariscina, inhibited PTP1B. In the present study, docking model between amentoflavone and PTP1B was determined using automated docking study. Based on this docking model and the interactions between the known inhibitors and PTP1B, we determined multiple pharmacophore maps which consisted of five features, two hydrogen bonding acceptors, two hydrogen bonding donors, and one lipophilic. Using receptor-oriented pharmacophore-based in silico screening, we searched the biflavonoid database including 40 naturally occurring biflavonoids. From these results, it can be proposed that two biflavonoids, sumaflavone and tetrahydroamentoflavone can be potent allosteric inhibitors, and the linkage at 5',8''-position of two flavones and a hydroxyl group at 4'-position are the critical factors for their allosteric inhibition. This study will be helpful to understand the mechanism of allosteric inhibition of PTP1B by biflavonoids and give insights to develop potent inhibitors of PTP1B.

PTP1B Inhibitory Secondary Metabolites from Marine-Derived Fungal Strains Penicillium spp. and Eurotium sp.

  • Sohn, Jae Hak;Lee, Yu-Ri;Lee, Dong-Sung;Kim, Youn-Chul;Oh, Hyuncheol
    • Journal of Microbiology and Biotechnology
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    • 제23권9호
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    • pp.1206-1211
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    • 2013
  • The selective inhibition of PTP1B has been widely recognized as a potential drug target for the treatment of type 2 diabetes and obesity. In the course of screening for PTP1B inhibitory fungal metabolites, the organic extracts of several fungal species isolated from marine environments were found to exhibit significant inhibitory effects, and the bioassay-guided investigation of these extracts resulted in the isolation of fructigenine A (1), cyclopenol (2), echinulin (3), flavoglaucin (4), and viridicatol (5). The structures of these compounds were determined mainly by analysis of NMR and MS data. These compounds inhibited PTP1B activity with 50% inhibitory concentration values of 10.7, 30.0, 29.4, 13.4, and 64.0 ${\mu}M$, respectively. Furthermore, the kinetic analysis of PTP1B inhibition by compounds 1 and 5 suggested that compound 1 inhibited PTP1B activity in a noncompetitive manner, whereas compound 5 inhibited PTP1B activity in a competitive manner.

TK-PTP, Protein Tyrosine Phosphatase from Hyperthermophilic Archaeon Thermococcus kadakaraensis KODI : Enzymatic Characteristics and Isolation of its Substrate Proteins

  • Jeon, Sung-Jong;Kim, Byung-Woo
    • 한국미생물생명공학회:학술대회논문집
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    • 한국미생물생명공학회 2001년도 Proceedings of 2001 International Symposium
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    • pp.135-136
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    • 2001
  • The Tk-ptp gene encoding a protein tyrosine phosphatase (PTPase) from the hyperthermophilic archaeon Thermococcus kodakaraensis KODI was cloned and sequenced. Sequence analysis indicated that Tk-ptp encoded a protein consisting 147 amino acid residues (16,953 Da). The wild type and the mutants were expressed in Escherichia coli cells as His-tagged fusion proteins and examined for enzyme characteristics. Tk-PTP possessed two unique features that were not found in eucaryal and bacterial counterparts. First, the recombinant Tk-PTP showed the phosphatase activity not only for the phosphotyrosine but also phosphoserine. Second, the conserved Asp (Asp-63), which was considered to be a critical residue, was not involved in catalysis. In order to know a specific substrate for Tk-PTP, C93S mutant was used to trap substrate protein. Proteins of 120, 60 and 53 kDa were isolated specifically from KODI cell lysates by affinity chromatography with Tk-PTP-C93S. It is suggested that these proteins are tyrosine-phosphorylated substrates of Tk-PTP.

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Polythiophene막을 이용한 네마틱액정의 배향효과 (Alignment effects of the nematic liquid crystal on polythiophene Surfaces)

  • 서대식
    • 한국전기전자재료학회:학술대회논문집
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    • 한국전기전자재료학회 1997년도 춘계학술대회 논문집
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    • pp.127-129
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    • 1997
  • The high pretilt angles in nematic liquid crystals (NLCs) have been generated on robbed polythiophene (PTP) surfaces with alkyl chain lengths. The pretilt angle of the NLC was observed on unidirectionally rubbed PTP surfaces with alkyl chains with more than 9 carbon atoms. We obtained the Pretilt angle of 15~40$^{\circ}$ on rubbed PTP surfaces with 10 carbon atoms in the a1ky1 chain. Also, the pretilt angles of 65~80$^{\circ}$ of NLC were obtained on rubbed PTP surfaces with 11 and 12 carbon atoms in the alkyl chain. We suggest that this high pretilt angle generation in NLC is due to the surface-excluded volume effect by the alkyl chain lengths between. the LCs and the PTP surfaces. Finally, we conclude the odd-even effect on rubbed PTP surfaces is clearly contributed to the pretilt angle generation.

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Screening of Marine Microbial Extracts for Tyrosine Phosphatase 1B Inhibitors

  • Sohn, Jae-Hak;Park, Sun Jung;Seo, Changon;Chun, Bokyung;Oh, Hyuncheol
    • 한국해양바이오학회지
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    • 제2권4호
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    • pp.230-233
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    • 2007
  • Protein tyrosine phosphatase 1B (PTP1B) acts as a negative regulator of insulin signaling, and selective inhibition of PTP1B has served as a potential drug target for the treatment of type 2 diabetes. As part of our searching for PTP1B inhibitors from natural products, the extracts of marine microorganisms were screened for the inhibitory effects on the activity of protein tyrosine phosphatase 1B (PTP1B). Among the tested 304 extracts, 29 extracts exhibited inhibition rate ranging 40.1 - 83.6 % against PTP1B at the concentration level of $30{\mu}g/mL$.

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