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Journal articles on the topic 'Inside-out vesicles'

Author: Grafiati

Published: 6 September 2023

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1

Albertsson, Per-Åke, Per Svensson, Agneta Persson, G. Dallner, and Petter Gustafsson. "Subfractionation of Inside-Out Thylakoid Vesicles." Acta Chemica Scandinavica 41b (1987): 134–36. http://dx.doi.org/10.3891/acta.chem.scand.41b-0134.

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2

Palmgren, Michael Gjedde, Per Askerlund, Karin Fredrikson, Susanne Widell, Marianne Sommarin, and Christer Larsson. "Sealed Inside-Out and Right-Side-Out Plasma Membrane Vesicles." Plant Physiology 92, no. 4 (April 1, 1990): 871–80. http://dx.doi.org/10.1104/pp.92.4.871.

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3

Mankelow, Tosti J., Rebecca E. Griffiths, Joanna F. Flatt, and David J. Anstee. "Human Reticulocytes Extrude Inside-Out, Phosphatidylserine-Exposed, Autophagic Vesicles During The Final Step In The Formation Of Erythrocytes." Blood 122, no. 21 (November 15, 2013): 941. http://dx.doi.org/10.1182/blood.v122.21.941.941.

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Abstract During maturation to an erythrocyte, a reticulocyte must degrade or eliminate its residual cytosolic organelles and reduce its surface area. Using confocal microscopy, we show that in late reticulocytes produced from an in vitro culture system, this is achieved through a novel form of exocytosis whereby large (∼1.4um) intact, inside-out phosphatidylserine-exposed vesicles are expelled from the maturing reticulocyte. The vesicles contain organelle marker proteins and numerous erythroid membrane proteins, notably CD71, CD147 and stomatin. The presence of ubiquitin within these vesicles suggests a recognised mechanism for the targeting of proteins for extracellular export or degradation. The exocytosed vesicles are identical to intracellular GPA-decorated autophagic vesicles previously identified in cultured reticulocytes (Griffiths et al 2012). GPA-decorated vesicles are also seen in some cells in peripheral blood. Proteins involved in vesicle trafficking, SNARE (VAMP7), ESCRT (CHMP4B) and myosin, locate to defined positions at the point of vesicle extrusion. We hypothesize that the exposed “eat me” phosphatidylserine signal ensures that released autophagic vesicles are rapidly removed from circulation by professional phagocytic cells within the spleen thus ensuring maturation to erythrocytes without the release of potentially toxic material into circulation. Our results describe a previously unrecognised mode of exocytosis which may have significance beyond erythropoiesis particularly with respect to apoptosis and autophagy and reveal the final step in the formation of human erythrocytes. Reference Griffiths RE, Kupzig S, Cogan N, Mankelow TJ, Betin VM, Trakarnsanga K, Massey EJ, Lane JD, Parsons SF, Anstee DJ.Maturing reticulocytes internalize plasma membrane in glycophorin A-containing vesicles that fuse with autophagosomes before exocytosis. Blood. 2012 Jun 28;119(26):6296-306. Disclosures: No relevant conflicts of interest to declare.

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4

Schoenmakers, T. J., and G. Flik. "Sodium-extruding and calcium-extruding sodium/calcium exchangers display similar calcium affinities." Journal of Experimental Biology 168, no. 1 (July 1, 1992): 151–59. http://dx.doi.org/10.1242/jeb.168.1.151.

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Na+/Ca2+ exchange activities in purely inside-out and mixed inside-out and right-side-out fish enterocyte basolateral plasma membrane vesicle preparations display equal affinities for Ca2+, showing that only the intracellular Ca2+ transport site of the Na+/Ca2+ exchanger is detected in experiments on vesicle preparations with mixed orientation. Therefore, Ca2+ pump and Na+/Ca2+ exchange activity may be compared directly without correction for vesicle orientation. The Na+/Ca2+ exchange activity in fish enterocyte vesicles is compared to the activity found in dog erythrocyte vesicles. The calcium-extruding exchanger in fish basolateral plasma membranes shows values of Km and V(max) for calcium similar to those found for the sodium-extruding exchanger in dog erythrocyte membranes, indicating that differences in electrochemical gradients underlie the difference in cellular function of the two exchangers.

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5

LaBelle, E. F., S. V. Singh, S. K. Srivastava, and Y. C. Awasthi. "Dinitrophenyl glutathione efflux from human erythrocytes is primary active ATP-dependent transport." Biochemical Journal 238, no. 2 (September 1, 1986): 443–49. http://dx.doi.org/10.1042/bj2380443.

