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  • 1
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    Requirement of the inositol trisphosphate receptor for activation of store-operated Ca2+ channels (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: The coupling mechanism between endoplasmic reticulum (ER) calcium ion (Ca2+) stores and plasma membrane (PM) store-operated channels (SOCs) is crucial to Ca2+ signaling but has eluded detection. SOCs may be functionally related to the TRP family of receptor-operated channels. Direct comparison of endogenous SOCs with stably expressed TRP3 channels in human embryonic kidney (HEK293) cells revealed that TRP3 channels differ in being store independent. However, condensed cortical F-actin prevented activation of both SOC and TRP3 channels, which suggests that ER-PM interactions underlie coupling of both channels. A cell-permeant inhibitor of inositol trisphosphate receptor (InsP3R) function, 2-aminoethoxydiphenyl borate, prevented both receptor-induced TRP3 activation and store-induced SOC activation. It is concluded that InsP3Rs mediate both SOC and TRP channel opening and that the InsP3R is essential for maintaining coupling between store emptying and physiological activation of SOCs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, H T -- Patterson, R L -- van Rossum, D B -- Birnbaumer, L -- Mikoshiba, K -- Gill, D L -- AR07592/AR/NIAMS NIH HHS/ -- HL55426/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1647-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Maryland, School of Medicine, Baltimore, MD 21201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698739" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Boron Compounds/pharmacology ; Calcium/*metabolism ; Calcium Channels/chemistry/*metabolism ; *Calcium Signaling ; Carbachol/pharmacology ; Cell Line ; Cell Membrane/metabolism ; Diglycerides/metabolism/pharmacology ; Endoplasmic Reticulum/*metabolism ; Enzyme Inhibitors/pharmacology ; Humans ; Inositol 1,4,5-Trisphosphate Receptors ; Ionomycin/pharmacology ; Macrocyclic Compounds ; Oxazoles/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Receptors, Cytoplasmic and Nuclear/chemistry/*metabolism ; Strontium/metabolism ; TRPC Cation Channels ; Thapsigargin/pharmacology ; Transfection ; Type C Phospholipases/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Martin Rodbell (1925-1998) (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-04-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Birnbaumer, L -- New York, N.Y. -- Science. 1999 Mar 12;283(5408):1656.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, CA 90095, USA. lutzb@ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10189319" target="_blank"〉PubMed〈/a〉
    Keywords: History, 20th Century ; Models, Biological ; Physiology/history ; *Signal Transduction ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Newly identified brain potassium channels gated by the guanine nucleotide binding protein Go (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-09
    Description: Potassium channels in neurons are linked by guanine nucleotide binding (G) proteins to numerous neurotransmitter receptors. The ability of Go, the predominant G protein in the brain, to stimulate potassium channels was tested in cell-free membrane patches of hippocampal pyramidal neurons. Four distinct types of potassium channels, which were otherwise quiescent, were activated by both isolated brain G0 and recombinant Go alpha. Hence brain Go can couple diverse brain potassium channels to neurotransmitter receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉VanDongen, A M -- Codina, J -- Olate, J -- Mattera, R -- Joho, R -- Birnbaumer, L -- Brown, A M -- DK-19318/DK/NIDDK NIH HHS/ -- HL-31154/HL/NHLBI NIH HHS/ -- HL-37044/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1433-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144040" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Imidodiphosphate/pharmacology ; Animals ; Cattle ; Electric Conductivity ; GTP-Binding Proteins/*pharmacology ; Hippocampus/*physiology ; In Vitro Techniques ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Potassium Channels/drug effects/*physiology ; Pyramidal Tracts/physiology ; Rats ; Recombinant Proteins/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Splice variants of the alpha subunit of the G protein Gs activate both adenylyl cyclase and calcium channels (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-10
    Description: Signal transducing guanine nucleotide binding (G) proteins are heterotrimers with different alpha subunits that confer specificity for interactions with receptors and effectors. Eight to ten such G proteins couple a large number of receptors for hormones and neurotransmitters to at least eight different effectors. Although one G protein can interact with several receptors, a given G protein was thought to interact with but one effector. The recent finding that voltage-gated calcium channels are stimulated by purified Gs, which stimulates adenylyl cyclase, challenged this concept. However, purified Gs may have four distinct alpha-subunit polypeptides, produced by alternative splicing of messenger RNA. By using recombinant DNA techniques, three of the splice variants were synthesized in Escherichia coli and each variant was shown to stimulate both adenylyl cyclase and calcium channels. Thus, a single G protein alpha subunit may regulate more than one effector function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mattera, R -- Graziano, M P -- Yatani, A -- Zhou, Z -- Graf, R -- Codina, J -- Birnbaumer, L -- Gilman, A G -- Brown, A M -- DK-19318/DK/NIDDK NIH HHS/ -- HL-31164/HL/NHLBI NIH HHS/ -- HL-39262/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Feb 10;243(4892):804-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2536957" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*physiology ; Animals ; Calcium Channels/*physiology ; GTP-Binding Proteins/*genetics/physiology/ultrastructure ; In Vitro Techniques ; Macromolecular Substances ; RNA Splicing ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Heart rate regulation by G proteins acting on the cardiac pacemaker channel (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-07
