Potassium channels that contain two pores in tandem. They are responsible for baseline or leak currents and may be the most numerous of all K channels.
Cell membrane glycoproteins that are selectively permeable to potassium ions. At least eight major groups of K channels exist and they are made up of dozens of different subunits.
A central respiratory stimulant with a brief duration of action. (From Martindale, The Extra Pharmocopoeia, 30th ed, p1225)
An element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE.
Potassium channel whose permeability to ions is extremely sensitive to the transmembrane potential difference. The opening of these channels is induced by the membrane depolarization of the ACTION POTENTIAL.
Voltage-gated potassium channels whose primary subunits contain six transmembrane segments and form tetramers to create a pore with a voltage sensor. They are related to their founding member, shaker protein, Drosophila.
Potassium channels where the flow of K+ ions into the cell is greater than the outward flow.
A class of drugs that act by inhibition of potassium efflux through cell membranes. Blockade of potassium channels prolongs the duration of ACTION POTENTIALS. They are used as ANTI-ARRHYTHMIA AGENTS and VASODILATOR AGENTS.
A delayed rectifier subtype of shaker potassium channels that is selectively inhibited by a variety of SCORPION VENOMS.
Gated, ion-selective glycoproteins that traverse membranes. The stimulus for ION CHANNEL GATING can be due to a variety of stimuli such as LIGANDS, a TRANSMEMBRANE POTENTIAL DIFFERENCE, mechanical deformation or through INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS.
The opening and closing of ion channels due to a stimulus. The stimulus can be a change in membrane potential (voltage-gated), drugs or chemical transmitters (ligand-gated), or a mechanical deformation. Gating is thought to involve conformational changes of the ion channel which alters selective permeability.
A delayed rectifier subtype of shaker potassium channels that is the predominant VOLTAGE-GATED POTASSIUM CHANNEL of T-LYMPHOCYTES.
A delayed rectifier subtype of shaker potassium channels that is commonly mutated in human episodic ATAXIA and MYOKYMIA.
Voltage-dependent cell membrane glycoproteins selectively permeable to calcium ions. They are categorized as L-, T-, N-, P-, Q-, and R-types based on the activation and inactivation kinetics, ion specificity, and sensitivity to drugs and toxins. The L- and T-types are present throughout the cardiovascular and central nervous systems and the N-, P-, Q-, & R-types are located in neuronal tissue.
Potassium channels whose activation is dependent on intracellular calcium concentrations.
A family of voltage-gated potassium channels that are characterized by long N-terminal and C-terminal intracellular tails. They are named from the Drosophila protein whose mutation causes abnormal leg shaking under ether anesthesia. Their activation kinetics are dependent on extracellular MAGNESIUM and PROTON concentration.
The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization).
A shaker subfamily that is prominently expressed in NEURONS and are necessary for high-frequency, repetitive firing of ACTION POTENTIALS.
Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).
A voltage-gated potassium channel that is expressed primarily in the HEART.
The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
A family of delayed rectifier voltage-gated potassium channels that share homology with their founding member, KCNQ1 PROTEIN. KCNQ potassium channels have been implicated in a variety of diseases including LONG QT SYNDROME; DEAFNESS; and EPILEPSY.
A delayed rectifier subtype of shaker potassium channels that conducts a delayed rectifier current. It contributes to ACTION POTENTIAL repolarization of MYOCYTES in HEART ATRIA.
An electrophysiologic technique for studying cells, cell membranes, and occasionally isolated organelles. All patch-clamp methods rely on a very high-resistance seal between a micropipette and a membrane; the seal is usually attained by gentle suction. The four most common variants include on-cell patch, inside-out patch, outside-out patch, and whole-cell clamp. Patch-clamp methods are commonly used to voltage clamp, that is control the voltage across the membrane and measure current flow, but current-clamp methods, in which the current is controlled and the voltage is measured, are also used.
A fast inactivating subtype of shaker potassium channels that contains two inactivation domains at its N terminus.
A subfamily of shaker potassium channels that shares homology with its founding member, Shab protein, Drosophila. They regulate delayed rectifier currents in the NERVOUS SYSTEM of DROSOPHILA and in the SKELETAL MUSCLE and HEART of VERTEBRATES.
A major class of calcium activated potassium channels whose members are voltage-dependent. MaxiK channels are activated by either membrane depolarization or an increase in intracellular Ca(2+). They are key regulators of calcium and electrical signaling in a variety of tissues.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The study of the generation and behavior of electrical charges in living organisms particularly the nervous system and the effects of electricity on living organisms.
A family of membrane proteins that selectively conduct SODIUM ions due to changes in the TRANSMEMBRANE POTENTIAL DIFFERENCE. They typically have a multimeric structure with a core alpha subunit that defines the sodium channel subtype and several beta subunits that modulate sodium channel activity.
A very slow opening and closing voltage-gated potassium channel that is expressed in NEURONS and is commonly mutated in BENIGN FAMILIAL NEONATAL CONVULSIONS.
Heteromultimers of Kir6 channels (the pore portion) and sulfonylurea receptor (the regulatory portion) which affect function of the HEART; PANCREATIC BETA CELLS; and KIDNEY COLLECTING DUCTS. KATP channel blockers include GLIBENCLAMIDE and mitiglinide whereas openers include CROMAKALIM and minoxidil sulfate.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A very slow opening and closing voltage-gated potassium channel that is expressed in NEURONS and is closely related to KCNQ2 POTASSIUM CHANNEL. It is commonly mutated in BENIGN FAMILIAL NEONATAL CONVULSIONS.
A shaker subfamily of potassium channels that participate in transient outward potassium currents by activating at subthreshold MEMBRANE POTENTIALS, inactivating rapidly, and recovering from inactivation quickly.
A class of drugs that act by selective inhibition of calcium influx through cellular membranes.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A family of inwardly-rectifying potassium channels that are activated by PERTUSSIS TOXIN sensitive G-PROTEIN-COUPLED RECEPTORS. GIRK potassium channels are primarily activated by the complex of GTP-BINDING PROTEIN BETA SUBUNITS and GTP-BINDING PROTEIN GAMMA SUBUNITS.

