• Title/Summary/Keyword: membrane cascade

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A Possible Significance in Vertebrate Phototransduction of Multi-Protein Signaling Complexes on Raft-Like Membranes

  • Hayashi, Fumio;Liu, Han;Seno, Keiji
    • Journal of Photoscience
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    • v.9 no.2
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    • pp.47-50
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    • 2002
  • Raft is a distinctive membrane domain enriched in a certain class of lipids, cholesterol, and proteins observed on the plasma membrane. Growing evidence has revealed that such membrane domains play key roles in signal transduction, fertilization, development, transmitter release, and so on. Recently, we have isolated raft-like detergent-resistant membrane (DRM) fraction from bovine photoreceptor rod outer segments. Transducin and its effecter, cGMP-phosphodiesterase, elicited stimulus-dependent translocation between detergent-soluble membrane and DRM. This suggested potential importance of such distinct membrane domains in vertebrate phototransduction. Here, we will discuss physiological meaning of the translocation of major components of cGMP cascade to raft-like membrane in phototransduction. We would like to propose a hypothesis that raft-like membrane domains on the disk membrane are the place where cGMP cascade system could be quenched.

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Exploiting Negative Rejection to Achieve Reverse Selectivity Using Membrane Cascade (음배제율을 활용한 분리막 다단공정 기반의 역선택성 구현 연구)

  • Seung Hwan Kim;Jieun Kang;Jeong F. Kim
    • Membrane Journal
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    • v.33 no.6
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    • pp.409-415
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    • 2023
  • Apart from developing better membranes, a clever reconfiguration of membrane cascade process can improve the solute selectivity and minimize solvent consumption. In this work, solvent resistant cellulose nanofiltration membranes were fabricated and the solute rejection performance in various organic solvents were tested. Interestingly, cellulose membranes exhibited unique negative rejection profile in non-polar solvents. Such trend could be exploited to yield reverse selectivity, which showed that low molecular weight solute could be concentrated in the retentate. It was found that more than 3-fold solvent saving could be achieved at the same final purity.

Production of enantiopure epoxides by yeast epoxide hydrolase using a two-phase membrane bioreactor (한국생물공학회 정기총회 및 연구논문발표회 발표논문)

  • Choe, Won-Jae;Choe, Cha-Yong
    • 한국생물공학회:학술대회논문집
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    • 2000.04a
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    • pp.145-148
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    • 2000
  • Large-scale resolution of epoxides by the yeast Rhodotorula glutinis was demonstrated in an aqueous/organic two-phase cascade membrane bioreactor. Due to the chemical instability and low solubility of epoxides in aqueous phases, an organic solvent was introduced into the reaction mixture in order to enhance resolution of epoxide. A cascade hollow-fiber membrane bioreactor was used (i) to minimize the toxicity of organic solvents towards the epoxide hydrolase of Rhodotorula glutinis, and (ii) to remove inhibitory amounts of formed diol from the yeast cell containing aqueous phase. Dodecane was selected as a suitable solvent and 1,2-epoxyhexane as a model substrate. By use of this membrane bioreactor, highly concentrated (0.9 M in dodecane) enantiopure (>98% ee) (S)-1,2-epoxyhexane (6.5 g, 30% yield) was obtained from its racemic mixture.

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Chemistry and Biology of Ras Farnesyltransferase

  • Cho, Kwang-Nym;Lee, Kee-In
    • Archives of Pharmacal Research
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    • v.25 no.6
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    • pp.759-769
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    • 2002
  • Mutated forms of ras are found in many human tumors and the rate of incidence is significantly higher in colon and pancreatic cancers. The protein product from the ras oncogene is a small G-protein, $p21^{ras}{\;}(Ras)$ that is known to playa key role in the signal transduction cascade and cell differentiation and proliferation. Mutated Ras is unable to regulate itself and remains constantly activated, leading to uncontrolled cell growth. The function of Ras in signal transduction requires its location near the growth factor receptor at the cell membrane. However, Ras does not have a transmembrane domain. Ras requires farnesylation to increase its hydrophobicity and subsequent plasma membrane association for its transforming activity. This key post-translational modification is catalyzed by the enzyme Ras farnesyltransferase (FTase), which transfers a farnesyl group from farnesylpyrophosphate to the C-terminal cysteine of the Ras protein. The requirement has focused attention on FTase as a target for therapeutic intervention. Selective inhibition of FTase will prevent Ras protein from association with the plasma membrane, leading to a disruption of oncogenic Ras function.

