pubmed-article:9348332 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C0060608 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C1157322 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9348332 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:9348332 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:9348332 | pubmed:dateCreated | 1997-12-10 | lld:pubmed |
pubmed-article:9348332 | pubmed:abstractText | The neuropeptide Phe-Met-Arg-Phe-amide (FMRFa) dose dependently (ED50 = 23 nM) activated a K+ current in the peptidergic caudodorsal neurones that regulate egg laying in the mollusc Lymnaea stagnalis. Under standard conditions ([K+]o = 1.7 mM), only outward current responses occurred. In high K+ salines ([K+]o = 20 or 57 mM), current reversal occurred close to the theoretical reversal potential for K+. In both salines, no responses were measured below -120 mV. Between -120 mV and the K+ reversal potential, currents were inward with maximal amplitudes at approximately -60 mV. Thus, U-shaped current-voltage relations were obtained, implying that the response is voltage dependent. The conductance depended both on membrane potential and extracellular K+ concentration. The voltage sensitivity was characterized by an e-fold change in conductance per approximately 14 mV at all [K+]o. Since this result was also obtained in nearly symmetrical K+ conditions, it is concluded that channel gating is voltage dependent. In addition, outward rectification occurs in asymmetric K+ concentrations. Onset kinetics of the response were slow (rise time approximately 650 ms at -40 mV). However, when FMRFa was applied while holding the cell at -120 mV, to prevent activation of the current but allow activation of the signal transduction pathway, a subsequent step to -40 mV revealed a much more rapid current onset. Thus, onset kinetics are largely determined by steps preceding channel activation. With FMRFa applied at -120 mV, the time constant of activation during the subsequent test pulse decreased from approximately 36 ms at -60 mV to approximately 13 ms at -30 mV, confirming that channel opening is voltage dependent. The current inactivated voltage dependently. The rate and degree of inactivation progressively increased from -120 to -50 mV. The current is blocked by internal tetraethylammonium and by bath- applied 4-aminopyridine, tetraethylammonium, Ba2+, and, partially, Cd2+ and Cs+. The response to FMRFa was affected by intracellular GTPgammaS. The response was inhibited by blockers of phospholipase A2 and lipoxygenases, but not by a cyclo-oxygenase blocker. Bath-applied arachidonic acid induced a slow outward current and occluded the response to FMRFa. These results suggest that the FMRFa receptor couples via a G-protein to the lipoxygenase pathway of arachidonic acid metabolism. The biophysical and pharmacological properties of this transmitter operated, but voltage-dependent K+ current distinguish it from other receptor-driven K+ currents such as the S-current- and G-protein-dependent inward rectifiers. | lld:pubmed |
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pubmed-article:9348332 | pubmed:language | eng | lld:pubmed |
pubmed-article:9348332 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9348332 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9348332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9348332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9348332 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9348332 | pubmed:month | Nov | lld:pubmed |
pubmed-article:9348332 | pubmed:issn | 0022-1295 | lld:pubmed |
pubmed-article:9348332 | pubmed:author | pubmed-author:KitsK SKS | lld:pubmed |
pubmed-article:9348332 | pubmed:author | pubmed-author:LodderJ CJC | lld:pubmed |
pubmed-article:9348332 | pubmed:author | pubmed-author:VeermanM JMJ | lld:pubmed |
pubmed-article:9348332 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9348332 | pubmed:volume | 110 | lld:pubmed |
pubmed-article:9348332 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9348332 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9348332 | pubmed:pagination | 611-28 | lld:pubmed |
pubmed-article:9348332 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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