赤血球ゴースト
- 関
- erythrocyte cytoskeleton、erythrocyte ghost、erythrocyte membrane、red blood cell ghost
WordNet
- small room in which a monk or nun lives (同)cubicle
- a device that delivers an electric current as the result of a chemical reaction (同)electric cell
- a room where a prisoner is kept (同)jail cell, prison cell
- (biology) the basic structural and functional unit of all organisms; they may exist as independent units of life (as in monads) or may form colonies or tissues as in higher plants and animals
- any small compartment; "the cells of a honeycomb"
- a small unit serving as part of or as the nucleus of a larger political movement (同)cadre
- of a color at the end of the color spectrum (next to orange); resembling the color of blood or cherries or tomatoes or rubies (同)reddish, ruddy, blood-red, carmine, cerise, cherry, cherry-red, crimson, ruby, ruby-red, scarlet
- red color or pigment; the chromatic color resembling the hue of blood (同)redness
- move like a ghost; "The masked men ghosted across the moonlit yard"
- a mental representation of some haunting experience; "he looked like he had seen a ghost"; "it aroused specters from his past" (同)shade, spook, wraith, specter, spectre
- the visible disembodied soul of a dead person
- write for someone else; "How many books have you ghostwritten so far?" (同)ghostwrite
- the syllable naming the second (supertonic) note of any major scale in solmization (同)ray
- a tributary of the Mississippi River that flows eastward from Texas along the southern boundary of Oklahoma and through Louisiana (同)Red River
PrepTutorEJDIC
- (刑務所の)『独房』;(修道院の)小さい独居室 / (ミツバチの)みつ房,巣穴 / 小さい部屋 / 『細胞』 / 電池 / 花粉室 / (共産党などの)細胞
- 〈U〉〈C〉『赤,』『赤色;』赤い絵の具(染料) / 〈U〉赤い服 / 〈C〉《しばしば『R-』》《話》《時に軽べつして》アカ,共産主義者;過激論(主義)者 / 〈U〉《通例the ~》(会計の)赤字,負債 / 『赤い』,赤色の / (顔・目などが)赤くなった;血に染った / 赤い服を着た;赤毛の / 《しばしば『R-』》《話》《軽べつして》共産主義の;過激な
- 『幽霊』,亡霊,死者の霊 / (…の)ほんのわずか《+『of』+『名』》 / (…の)幻,面影《+『of』+『名』》 / =ghost writer / (テレビの画面の)ゴースト / =ghostwrite
- レ(全音階の第2音)
UpToDate Contents
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English Journal
- Regional Blood Acidification Enhances Extracorporeal Carbon Dioxide Removal: A 48-hour Animal Study.
- Zanella A, Mangili P, Redaelli S, Scaravilli V, Giani M, Ferlicca D, Scaccabarozzi D, Pirrone F, Albertini M, Patroniti N, Pesenti A.Author information From the Dipartimento di Scienze della Salute, Università di Milano-Bicocca, Ospedale San Gerardo Nuovo dei Tintori, Monza, Italy (A.Z., P.M., S.R., V.S., M.G., D.F., N.P., and A.P.); Dipartimento di Patologia animale, Igiene e Sanità pubblica veterinaria, sez. di Biochimica e Fisiologia, Università degli studi di Milano, Milan, Italy (F.P. and M.A.); and Dipartimento di Scienze Farmacologiche e Biomolecolari (DiSFeB), Scuola di Scienze del Farmaco, Università degli studi di Milano, Milan, Italy (D.S.).AbstractBACKGROUND: Extracorporeal carbon dioxide removal has been proposed to achieve protective ventilation in patients at risk for ventilator-induced lung injury. In an acute study, the authors previously described an extracorporeal carbon dioxide removal technique enhanced by regional extracorporeal blood acidification. The current study evaluates efficacy and feasibility of such technology applied for 48 h.
- Anesthesiology.Anesthesiology.2014 Feb;120(2):416-24. doi: 10.1097/ALN.0000000000000099.
- BACKGROUND: Extracorporeal carbon dioxide removal has been proposed to achieve protective ventilation in patients at risk for ventilator-induced lung injury. In an acute study, the authors previously described an extracorporeal carbon dioxide removal technique enhanced by regional extracorporeal blo
- PMID 24451414
- Homologous Hevea brasiliensis REF (Hevb1) and SRPP (Hevb3) present different auto-assembling.
