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- Table of Contents
Facts about Potassium voltage-gated channel subfamily KQT member 5.
May contribute, together with other potassium channels, to the molecular diversity of a heterogeneous population of M- channels, varying in kinetic and pharmacological properties, which underlie this physiologically significant current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991.
Human | |
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Gene Name: | KCNQ5 |
Uniprot: | Q9NR82 |
Entrez: | 56479 |
Belongs to: |
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potassium channel family |
KQT-like 5; Kv7.5; potassium channel protein; Potassium channel subunit alpha KvLQT5; potassium voltage-gated channel subfamily KQT member 5; potassium voltage-gated channel, KQT-like subfamily, member 5; Voltage-gated potassium channel subunit Kv7.5
Mass (kDA):
102.179 kDA
Human | |
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Location: | 6q13 |
Sequence: | 6; NC_000006.12 (72621843..73198853) |
Strongly expressed in brain and skeletal muscle. In brain, expressed in cerebral cortex, occipital pole, frontal lobe and temporal lobe. Lower levels in hippocampus and putamen. Low to undetectable levels in medulla, cerebellum and thalamus.
Cell membrane; Multi-pass membrane protein.
In situ hybridization and staining patterns of the KCNQ5 message are briefly summarized in this article. I'll also briefly discuss its biophysical and pharmacological properties. I will also discuss its applications in cellular signaling. Keep reading to learn more. Enjoy this quick overview. Happy labelling!
In situ hybridization revealed that KCNQ5 messages were located in the retina of the monkey retina. The anti-KCNQ5 antibody was used to label RPE cells. This allowed the message to be visualized in the inner and outer nuclear layers of RPE cells. In situ hybridization of KCNQ5 messages from the monkey retina also revealed that it was located in the inner segments and cone photoreceptors as well as the RPE's basal membrane. The RPE and Bruch’s membrane contained the corresponding cellular structures, which also exhibit blue emission channel autofluorescence.
In situ hybridization employs radioactive or chemically-labeled probes to detect specific sequences of nucleic acid in a tissue sample. The probes that are labeled bind to DNA strands. To determine the exact sequence, the riboprobes were labeled with fluorescent labels and incubated overnight @ 57degC. The sections were then rinsed with PBST. The sections were then incubated overnight in a hybridization solution that contained 1 mg/ml riboprobe, 5x SSC (pH 7.0), 0.2 mg/ml yeast tRNA, 0.2% Tween-20, and 0.1 mg/ml heparin.
The procedure to detect Vglut2 mRNA was the same as previously described (9, 45). The sections were washed with 0.1% Tween-20, treated with proteinase K for 10 min, and postfixed with 4% PFA for 10 min at 37degC. After the incubation period was over, the sections were embedded for 20 minutes in methanol containing 0.3% O2 for 20 min.
The two-hour in situ HCR used two different probe-hairpin pairs to detect the mRNAs of Drd2, Penk, and Drd1. A combined Alexa488 hairpin DNA was used to visualize each gene's signal intensity. Multiplex staining was also easy because the probes were marked with different fluorescent proteins.
KCNQ5 is detected in the retina by in situ hybridization. This technique is an effective tool for gene expression analysis. It uses cDNA probes that have been produced by using specific primers and SP6 RNA polymerase. Marinol was then used to mount the probes. The resulting sections could then be analyzed using Western Blotting.
The retina is where the antibody against KCNQ5 is located. The antibody was able to label the inner plexiform layer and inner segments of rod and conical photoreceptors as well as punctate structures close to the RPE basal Membrane. It also showed autofluorescence through the blue emission canal. It is useful for studying retinal neurons function and KCNQ5 Subunits.
KCNQ5 in RPE was immunolabeled. It was found near Bruch and the basal membranes. This marker did NOT colocalize with CD29. Although lipofuscin and KCNQ5 were similar in immunoreactivity, the latter did not colocalize well with the former. In addition, immunolabeling of KCNQ5 was weaker in the neural retina than in the outer plexiform layer.
KCNQ5 exhibited immunoreactivity in hippocampi neurons from mice that were genetically derived KCNQ5 genes. KCNQ5 is expressed predominantly in the CA3 area. KCNQ5G278S mutant protein has altered expression within the hippocampus. KCNQ5G278S mice also show preferential labelling for cell somata that are not located in the pyramidal layers. This may be due in part to the cell body's retention the mutant protein.
However, despite the fact that a KCNQ5 marker is not expressed in the RPE, it is present in most retinal neurons. PCR results obtained using cDNA from isolated RPE sheets confirmed the presence of KCNQ5 transcript in the retina. These findings also support KCNQ5's presence in the tissues of monkeys. Although KCNQ5 mRNA is present in the RPE, there is no evidence to support this.
KCNQ5 is expressed in both the RPE (nerve retina) and RPE (research paper). KCNQ5 is only expressed in the RPE. It is also present in the inner segments of rods and cones. Primate primates have a high level of expression of the KCNQ5 gene in their neural retinas. RPE is where the majority of this protein is expressed. In humans, however, it is not expressed in the RPE.
