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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 170 (1984), S. 383-386 
    ISSN: 0014-5793
    Keywords: Calmodulin ; Contraction control ; Myosin light chain kinase ; Smooth muscle ; Taenia coli
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Myocardial contractility ; Troponin phosphorylation ; c-AMP ; Calcium ions ; Myocardial skinned fibres
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Glycerinated myocardial fibres treated with a detergent (Lubrol WX) and suspended in ATP salt solution produce half maximum isometric tension at pCa 6.2 (at pH 6.7). After addition of cyclic AMP (1–100 μM), the pCa required for half maximum activation is 5.9. c-AMP in concentrations of 1–100 μM induces a dose dependent inhibition (up to 40$ at pCa 6), and this effect can be amplified by the phosphodiesterase inhibitor IBMX (3-isobutyl-1-methylxanthine) 10−4 M. The effect is similar in presence and absence of sodium fluoride 10 mM. Since in detergent treated skinned fibres the cell membrane and the sarcoplasmic reticulum are extracted and since the Ca2+ ion concentration was kept constant and buffered, we propose that c-AMP does not act via the cell membrane or the sarcoplasmic reticulum, but via phosphorylation of troponin I. The latter is the only component which becomes phosphorylated in skinned fibres during c-AMP induced relaxation, an effect which is also responsible for the inhibition of actomyosin ATPase at constant Ca2+ ion concentration (cf. Ray and England 1976).
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-2013
    Keywords: Skinned coronary arteries ; Smooth muscle ; Regulation of contractile tone ; cAMP-dependent protein kinase ; cAMP-dependent modulation of contractile tone ; Calmodulin ; Calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Maximally contracted detergent skinned coronary smooth muscle fibres are relaxed by lowering the concentration of free Ca2+. The extent and rate of relaxation depends on the concentration of free Ca2+ and calmodulin (CaM) suggesting that it is the Ca2+. CaM complex which is responsible for maintaining tension. At a fixed concentration of Ca2+ and CaM further relaxation can be achieved by addition of the catalytic subunit of the cAMP-dependent protein kinase (cAMP-kinase). The extent as well as the relaxation rate depend on the concentration of cAMP-kinase (0.01–0.5 μM) and both are antagonized by high concentrations of Ca2+ and CaM. The Ca2+-requirement for obtaining half maximal concentration is shifted from 1.1 μM to 6.3 μM Ca2+ in the presence of 0.5 μM cAMP-kinase. These data indicate that the response of the contractile apparatus to a change in the free [Ca2+] can be modulated by cAMP-kinase at the level of the contractile proteins. It is further suggested that the tone of coronary smooth muscle is determined by the relative and not by the absolute concentrations of Ca2+, CaM and cAMP-kinase.
    Type of Medium: Electronic Resource
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