TWIK-2, a new weak inward rectifying member of the tandem pore domain potassium channel family. (1/374)

Potassium channels are found in all mammalian cell types, and they perform many distinct functions in both excitable and non-excitable cells. These functions are subserved by several different families of potassium channels distinguishable by primary sequence features as well as by physiological characteristics. Of these families, the tandem pore domain potassium channels are a new and distinct class, primarily distinguished by the presence of two pore-forming domains within a single polypeptide chain. We have cloned a new member of this family, TWIK-2, from a human brain cDNA library. Primary sequence analysis of TWIK-2 shows that it is most closely related to TWIK-1, especially in the pore-forming domains. Northern blot analysis reveals the expression of TWIK-2 in all human tissues assayed except skeletal muscle. Human TWIK-2 expressed heterologously in Xenopus oocytes is a non-inactivating weak inward rectifier with channel properties similar to TWIK-1. Pharmacologically, TWIK-2 channels are distinct from TWIK-1 channels in their response to quinidine, quinine, and barium. TWIK-2 is inhibited by intracellular, but not extracellular, acidification. This new clone reveals the existence of a subfamily in the tandem pore domain potassium channel family with weak inward rectification properties.  (+info)

Fatty acid block of the transient outward current in adult human atrium. (2/374)

Fatty acids represent an essential source of fuel for the heart and play an important role in the mechanical, electrical, and synthetic activities of cardiac cells. Under pathological conditions, such as ischemia followed by reperfusion, the myocardium is exposed to very high levels of fatty acids, in particular the monounsaturated fatty acid, oleic acid. Elevated plasma fatty acids have been linked to an increased risk for cardiac arrhythmias. In other species, fatty acids have been shown to modulate several cardiac ion channels, most notably potassium channels. Virtually nothing is known about the actions of oleic acid on potassium channels in human heart. We therefore characterized the effects of oleic acid on the transient outward current, sustained current, and inwardly rectifying current, some of the major potassium channels present in human atrium, using the whole-cell patch clamp method. Exposure of cells to oleic acid (5 microM) reduced the transient outward potassium current to 3.7 +/- 0.8 pA/pF (n = 4) compared with 7.0 +/- 0.7 pA/pF (n = 4) (P <. 05) for cells not exposed. In contrast, oleic acid had little effect on either the sustained current (4.3 +/- 0.3 pA/pF, n = 4 for oleic acid versus 4.8 +/- 0.5, n = 5 for control) present after the decay of the transient outward current or on the amplitude of IK1 measured at -100 mV (1.4 +/- 0.4 pA/pF, n = 4 for oleic acid versus 1.3 +/- 0. 4 pA/pF, n = 6 for control). In addition, oleic acid significantly slowed the rate of recovery of the transient outward current, which is predicted to result in a use-dependent reduction in current amplitude in the beating heart. These results suggest a possible contributing role for oleic acid block of the transient outward current in the pathological consequences of myocardial ischemia.  (+info)

Cloning of a new mouse two-P domain channel subunit and a human homologue with a unique pore structure. (3/374)

Mouse KCNK6 is a new subunit belonging to the TWIK channel family. This 335-amino acid polypeptide has four transmembrane segments, two pore-forming domains, and a Ca2+-binding EF-hand motif. Expression of KCNK6 transcripts is principally observed in eyes, lung, stomach and embryo. In the eyes, immunohistochemistry reveals protein expression only in some of the retina neurons. Although KCNK6 is able to dimerize as other functional two-P domain K+ channels when it is expressed in COS-7 cells, it remains in the endoplasmic reticulum and is unable to generate ionic channel activity. Deletions, mutations, and chimera constructions suggest that KCNK6 is not an intracellular channel but rather a subunit that needs to associate with a partner, which remains to be discovered, in order to reach the plasma membrane. A closely related human KCNK7-A subunit has been cloned. KCNK7 displays an intriguing GLE sequence in its filter region instead of the G(Y/F/L)G sequence, which is considered to be the K+ channel signature. This subunit is alternatively spliced and gives rise to the shorter forms KCNK7-B and -C. None of the KCNK7 structures can generate channel activity by itself. The KCNK7 gene is situated on chromosome 11, in the q13 region, where several candidate diseases have been identified.  (+info)

Identification and cloning of TWIK-originated similarity sequence (TOSS): a novel human 2-pore K+ channel principal subunit. (4/374)