- Berthelot K1, Lecomte S2, Estevez Y3, Coulary-Salin B4, Peruch F5.Author information 1CNRS, LCPO, UMR 5629, F-33600 Pessac, France; Univ. Bordeaux, LCPO, UMR 5629, F- 33600 Pessac, France. Electronic address: kberthelot@enscbp.fr.2CNRS, CBMN, UMR 5248, F-33600 Pessac, France; Univ. Bordeaux, CBMN, UMR 5248, F-33600 Pessac, France.3CNRS, LCPO, UMR 5629, F-33600 Pessac, France; Univ. Bordeaux, LCPO, UMR 5629, F- 33600 Pessac, France.4Univ. Bordeaux 2, CNRS, IBGC, UMR 5095, F-33000 Bordeaux, France.5CNRS, LCPO, UMR 5629, F-33600 Pessac, France; Univ. Bordeaux, LCPO, UMR 5629, F- 33600 Pessac, France. Electronic address: peruch@enscbp.fr.AbstractHbREF and HbSRPP are two Hevea brasiliensis proteins present on rubber particles, and probably involved in the coagulation of latex. Their function is unclear, but we previously discovered that REF had amyloid properties, which could be of particular interest during the coagulation process. First, we confirmed that REF and SRPP, homologous and principal proteins in hevea latex, are not glycoproteins. In this work, we investigated various aspects of protein interactions: aggregation, auto-assembling, yeast and erythrocyte agglutination, co-interactions by various biochemical (PAGE, spectroscopy, microscopy), biophysical (DLS, ellipsometry) and structural (TEM, ATR-FTIR, PM-IRRAS) approaches. We demonstrated that both proteins are auto-assembling into different aggregative states: REF polymerizes as an amyloid rich in β-sheets and forms quickly large aggregates (>μm), whereas SRPP auto-assembles in solution into stable nanomultimers of a more globular nature. Both proteins are however able to interact together, and SRPP may inhibit the amyloidogenesis of REF. REF is also able to interact with the membranes of yeasts and erythrocytes, leading to their agglutination. In addition, we also showed that both REF and SRPP did not have antimicrobial activity, whereas their activity on membranes has been clearly evidenced. We may suspect that these aggregative properties, even though they are clearly different, may occur during coagulation, when the membrane is destabilized. The interaction of proteins with membranes could help in the colloidal stability of latex, whereas the protein-protein interactions would contribute to the coagulation process, by bringing rubber particles together or eventually disrupting the particle monomembranes.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb;1844(2):473-85. doi: 10.1016/j.bbapap.2013.10.017. Epub 2013 Nov 12.
- HbREF and HbSRPP are two Hevea brasiliensis proteins present on rubber particles, and probably involved in the coagulation of latex. Their function is unclear, but we previously discovered that REF had amyloid properties, which could be of particular interest during the coagulation process. First, w
- PMID 24239687
- The Protein 4.1 family: Hub proteins in animals for organizing membrane proteins.
- Baines AJ1, Lu HC2, Bennett PM3.Author information 1School of Biosciences, University of Kent, Canterbury, UK.2Randall Division of Cell and Molecular Biophysics, King's College London, UK.3Randall Division of Cell and Molecular Biophysics, King's College London, UK. Electronic address: pauline.bennett@kcl.ac.uk.AbstractProteins of the 4.1 family are characteristic of eumetazoan organisms. Invertebrates contain single 4.1 genes and the Drosophila model suggests that 4.1 is essential for animal life. Vertebrates have four paralogues, known as 4.1R, 4.1N, 4.1G and 4.1B, which are additionally duplicated in the ray-finned fish. Protein 4.1R was the first to be discovered: it is a major mammalian erythrocyte cytoskeletal protein, essential to the mechanochemical properties of red cell membranes because it promotes the interaction between spectrin and actin in the membrane cytoskeleton. 