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  • 1
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    Purification and reconstitution of chloride channels from kidney and trachea (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-23
    Description: Chloride channels mediate absorption and secretion of fluid in epithelia, and the regulation of these channels is now known to be defective in cystic fibrosis. Indanyl-oxyacetic acid 94 (IAA-94) is a high-affinity ligand for the chloride channel, and an affinity resin based on that structure was developed. Solubilized proteins from kidney and trachea membranes were applied to the affinity matrix, and four proteins with apparent molecular masses of 97, 64, 40, and 27 kilodaltons were eluted from the column by excess IAA-94. A potential-dependent 36Cl- uptake was observed after reconstituting these proteins into liposomes. Three types of chloride channels with single-channel conductances of 26, 100, and 400 picosiemens were observed after fusion of these liposomes with planar lipid bilayers. Similar types of chloride channels have been observed in epithelia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landry, D W -- Akabas, M H -- Redhead, C -- Edelman, A -- Cragoe, E J Jr -- Al-Awqati, Q -- DK-20999/DK/NIDDK NIH HHS/ -- DK-39532/DK/NIDDK NIH HHS/ -- DK-41146/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Jun 23;244(4911):1469-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2472007" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteriorhodopsins/metabolism ; Cattle ; Chloride Channels ; Chlorides/*isolation & purification/physiology ; Chlorine/metabolism ; Chromatography, Affinity ; Electric Conductivity ; Electrophoresis, Polyacrylamide Gel ; Indans ; *Ion Channels/physiology ; Kidney Cortex/*analysis ; Light ; Liposomes/metabolism ; Membrane Potentials/drug effects ; Membrane Proteins/*isolation & purification/physiology ; Molecular Weight ; Radioisotopes ; Trachea/*analysis ; Valinomycin/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Acetylcholine receptor channel structure probed in cysteine-substitution mutants (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: In order to understand the structural bases of ion conduction, ion selectivity, and gating in the nicotinic acetylcholine receptor, mutagenesis and covalent modification were combined to identify the amino acid residues that line the channel. The side chains of alternate residues--Ser248, Leu250, Ser252, and Thr254--in M2, a membrane-spanning segment of the alpha subunit, are exposed in the closed channel. Thus alpha 248-254 probably forms a beta strand, and the gate is closer to the cytoplasmic end of the channel than any of these residues. On channel opening, Leu251 is also exposed. These results lead to a revised view of the closed and open channel structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akabas, M H -- Stauffer, D A -- Xu, M -- Karlin, A -- NS07065/NS/NINDS NIH HHS/ -- NS07258/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):307-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1384130" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism/pharmacology ; Amino Acid Sequence ; Animals ; Cysteine/*chemistry ; Gene Expression ; Ion Channel Gating ; Ion Channels/*chemistry/physiology ; Mice ; Molecular Sequence Data ; Muscles/chemistry ; *Mutagenesis ; Oocytes/metabolism ; Receptors, Cholinergic/*chemistry/genetics ; Structure-Activity Relationship ; Sulfhydryl Reagents/pharmacology ; Thermodynamics ; Transfection ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Osmotic swelling of phospholipid vesicles causes them to fuse with a planar phospholipid bilayer membrane (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-30
    Description: Fusion of phospholipid vesicles with planar bilayer membranes occurs if the vesicles that contact the planar membrane swell osmotically after the replacement in their medium of an impermeant solute by a permeant one. This finding directly demonstrates that osmotic swelling is a driving force for vesicle-planar membrane fusion. The method used to induce vesicle swelling and fusion may have relevance for biological systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, F S -- Akabas, M H -- Finkelstein, A -- 5T32GM7288/GM/NIGMS NIH HHS/ -- GM 27367-02/GM/NIGMS NIH HHS/ -- GM29210-05/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Jul 30;217(4558):458-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6283637" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium/pharmacology ; *Lipid Bilayers ; Liposomes ; *Membrane Fusion ; Membrane Proteins/metabolism ; Organoids/physiology ; Osmotic Pressure ; Phospholipids ; Porins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    A bitter substance induces a rise in intracellular calcium in a subpopulation of rat taste cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: The sense of taste permits animals to discriminate between foods that are safe and those that are toxic. Because most poisonous plant alkaloids are intensely bitter, bitter taste warns animals of potentially hazardous foods. To investigate the mechanism of bitter taste transduction, a preparation of dissociated rat taste cells was developed that can be studied with techniques designed for single-cell measurements. Denatonium, a very bitter substance, caused a rise in the intracellular calcium concentration due to release from internal stores in a small subpopulation of taste cells. Thus, the transduction of bitter taste may occur via a receptor-second messenger mechanism leading to neurotransmitter release and may not involve depolarization-mediated calcium entry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akabas, M H -- Dodd, J -- Al-Awqati, Q -- DK 20999/DK/NIDDK NIH HHS/ -- DK 34742/DK/NIDDK NIH HHS/ -- NS22993/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1047-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194756" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Calcium/*physiology ; Cell Separation ; Cytoplasm/physiology ; Extracellular Space/physiology ; Membrane Potentials ; Quaternary Ammonium Compounds/*pharmacology ; Rats ; Sensory Receptor Cells/physiology ; Taste/*physiology ; Taste Buds/cytology/immunology/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    Using molecular dynamics to elucidate the structural basis for function in pLGICs (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-10-04
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 6
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    Structural basis for function in pLGICs [Biophysics and Computational Biology] (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-10-16
    Description: Ligand-gated ion channels incorporate neurotransmitter binding sites and a transmembrane ion channel into a single protein complex. At fast chemical synapses, they detect the presence of extracellular neurotransmitters and open and alter the cellular membrane potential. The pentameric ligand-gated ion channels (pLGICs), also known as the Cys-loop receptors, are a...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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