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Dinitrophenyl S-glutathione is accumulated by inside-out vesicles made from human erythrocytes in a process totally dependent on ATP and Mg2+. The vesicles were shown to accumulate dinitrophenyl S-glutathione against a concentration gradient. The vesicles were able to concentrate this glutathione derivative even in the absence of membrane potential. This indicated that the ATP-dependent uptake of dinitrophenyl S-glutathione by inside-out vesicles represented an active transport process. Neither extravesicular EGTA nor intravesicular ouabain inhibited the transport process, indicating that neither the Ca2+-ATPase nor the Na+, K+-ATPase were involved. These results indicated that dinitrophenyl S-glutathione uptake by inside-out vesicles probably represented primary active transport. The uptake of dinitrophenyl S-glutathione was a linear function of time (up to 5 h) and vesicle protein. The rate of uptake was optimal between pH 7.0 and 8.0 and at 37 degrees C. The Km values determined for dinitrophenyl S-glutathione and ATP were 0.29 mM and 1 mM, respectively. The transport process was completely inhibited by vanadate and by p-hydroxymercuribenzene sulphonate and inhibited to a lesser extent by N-ethylmaleimide. GTP could efficiently substitute for ATP as an energy source for the transport process, but CTP and UTP were comparatively much less effective.

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6

Ames, G. F., K. Nikaido, J. Groarke, and J. Petithory. "Reconstitution of periplasmic transport in inside-out membrane vesicles." Journal of Biological Chemistry 264, no. 7 (March 1989): 3998–4002. http://dx.doi.org/10.1016/s0021-9258(19)84951-7.

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7

Nilsson, Fredrik, David J. Simpson, Alison C. Stewart, and Bertil Andersson. "Generation and isolation of cyanobacterial inside-out thylakoid vesicles." Archives of Biochemistry and Biophysics 265, no. 2 (September 1988): 321–28. http://dx.doi.org/10.1016/0003-9861(88)90134-8.

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8

ERICKSON, Hans K., and Jack KYTE. "Lysine-691 of the anion exchanger from human erythrocytes is located on its cytoplasmic surface." Biochemical Journal 336, no. 2 (December 1, 1998): 443–49. http://dx.doi.org/10.1042/bj3360443.

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A combination of vectorial modification and site-directed immunochemistry has been used to determine the disposition, with respect to the membrane, of Lys-691 of the anion exchanger from human erythrocytes. Intact erythrocytes and inside-out vesicles were vectorially modified in the same container with pyridoxal phosphate and sodium [3H]borohydride. The modified inside-out vesicles were separated from erythrocytes by differential centrifugation and the vesicles and erythrocyte membranes were treated with alkali and digested with trypsin and thermolysin to liberate the peptides IVSKPER and IVSK{Nε-[4´-(5´-phospho-[4-3H]pyridoxyl)]}PER. These peptides, containing the unmodified and modified versions of Lys-691, were retrieved from the digests by site-directed immunochemistry and were identified by HPLC and liquid scintillation spectroscopy. Both the inside-out vesicles and the intact erythrocytes contained the peptide IVSKPER, however, the 3H-label from the phosphopyridoxylated peptide could be detected only in the inside-out vesicles. The incorporation of 3H into Lys-691 of the anion exchanger from inside-out vesicles was at least 30-fold greater than the incorporation into Lys-691 of the anion exchanger from intact erythrocytes. It follows that Lys-691 of the anion exchanger is located on the cytoplasmic surface of the plasma membrane.

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9

Lew, Virgilio L., Austin Hockaday, Maria-Isabel Sepulveda, Andrew P. Somlyo, Avril V. Somlyo, Olga E. Ortiz, and Robert M. Bookchin. "Compartmentalization of sickle-cell calcium in endocytic inside-out vesicles." Nature 315, no. 6020 (June 1985): 586–89. http://dx.doi.org/10.1038/315586a0.

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10

Lew, V. L., A. Hockaday, C. J. Freeman, and R. M. Bookchin. "Mechanism of spontaneous inside-out vesiculation of red cell membranes." Journal of Cell Biology 106, no. 6 (June 1, 1988): 1893–901. http://dx.doi.org/10.1083/jcb.106.6.1893.

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In certain conditions, human red cell membranes spontaneously form inside out vesicles within 20 min after hypotonic lysis. Study of the geometry of this process now reveals that, contrary to earlier views of vesiculation by endocytosis or by the mechanical shearing of cytoskeleton-depleted membrane, lysis generates a persistent membrane edge which spontaneously curls, cuts, and splices the membrane surface to form single or concentric vesicles. Analysis of the processes by which proteins may stabilize a free membrane edge led us to formulate a novel zip-type mechanism for membrane cutting-splicing and fusion even in the absence of free edges. Such protein-led membrane fusion represents an alternative to mechanisms of membrane fusion based on phospholipid interactions, and may prove relevant to processes of secretion, endocytosis, phagocytosis, and membrane recycling in many cell types.

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11

Sonesson, A., and Susanne Widell. "Cytoskeleton components of inside-out and right-side-out plasma membrane vesicles from plants." Protoplasma 177, no. 1-2 (March 1993): 45–52. http://dx.doi.org/10.1007/bf01403398.