We have identified and cloned a new member of the mammalian tandem pore domain K+ channel subunit family, TWIK-originated similarity sequence, from a human testis cDNA library. The 939 bp open reading frame encodes a 313 amino acid polypeptide with a calculated Mr of 33.7 kDa. Despite the same predicted topology, there is a relatively low sequence homology between TWIK-originated similarity sequence and other members of the mammalian tandem pore domain K+ channel subunit family group. TWIK-originated similarity sequence shares a low (< 30%) identity with the other mammalian tandem pore domain K+ channel subunit family group members and the highest identity (34%) with TWIK-1 at the amino acid level. Similar low levels of sequence homology exist between all members of the mammalian tandem pore domain K+ channel subunit family. Potential glycosylation and consensus PKC sites are present. Northern analysis revealed species and tissue-specific expression patterns. Expression of TWIK-originated similarity sequence is restricted to human pancreas, placenta and heart, while in the mouse, TWIK-originated similarity sequence is expressed in the liver. No functional currents were observed in Xenopus laevis oocytes or HEK293T cells, suggesting that TWIK-originated similarity sequence may be targeted to locations other than the plasma membrane or that TWIK-originated similarity sequence may represent a novel regulatory mammalian tandem pore domain K+ channel subunit family subunit.  (+info)

Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel. (5/374)

TREK-1 is a member of the novel structural class of K(+) channels with four transmembrane segments and two pore domains in tandem (1,2). TREK-1 is opened by membrane stretch and arachidonic acid. It is also an important target for volatile anesthetics (2,3). Here we show that internal acidification opens TREK-1. Indeed, lowering pH(i) shifts the pressure-activation relationship toward positive values and leads to channel opening at atmospheric pressure. The pH(i)-sensitive region in the carboxyl terminus of TREK-1 is the same that is critically involved in mechano-gating as well as arachidonic acid activation. A convergence, which is dependent on the carboxyl terminus, occurs between mechanical, fatty acids and acidic stimuli. Intracellular acidosis, which occurs during brain and heart ischemia, will induce TREK-1 opening with subsequent K(+) efflux and hyperpolarization.  (+info)

Transient outward K+ currents across the plasma membrane of laticifer from Hevea brasiliensis. (6/374)

Non-inactivating outward rectifying K+ channel currents have been identified in a variety of plant cell types and species. The present study of laticifer protoplasts from Hevea brasiliensis, cells which are specialized for stress response, has revealed, through a switch-clamp method, an outward rectifying current displaying rapid inactivation. The inactivation depended on the external K+ concentration and on the voltage. This current inactivation appeared clearly different from all those previously described in plant cells and it shared homology with current kinetics of animal Shaker family channels. These results, given the recent cloning of plant K+ channel beta-subunits, shed new light on possible plant K+ channel regulation.  (+info)

TBAK-1 and TASK-1, two-pore K(+) channel subunits: kinetic properties and expression in rat heart. (7/374)

A mammalian K(+) channel subunit (TBAK-1/TASK-1) containing two pore domains and four transmembrane segments and whose mRNA is highly expressed in the heart has been cloned recently. TBAK-1 and TASK-1 are identical except for the additional nine amino acids in the NH(2) terminus of TBAK-1. We examined their kinetic properties, pH sensitivity, and regional cardiac mRNA expression and determined whether a native cardiac K(+) channel with similar kinetic properties was present. When TBAK-1 or TASK-1 was transiently expressed in COS-7 cells, time- and voltage-independent whole cell currents were observed. Single-channel conductances of TBAK-1 and TASK-1 were 14.6 +/- 1.0 and 13.8 +/- 2.8 pS, respectively, at -80 mV in 140 mM extracellular K(+), and the mean open times were 0.8 +/- 0.1 and 0.6 +/- 0.1 ms, respectively. Both TBAK-1 and TASK-1 were highly sensitive to extracellular pH such that a decrease from 7.2 to 6.4 reduced their open probability (P(o)) by 81 +/- 14% and 80 +/- 16%, whereas a decrease in intracellular pH from 7.2 to 6.4 reduced the P(o) by 42 +/- 10% and 47 +/- 12%, respectively. TBAK-1/TASK-1 mRNA was expressed in all regions of the rat heart, with the highest level of expression in the right atrium. A 14-pS K(+) channel with kinetic properties similar to those of TBAK-1/TASK-1 was identified in rat atrial and ventricular cells. These results indicate that TBAK-1/TASK-1 represents a functional native K(+) channel in the rat heart.  (+info)

Arrhythmic disorder mapped to chromosome 1q42-q43 causes malignant polymorphic ventricular tachycardia in structurally normal hearts. (8/374)

OBJECTIVES: The purpose of this study was to provide clinical and anatomical characteristics as well as genetic background of a malignant arrhythmogenic disorder. BACKGROUND: An inherited autosomally dominant cardiac syndrome causing stress-induced polymorphic ventricular tachycardia and syncope in the absence of structural myocardial changes was detected in two families. METHODS: Two unrelated families with six victims of sudden death and 51 living members were evaluated. Resting and exercise electrocardiograms (ECG), echocardiography, magnetic resonance imaging (MRI), cineangiography, microscopic examination of endomyocardial biopsies and a drug testing with a class IC antiarrhythmic agent flecainide were performed. A genetic linkage analysis was carried out to map the gene locus. RESULTS: Of the 24 affected individuals, 10 had succumbed with six cases of sudden death, and 14 survivors showed evidence of disease. Exercise stress test induced ventricular bigeminy or polymorphic ventricular tachycardia in affected individuals. Three children initially examined before 10 years of age developed arrhythmias during a four-year follow-up. Resting ECGs were normal in affected subjects except a slight prolongation of the QT intervals adjusted for heart rate (QTc) (430 +/- 18 vs. 409 +/- 19 ms, affected vs. nonaffected, p < 0.01). Administration of flecainide did not induce ECG abnormalities encountered in familial idiopathic ventricular fibrillation. Ventricular volumes, contractility and wall measurements were normal by echocardiography, right ventricular cineangiography and MRI. Histopathological examination showed no fibrosis or fatty infiltration. The cumulative cardiac mortality by the age of 30 years was 31%. The disease locus was assigned to chromosome 1q42-q43, with a maximal pairwise lod score of 4.74 in the two families combined. Only one heterozygous carrier was clinically unaffected suggesting high disease penetrance in adulthood. CONCLUSIONS: A distinct cardiac disorder linked to chromosome 1q42-q43 causes exercise-induced polymorphic ventricular tachycardia in structurally normal hearts and is highly malignant. Delayed clinical manifestation necessitates repeated exercise electrocardiography to assure diagnosis in young individuals of the families.  (+info)

