Cyclic nucleotide-gated ion channel
From Wikipedia, the free encyclopedia
A cyclic nucleotide-gated ion channel is any ion channel that opens in the presence of cyclic nucleotides.
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[edit] Mechanism
The channels are gated by a chemical ligand (the cyclic nucleotide), but they are more similar in structure to the family of voltage-gated ion channels than to the ligand gated ones. In fact, the cyclic nucleotide-gated channels often have positively- or negatively-charged areas that may respond to changes in membrane potential. The purpose and function of these charged areas are not yet fully understood.
[edit] Functions
Cyclic nucleotide-gated channels are particularly important in several systems:
- In the visual system, a cGMP- (cyclic guanosine monophosphate-) gated channel is found in the outer membrane of retinal photoreceptor cells. In response to high levels of cGMP, the channels are open and allow positively-charged ions to flow into the cell, causing depolarization. This is the state of the cell in the dark (called the dark current), but a photon striking a photoreceptor in the cell causes a chain reaction that results in lower levels of cGMP and therefore hyperpolarization. Thus, these cells are actually more active in dark than in light.
- Funny currents have been associated with the HCN channels.[2]
- cGMP-gated cation channels are present in the inner medullary collecting ducts of the kidney. They promote Na+ reabsorption. A part of the atrial natriuretic peptide mechanism of action is inhibition of these channels[3], just as the diuretic drug amiloride[3]. Aldosterone has an opposite effect.[3]
[edit] Examples
[edit] Alpha
"Cyclic nucleotide gated channel alpha" subunits include
- Cyclic nucleotide-gated channel alpha 1 (CNGA1)
- Cyclic nucleotide-gated channel alpha 2 (CNGA2)
- Cyclic nucleotide-gated channel alpha 3 (CNGA3)
- Cyclic nucleotide-gated channel alpha 4 (CNGA4)
Beta-subunits include:
[edit] Hyperpolarization-activated
Other examples include the following "hyperpolarization-activated cyclic nucleotide-gated potassium channels" (HCN channels): HCN1, HCN2, HCN3, HCN4
[edit] References
- ^ Jenkins PM, Hurd TW, Zhang L, et al (2006). "Ciliary targeting of olfactory CNG channels requires the CNGB1b subunit and the kinesin-2 motor protein, KIF17". Curr. Biol. 16 (12): 1211-6. doi:. PMID 16782012.
- ^ DiFrancesco D (2006). "Serious workings of the funny current". Prog. Biophys. Mol. Biol. 90 (1-3): 13-25. doi:. PMID 15975637.
- ^ a b c Walter F., PhD. Boron. Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. ISBN 1-4160-2328-3. Page 875
[edit] External links
- MeSH cyclic-nucleotide-gated+ion+channels
- Overview at wustl.edu
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