KCNQ5 was expressed in mice at a level of less than 0.0002. It is two-fold higher in brain than in heart. KCNQ2 to 5, which was expressed in the brain, was expressed at a level of 0.02, while KCNQ4's expression was 0.002+-0.0042. KCNQ5's expression in mice was lower than in humans. Also, the gene is expressed only in the hippocampus.
Despite the presence other markers in the cell type, it is still not clear what the biophysical or pharmacological characteristics of KCNQ5 gene marker are. KCNQ genes have been shown to be expressed in the nodose neurons of the airway in a mouse model. KCNQ3-KCNQ4 are both known neuronal excitability factors. However, it's not known if they are also involved in the regulation of airway reflex activity sensitivity and activity. To address this issue, single-cell RT-PCR methods were used to investigate the gene expression of single nodose neurons in the lung. These experiments suggest that the KCNQ3/Kv7.3 subunit of the nodose nerve is a key component.
KCNQ5 marks neuronal function and is found in the vestibular area. KCNQ5 is expressed in the same cell as KCNQ4 and has similar biophysical and pharmaceutical properties. In addition, the marker KCNQ5 has similar pharmacological properties to KCNQ4 and KCNQ1b. Both receptors are found within vestibular hair cells. They also have similar biophysical characteristics.
However, KCNQ4 affects the function of hair cells in mice. A study by Kubisch et al. Kubisch and colleagues found that KCNQ4 mice with hearing loss are more susceptible to hearing loss than mice without it. KCNQ4 knockout mice had higher OHC levels than KO mice. This may be due to the dominant negative effect of the KCNQ4 protein.
In addition to KCNQ5, the gene also binds calretinin and presenin. These two proteins interact physical with each other and this interaction may explain KCNQ1’s involvement in the heart rat. A recent study also showed that KCNQ1a, KCNQ1b were required for CAT activity. These results are encouraging, but further studies are necessary to understand the role of KCNQ1 in regulating heart rate.
The KCNQ gene encodes four alpha subunits of voltage-gated potassium channels. KCNQ1-KCNQ3 form a base-lateral K+ channel in the brain. Both KCNQ1 and KCNQ3 genes are responsible for a variety human genetic disorders, including epilepsy, encephalopathy, long-QT syndrome, epilepsy, and encephalopathy. It is thought that the KCNQ gene family is important in the regulation of cyclic AMP in colonic crypt cells.
KCNQ5 is a marker gene that is expressed throughout brain. It contributes to AHP currents in the CA3 area and is found in the somata of neuronal cells in the human cortex. KCNQ5 can also be found in glutamatergic synapses of several rat brain stem nuclei. It is also located in the postsynaptic membrane at vestibular calyx terminals. KCNQ5 was previously thought to be located at Held's calyx.
The expression of KCNQ has been studied in cardiac and neuronal cells. The K+ channels play a crucial role in controlling vascular reactiveness. KCNQ5 expression was detected in smooth muscle cells of murine portal vein. Despite the lack of ERG K+ channels in murine portal vein, KCNQ5 was expressed in a small number of PV myocytes.
The labelling of KCNQ5 in the CA3 area of mice was similar to that seen in Kcnq5dn/dn mice. Mice that expressed KCNQ5 were crossed to mice that possessed the GAD67GFP marker, which labels GABAergic cells. In these mice, KCNQ5 labelling amounted to 12.3%. KCNQ5 labelled interneurons in the lacunosum-molecularum, st. radiatum, and oriens, and co-localized with the markers for GluR2 and GAD65/67.
KCNQ2/3 has been associated with epilepsy in mice. KCNQ5 appears to be more common in neurons that KCNQ2, which is expressed at excitatory synapses and interneurons. KCNQ2 & -3 are involved in epilepsy. KCNQ5 is not. It is also linked to seizures, and other neurologic disorders.
KCNQ genes encode potassium channel genes that regulate the electrical excitability cardiac myocytes as well as neurons. Five members of the KCNQ family are represented. KCNQ1 is responsible for slow component of delayed rectifier K+ voltages in cardiac muscles. KCNQ2 and KCNQ2 are more common in the brain and in sympathetic neurons. KCNQ channels have different electrophysiological properties, and co-expression of regulatory subunits encoded in KCNE genes modifies the function.
KCNQ activation at 20% was significantly accelerated (t=114msvs.313ms), with the voltage dependence of activation shifting slightly towards more negative potentials. KCNQ current, however, did not affect activation after DAG concentration. This indicates that KCNQ is inactive among mice. This may be due to the lack of KCNQ5 specific inhibitors in mice.
PMID: 10787416 by Lerche C., et al. Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity.
PMID: 10816588 by Schroeder B.C., et al. KCNQ5, a novel potassium channel broadly expressed in brain, mediates M-type currents.