• 제목/요약/키워드: Transmembrane

검색결과 592건 처리시간 0.029초

개구리 피부(皮腐)의 막전위(膜電位) 및 단락전류(短絡電流)에 미치는 Morphine의 영향 (Effects of Morphine on the Transmembrane Potential and the Short Circuit Current of Frog Skin)

  • 채수완;조규박
    • 대한약리학회지
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    • 제20권1호
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    • pp.23-32
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    • 1984
  • 정상 또는 morphine을 처리한 개구리(Rana nigromaculate)의 피부에서 Ussing 등의 방법에 의하여 막전위와 단락전류에 미치는 morphine의 작용과 morphine 작용에 미치는 전해질의 영향을 관찰하여 다음과 같은 성적을 얻었다. 1) Morphine $5{\pm}10^{-3}$은 개구리 피부의 막전위와 단락전류를 현저히 감소시켰으며 약물투여후 60분후에 최고의 효과를 나타냈다. 2) Naloxone $10^{-4}$은 morphine의 막전위 및 단란전류 억제작용을 차단치 못하였다. 3) 영양액내 $Na^+$ 농도감소, $K^+$ 농도증가 및 $Ca^{2+}$농도증가는 morphine의 막전위 및 단란전류 억제작용ㅇ르 현저히 강화하였으며, $Mn^{2+}$첨가는 morphine의 막전위 억제효과만을 강화시켰다. 한편 $Ca^{2+}$ 농도의 감소로써 morphine의 단락전류억제 효과는 현저히 약화되었으며 $Ma^{2+}$농도 감소로써 morphine의 단락전류 억제효과로 더불어 막전위 억제효과도 감약되었다. 4) Morphine 처리 표본에서 막전위와 단락전류는 morphine 처리 초기에 일시적인 감소를 일으킨 후 증가하여 morphine 처리 $4{\sim}8$일에는 대조군에 비하여 현저히 상승하였다. 또한 morphine의 막전위 및 단락전류 억제효과에 있어서도 morphine처리 $1{\sim}2$일에는 morphine의 억제효과가 강화되나 morphine의 처리 4 또는 8일에는 현저히 약화되었다. 이상의 실험성적으로 morphine의 약물내성을 포함한 그 약리적작용이 생체막에서의 전해질수송 또는 전해질 투과성에 영향을 미쳐 초래될 수 있음을 시사하는 것으로 추측하였다.

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Structure Determination of Syndecan-4 Transmembrane Domain using PISA Wheel Pattern and Molecular Dynamics simulation

  • Choi, Sung-Sub;Jeong, Ji-Ho;Kim, Ji-Sun;Kim, Yongae
    • 한국자기공명학회논문지
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    • 제18권2호
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    • pp.58-62
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    • 2014
  • Human transmembrane proteins (hTMPs) are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these hTMPs, it is important to prepare reasonable amounts of proteins. However, their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of hTMPs. We tried to produce large amounts of Syndecan-4 transmembrane domain (Syd4-TM) that is related to the healing wounds and tumor for a long time. In this study, we performed the structure determination of Syd4-TM combining the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on $^{15}N-^1H$ 2D SAMPI-4 solid-state NMR of expressed Syd4-TM and Molecular Dynamics (MD) simulation using Discovery Studio 3.1.

NMR and Circular Dichroism Studies on Human CD99 Transmembrane Domain

  • Kim, Hai-Young;Shin, Joon;Shin, Young-Kee;Park, Seong-Hoe;Lee, Weon-Tae
    • 한국자기공명학회논문지
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    • 제7권1호
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    • pp.37-45
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    • 2003
  • Human CD99 is a ubiquitous 32-kDa transmembrane protein encoded by mic2 gene. Recently it has been reported that expression of a splice variant of CD99 transmembrane protein (Type I and Type II) increases invasive ability of human breast cancer cells. To understand structural basis for cellular functions of CD99 Type II, we have initiated studies on hCD99$\^$TMcytoI/ using circular dichroism (CD) and multi-dimensional NMR spectroscopy. CD spectrum of hCD99$\^$TMytoI/ in the presence of 200mM DPC and CHAPS displayed an existence ${\alpha}$-helical conformation, showing that it could form an ${\alpha}$-helix under membrane environments. In addition, we have found that the cytoplasmic domain of CD99 would form symmetric dimmer in the presence of transmembrane domain. Although it has been rarely figured out the correlation between structure and functional mechanism of hCD99$\^$TMcytoI/, the dimerization or oligomerization would play an important role in its biological function.