Tandem pore domain potassium (K2P) channels are a subfamily of potassium channels that contain two pore-forming domains in a single polypeptide chain. These channels are also known as "double-barreled" or "leak" potassium channels because they provide a background leak conductance for potassium ions across the cell membrane. They are involved in regulating the resting membrane potential and excitability of cells, and are targets for various therapeutic agents. Examples of K2P channels include TREK, TRAAK, TASK, TWIK, and THIK families.

Potassium channels are membrane proteins that play a crucial role in regulating the electrical excitability of cells, including cardiac, neuronal, and muscle cells. These channels facilitate the selective passage of potassium ions (K+) across the cell membrane, maintaining the resting membrane potential and shaping action potentials. They are composed of four or six subunits that assemble to form a central pore through which potassium ions move down their electrochemical gradient. Potassium channels can be modulated by various factors such as voltage, ligands, mechanical stimuli, or temperature, allowing cells to fine-tune their electrical properties and respond to different physiological demands. Dysfunction of potassium channels has been implicated in several diseases, including cardiac arrhythmias, epilepsy, and neurodegenerative disorders.

Doxapram is a central stimulant drug that acts on the respiratory system. It is primarily used to stimulate breathing and promote wakefulness in patients who have reduced levels of consciousness or are experiencing respiratory depression due to various causes, such as anesthesia or medication overdose.

Doxapram works by stimulating the respiratory center in the brainstem, increasing the rate and depth of breathing. It also has a mild stimulant effect on the central nervous system, which can help to promote wakefulness and alertness.

The drug is available in various forms, including injectable solutions and inhaled powders. It is typically administered under medical supervision in a hospital or clinical setting due to its potential for causing adverse effects such as agitation, anxiety, and increased heart rate and blood pressure.

It's important to note that doxapram should only be used under the direction of a healthcare professional, as improper use can lead to serious complications.

Potassium is a essential mineral and an important electrolyte that is widely distributed in the human body. The majority of potassium in the body (approximately 98%) is found within cells, with the remaining 2% present in blood serum and other bodily fluids. Potassium plays a crucial role in various physiological processes, including:

1. Regulation of fluid balance and maintenance of normal blood pressure through its effects on vascular tone and sodium excretion.
2. Facilitation of nerve impulse transmission and muscle contraction by participating in the generation and propagation of action potentials.
3. Protein synthesis, enzyme activation, and glycogen metabolism.
4. Regulation of acid-base balance through its role in buffering systems.

The normal serum potassium concentration ranges from 3.5 to 5.0 mEq/L (milliequivalents per liter) or mmol/L (millimoles per liter). Potassium levels outside this range can have significant clinical consequences, with both hypokalemia (low potassium levels) and hyperkalemia (high potassium levels) potentially leading to serious complications such as cardiac arrhythmias, muscle weakness, and respiratory failure.

Potassium is primarily obtained through the diet, with rich sources including fruits (e.g., bananas, oranges, and apricots), vegetables (e.g., leafy greens, potatoes, and tomatoes), legumes, nuts, dairy products, and meat. In cases of deficiency or increased needs, potassium supplements may be recommended under the guidance of a healthcare professional.

Voltage-gated potassium channels are a type of ion channel found in the membrane of excitable cells such as nerve and muscle cells. They are called "voltage-gated" because their opening and closing is regulated by the voltage, or electrical potential, across the cell membrane. Specifically, these channels are activated when the membrane potential becomes more positive, a condition that occurs during the action potential of a neuron or muscle fiber.

When voltage-gated potassium channels open, they allow potassium ions (K+) to flow out of the cell down their electrochemical gradient. This outward flow of K+ ions helps to repolarize the membrane, bringing it back to its resting potential after an action potential has occurred. The precise timing and duration of the opening and closing of voltage-gated potassium channels is critical for the normal functioning of excitable cells, and abnormalities in these channels have been linked to a variety of diseases, including cardiac arrhythmias, epilepsy, and neurological disorders.

The Shaker superfamily of potassium channels, also known as Kv channels (voltage-gated potassium channels), refers to a group of ion channels that are responsible for the selective transport of potassium ions across the cell membrane. These channels are crucial for regulating the electrical excitability of cells, particularly in neurons and muscle cells.

The Shaker superfamily is named after the Drosophila melanogaster (fruit fly) gene shaker, which was the first voltage-gated potassium channel to be identified and cloned. The channels in this family share a common structure, consisting of four subunits that each contain six transmembrane domains. The fourth domain contains the voltage sensor, which responds to changes in membrane potential and triggers the opening or closing of the channel pore.

