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  • 1
    Publication Date: 1984-06-15
    Description: Iontophoretic injection of phosphorylase kinase, a Ca2+-calmodulin-dependent protein kinase, increased input resistance, enhanced the long-lasting depolarization component of the light response, and reduced the early transient outward K+ current, IA, and the late K+ currents, IB, in type B photoreceptors of Hermissenda crassicornis in a Ca2+-dependent manner. Since behavioral and biophysical studies have shown that similar membrane changes persist after associative conditioning, these results suggest that Ca2+-dependent protein phosphorylation could mediate the long-term modulation of specific K+ channels as a step in the generation of a coditioned behavioral change.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Acosta-Urquidi, J -- Alkon, D L -- Neary, J T -- New York, N.Y. -- Science. 1984 Jun 15;224(4654):1254-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6328653" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials/drug effects ; Animals ; *Association Learning ; Horseshoe Crabs ; Ion Channels/drug effects ; Iontophoresis ; *Learning ; Light ; Mollusca ; Phosphorylase Kinase/*pharmacology ; Photoreceptor Cells/*drug effects ; Potassium/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
    Publication Date: 1983-01-21
    Description: Intracellular iontophoretic injection of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase increased input resistance and decreased a delayed voltage-dependent K+ current of the type B photoreceptor in the nudibranch Hermissenda crassicornis to a greater extent than an early, rapidly inactivating K+ current (IA). This injection also enhanced the long-lasting depolarization of type B cells after a light step. These findings suggest the involvement of cyclic adenosine monophosphate-dependent phosphorylation in the differential regulation of photoreceptor K+ currents particularly during illumination. On the other hand, conditioning-induced changes in IA may also be regulated by a different type of phosphorylation (for example, Ca2+-dependent).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alkon, D L -- Acosta-Urquidi, J -- Olds, J -- Kuzma, G -- Neary, J T -- New York, N.Y. -- Science. 1983 Jan 21;219(4582):303-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6294830" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/physiology ; Calmodulin/physiology ; Cyclic AMP/physiology ; Ion Channels/physiology ; Mollusca ; Phosphoproteins/physiology ; Photoreceptor Cells/*physiology ; Potassium/*physiology ; Protein Kinases/*physiology
    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
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    General and Comparative Endocrinology 40 (1980), S. 241-244 
    ISSN: 0016-6480
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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