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12

Rauterberg, Ernst Wilhard. "Inside-Out Vesicles Prepared from Complement Lysed Sheep Red Blood Cells." Complement 2, no. 4 (1985): 211–18. http://dx.doi.org/10.1159/000467864.

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13

Kwon, Seomun, Constance Tisserant, Markus Tulinski, Arne Weiberg, and Michael Feldbrügge. "Inside-out: from endosomes to extracellular vesicles in fungal RNA transport." Fungal Biology Reviews 34, no. 2 (June 2020): 89–99. http://dx.doi.org/10.1016/j.fbr.2020.01.001.

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14

Dargemont, C., M. Hilly, M. Claret, and J. P. Mauger. "Characterization of Ca2+ fluxes in rat liver plasma-membrane vesicles." Biochemical Journal 256, no. 1 (November 15, 1988): 117–24. http://dx.doi.org/10.1042/bj2560117.

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Inside-out plasma-membrane vesicles isolated from rat liver [Prpic, Green, Blackmore & Exton (1984) J. Biol. Chem. 259, 1382-1385] accumulated a substantial amount of 45Ca2+ when they were incubated in a medium whose ionic composition and pH mimicked those of cytosol and which contained MgATP. The Vmax of the initial 45Ca2+ uptake rate was 2.9 +/- 0.6 nmol/min per mg and the Km for Ca2+ was 0.50 +/- 0.08 microM. The ATP-dependent 45Ca2+ uptake by inside-out plasma-membrane vesicles was about 20 times more sensitive to saponin than was the ATP-dependent uptake by a microsomal preparation. The 45Ca2+ efflux from the inside-out vesicles, which is equivalent to the Ca2+ influx in intact cells, was increased when the free Ca2+ concentration in the medium was decreased. The Ca2+ antagonists La3+ and Co2+ inhibited the 45Ca2+ efflux from the vesicles. Neomycin stimulated the Ca2+ efflux in the presence of either a high or a low free Ca2+ concentration. These results confirm that polyvalent cations regulate Ca2+ fluxes through the plasma membrane.

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15

Putnam, R. W., P. B. Douglas, and N. A. Ritucci. "Membrane domain localization of pH-regulating transporters in frog skeletal muscle membrane vesicles." American Journal of Physiology-Cell Physiology 271, no. 4 (October 1, 1996): C1367—C1379. http://dx.doi.org/10.1152/ajpcell.1996.271.4.c1367.

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The distribution of pH-regulating transporters in surface and transverse (T) tubular membrane (TTM) domains of frog skeletal muscle was studied. 2',7'-Bis(carboxyethyl)-5(6)- carboxyfluorescein-loaded giant sarcolemmal vesicles, containing surface membrane, exhibited reversible Na+/H+ exchange. A microsomal vesicle fraction was shown to be enriched in TTM on the basis of high Na(+)-K(+)-ATPase and Mg(2+)-ATPase activity, high ouabain and nitrendipine binding, and low Ca(2+)-ATPase activity. TTM vesicles were well sealed and oriented inside out. Vesicles were loaded with the pH-sensitive dye pyranine. In response to an inwardly directed Na+ gradient, vesicles displayed virtually no alkalinization unless monensin was present. No pH response to an imposed Na+ gradient was seen regardless of the direction of the pH gradient across the vesicles, after phosphorylation of the vesicles with protein kinase C, or when exposed to guanosine 5'-O-(3-thiotriphosphate). In the presence of CO2, addition of Na+ or Cl- had no effect on vesicle pH. These data indicate that the TTM lacks functional pH-regulating transporters [Na+/H+ and (Na+ + HCO3-)/Cl- exchangers], suggesting that pH-regulating transporters are localized only to the surface membrane domain in frog muscle.

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16

Matsushita, Kazunobu, Taketo Inoue, Osao Adachi, and Hirohide Toyama. "Acetobacter aceti Possesses a Proton Motive Force-Dependent Efflux System for Acetic Acid." Journal of Bacteriology 187, no. 13 (July 1, 2005): 4346–52. http://dx.doi.org/10.1128/jb.187.13.4346-4352.2005.

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ABSTRACT Acetic acid bacteria are obligate aerobes able to oxidize ethanol, sugar alcohols, and sugars into their corresponding acids. Among them, Acetobacter and Gluconacetobacter species have very high ethanol oxidation capacity, leading to accumulation of vast amounts of acetic acid outside the cell. Since these bacteria are able to grow in media with high concentrations of acetic acid, they must possess a specific mechanism such as an efflux pump by which they can resist the toxic effects of acetic acid. In this study, the efflux pump of Acetobacter aceti IFO 3283 was examined using intact cells and membrane vesicles. The accumulation of acetic acid/acetate in intact cells was increased by the addition of a proton uncoupler and/or cyanide, suggesting the presence of an energy-dependent efflux system. To confirm this, right-side-out and inside-out membrane vesicles were prepared from A. aceti IFO 3283, and the accumulation of acetic acid/acetate in the vesicles was examined. Upon the addition of a respiratory substrate, the accumulation of acetic acid/acetate in the right-side-out vesicles was largely decreased, while its accumulation was very much increased in the inside-out vesicles. These respiration-dependent phenomena observed in both types of membrane vesicles were all sensitive to a proton uncoupler. Acetic acid/acetate uptake in the inside-out membrane vesicles was dependent not on ATP but on the proton motive force. Furthermore, uptake was shown to be rather specific for acetic acid and to be pH dependent, because higher uptake was observed at lower pH. Thus, A. aceti IFO 3283 possesses a proton motive force-dependent efflux pump for acetic acid.