The Shaker superfamily is further divided into several subfamilies based on their sequence similarity and functional properties. These include the Shaw, Shab, and Shal subfamilies, among others. Each subfamily has distinct biophysical and pharmacological properties that allow for selective activation or inhibition by various drugs and toxins.

Overall, the Shaker superfamily of potassium channels plays a critical role in maintaining the electrical excitability of cells and is involved in a wide range of physiological processes, including nerve impulse transmission, muscle contraction, and hormone secretion.

Inwardly rectifying potassium channels (Kir) are a type of potassium channel that allow for the selective passage of potassium ions (K+) across cell membranes. The term "inwardly rectifying" refers to their unique property of allowing potassium ions to flow more easily into the cell (inward current) than out of the cell (outward current). This characteristic is due to the voltage-dependent blockage of these channels by intracellular magnesium and polyamines at depolarized potentials.

These channels play crucial roles in various physiological processes, including:

1. Resting membrane potential maintenance: Kir channels help establish and maintain the negative resting membrane potential in cells by facilitating potassium efflux when the membrane potential is near the potassium equilibrium potential (Ek).
2. Action potential repolarization: In excitable cells like neurons and muscle fibers, Kir channels contribute to the rapid repolarization phase of action potentials, allowing for proper electrical signaling.
3. Cell volume regulation: Kir channels are involved in regulating cell volume by mediating potassium influx during osmotic stress or changes in intracellular ion concentrations.
4. Insulin secretion: In pancreatic β-cells, Kir channels control the membrane potential and calcium signaling necessary for insulin release.
5. Renal function: Kir channels are essential for maintaining electrolyte balance and controlling renal tubular transport in the kidneys.

There are several subfamilies of inwardly rectifying potassium channels (Kir1-7), each with distinct biophysical properties, tissue distributions, and functions. Mutations in genes encoding these channels can lead to various human diseases, including cardiac arrhythmias, epilepsy, and Bartter syndrome.

Potassium channel blockers are a class of medications that work by blocking potassium channels, which are proteins in the cell membrane that control the movement of potassium ions into and out of cells. By blocking these channels, potassium channel blockers can help to regulate electrical activity in the heart, making them useful for treating certain types of cardiac arrhythmias (irregular heart rhythms).

There are several different types of potassium channel blockers, including:

1. Class III antiarrhythmic drugs: These medications, such as amiodarone and sotalol, are used to treat and prevent serious ventricular arrhythmias (irregular heart rhythms that originate in the lower chambers of the heart).
2. Calcium channel blockers: While not strictly potassium channel blockers, some calcium channel blockers also have effects on potassium channels. These medications, such as diltiazem and verapamil, are used to treat hypertension (high blood pressure), angina (chest pain), and certain types of arrhythmias.
3. Non-selective potassium channel blockers: These medications, such as 4-aminopyridine and tetraethylammonium, have a broader effect on potassium channels and are used primarily in research settings to study the electrical properties of cells.

It's important to note that potassium channel blockers can have serious side effects, particularly when used in high doses or in combination with other medications that affect heart rhythms. They should only be prescribed by a healthcare provider who is familiar with their use and potential risks.

The Kv1.2 potassium channel is a type of voltage-gated potassium channel that is widely expressed in the nervous system and other tissues. It is composed of four pore-forming α subunits, each of which contains six transmembrane domains and a voltage-sensing domain. These channels play important roles in regulating neuronal excitability, repolarization of action potentials, and controlling neurotransmitter release.

Kv1.2 channels are activated by membrane depolarization and mediate the rapid efflux of potassium ions from cells, which helps to restore the resting membrane potential. They can also be modulated by various intracellular signaling pathways and pharmacological agents, making them targets for therapeutic intervention in a variety of neurological disorders.

Mutations in the KCNA2 gene, which encodes the Kv1.2 channel, have been associated with several human diseases, including episodic ataxia type 1, familial hemiplegic migraine, and spinocerebellar ataxia type 13. These mutations can alter channel function and lead to abnormal neuronal excitability, which may contribute to the symptoms of these disorders.

Ion channels are specialized transmembrane proteins that form hydrophilic pores or gaps in the lipid bilayer of cell membranes. They regulate the movement of ions (such as sodium, potassium, calcium, and chloride) across the cell membrane by allowing these charged particles to pass through selectively in response to various stimuli, including voltage changes, ligand binding, mechanical stress, or temperature changes. This ion movement is essential for many physiological processes, including electrical signaling, neurotransmission, muscle contraction, and maintenance of resting membrane potential. Ion channels can be categorized based on their activation mechanisms, ion selectivity, and structural features. Dysfunction of ion channels can lead to various diseases, making them important targets for drug development.

Ion channel gating refers to the process by which ion channels in cell membranes open and close in response to various stimuli, allowing ions such as sodium, potassium, and calcium to flow into or out of the cell. This movement of ions is crucial for many physiological processes, including the generation and transmission of electrical signals in nerve cells, muscle contraction, and the regulation of hormone secretion.

Ion channel gating can be regulated by various factors, including voltage changes across the membrane (voltage-gated channels), ligand binding (ligand-gated channels), mechanical stress (mechanosensitive channels), or other intracellular signals (second messenger-gated channels). The opening and closing of ion channels are highly regulated and coordinated processes that play a critical role in maintaining the proper functioning of cells and organ systems.

