Reconstitution of D-glucose transporter from human placental microvillous plasma membranes.

J. M. Bissonnette, J. A. Black, Kent Thornburg, K. M. Acott, P. L. Koch

    Research output: Contribution to journalArticle

    8 Citations (Scopus)

    Abstract

    Proteins from microvillous plasma membrane vesicles of the maternal surface of human trophoblast were solubilized with octyl beta-D-glucoside. After incorporation of the soluble protein into phospholipid liposomes D-glucose uptake exceeded that of L-glucose. The reconstituted system showed that D-glucose uptake was not sodium dependent and was inhibited by cytochalasin B. Efflux of D-glucose from the proteoliposomes was retarded by cytochalasin B. D-Glucose uptake, but not L-glucose, was proportional to the amount of protein used in the reconstitution procedure. Membrane protein was also solubilized with octylglucoside from vesicles that had been extracted previously by dimethylmaleic anhydride. Proteoliposomes prepared from these latter proteins showed D-glucose uptake threefold greater than that from octylglucoside solubilization alone, but sodium dodecyl sulfate polyacrylamide gel electrophoresis of the extracted protein showed no clear difference between the double extraction procedure and the pattern obtained with the single detergent.

    Original languageEnglish (US)
    JournalThe American journal of physiology
    Volume242
    Issue number3
    StatePublished - Mar 1982

    Fingerprint

    Facilitative Glucose Transport Proteins
    Cell Membrane
    Glucose
    Cytochalasin B
    Proteins
    Cytochalasin D
    Anhydrides
    Trophoblasts
    Liposomes
    Sodium Dodecyl Sulfate
    Detergents
    Polyacrylamide Gel Electrophoresis
    Phospholipids
    Membrane Proteins
    Sodium
    Mothers
    octyl-beta-D-glucoside

    ASJC Scopus subject areas

    • Medicine(all)

    Cite this

    Reconstitution of D-glucose transporter from human placental microvillous plasma membranes. / Bissonnette, J. M.; Black, J. A.; Thornburg, Kent; Acott, K. M.; Koch, P. L.

    In: The American journal of physiology, Vol. 242, No. 3, 03.1982.

    Research output: Contribution to journalArticle

    @article{90c5ec916b2a4de29cf6774ab00d2e24,
    title = "Reconstitution of D-glucose transporter from human placental microvillous plasma membranes.",
    abstract = "Proteins from microvillous plasma membrane vesicles of the maternal surface of human trophoblast were solubilized with octyl beta-D-glucoside. After incorporation of the soluble protein into phospholipid liposomes D-glucose uptake exceeded that of L-glucose. The reconstituted system showed that D-glucose uptake was not sodium dependent and was inhibited by cytochalasin B. Efflux of D-glucose from the proteoliposomes was retarded by cytochalasin B. D-Glucose uptake, but not L-glucose, was proportional to the amount of protein used in the reconstitution procedure. Membrane protein was also solubilized with octylglucoside from vesicles that had been extracted previously by dimethylmaleic anhydride. Proteoliposomes prepared from these latter proteins showed D-glucose uptake threefold greater than that from octylglucoside solubilization alone, but sodium dodecyl sulfate polyacrylamide gel electrophoresis of the extracted protein showed no clear difference between the double extraction procedure and the pattern obtained with the single detergent.",
    author = "Bissonnette, {J. M.} and Black, {J. A.} and Kent Thornburg and Acott, {K. M.} and Koch, {P. L.}",
    year = "1982",
    month = "3",
    language = "English (US)",
    volume = "242",
    journal = "American Journal of Physiology - Renal Fluid and Electrolyte Physiology",
    issn = "1931-857X",
    publisher = "American Physiological Society",
    number = "3",

    }

    TY - JOUR

    T1 - Reconstitution of D-glucose transporter from human placental microvillous plasma membranes.

    AU - Bissonnette, J. M.

    AU - Black, J. A.

    AU - Thornburg, Kent

    AU - Acott, K. M.

    AU - Koch, P. L.

    PY - 1982/3

    Y1 - 1982/3

    N2 - Proteins from microvillous plasma membrane vesicles of the maternal surface of human trophoblast were solubilized with octyl beta-D-glucoside. After incorporation of the soluble protein into phospholipid liposomes D-glucose uptake exceeded that of L-glucose. The reconstituted system showed that D-glucose uptake was not sodium dependent and was inhibited by cytochalasin B. Efflux of D-glucose from the proteoliposomes was retarded by cytochalasin B. D-Glucose uptake, but not L-glucose, was proportional to the amount of protein used in the reconstitution procedure. Membrane protein was also solubilized with octylglucoside from vesicles that had been extracted previously by dimethylmaleic anhydride. Proteoliposomes prepared from these latter proteins showed D-glucose uptake threefold greater than that from octylglucoside solubilization alone, but sodium dodecyl sulfate polyacrylamide gel electrophoresis of the extracted protein showed no clear difference between the double extraction procedure and the pattern obtained with the single detergent.

    AB - Proteins from microvillous plasma membrane vesicles of the maternal surface of human trophoblast were solubilized with octyl beta-D-glucoside. After incorporation of the soluble protein into phospholipid liposomes D-glucose uptake exceeded that of L-glucose. The reconstituted system showed that D-glucose uptake was not sodium dependent and was inhibited by cytochalasin B. Efflux of D-glucose from the proteoliposomes was retarded by cytochalasin B. D-Glucose uptake, but not L-glucose, was proportional to the amount of protein used in the reconstitution procedure. Membrane protein was also solubilized with octylglucoside from vesicles that had been extracted previously by dimethylmaleic anhydride. Proteoliposomes prepared from these latter proteins showed D-glucose uptake threefold greater than that from octylglucoside solubilization alone, but sodium dodecyl sulfate polyacrylamide gel electrophoresis of the extracted protein showed no clear difference between the double extraction procedure and the pattern obtained with the single detergent.

    UR - http://www.scopus.com/inward/record.url?scp=0020109039&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0020109039&partnerID=8YFLogxK

    M3 - Article

    C2 - 7065166

    AN - SCOPUS:0020109039

    VL - 242

    JO - American Journal of Physiology - Renal Fluid and Electrolyte Physiology

    JF - American Journal of Physiology - Renal Fluid and Electrolyte Physiology

    SN - 1931-857X

    IS - 3

    ER -