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17

Ferrari, Patrizia, Lucia Torielli, Massimo Cirillo, Sergio Salardi, and Giuseppe Bianchi. "Sodium transport kinetics in erythrocytes and inside-out vesicles from Milan rats." Journal of Hypertension 9, no. 8 (August 1991): 703–11. http://dx.doi.org/10.1097/00004872-199108000-00003.

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18

Chao, Tsung Shu, and Mariano Tao. "Modulation of protein 4.1 binding to inside-out membrane vesicles by phosphorylation." Biochemistry 30, no. 43 (October 1991): 10529–35. http://dx.doi.org/10.1021/bi00107a023.

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19

LAZENBY, CHARLES M., and ERNEST S. HARPUR. "Effects of neomycin on K+ transport into inside-out erythrocyte membrane vesicles." Biochemical Society Transactions 16, no. 4 (August 1, 1988): 598–99. http://dx.doi.org/10.1042/bst0160598.

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20

Marín, Reinaldo, Teresa Proverbio, and Fulgencio Proverbio. "Inside-out basolateral plasma membrane vesicles from rat kidney proximal tubular cells." Biochimica et Biophysica Acta (BBA) - Biomembranes 858, no. 1 (June 1986): 195–201. http://dx.doi.org/10.1016/0005-2736(86)90306-8.

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21

Mankelow, Tosti J., Rebecca E. Griffiths, Sara Trompeter, Joanna F. Flatt, Nicola M. Cogan, Edwin J. Massey, and David J. Anstee. "Autophagic vesicles on mature human reticulocytes explain phosphatidylserine-positive red cells in sickle cell disease." Blood 126, no. 15 (October 8, 2015): 1831–34. http://dx.doi.org/10.1182/blood-2015-04-637702.

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Key Points Reticulocyte maturation involves the release of intact, inside-out autophagic vesicles with PS exposed on their surface. Elevated levels of autophagic vesicles on circulating reticulocytes cause PS exposure in patients with SCD.

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22

Rubinacci, A., B. Fuller, F. Wuytack, and W. De Loecker. "Ca2+ transport and permeability in inside-out red cell membrane vesicles after freezing." Cryobiology 23, no. 2 (April 1986): 134–40. http://dx.doi.org/10.1016/0011-2240(86)90004-0.

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23

Rubinacci, Alessandro, Paola Divieti, Stefano Lodigiani, Alessandro De Ponti, and Michele Samaja. "Thyroid hormones and active calcium transport of inside-out red cell membrane vesicles." Biochemical Medicine and Metabolic Biology 48, no. 3 (December 1992): 235–40. http://dx.doi.org/10.1016/0885-4505(92)90070-f.

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24

Flik, G., P. M. Verbost, W. Atsma, and C. Lucu. "Calcium transport in gill plasma membranes of the crab Carcinus maenas: evidence for carriers driven by ATP and a Na+ gradient." Journal of Experimental Biology 195, no. 1 (October 1, 1994): 109–22. http://dx.doi.org/10.1242/jeb.195.1.109.

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A procedure was developed for the preparation of inside-out vesicles from plasma membranes isolated from the branchial epithelium of the green shore crab Carcinus maenas (L.). Procedures normally applied to fish branchial epithelium required the introduction of an additional hypotonic shock to obtain a preparation containing 22% inside-out vesicles, 33% right-side-out vesicles and 45% leaky membrane fragments. In such membrane preparations, the first direct evidence for uphill (against a [Ca2+] gradient) ATP-dependent and Na(+)-gradient-dependent Ca2+ transport in crustacean gills was found. The affinity for Ca2+ of the ATP-driven Ca2+ transporter was 149 nmol l-1 and that of the Na+/Ca2+ exchanger was 1.78 mumol l-1; the Vmax values were 1.73 and 9.88 nmol min-1 mg-1 protein respectively. The relative importance of these carriers for Ca2+ transport in the branchial epithelium of the crab is evaluated on the basis of their calcium kinetics.

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25

Velema, J., F. T. M. van Amsterdam, and J. Zaagsma. "Separation and characteristics of inside-out and right side-out vesicles from a rat cardiac sarcolemma preparation." International Journal of Biochemistry 19, no. 5 (January 1987): 467–70. http://dx.doi.org/10.1016/0020-711x(87)90069-3.