The Kv1.3 potassium channel is a type of voltage-gated potassium channel that is widely expressed in various tissues, including immune cells such as T lymphocytes. It plays a crucial role in regulating the electrical activity of cells and controlling the flow of potassium ions across the cell membrane.

Kv1.3 channels are composed of four pore-forming alpha subunits, each containing six transmembrane domains. These channels open and close in response to changes in the membrane potential, allowing potassium ions to flow out of the cell when the channel is open. This movement of ions helps to restore the resting membrane potential and regulate the excitability of the cell.

In T lymphocytes, Kv1.3 channels are involved in the regulation of calcium signaling and activation of immune responses. They play a critical role in maintaining the membrane potential and controlling the release of calcium from intracellular stores, which is necessary for T-cell activation and proliferation. Inhibition or blockade of Kv1.3 channels has been shown to suppress T-cell activation and could have potential therapeutic implications in the treatment of autoimmune diseases and transplant rejection.

Kv1.1 potassium channel, also known as KCNA1, is a type of voltage-gated potassium channel that plays a crucial role in the regulation of electrical excitability in neurons and other excitable cells. It is encoded by the KCNA1 gene located on chromosome 12p13.

The Kv1.1 channel is composed of four α-subunits, each containing six transmembrane domains with a pore-forming region between the fifth and sixth domains. These channels are responsible for the rapid repolarization of action potentials in neurons, which helps to control the frequency and pattern of neural activity.

Mutations in the KCNA1 gene have been associated with various neurological disorders, including episodic ataxia type 1 (EA1) and familial hemiplegic migraine (FHM). EA1 is characterized by brief episodes of cerebellar ataxia, myokymia, and neuromyotonia, while FHM is a severe form of migraine with aura that can cause temporary paralysis on one side of the body.

Overall, Kv1.1 potassium channels play an essential role in maintaining normal neural excitability and are critical for proper neurological function.

Calcium channels are specialized proteins that span the membrane of cells and allow calcium ions (Ca²+) to flow in and out of the cell. They are crucial for many physiological processes, including muscle contraction, neurotransmitter release, hormone secretion, and gene expression.

There are several types of calcium channels, classified based on their biophysical and pharmacological properties. The most well-known are:

1. Voltage-gated calcium channels (VGCCs): These channels are activated by changes in the membrane potential. They are further divided into several subtypes, including L-type, P/Q-type, N-type, R-type, and T-type. VGCCs play a critical role in excitation-contraction coupling in muscle cells and neurotransmitter release in neurons.
2. Receptor-operated calcium channels (ROCCs): These channels are activated by the binding of an extracellular ligand, such as a hormone or neurotransmitter, to a specific receptor on the cell surface. ROCCs are involved in various physiological processes, including smooth muscle contraction and platelet activation.
3. Store-operated calcium channels (SOCCs): These channels are activated by the depletion of intracellular calcium stores, such as those found in the endoplasmic reticulum. SOCCs play a critical role in maintaining calcium homeostasis and signaling within cells.

Dysregulation of calcium channel function has been implicated in various diseases, including hypertension, arrhythmias, migraine, epilepsy, and neurodegenerative disorders. Therefore, calcium channels are an important target for drug development and therapy.

Calcium-activated potassium channels are a type of ion channel found in the membranes of cells. These channels are activated by an increase in intracellular calcium levels and play a crucial role in regulating various cellular processes, including electrical excitability, neurotransmitter release, hormone secretion, and vascular tone.

Once activated, calcium-activated potassium channels allow potassium ions (K+) to flow out of the cell, which can lead to membrane hyperpolarization or stabilization of the resting membrane potential. This process helps control the frequency and duration of action potentials in excitable cells such as neurons and muscle fibers.

There are several subtypes of calcium-activated potassium channels, including:

1. Large conductance calcium-activated potassium (BK) channels: These channels have a large single-channel conductance and are activated by both voltage and intracellular calcium. They play essential roles in regulating vascular tone, neurotransmitter release, and neuronal excitability.
2. Small conductance calcium-activated potassium (SK) channels: These channels have a smaller single-channel conductance and are primarily activated by intracellular calcium. They contribute to the regulation of neuronal excitability and neurotransmitter release.
3. Intermediate conductance calcium-activated potassium (IK) channels: These channels have an intermediate single-channel conductance and are activated by both voltage and intracellular calcium. They play a role in regulating epithelial ion transport, smooth muscle cell excitability, and neurotransmitter release.

Dysfunction of calcium-activated potassium channels has been implicated in various pathological conditions, such as hypertension, epilepsy, chronic pain, and neurological disorders.

Ether-à-go-go (EAG) potassium channels are a type of voltage-gated potassium channel that are widely expressed in the heart, brain, and other tissues. They are named after the ethereal dance movements observed in fruit flies with mutations in these channels.

EAG potassium channels play important roles in regulating electrical excitability and signaling in excitable cells. In the heart, they help to control the duration of the action potential and the refractory period, which is critical for maintaining normal heart rhythm. In the brain, they are involved in regulating neuronal excitability and neurotransmitter release.

Mutations in EAG potassium channels have been associated with various human diseases, including cardiac arrhythmias, epilepsy, and bipolar disorder. The medical definition of "Ether-A-Go-Go Potassium Channels" refers to the genetic components that make up these channels and their role in physiological processes and disease states.

