MEMBRANE
Online ISSN : 1884-6440
Print ISSN : 0385-1036
ISSN-L : 0385-1036
Volume 35, Issue 6
Displaying 1-9 of 9 articles from this issue
Foreword
Special Topic : Membrane intrinsic proteins and disease
Review Article
  • Mutsumi Inaba
    2010 Volume 35 Issue 6 Pages 262-267
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Mutations of the anion exchanger 1 (AE1, SLC4A1, also called band 3) cause erythroid disorders of hereditary spherocytosis, hereditary stomatocytosis, and ovalocytosis associated with hemolytic anemia. A largely discrete set of AE1 mutations causes familial distal renal tubular acidosis. Red cell phenotypes are attributed to the disordered membrane stability or the cation leak, while most cases of the distal renal tubular acidosis are caused by abnormal AE1 trafficking. A growing body of structure-function data obtained from pathobiology of AE1 mutants, together with emerging information about physiological structure and function, is advancing our understanding of this multifunctional polytopic membrane protein, AE1.
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  • Hiroshi Suzuki
    2010 Volume 35 Issue 6 Pages 268-277
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Ca2+-ATPases on sarco (endo) plasmic reticulum and on plasma membrane are the representative members of P-type ATPase family and catalyze Ca2+ transport coupled with ATP hydrolysis, thereby play critical roles in Ca2+ homeostasis and cell functions. Their dysfunction by mutations and changes in expression levels result in various isoform-specific diseases. To understand molecular bases of the disruption of Ca2+ homeostasis and diseases, it is critically important to know how the Ca2+-ATPase functions, i.e. its structure-function relationship. In this manuscript, most recent atomic level-understanding of the Ca2+-ATPase and diseases caused by its defects will be reviewed.
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  • Shinji Asano
    2010 Volume 35 Issue 6 Pages 278-284
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    ERM (Ezrin, Radixin, Moesin) proteins are cross-linkers between the plasma membranes and the actin cytoskeleton. They are essential for morphogenesis of the apical domain of epithelial cells. Recently, the ERM proteins have been reported to be involved in membrane fusion, endocytosis/exocytosis, and targeting of specific transport proteins to the cell surface under the control of hormones and cellular signals. In this review, I will discuss the involvement of ERM proteins in the regulation of membrane transport proteins especially for their delivery to the cell surface by introducing the phenotypes observed in animals in which the ERM protein gene was inactivated. Some of these phenotypes were similar to those found in human hereditary disease.
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  • Taro Fujikawa, Ken Kitamura
    2010 Volume 35 Issue 6 Pages 285-290
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Recently, the structure of Na+/K+-ATPase and its functional analysi has been dramatically evolved, and our knowledge brings a new dimension to not only resolving the kinetics and functional properties of sodium pump but also elucidating the pathophysiology of Na+/K+-ATPase related diseases. Mutations affecting the Na+/K+-ATPase α subunit have been identified at least two distinct rare diseases, Familial hemiplegic migraine type2 (FHM2) and Rapid-onset dystonia-parkinsonism (RDP). Most of their mutation patterns are single amino acid changes or heterozygous missense mutations, which might be associated with a dominant-negative effect pathology. Moreover, more frequent conditions, such as hypertension and bipolar disorder, are also correlated with Na+/K+-ATPase deficiency and more and more experimental data support it. Besides, recent data suggests that Na+/K+-ATPase β subunit play a role in developing a certain type of sensorineural hearing loss. Here, we review some Na+/K+-ATPase related diseases and discuss on their pathophysiology.
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  • [in Japanese]
    2010 Volume 35 Issue 6 Pages 291-296
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Ion permeating membrane proteins, ion channels, provide pathway for ions to travel across the membrane along the ionic concentration gradient without necessity of energy. Mutations in genes encoding ion channel produce variety of diseases, called “channelopathy” . Channelopathy exhibit phenotypes due to malfunction of transcription/ translation, membrane trafficking, protein processing, protein degradation, proper localization, kinetics of ion channels. Disordered molecules or milieu regulating ion channel function, such as lipid-rich membrane domain “caveola” , also cause variety of diseases. This review discusses representative channelopathy and disordered channel-regulating molecules and milieu.
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Original Contribution
  • Ryoko Yumoto, Eri Kimura, Satoshi Suzuki, Hiroaki Imaoka, Junya Nagai, ...
    2010 Volume 35 Issue 6 Pages 297-304
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Transport characteristics of ribavirin in human erythrocytes were evaluated using rightside-out membrane vesicles (ROVs) prepared from fresh blood, and compared with those in intact erythrocytes. [3H]Ribavirin uptake by ROVs at 23 °C was fairly rapid, and reached equilibrium at about 30 sec. The uptake of [3H]ribavirin by ROVs showed saturation kinetics with the Km value of 1.9 mM. The uptake by ROVs was inhibited by uridine (a typical substrate of equilibrative nucleoside transporter ENT1), S-(4-nitrobenzyl)-6-thioinosine (a specific inhibitor of ENT1), and dipyridamole (an inhibitor of ENT1). These characteristics of [3H]ribavirin transport in ROVs were similar to those observed in intact erythrocytes, though the affinity of [3H]ribavirin to the transport system and sensitivity to various inhibitors were lower in ROVs. Next, the interaction of ribavirin with ATP-dependent efflux transporters was evaluated using inside-out membrane vesicles (IOVs). Ribavirin weakly inhibited ATP-dependent uptake of methotrexate by multidrug resistance-associated protein (MRP) 4, but not the uptake of 5-(and 6)-carboxy-2', 7'-dichlorofluorescein by MRP5, by IOVs. However, ATP-dependent uptake of [3H]ribavirin by IOVs was not observed. These results suggest that ribavirin is transported by ENT1 across human erythrocyte membranes, while ATP-dependent efflux transporters would not be involved in ribavirin transport.
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  • Kohei Miyazaki, Nobuyoshi Shoji, Yuki Asari, Kazuyoshi Miyoshi, Daisuk ...
    2010 Volume 35 Issue 6 Pages 305-310
    Published: 2010
    Released on J-STAGE: June 17, 2015
    JOURNAL OPEN ACCESS
    Bromo-butyl styrene (BBS) was graft-polymerized onto a high-density polyethylene film with a thickness of 35 μm, previously irradiated with an electron beam. The BBS-grafted film was converted into a strongly basic anionexchange membrane (BBS-TMA membrane) by reacting with trimethylamine hydrochloride. The thickness and resistance of the BBS-TMA membrane with a BBS grafting degree of 140% and a TMA group density of 2.2 mol/kg were 50 μm and 0.57 Ωcm2, respectively, in 0.50 M sodium chloride at 298 K. After 42-day immersion of this membrane in 5.0 M NaOH at 353 K, the transport number of the BBS-TMA membrane decreased by 1.6% to 0.925 from its initial value of 0.94.
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