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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of intracellular calcium by a signalling complex of IRAG, IP 3 receptor and cGMP kinase Iβ (2000)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 404 (2000), S. 197-201 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Calcium release from the endoplasmic reticulum controls a number of cellular processes, including proliferation and contraction of smooth muscle and other cells. Calcium release from inositol 1,4,5-trisphosphate (IP3)-sensitive stores is negatively regulated by binding of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35004606
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  • 2
    Electronic Resource
    Electronic Resource
    A family of hyperpolarization-activated mammalian cation channels (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 393 (1998), S. 587-591 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Pacemaker activity of spontaneously active neurons and heart cells is controlled by a depolarizing, mixed Na+/K+ current, named Ih (or If in the sinoatrial node of the heart),. This current is activated on hyperpolarization of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/31255
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular diversity of cyclic nucleotide-gated cation channels (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 353 (1995), S. 1-10 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00168909
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular diversity of cyclic nucleotide-gated cation channels (1995)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 353 (1995), S. 1-10 
    Details
    ISSN: 1432-1912
    Keywords: 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 roviding a second messenger-regulated pathway for Ca2+ influx.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168909
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Cyclic nucleotide-gated channels – mediators of NO:cGMP-regulated processes (1998)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 358 (1998), S. 140-144 
    Details
    ISSN: 1432-1912
    Keywords: Key words Cyclic nucleotide-gated channels ; Nitric ; oxide ; Cyclic GMP ; Cyclic AMP ; Calcium ; Gene family
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cyclic nucleotide-gated (CNG) channels represent one of the three known cellular receptor classes for cGMP. Activation of CNG channels by binding of cyclic nucleotides to a site in the C-terminus results in opening of the channel pore, entry of Ca2+ into the cell and subsequent induction of Ca2+-dependent processes. In this review we will summarize new data on the complex molecular structure and the activation mechanism of CNG channels. In addition, we will discuss the role of CNG channels as mediators of NO:cGMP-dependent cellular processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00005235
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  • 6
    Electronic Resource
    Electronic Resource
    On the regulation of the expressed L-type calcium channel by cAMP-dependent phosphorylation (1995)
    Springer
    Pflügers Archiv 430 (1995), S. 340-347 
    Details
    ISSN: 1432-2013
    Keywords: L-Type calcium channels ; cAMP-dependent regulation of calcium channels ; Transient and stable expression of calcium channels ; CHO cells ; HEK 293 cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The Ca2+ channel subunits α1C-a and α1C-b were stably expressed in Chinese hamster ovary (CHO) and human embryonic kidney (HEK) 293 cells. The peak Ba2+ current (I Ba) of these cells was not affected significantly by internal dialysis with 0.1 mM cAMP-dependent protein kinase inhibitor peptide (mPKI), 25 μM cAMP-dependent protein kinase catalytic subunit (PKA), or a combination of 25 μM PKA and 1 μM okadaic acid. The activity of the α1C-b channel subunit expressed stably in HEK 293 cells was depressed by 1 μM H 89 and was not increased by superfusion with 5 μM forskolin plus 20 μM isobutylmethylxanthine (IBMX). The α1C-a·β2·α2/δ complex was transiently expressed in HEK 293 cells; it was inhibited by internal dialysis of the cells with 1 μM H 89, but was not affected by internal dialysis with mPKI, PKA or microcystin. Internal dialysis of cells expressing the α1C-a·β2·α2/δ channel with 10 μM PKA did not induce facilitation after a 150-ms prepulse to +50 mV. The Ca2+ current (I Ca) of cardiac myocytes increased threefold during internal dialysis with 5 μM PKA or 25 μM microcystin and during external superfusion with 0.1 μM isoproterenol or 5 μM forskolin plus 50 μM IBMX. These results indicate that the L-type Ca2+ channel expressed is not modulated by cAMP-dependent phosphorylation to the same extent as in native cardiac myocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373908
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