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26

Park, Yongkyu, and Chankyu Park. "Topology of RbsC, a Membrane Component of the Ribose Transporter, Belonging to the AraH Superfamily." Journal of Bacteriology 181, no. 3 (February 1, 1999): 1039–42. http://dx.doi.org/10.1128/jb.181.3.1039-1042.1999.

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ABSTRACT RbsC of Escherichia coli is the hydrophobic membrane component of ribose uptake system classified as the ATP-binding cassette transporter. To understand the structure and function of RbsC, its transmembrane topology was investigated by using 64 RbsC-PhoA fusions isolated either specifically or randomly. In order to confirm the cytoplasmic location of the short C-terminal region (5 amino acids), inside-out or right-side-out membrane vesicles were generated, and the C-terminal region was found to be digested by carboxypeptidase A only in inside-out vesicles. This result is consistent with the model, based on the results of alkaline phosphatase fusions, in which the protein traverses the membrane six times and the N and C termini are exposed to the cytoplasm.

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27

Mandla, S., C. R. Scriver, and H. S. Tenenhouse. "Decreased transport in renal basolateral membrane vesicles from hypertaurinuric mice." American Journal of Physiology-Renal Physiology 255, no. 1 (July 1, 1988): F88—F95. http://dx.doi.org/10.1152/ajprenal.1988.255.1.f88.

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Basolateral membrane vesicles were prepared from mouse kidney by use of a Percoll density gradient method. The preparation was enriched ninefold in Na+-K+-ATPase with minimal contamination by other cellular membranes. The basolateral membranes were a mixture of sealed inside-out and right-side-out vesicles (30%) and leaky vesicles or sheets (70%). Taurine uptake into basolateral membrane vesicles was osmotically sensitive, sodium dependent, temperature sensitive, inhibited by beta-alanine, and saturable (apparent Km, 360 microM; Vmax, 25.4 pmol.mg protein-1.15 s-1), indicating transport by a carrier-mediated process. The function of this transporter was examined in an inbred mouse strain, C57BL/6J, which has selective hypertaurinuria, presumably a result of decreased basolateral membrane permeability to taurine [Rozen et al., Am. J. Physiol. 244 (Renal Fluid Electrolyte Physiol. 13): F150-F155, 1983]. The sodium-dependent component of taurine uptake was significantly lower in C57BL/6J vesicles relative to control (C3H/HeJ strain): 2.9 +/- 0.7 vs. 9.4 +/- 0.3 (SE) pmol.mg protein-1.15 s-1, respectively; P less than 0.001. The interstrain difference in uptake was specific for taurine and could not be ascribed to differences in vesicle purification, integrity, orientation, or size. These findings indicate that the renal basolateral membrane is the site of a transport defect, which explains decreased net taurine reabsorption in vivo in the C57BL/6J strain, and corroborate earlier observations in the renal cortical slice preparation.

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28

Andersson, Bertil, Cecilia Sundby, Hans-Erik Akerlund, and Per-Ake Albertsson. "Inside-out thylakoid vesicles. An important tool for the characterization of the photosynthetic membrane." Physiologia Plantarum 65, no. 3 (November 1985): 322–30. http://dx.doi.org/10.1111/j.1399-3054.1985.tb02403.x.

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29

Kawai, Norio, and Ichiro Ichihara. "Reactivity of Lysosomes to Inside-out Cell Membrane Vesicles in a Cell-free System." Cell Structure and Function 19, no. 1 (1994): 11–19. http://dx.doi.org/10.1247/csf.19.11.

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30

Kegyarikova, Karina A., and Andrei D. Vinogradov. "Kinetics of oxidative phosphorylation catalyzed by inside-out plasma membrane vesicles of Paracoccus denitrificans." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1797 (July 2010): 35. http://dx.doi.org/10.1016/j.bbabio.2010.04.121.

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31

Sabolic, I., and D. Brown. "Na+(Li+)-H+ exchange in rat renal cortical vesicles with endosomal characteristics." American Journal of Physiology-Renal Physiology 258, no. 5 (May 1, 1990): F1245—F1253. http://dx.doi.org/10.1152/ajprenal.1990.258.5.f1245.