Membrane potential is the electrical potential difference across a cell membrane, typically for excitable cells such as nerve and muscle cells. It is the difference in electric charge between the inside and outside of a cell, created by the selective permeability of the cell membrane to different ions. The resting membrane potential of a typical animal cell is around -70 mV, with the interior being negative relative to the exterior. This potential is generated and maintained by the active transport of ions across the membrane, primarily through the action of the sodium-potassium pump. Membrane potentials play a crucial role in many physiological processes, including the transmission of nerve impulses and the contraction of muscle cells.

Shaw potassium channels, also known as KCNA4 channels, are a type of voltage-gated potassium channel that is encoded by the KCNA4 gene in humans. These channels play a crucial role in regulating the electrical excitability of cells, particularly in the heart and nervous system.

Shaw channels are named after James E. Shaw, who first identified them in 1996. They are composed of four subunits that arrange themselves to form a central pore through which potassium ions can flow. The channels are activated by depolarization of the cell membrane and help to repolarize the membrane during action potentials.

Mutations in the KCNA4 gene have been associated with various cardiac arrhythmias, including familial atrial fibrillation and long QT syndrome type 3. These conditions can cause irregular heart rhythms and may increase the risk of sudden cardiac death. Therefore, understanding the function and regulation of Shaw potassium channels is important for developing therapies to treat these disorders.

An oocyte, also known as an egg cell or female gamete, is a large specialized cell found in the ovary of female organisms. It contains half the number of chromosomes as a normal diploid cell, as it is the product of meiotic division. Oocytes are surrounded by follicle cells and are responsible for the production of female offspring upon fertilization with sperm. The term "oocyte" specifically refers to the immature egg cell before it reaches full maturity and is ready for fertilization, at which point it is referred to as an ovum or egg.

The KCNQ1 potassium channel, also known as the Kv7.1 channel, is a voltage-gated potassium ion channel that plays a crucial role in the regulation of electrical excitability in cardiac myocytes and inner ear epithelial cells. In the heart, it helps to control the duration and frequency of action potentials, thereby contributing to the maintenance of normal cardiac rhythm. Mutations in the KCNQ1 gene can lead to various cardiac disorders, such as long QT syndrome type 1 and familial atrial fibrillation. In the inner ear, it helps regulate potassium homeostasis and is essential for hearing and balance functions. Dysfunction of this channel has been linked to deafness and balance disorders.

"Xenopus laevis" is not a medical term itself, but it refers to a specific species of African clawed frog that is often used in scientific research, including biomedical and developmental studies. Therefore, its relevance to medicine comes from its role as a model organism in laboratories.

In a broader sense, Xenopus laevis has contributed significantly to various medical discoveries, such as the understanding of embryonic development, cell cycle regulation, and genetic research. For instance, the Nobel Prize in Physiology or Medicine was awarded in 1963 to John R. B. Gurdon and Sir Michael J. Bishop for their discoveries concerning the genetic mechanisms of organism development using Xenopus laevis as a model system.

"Xenopus" is not a medical term, but it is a genus of highly invasive aquatic frogs native to sub-Saharan Africa. They are often used in scientific research, particularly in developmental biology and genetics. The most commonly studied species is Xenopus laevis, also known as the African clawed frog.

In a medical context, Xenopus might be mentioned when discussing their use in research or as a model organism to study various biological processes or diseases.

KCNQ potassium channels, also known as Kv7 channels, are a type of voltage-gated potassium channel that play important roles in regulating electrical excitability in various tissues, including the heart and nervous system. These channels are composed of several subunits, typically formed by combinations of KCNQ1 to KCNQ5 proteins, which form a pore through which potassium ions can flow in response to changes in membrane voltage.

KCNQ channels are characterized by their slow activation and deactivation kinetics, which contribute to their role in setting the resting membrane potential and modulating the frequency of action potentials in neurons. In the heart, KCNQ channels help to regulate the duration of the cardiac action potential and are therefore important for maintaining normal heart rhythm.

Mutations in KCNQ channel genes have been associated with a variety of inherited disorders, including long QT syndrome, a condition characterized by abnormalities in the electrical repolarization of the heart that can lead to life-threatening arrhythmias. Other diseases associated with KCNQ channel dysfunction include epilepsy, migraine, and various forms of hearing loss.

The Kv1.5 potassium channel, also known as KCNA5, is a type of voltage-gated potassium channel that is widely expressed in various tissues, including the heart and blood vessels. It plays a crucial role in regulating electrical excitability and maintaining physiological functions in these tissues.

In the heart, Kv1.5 channels are primarily located in the atria and contribute to the repolarization phase of the cardiac action potential. They help establish the rapid delayed rectifier current (IKr), which is essential for normal atrial electrical activity and maintaining proper heart rhythm. Mutations or dysfunctions in Kv1.5 channels can lead to various cardiac arrhythmias, such as atrial fibrillation.

In blood vessels, Kv1.5 channels are involved in the regulation of vascular tone and blood pressure. They contribute to the hyperpolarization of vascular smooth muscle cells, which leads to vasodilation and decreased peripheral resistance. Dysregulation of Kv1.5 channels has been implicated in several cardiovascular diseases, including hypertension and atherosclerosis.

Overall, Kv1.5 potassium channels are critical for maintaining proper electrical activity in the heart and regulating vascular tone, making them an important target for therapeutic interventions in various cardiovascular disorders.

Patch-clamp techniques are a group of electrophysiological methods used to study ion channels and other electrical properties of cells. These techniques were developed by Erwin Neher and Bert Sakmann, who were awarded the Nobel Prize in Physiology or Medicine in 1991 for their work. The basic principle of patch-clamp techniques involves creating a high resistance seal between a glass micropipette and the cell membrane, allowing for the measurement of current flowing through individual ion channels or groups of channels.