Upstream paths for Hippo signaling in Drosophila organ development

  • Choi, Kwang-Wook
    • BMB Reports
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    • v.51 no.3
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    • pp.134-142
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    • 2018
  • Organ growth is fundamental to animal development. One of major mechanisms for growth control is mediated by the conserved Hippo signaling pathway initially identified in Drosophila. The core of this pathway in Drosophila consists of a cascade of protein kinases Hippo and Warts that negatively regulate transcriptional coactivator Yorkie (Yki). Activation of Yki promotes cell survival and proliferation to induce organ growth. A key issue in Hippo signaling is to understand how core kinase cascade is activated. Activation of Hippo kinase cascade is regulated in the upstream by at least two transmembrane proteins Crumbs and Fat that act in parallel. These membrane proteins interact with additional factors such as FERM-domain proteins Expanded and Merlin to modulate subcellular localization and function of the Hippo kinase cascade. Hippo signaling is also influenced by cytoskeletal networks and cell tension in epithelia of developing organs. These upstream events in the regulation of Hippo signaling are only partially understood. This review focuses on our current understanding of some upstream processes involved in Hippo signaling in developing Drosophila organs.

Water cost analysis of different membrane distillation process configurations for brackish water desalination

  • Saleh, Jehad M;Ali, Emad M.;Orfi, Jamel A;Najib, Abdullah M
    • Membrane and Water Treatment
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    • v.11 no.5
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    • pp.363-374
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    • 2020
  • Membrane distillation (MD) is a process used for water desalination. However, its commercialization is still hindered by its increased specific cost of production. In this work, several process configurations comprising Direct Contact and Permeate Gap distillation membrane units (PGMD/DCMD) were investigated to maximize the production rate and consequently reduce the specific water cost. The analysis was based on a cost model and an experimentally validated MD model. It was revealed that the best achievable water cost was approximately 5.1 $/㎥ with a production rate of 8000 ㎥/y. This cost can be further decreased to approximately 2 $/㎥ only if the heating and cooling energies are free of cost. Therefore, it is necessary to decrease the MD capital investment to produce pure water at economical prices.

Apoptotic Signaling Pathways: Caspases and Stress-Activated Protein Kinases

  • Cho, Ssang-Goo;Choi, Eui-Ju
    • BMB Reports
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    • v.35 no.1
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    • pp.24-27
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    • 2002
  • Apoptotic cell death is an active process mediated by various signaling pathways, which include the caspase cascade and the stress-activated protein kinase pathways. The caspase cascade is activated by two distinct routes: one from cell surface and the other from mitochondria. Activation of the route from cell surface requires the cellular components that include membrane receptors, adaptor proteins such as TRADD and FADD, and caspase-8, while activation of the other from mitochondria requires Apaf-1, caspase-9, and cytosolic cytochrome c. On the other hand, persistent stimulation of the stress-activated protein kinase pathway is also shown to mediate apoptosis in many cell types. Gene-targeting studies with jnk- or jip-null mice, in particular, strongly suggest that this signaling pathway plays a pivotal role in the cellular machinery for apoptosis.

Diffusion-based determination of protein homodimerization on reconstituted membrane surfaces

  • Jepson, Tyler A.;Chung, Jean K.
    • BMB Reports
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    • v.54 no.3
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    • pp.157-163
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    • 2021
  • The transient interactions between cellular components, particularly on membrane surfaces, are critical in the proper function of many biochemical reactions. For example, many signaling pathways involve dimerization, oligomerization, or other types of clustering of signaling proteins as a key step in the signaling cascade. However, it is often experimentally challenging to directly observe and characterize the molecular mechanisms such interactions-the greatest difficulty lies in the fact that living cells have an unknown number of background processes that may or may not participate in the molecular process of interest, and as a consequence, it is usually impossible to definitively correlate an observation to a well-defined cellular mechanism. One of the experimental methods that can quantitatively capture these interactions is through membrane reconstitution, whereby a lipid bilayer is fabricated to mimic the membrane environment, and the biological components of interest are systematically introduced, without unknown background processes. This configuration allows the extensive use of fluorescence techniques, particularly fluorescence fluctuation spectroscopy and single-molecule fluorescence microscopy. In this review, we describe how the equilibrium diffusion of two proteins, K-Ras4B and the PH domain of Bruton's tyrosine kinase (Btk), on fluid lipid membranes can be used to determine the kinetics of homodimerization reactions.

New Insights in Arachidonate Cascade: Biochemical Characterization and Biological Significance of Three Distinct Prostaglandin E Synthases

  • Kudo, Ichiro
    • Proceedings of the PSK Conference
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    • 2003.04a
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    • pp.111-113
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    • 2003
  • Biosynthsis of prostaglandin E2 (PGE2), the most common prostanoid with potent and diverse bio-activities, is regulated by three sequential enzymatic steps composed of phospholipase A2, cyclooxygenase (COX), and prostaglandin E synthase (PGES). Recently, three distinct PGESs have been identified; two of them are membrane-bound enzymes, mPGES-1 and mPGES-2, and the third one is a cytosolic enzyme, cPGES. (omitted)

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