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Preparations of rat renal cortical endocytic vesicles, loaded with fluorescein isothiocyanate-labeled dextran (FITC-dextran) in vivo had an ATP-dependent N-ethylmaleimide (NEM)-sensitive H+ pump and, in addition, showed a limited activity of an electroneutral Na(+)-H+ and Li(+)-H+ exchanger. However, the majority of FITC-dextran-containing vesicles possessed only the H+ pump. The H+ pump and the electroneutral Na+(Li+)-H+ antiporter colocalized in only a small proportion of FITC-dextran-containing vesicles. These vesicles also exhibited marked electrically coupled Na+, Li+, and H+ movement due to conductances in the vesicle membrane for these cations. As measured by the acridine orange fluorescence quench method, the electroneutral Na(+)-H+ exchange in endosomal preparations obeyed hyperbolic kinetics with an apparent Michaelis constant (Km) for Na+ of 5.9 mM and resembled that of brush-border membrane vesicles (BBMV) isolated from the same tissue (Km for Na+, 3.7 mM). The endosomal Na+(Li+)-H+ exchange was not affected by the presence or absence of ATP or NEM. However, Li+, added before or simultaneously with Na+, inhibited the endosomal Na(+)-H+ antiporter. The Na+(Li+)-H+ antiporter was insensitive to extravesicular amiloride but was partially inhibited by intravesicular amiloride. Acidic buffers stimulated the activity of the electroneutral exchanger. We found that vesicles with similar characteristics contaminate preparations of right-side-out BBMV. We conclude that the vesicles with endosomal characteristics, which contain both a vacuolar-type H+ pump and the Na+(Li+)-H+ antiporter, are either a special pool of endocytic vesicles responsible for the trafficking of the exchanger between intracellular and luminal membranes or are inside-out BBMV that form during the homogenization of the tissue.

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32

Johansson, Fredrik, Malin Olbe, Marianne Sommarin, and Christer Larsson. "Brij 58, a polyoxyethylene acyl ether, creates membrane vesicles of uniform sidedness. A new tool to obtain inside-out (cytoplasmic side-out) plasma membrane vesicles." Plant Journal 7, no. 1 (January 1995): 165–73. http://dx.doi.org/10.1046/j.1365-313x.1995.07010165.x.

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33

Reshkin, S. J., and G. A. Ahearn. "Basolateral glucose transport by intestine of teleost, Oreochromis mossambicus." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 252, no. 3 (March 1, 1987): R579—R586. http://dx.doi.org/10.1152/ajpregu.1987.252.3.r579.

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Transport characteristics of D-glucose by isolated basolateral membrane vesicles of the teleost fish, Oreochromis mossambicus, were measured. Specific activity of the vesicle Na-K-adenosinetriphosphatase was increased 11-fold, whereas specific activities of brush-border and organelle membrane enzymes were enriched only 0.3- to 0.8-fold. Vesicles had diameters of 0.1-0.4 micron, 70% of vesicles were leaky (unsealed), and 60% of sealed vesicles were inside out. D-Glucose transport occurred by stereospecific facilitated diffusion, independent of 120 mM gradients of either NaCl or KCl, and was inhibited by sulfhydryl reagents, phloretin, and cytochalasin B, but not by phloridzin. Competition studies with a range of sugars demonstrated that aldohexoses in the C-1 chair conformation were preferred substrates and probably share the same carrier. Kinetic analysis of glucose influx yielded a Kt of 10 mM and a Jmax of 3,910 pmol X mg protein-1 X min-1. Fish intestinal basolateral D-glucose transport closely resembles that of mammalian or avian intestinal epithelia and of red blood cell plasma membrane. The magnitude of transport is much lower in fish than in other vertebrates, which may be related to lower metabolic rates in these poikilotherms.

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34

Grouzis, Jean-Pierre, Rémy Gibrat, Jacqueline Rigaud, and Claude Grignon. "Study of sidedness and tightness to H+ of corn root plasmalemma vesicles: preparation of a fraction enriched in inside-out vesicles." Biochimica et Biophysica Acta (BBA) - Biomembranes 903, no. 3 (October 1987): 449–64. http://dx.doi.org/10.1016/0005-2736(87)90052-6.

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35

Kotlyar, Alexander B., and Natalia Borovok. "NADH oxidation and NAD+ reduction catalysed by tightly coupled inside-out vesicles from Paracoccus denitrificans." European Journal of Biochemistry 269, no. 16 (August 2002): 4020–24. http://dx.doi.org/10.1046/j.1432-1033.2002.03091.x.

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36

Simon, Bernd J., and Gerhard Burckhardt. "Characterization of inside-out oriented H+-ATPases in cholate-pretreated renal brush-border membrane vesicles." Journal of Membrane Biology 117, no. 2 (August 1990): 141–51. http://dx.doi.org/10.1007/bf01868681.

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37

Larsson, Christer, Susanne Widell, and Marianne Sommarin. "Inside-out plant plasma membrane vesicles of high purity obtained by aqueous two-phase partitioning." FEBS Letters 229, no. 2 (March 14, 1988): 289–92. http://dx.doi.org/10.1016/0014-5793(88)81142-6.

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Wiser, Mark F., Alan C. Sartorelli, and Curtis L. Patton. "Association of Plasmodium berghei proteins with the host erythrocyte membrane: binding to inside-out vesicles." Molecular and Biochemical Parasitology 38, no. 1 (January 1990): 121–34. http://dx.doi.org/10.1016/0166-6851(90)90212-5.

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Atta-Asafo-Adjei, Emmanuel, and Richard A. Dilley. "Plastocyanin stimulation of whole chain and photosystem I electron transport in inside-out thylakoid vesicles." Archives of Biochemistry and Biophysics 243, no. 2 (December 1985): 660–67. http://dx.doi.org/10.1016/0003-9861(85)90544-2.