4.1R also binds certain phospholipids and is required for the stable cell surface accumulation of a number of erythrocyte transmembrane proteins that span multiple functional classes; these include cell adhesion molecules, transporters and a chemokine receptor. The vertebrate 4.1 proteins are expressed in most tissues, and they are required for the correct cell surface accumulation of a very wide variety of membrane proteins including G-Protein coupled receptors, voltage-gated and ligand-gated channels, as well as the classes identified in erythrocytes. Indeed, such large numbers of protein interactions have been mapped for mammalian 4.1 proteins, most especially 4.1R, that it appears that they can act as hubs for membrane protein organization. The range of critical interactions of 4.1 proteins is reflected in disease relationships that include hereditary anaemias, tumour suppression, control of heartbeat and nervous system function. The 4.1 proteins are defined by their domain structure: apart from the spectrin/actin-binding domain they have FERM and FERM-adjacent domains and a unique C-terminal domain. Both the FERM and C-terminal domains can bind transmembrane proteins, thus they have the potential to be cross-linkers for membrane proteins. The activity of the FERM domain is subject to multiple modes of regulation via binding of regulatory ligands, phosphorylation of the FERM associated domain and differential mRNA splicing. Finally, the spectrum of interactions of the 4.1 proteins overlaps with that of another membrane-cytoskeleton linker, ankyrin. Both ankyrin and 4.1 link to the actin cytoskeleton via spectrin, and we hypothesize that differential regulation of 4.1 proteins and ankyrins allows highly selective control of cell surface protein accumulation and, hence, function. This article is part of a Special Issue entitled: Reciprocal influences between cell cytoskeleton and membrane channels, receptors and transporters. Guest Editor: Jean Claude Hervé
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb;1838(2):605-19. doi: 10.1016/j.bbamem.2013.05.030. Epub 2013 Jun 4.
- Proteins of the 4.1 family are characteristic of eumetazoan organisms. Invertebrates contain single 4.1 genes and the Drosophila model suggests that 4.1 is essential for animal life. Vertebrates have four paralogues, known as 4.1R, 4.1N, 4.1G and 4.1B, which are additionally duplicated in the ray-fi
- PMID 23747363
Japanese Journal
- One-step direct reconstitution of biomembranes onto cationic organic polymer bead supports.
- Osei-Asante Samuel,Haratake Mamoru,Fuchigami Takeshi,Nakayama Morio
- Journal of colloid and interface science 351(1), 96-101, 2010-11-01
- … In this study, we addressed the straightforward reconstitution of red blood cell (RBC) membranes on the surface of cationic organic polymer beads. … The RBC membrane-bead complex was obtained by the incubation of white, unsealed rat RBC ghost membranes with a nonporous quaternary ammonium-type anion-exchange polymer bead with a 350-550 microm diameter. …
- NAID 120002400753
- The covalent modification of spectrin in red cell membranes by the lipid peroxidation product 4-hydroxy-2-nonenal
- Arashiki Nobuto,Otsuka Yayoi,Ito Daisuke,Yang Mira,Komatsu Tomohiko,Sato Kota,Inaba Mutsumi
- Biochemical and Biophysical Research Communications 391(3), 1543-1547, 2010-01-15
- … Spectrin strengthens the red cell membrane through its direct association with membrane lipids and through protein-protein interactions. … Here, we showed that α- and β-spectrin in human red cells are the primary targets of the lipid peroxidation product 4-hydroxy-2-nonenal (HNE) by immunoblotting and mass spectrometry analyses. …
- NAID 120002317142
Related Links
- Ghost. (redirected from red cell ghost). Also found in: Dictionary/thesaurus, Legal, Encyclopedia, Wikipedia, Hutchinson, 0.01 sec. ghost (gōst) a faint or shadowy figure lacking the customary substance of reality. red cell ghost an erythrocyte ...
- The spirit of a dead person, especially one believed to appear in bodily likeness to living persons or to haunt former habitats. 2. The center of spiritual life; the soul . 3. A demon or spirit. 4. A returning or haunting memory or image. 5. a. A slight ...
Related Pictures
★リンクテーブル★
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赤血球ゴースト
- 関
- erythrocyte cytoskeleton、erythrocyte membrane、red blood cell ghost、red cell ghost
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- 英
- erythrocyte ghost、red cell ghost、red blood cell ghost
- 関
- 赤血球膜、赤血球骨格
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- 関
- erythrocyte cytoskeleton、erythrocyte ghost、red cell ghost
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- 関
- erythrocyte ghost、erythrocyte membrane、red cell ghost
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赤血球ゴースト
- 関
- erythrocyte ghost、red cell ghost
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- 関
- erythrocyte、erythrocytic、erythroid、RBC、red blood cell、red corpuscle
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- 関
- erythro
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細胞