    Description: Heart rate is determined by pacemaker currents, of which the most important is the hyperpolarization-activated current I(f). Heart rate and I(f) are increased by beta-adrenergic agonists and decreased by muscarinic agonists released from cardiac sympathetic and vagal nerves, respectively. The hypothesis that the receptors for each agonist are directly coupled to I(f) channels by G proteins was tested. Under substrate-free conditions, preactivated G protein Gs stimulated and preactivated G protein G(o) inhibited I(f) channels of sinoatrial node pacemaker cells. These effects were mimicked by the corresponding preactivated alpha subunits of the G proteins. Unexpectedly, the two G proteins acted simultaneously, with G(o) being the more potent. This result may explain in molecular terms the classical observation in cardiac physiology, that vagal inhibition of heart rate is much greater on a background of sympathetic stimulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Okabe, K -- Codina, J -- Birnbaumer, L -- Brown, A M -- DK19318/DK/NIDDK NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- HL39262/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1990 Sep 7;249(4973):1163-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1697697" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/physiology ; Cell-Free System ; Electric Conductivity ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/pharmacology ; *Heart Rate ; In Vitro Techniques ; Ion Channels/*physiology ; Rabbits ; Receptors, Adrenergic/physiology ; Receptors, Muscarinic/physiology ; Sinoatrial Node/*physiology ; Thionucleotides/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Potentiation by the beta subunit of the ratio of the ionic current to the charge movement in the cardiac calcium channel (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: The voltage-activated rabbit cardiac calcium channel alpha 1 subunit was expressed in Xenopus oocytes. The charge movement of its voltage sensor was measured and related to the opening of the ion-conducting pore. The half-activation potential for charge movement was 35 millivolts more negative than that for pore opening. Coexpression of the cardiac calcium channel beta subunit reduced this difference without affecting charge movement. Thus, intramolecular coupling between the voltage sensor and the channel pore opening can be facilitated by a regulatory subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neely, A -- Wei, X -- Olcese, R -- Birnbaumer, L -- Stefani, E -- AR38970/AR/NIAMS NIH HHS/ -- HL37044/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):575-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211185" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Barium/metabolism ; Calcium Channels/*metabolism ; Electric Conductivity ; *Ion Channel Gating ; Membrane Potentials ; Myocardium/*metabolism ; Oocytes/metabolism ; Rabbits ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    A monoclonal antibody to the alpha subunit of Gk blocks muscarinic activation of atrial K+ channels (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: The activated heterotrimeric guanine nucleotide binding (G) protein Gk, at subpicomolar concentrations, mimics muscarinic stimulation of a specific atrial potassium current. Reconstitution studies have implicated the alpha and beta gamma subunits as mediators, but subunit coupling by the endogenous G protein has not been analyzed. To study this process, a monoclonal antibody (4A) that binds to alpha k but not to beta gamma was applied to the solution bathing an inside-out patch of atrial membrane; the antibody blocked carbachol-activated currents irreversibly. The state of the endogenous Gk determined its susceptibility to block by the antibody. When agonist was absent or when activation by muscarinic stimulation was interrupted by withdrawal of guanosine triphosphate (GTP) in the presence or absence of guanosine diphosphate (GDP), the effects of the antibody did not persist. Thus, monoclonal antibody 4A blocked muscarinic activation of potassium channels by binding to the activated G protein in its holomeric form or by binding to the dissociated alpha subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Hamm, H -- Codina, J -- Mazzoni, M R -- Birnbaumer, L -- Brown, A M -- DK19318/DK/NIDDK NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- HL37044/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2457252" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/*pharmacology ; Animals ; *Antibodies, Monoclonal ; Atrial Function ; Carbachol/*pharmacology ; GTP-Binding Proteins/immunology/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Diphosphate/pharmacology ; Guanosine Triphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; In Vitro Techniques ; Ion Channels/drug effects/*physiology ; Myocardium/*metabolism ; Potassium/*metabolism ; Receptors, Muscarinic/drug effects/*physiology ; Thionucleotides/pharmacology
    Print ISSN: 0036-8075
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  • 8