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Hemauer, Sarah J., Svetlana L. Patrikeeva, Tatiana N. Nanovskaya, Gary D. V. Hankins, and Mahmoud S. Ahmed. "Opiates inhibit paclitaxel uptake by P-glycoprotein in preparations of human placental inside-out vesicles." Biochemical Pharmacology 78, no. 9 (November 2009): 1272–78. http://dx.doi.org/10.1016/j.bcp.2009.07.002.

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Akerboom, Theodorus P. M., Grzegorz Bartosz, and Helmut Sies. "Low- and high-Km transport of dinitrophenyl glutathione in inside out vesicles from human erythrocytes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1103, no. 1 (January 1992): 115–19. http://dx.doi.org/10.1016/0005-2736(92)90064-s.

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Angel, R. C., J. A. Botta, and R. N. Farias. "High affinity L-triiodothyronine binding to right-side-out and inside-out vesicles from rat and human erythrocyte membrane." Journal of Biological Chemistry 264, no. 32 (November 1989): 19143–46. http://dx.doi.org/10.1016/s0021-9258(19)47279-7.

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Palmgren, Michael Gjedde, Marianne Sommarin, Peter Ulvskov, and Christer Larsson. "Effect of detergents on the H+-ATPase activity of inside-out and right-side-out plant plasma membrane vesicles." Biochimica et Biophysica Acta (BBA) - Biomembranes 1021, no. 2 (January 1990): 133–40. http://dx.doi.org/10.1016/0005-2736(90)90025-j.

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44

Noël, Josette, Angelica Fleser, François Bellemare, Georges Thiéry, Raynald Laprade, Gerhard Burckhardt, and Patrick Vinay. "Effect of cholate on H+-ATPase and other proteins of dog renal brush-border membrane." Biochemistry and Cell Biology 71, no. 7-8 (July 1, 1993): 390–400. http://dx.doi.org/10.1139/o93-057.

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Abstract:

A short treatment of dog renal brush-border membrane vesicles (BBMV) with sodium cholate, followed by dialysis of the detergent, reorients the polarity of H+-ATPase in the membrane and exposes its ATP binding sites to the extravesicular space, as previously shown with pig BBMV. In cholate-pretreated vesicles, the H+-ATPase remains fully active, but is inserted under the reversed polarity in sealed vesicles. A large spontaneous N-ethylmaleimide-sensitive ATPase activity is thus observed, as well as a steep intravesicular acidification upon external ATP addition, two findings absent in native vesicles. The ability of nitrate plus ATP to dissociate the hydrolytic subunits of the proton pump in cholate-pretreated vesicles, but not in native vesicles, demonstrates that most of the ATP binding subunits are accessible to ATP following cholate treatment. The sensitivity of the cytoplasmic domain of the H+-ATP activity to trypsin also confirms the reorientation of the enzyme in cholate-pretreated vesicles. The H+-ATPase and alkaline phosphatase remain largely associated with the membranes after the treatment with cholate, but γ-glutamyltranspeptidase, aminopeptidase N, and neutral endopeptidase are largely solubilized. Upon dialysis of cholate, all these enzymes are in part reinserted in the membrane according to their original polarity. The reorientation process is however specific for the H+-ATPase. Cholate treatment does not increase the formation of inside-out vesicles. Thus the treatment with cholate really reorients the polarity of the H+-ATPase in vesicles and allows for study of the proton pumping capacity of vacuolar H+-ATPase of proximal tubules.Key words: H+-ATPase polarity, kinetics, ectoATPases, brush-border membrane marker enzymes, vesicle polarity.

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ROBERTSON, A. P., R. J. MARTIN, and J. R. KUSEL. "A vesicle preparation for resolving single-channel currents in tegument of male Schistosoma mansoni." Parasitology 115, no. 2 (August 1997): 183–92. http://dx.doi.org/10.1017/s0031182097001273.

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A tegumental vesicle preparation from adult male Schistosoma mansoni was developed that allows the resolution of single ion-channel currents. Adult male schistosomes were exposed to a low pH (3·75) medium for a period of approximately 30 min at 37°C. During this period smooth vesicles formed from the tegument. Fluorescence microscopy following staining of the tegument with the dye, 5-N-[octadecanoyl]aminofluorescein (AF-18), transmission electron microscopy and scanning electron microscopy revealed that the vesicles were produced from the outer tegumental membrane. The fluorescence studies showed the presence of the double bilayer structure of the outer membrane in >41% of the vesicles. These studies suggested that the preparation is suitable for single-channel recording with the patch-clamp technique. Cell-attached and isolated inside-out patch recordings of ion-channel activity were obtained with giga-ohm resistance seals. Different types of ion-channel were recorded from tegumental vesicles from male schistosomes, illustrating the potential of the technique. The channels observed included: a non-selective cation channel (360 pS); a K+ channel (with a conductance of 115 pS in high bath-K conditions); and a Cl− selective channel (20 pS). The currents of these ion-channels may cross the double bilayer of the outer tegumental membrane.