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Characterization of the cellular localization of C4orf34 as a novel endoplasmic reticulum resident protein

  • Jun, Mi-Hee;Jun, Young-Wu;Kim, Kun-Hyung;Lee, Jin-A;Jang, Deok-Jin
    • BMB Reports
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    • 제47권10호
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    • pp.563-568
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    • 2014
  • Human genome projects have enabled whole genome mapping and improved our understanding of the genes in humans. However, many unknown genes remain to be functionally characterized. In this study, we characterized human chromosome 4 open reading frame 34 gene (hC4orf34). hC4orf34 was highly conserved from invertebrate to mammalian cells and ubiquitously expressed in the organs of mice, including the heart and brain. Interestingly, hC4orf34 is a novel ER-resident, type I transmembrane protein. Mutant analysis showed that the transmembrane domain (TMD) of hC4orf34 was involved in ER retention. Overall, our results indicate that hC4orf34 is an ER-resident type I transmembrane protein, and might play a role in ER functions including $Ca^{2+}$ homeostasis and ER stress.

Targeting of Nuclear Encoded Proteins to Chloroplasts: a New Insight into the Mechanism

  • Lee, Yong-Jik;Kim, Yong-Woo;Pih, Kyeong-Tae;Hwang, Inhwan
    • 식물조직배양학회지
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    • 제27권5호
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    • pp.407-409
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    • 2000
  • Outer envelope membrane proteins of chloroplasts encoded by the nuclear genome are transported without the N-terminal transit peptide. Here, we investigated the targeting mechanism of AtOEP7, an Arabidopsis homolog of small outer envelope membrane proteins in vivo. AtOEP7 was expressed transiently in protoplasts or stably in transgenic plants as fusion proteins with GFP. In both cases AtOEP7:GFP was targeted to the outer envelope membrane when assayed under a fluorescent microscope or by Western blot analysis. Except the transmembrane domain, deletions of the N- or C-terminal regions of AtOEP7 did not affect targeting although a region closed to the C-terminal side of the transmembrane domain affected the targeting efficiency. Targeting experiments with various hybrid transmembrane mutants revealed that the amino acid sequence of the transmembrane domain determines the targeting specificity The targeting mechanism was further studied using a fusion protein, AtOEP7:NLS:GFP, that had a nuclear localization signal. AtOEP7:NLS:GFP was efficiently targeted to the chloroplast envelope despite the presence of the nuclear localization signal. Taken together, these results suggest that the transmembrane domain of AtOEP7 functions as the sole determinant of targeting specificity and that AtOEP7 may be associated with a cytosolic component during translocation to the chloroplast envelope membrane.

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Integrin activation

  • Ginsberg, Mark H.
    • BMB Reports
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    • 제47권12호
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    • pp.655-659
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    • 2014
  • Integrin-mediated cell adhesion is important for development, immune responses, hemostasis and wound healing. Integrins also function as signal transducing receptors that can control intracellular pathways that regulate cell survival, proliferation, and cell fate. Conversely, cells can modulate the affinity of integrins for their ligands a process operationally defined as integrin activation. Analysis of activation of integrins has now provided a detailed molecular understanding of this unique form of "inside-out" signal transduction and revealed new paradigms of how transmembrane domains (TMD) can transmit long range allosteric changes in transmembrane proteins. Here, we will review how talin and mediates integrin activation and how the integrin TMD can transmit these inside out signals.

Monoacylglycerol O-acyltransferase 1 (MGAT1) localizes to the ER and lipid droplets promoting triacylglycerol synthesis

  • Lee, Yoo Jeong;Kim, Jae-woo
    • BMB Reports
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    • 제50권7호
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    • pp.367-372
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    • 2017
  • Monoacylglycerol acyltransferase 1 (MGAT) is a microsomal enzyme that catalyzes the synthesis of diacylglycerol (DAG) and triacylglycerol (TAG). However, the subcellular localization and catalytic function domain of this enzyme is poorly understood. In this report, we identified that murine MGAT1 localizes to the endoplasmic reticulum (ER) under normal conditions, whereas MGAT1 co-localize to the lipid droplets (LD) under conditions of enriching fatty acids, contributing to TAG synthesis and LD expansion. For the enzyme activity, both the N-terminal transmembrane domain and catalytic HPHG motif are required. We also show that the transmembrane domain of MGAT1 consists of two hydrophobic regions in the N-terminus, and the consensus sequence FLXLXXXn, a putative neutral lipid-binding domain, exists in the first transmembrane domain. Finally, MGAT1 interacts with DGAT2, which serves to synergistically increase the TAG biosynthesis and LD expansion, leading to enhancement of lipid accumulation in the liver and fat.

