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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 353 (1995), S. 1-10 
    ISSN: 1432-1912
    Keywords: Key words Cyclic nucleotide-gated channels ; Second messenger ; Cyclic GMP ; Calcium ; Nitric oxide ; Molecular cloning ; Gene family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cyclic nucleotide-gated cation channels (CNG channels) form a multi-gene family consisting of at least five distinct members (CNG1–5). Expression studies have indicated that only CNG1–3 are able to form functional homooligomeric channels. Although structurally related, the cDNAs of CNG4–5 fail to induce cyclic nucleotide-dependent currents when expressed alone. However, when co-expressed with CNG1–3 they confer some of the physiologically observed properties of native CNG channels which are absent from the homooligomeric CNG1–3 channels. CNG channels are expressed in several tissues and cell types pointing to a general function of these channels in a wide variety of cellular systems. There is now increasing evidence that a major function of CNG channels may consist in providing a second messenger-regulated pathway for Ca2+ influx.
    Type of Medium: Electronic Resource
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