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    The alpha subunit of the GTP binding protein Gk opens atrial potassium channels (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-04-24
    Description: Guanine nucleotide binding (G) proteins (subunit composition alpha beta gamma) dissociate on activation with guanosine triphosphate (GTP) analogs and magnesium to give alpha-guanine nucleotide complexes and free beta gamma subunits. Whether the opening of potassium channels by the recently described Gk in isolated membrane patches from mammalian atrial myocytes was mediated by the alpha k subunit or beta gamma dimer was tested. The alpha k subunit was found to be active, while the beta gamma dimer was inactive in stimulating potassium channel activity. Thus, Gk resembles Gs, the stimulatory regulatory component of adenylyl cyclase, and transducin, the regulatory component of the visual system, in that it regulates its effector function--the activity of the ligand-gated potassium channel--through its guanine nucleotide binding subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Codina, J -- Yatani, A -- Grenet, D -- Brown, A M -- Birnbaumer, L -- DK-19318/DK/NIDDK NIH HHS/ -- HD-09581/HD/NICHD NIH HHS/ -- HL-31154/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Apr 24;236(4800):442-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2436299" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Atrial Function ; Cattle ; Electric Conductivity ; Erythrocyte Membrane/metabolism ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Guinea Pigs ; Humans ; In Vitro Techniques ; Ion Channels/*physiology ; Macromolecular Substances ; Potassium/*physiology ; Receptors, Muscarinic/*physiology ; Thionucleotides/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    A G protein directly regulates mammalian cardiac calcium channels (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-11-27
    Description: A possible direct effect of guanine nucleotide binding (G) proteins on calcium channels was examined in membrane patches excised from guinea pig cardiac myocytes and bovine cardiac sarcolemmal vesicles incorporated into planar lipid bilayers. The guanosine triphosphate analog, GTP gamma S, prolonged the survival of excised calcium channels independently of the presence of adenosine 3',5'-monophosphate (cAMP), adenosine triphosphate, cAMP-activated protein kinase, and the protein kinase C activator tetradecanoyl phorbol acetate. A specific G protein, activated Gs, or its alpha subunit, purified from the plasma membranes of human erythrocytes, prolonged the survival of excised channels and stimulated the activity of incorporated channels. Thus, in addition to regulating calcium channels indirectly through activation of cytoplasmic kinases, G proteins can regulate calcium channels directly. Since they also directly regulate a subset of potassium channels, G proteins are now known to directly gate two classes of membrane ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Codina, J -- Imoto, Y -- Reeves, J P -- Birnbaumer, L -- Brown, A M -- HL-31154/HL/NHLBI NIH HHS/ -- HL-36930/HL/NHLBI NIH HHS/ -- HL-37044/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 27;238(4831):1288-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2446390" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Pyridinecarboxylic acid, ; 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl ; ester/pharmacology ; Animals ; Calcium/metabolism ; Colforsin/pharmacology ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/*physiology ; Ion Channels/drug effects/*physiology ; Isoproterenol/pharmacology ; Leupeptins/pharmacology ; Membrane Potentials/drug effects ; Phosphorylation ; Thionucleotides/pharmacology ; Ventricular Function
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Direct activation of mammalian atrial muscarinic potassium channels by GTP regulatory protein Gk (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-01-09
    Description: The mammalian heart rate is regulated by the vagus nerve, which acts via muscarinic acetylcholine receptors to cause hyperpolarization of atrial pacemaker cells. The hyperpolarization is produced by the opening of potassium channels and involves an intermediary guanosine triphosphate-binding regulatory (G) protein. Potassium channels in isolated, inside-out patches of membranes from atrial cells now are shown to be activated by a purified pertussis toxin-sensitive G protein of subunit composition alpha beta gamma, with an alpha subunit of 40,000 daltons. Thus, mammalian atrial muscarinic potassium channels are activated directly by a G protein, not indirectly through a cascade of intermediary events. The G protein regulating these channels is identified as a potent Gk; it is active at 0.2 to 1 pM. Thus, proteins other than enzymes can be under control of receptor coupling G proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Codina, J -- Brown, A M -- Birnbaumer, L -- DK-19318/DK/NIDDK NIH HHS/ -- HL-31164/HL/NHLBI NIH HHS/ -- HL-36930/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):207-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432660" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/pharmacology ; Animals ; Atrial Function ; Electrophysiology ; Erythrocytes/analysis ; GTP-Binding Proteins/*pharmacology ; Guanosine 5'-O-(3-Thiotriphosphate) ; Guanosine Triphosphate/analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/*physiology ; Humans ; Ion Channels/drug effects/*physiology ; Potassium/*metabolism ; Receptors, Muscarinic/*physiology ; Thionucleotides/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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