Site-directed mutagenesis에 의한 PrrB histidine kinase의 신호인지 기능에 관련된 아미노산의 발굴 (Identification of Amino Acids Involved in the Sensory Function of the PrrB Histidine Kinase by Site-directed Mutagenesis)

  • 김용진;고인정;오정일
    • 생명과학회지
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    • 제16권3호
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    • pp.485-492
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    • 2006
  • 광합성세균인 Rhodobacter sphaeroides의 PrrBA two-component system은 산소분압의 변화에 따라 광합성 유전자의 발현을 조절하는 주요한 조절계 중 하나이다. PrrBA two-component system은 PrrB histidine kinase와 PrrA response regulator로 구성되어 있는데, PrrB의 N-말단 transmembrane 도메인은 신호인지 도메인으로서, 여섯 개의 transmembrane helix가 세 개의 periplasmic loop와 두 개의 cytoplasmic loop을 형성하고 있다. 그 중 세 번째, 네 번째 transmembrane helix와 두 번째 periplasmic loop가 산화/환원 인지 기능에 있어 중요한 역할을 할 것이라고 제안되었다. 본 연구에서는, 두 번째 periplasmic loop와 그 인접 부위에서의 돌연변이 (Asp-90, Gln-93, Leu-94, Leu-98, Asn-106)에 의해 PrrB의 인지 기능에 있어 심각한 결함이 생기는 것을 증명하였고, 이는 이 아미노산들이 PrrB의 산화/환원 인지 기능에 연관되어 있을 수 있다는 것을 보여준다. PrrB의 돌연변이 형태 (D90E, D90N, D90A)가 대장균에서 과발현되어서 affinity chromatography에 의해 정제되었고, 정제된 단백질의 자가인산화 반응이 측정되었다. PrrB D90N 변이형태는 PrrB wild-type보다 높은 자가인산화 활성을 가지는 반면에, PrrB D90E 변이형태는 PrrB wild-type보다 낮은 자가인산화 활성을 나타내었다. 그리고 D90A 변이형태는 PrrB의 자가인산화 활성이 매우 약화되었다.

Transmembrane Signaling Model of a Serine Chemotaxis Receptor

  • Kim, Kyeong-Kyu;Hisao Yokota;Kim, Sung-Hou
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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    • pp.20-20
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    • 1999
  • Bacterial chemotaxis receptors are some of the simplest and most studied transmembrane receptors. Their simple signaling pathway has elements relevant for understanding the mechanisms for signal recognition, transduction through the membrane, relays among the molecules in the pathway, and adaptation to a persistent signal.(omitted)

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SVM과 HMM을 이용한 $\alpha$-Helix 막횡단 단백질 예측 (Predicting Transmembrane $\alpha$-helix protein with SVM and HMM)

  • 송철환;유성준;김민경;설영주
    • 한국정보과학회:학술대회논문집
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    • 한국정보과학회 2003년도 가을 학술발표논문집 Vol.30 No.2 (2)
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    • pp.817-819
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    • 2003
  • 현재 바이오인포매틱스(Bioinformatics) 분야에서 가장 중요한 부분 중의 하나는 유전자 및 단백질의 구조와 기능을 정확하게 예측하는 것이다. 이는 질병 치료 및 신약개발에 유용하여 이로부터 나온 결과로부터 경제적 산업적 효과를 기대할 수 있다. 이 논문에서는 기계학습(Machine Learning)의 한 분야인 SVM(Support Vector Machine)과 HMM(Hidden Markov Model)를 결합하여 단백질의 막횡단(Transmembrane) $\alpha$-Helix 단백질 지역을 예측하는 새로운 알고리즘을 개발, 구현 및 실험하였다. 그 결과 이 두 가지 알고리즘이 결합된 방식을 사용함으로써 성능을 향상 시킬 수 있음을 증명했다.

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