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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 428 (1994), S. 415-417 
    ISSN: 1432-2013
    Keywords: Heart ; Cardiac muscle ; Contraction ; E-C coupling ; Calcium channels ; Ryanodine receptors ; Intracellular calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This paper examines the [Ca2+]i transient in isolated rat heart cells using a laser scanning confocal microscope and the calcium indicator fluo-3. We find that the depolarization-evoked [Ca2+]i transient is activated synchronously near the surface and in the middle of the heart cell with similar kinetics of activation. The time of rise of the transient did not depend on whether the sarcoplasmic reticulum (SR) Ca-release was abolished (by thapsigargin and ryanodine). The synchrony of activation and the similarity of levels of [Ca2+]i at the peripheral and deeper myoplasm (regardless of the availability of SR Ca-release) shows that sarcolemmal Ca channels and SR Ca-release channels are distributed throughout the rat heart cell and that the propagation of the action potential into the interior of the cell is rapid. In addition, the activation of calcium release from the SR by CICR is rapid (≪2 ms) when compared to the time-course of calcium influx via the sarcolemmal Ca channel.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Adenosine triphosphate ; Caged-adenosine triphosphate ; Potassium channel ; Metabolism ; Heart ; Cardiac ventricle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have used ‘caged-ATP’ to investigate the kinetic behavior of KATP channels in ventricular cells from rat heart. In whole cells, loaded with ‘caged-ATP’, an increase of intracellular [ATP] following a UV light flash produced a decrease of KATP channel current that was too slow (τ ≈ 300 ms) to be explained by the expected timecourse of ATP release (τ ≈ 3 ms) and the time-course of channel blockade by ATP (τ ≈ 20 ms). In isolated membrane patches, caged-ATP itself caused partial blockade of KATP channels. Under these conditions, photorelease of ATP caused channel activity to decline further. The results suggest that caged-ATP can bind to the KATP channel but, on binding, decreases the open probability to a lesser extent than does ATP. Additionally, the observations indicate that for photolytically-generated ATP to bind to the channel, caged-ATP must first unbind (slowly) from the channel. We conclude that ‘caged-ATP’ is not fully caged with respect to its allosteric action on the KATP channel.
    Type of Medium: Electronic Resource
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