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Fraser, C. L., C. Cummings, and G. Cassafer. "Inhibition of Na+/Ca2+ exchange in renal BLMV by IP3 depends on site of action and direction of Ca2+ flux." American Journal of Physiology-Renal Physiology 266, no. 5 (May 1, 1994): F785—F790. http://dx.doi.org/10.1152/ajprenal.1994.266.5.f785.

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It has previously been shown in synaptosomes that inositol 1,4,5-trisphosphate (1,4,5-IP3) inhibits Ca2+ transport by the plasma membrane-bound Na+/Ca2+ exchanger. The present study was therefore designed to determine if the effect of 1,4,5-IP3 was dependent on its site of action at the plasma membrane or on the direction of Ca2+ flux. To investigate this possibility, studies were performed in basolateral membrane vesicles (BLMV) isolated from rat renal cortex. As with synaptosomes, Ca2+ transport was inhibited by 1,4,5-IP3 in a concentration-dependent manner. At a concentration of 10(-6) M, 1,4,5-IP3 significantly (P < 0.005) inhibited Ca2+ transport by 36%. When Ca2+ transport was carried out in inside-out vesicles, 10(-6) M 1,4,5-IP3 significantly (P < 0.002) increased the degree of inhibition by an additional 75% (63 vs. 36%). However, 1,4,5-IP3 had no significant effect on Ca2+ transport in inside-out vesicles when Ca2+ flux was reversed (i.e., Ca2+ efflux). These data in renal BLMV confirm the novel action of 1,4,5-IP3 on the Na+/Ca2+ exchanger previously described in brain synaptosomes. These results also suggest that the action of 1,4,5-IP3 depends on both its site of action at the plasma membrane and on the direction of Ca2+ flux.

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Musch, Mark W., Erin M. Davis-Amaral, Karen L. Leibowitz, and Leon Goldstein. "Hypotonic-stimulated taurine efflux in skate erythrocytes: regulation by tyrosine phosphatase activity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 274, no. 6 (June 1, 1998): R1677—R1686. http://dx.doi.org/10.1152/ajpregu.1998.274.6.r1677.

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Treatment of skate erythrocytes with FCCP, dinitrophenol, or sodium azide lowers ATP levels and inhibits Na+-independent taurine uptake after hypotonic volume expansion. Inside-out vesicles isolated from hypotonic volume-expanded cells demonstrate greater Na+-independent taurine uptake, and pretreatment of cells with FCCP abolishes this stimulation. Addition of ATP to the vesicles does not restore stimulated taurine uptake, suggesting that ATP does not act as a ligand modulator on the transporter. Therefore the role of protein phosphorylation was investigated. Because known protein kinase inhibitors have previously been found to have little effect on taurine fluxes in skate erythrocytes, we focused on the effects of protein phosphatase inhibition. When volume-expanded cells were returned to isotonic medium, taurine flux returned to basal values more slowly after treatment with the tyrosine phosphatase inhibitor pervanadate, suggesting that dephosphorylation may regulate inactivation. A similar effect of phosphatase inhibitors was observed in the inside-out vesicles from volume-expanded cells: the reversal of stimulated taurine uptake takes place more slowly in vesicles prepared from cells that had been incubated with pervanadate. Band 3, a major protein involved in the taurine transport pathway, shows increased tyrosine phosphorylation after hypotonic volume expansion. Pervanadate treatment of the cells potentiates and prolongs the increased phosphorylation. Therefore tyrosine phosphorylation of band 3 may play an important role in the activation of taurine fluxes after volume expansion.

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Rodríguez-Hernández, Juan, and Sébastien Lecommandoux. "Reversible Inside−Out Micellization of pH-responsive and Water-Soluble Vesicles Based on Polypeptide Diblock Copolymers." Journal of the American Chemical Society 127, no. 7 (February 2005): 2026–27. http://dx.doi.org/10.1021/ja043920g.

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Lorand, L., S. N. P. Murthy, P. T. Velasco, and F. Karush. "Identification of transglutaminase substrates in inside-out vesicles from human erythrocytes: Immunoblotting with anti-dansyl antibody." Biochemical and Biophysical Research Communications 134, no. 2 (January 1986): 685–89. http://dx.doi.org/10.1016/s0006-291x(86)80474-0.

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Hemauer, Sarah, Svetlana Patrikeeva, Tatiana Nanovskaya, Gary D. V. Hankins, and Mahmoud S. Ahmed. "232: Transport of opiates by P-glycoprotein expressed in preparations of human placental inside-out vesicles." American Journal of Obstetrics and Gynecology 204, no. 1 (January 2011): S100. http://dx.doi.org/10.1016/j.ajog.2010.10.248.

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