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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 333 (1993), S. 315-318 
    ISSN: 0014-5793
    Keywords: Calmodulin ; Isoform ; Protein kinase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 291 (1975), S. 1-15 
    ISSN: 1432-1912
    Keywords: Heart ; Noradrenaline release ; Potassium ; Calcium ; Methacholine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Noradrenaline release from the isolated rabbit heart was evoked by perfusion with a medium containing 135 mM potassium and 17 mM sodium ions (high K+-low Na+). 2. The noradrenaline output in response to high K+-low Na+ was dose-dependently decreased by methacholine (0.625–320 μM) and this effect was reserved by atropine 1.44 μM. 3. Lowering the calcium concentration of high K+-low Na+ from 1.8–0.1125 mM decreased the noradrenaline output by 85%. The effect of methacholine, expressed as % inhibition of noradrenaline release, was potentiated by lowering of the calcium concentration. 4. Both at normal and lowered calcium concentrations the inhibitory action of methacholine was larger from 0–5 than from 5–10 min after perfusion with high K+-low Na+. 5. Perfusion of hearts with media containing high K+-high Na+ or normal K+-low Na+ caused noradrenaline outputs somewhat smaller than those after high K+-low Na+. The release from 0–5 min was both calcium-dependent and inhibited by methacholine. 6. High K+ and/or low Na+ solutions caused an increase in coronary perfusion pressure which was little affected by the noradrenaline released simultaneously. 7. It is concluded that activation of muscarine receptors at the terminal adrenergic fibre decreases the availability of calcium for transmitter release.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1435-1803
    Keywords: Calcium ; calmodulin ; protein kinase ; calmodulin dependent protein kinase ; isoform
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Calcium/calmodulindependent protein kinase type II (CaM kinase II) is an intracellular enzyme discovered several years ago in the brain which is obviously involved in intracellular signal transmission. Meanwhile it was detected in virtually every mammalian tissue. Several isoforms have been found to exist. Most recently the tissue distribution and the molecular structure of these isoforms have suggested that each form entails a particular function. In the present study we describe the identification, cloning, and nucleotide sequencing of two novel CaM kinase II isoforms which we discovered in rat heart. The presence of these additional subtypes makes the heart the organ which possesses the greatest number of different and unusual CaM kinase II isoforms throughout the body except for the brain. The importance of this finding is underscored by the fact that calcium is involved in the regulation of many crucial cardial parameters. The deduced amino acid sequence that we have obtained from the new CaM kinase II isoforms indicates a molecular organization which could make the design of subtype-specific inhibitory drugs for CaM kinase II possible. Such compounds would act similarly to but much more selectively than digitalis glycosides and would be likely to possess less side effects.
    Type of Medium: Electronic Resource
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