There are several different configurations of patch-clamp techniques, including:

1. Cell-attached configuration: In this configuration, the micropipette is attached to the outer surface of the cell membrane, and the current flowing across a single ion channel can be measured. This configuration allows for the study of the properties of individual channels in their native environment.
2. Whole-cell configuration: Here, the micropipette breaks through the cell membrane, creating a low resistance electrical connection between the pipette and the inside of the cell. This configuration allows for the measurement of the total current flowing across all ion channels in the cell membrane.
3. Inside-out configuration: In this configuration, the micropipette is pulled away from the cell after establishing a seal, resulting in the exposure of the inner surface of the cell membrane to the solution in the pipette. This configuration allows for the study of the properties of ion channels in isolation from other cellular components.
4. Outside-out configuration: Here, the micropipette is pulled away from the cell after establishing a seal, resulting in the exposure of the outer surface of the cell membrane to the solution in the pipette. This configuration allows for the study of the properties of ion channels in their native environment, but with the ability to control the composition of the extracellular solution.

Patch-clamp techniques have been instrumental in advancing our understanding of ion channel function and have contributed to numerous breakthroughs in neuroscience, pharmacology, and physiology.

The Kv1.4 potassium channel, also known as the KCNA4 channel, is a type of voltage-gated potassium channel that is widely expressed in various tissues, including the heart, brain, and skeletal muscle. It plays a crucial role in regulating electrical excitability and membrane potential in these cells.

The Kv1.4 channel is composed of four α-subunits, each containing six transmembrane domains with a pore-forming region between the fifth and sixth domains. The channel opens in response to depolarization of the membrane potential, allowing potassium ions to flow out of the cell, which helps to repolarize the membrane and terminate the action potential.

In the heart, Kv1.4 channels are expressed in the pacemaker cells of the sinoatrial node and help to regulate the heart rate. In the brain, they are involved in regulating neuronal excitability and neurotransmitter release. In skeletal muscle, Kv1.4 channels contribute to the regulation of membrane potential during muscle contraction and relaxation.

Mutations in the KCNA4 gene, which encodes the Kv1.4 channel, have been associated with various inherited arrhythmia syndromes, including familial atrial fibrillation and progressive conduction disease.

Shaker-related Kv1.5 potassium channels, also known as "Shab potassium channels," are a type of voltage-gated potassium channel that play a crucial role in regulating the electrical activity of cells, particularly in the heart and nervous system. These channels are named after the Shaker gene in Drosophila melanogaster (fruit flies) where they were first discovered and characterized.

The Kv1.5 channel is composed of four pore-forming α-subunits that assemble to form a tetrameric complex. Each α-subunit contains six transmembrane domains, with the voltage-sensing domain located in the fourth transmembrane segment and the potassium selectivity filter located in the pore region between the fifth and sixth transmembrane segments.

Kv1.5 channels are activated by membrane depolarization and contribute to the repolarization phase of the action potential in cardiac myocytes, helping to maintain the normal rhythm of the heart. In addition, Kv1.5 channels play a role in regulating neuronal excitability and neurotransmitter release in the nervous system.

Mutations in the KCNA5 gene, which encodes the Kv1.5 channel, have been associated with various cardiac arrhythmias, including atrial fibrillation and Brugada syndrome. Pharmacological blockade of Kv1.5 channels has also been shown to have potential therapeutic benefits in the treatment of atrial fibrillation and other cardiovascular disorders.

Large-conductance calcium-activated potassium channels (BK channels) are a type of ion channel found in the membranes of many types of cells, including excitable cells such as neurons and muscle cells. These channels are characterized by their large conductance to potassium ions (K+), which allows them to significantly impact the electrical excitability of cells.

BK channels are activated by both voltage and intracellular calcium ions (Ca2+). They are therefore also known as Ca2+-activated K+ (KCa) channels. When the membrane potential becomes more positive (depolarized), and/or when intracellular Ca2+ levels rise, BK channels open, allowing K+ to flow out of the cell. This efflux of K+ tends to hyperpolarize the membrane potential, making it more difficult for the cell to generate further action potentials or contractile responses.

BK channels play important roles in regulating a variety of physiological processes, including neuronal excitability, neurotransmitter release, vascular tone, and cardiac electrical activity. Dysfunction of BK channels has been implicated in several diseases, such as hypertension, epilepsy, and chronic pain.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Electrophysiology is a branch of medicine that deals with the electrical activities of the body, particularly the heart. In a medical context, electrophysiology studies (EPS) are performed to assess abnormal heart rhythms (arrhythmias) and to evaluate the effectiveness of certain treatments, such as medication or pacemakers.

During an EPS, electrode catheters are inserted into the heart through blood vessels in the groin or neck. These catheters can record the electrical activity of the heart and stimulate it to help identify the source of the arrhythmia. The information gathered during the study can help doctors determine the best course of treatment for each patient.

In addition to cardiac electrophysiology, there are also other subspecialties within electrophysiology, such as neuromuscular electrophysiology, which deals with the electrical activity of the nervous system and muscles.

Voltage-gated sodium channels are specialized protein complexes found in the membranes of excitable cells, such as neurons and muscle cells. They play a crucial role in the generation and propagation of action potentials, which are the electrical signals that allow these cells to communicate and coordinate their activities.

Structurally, voltage-gated sodium channels consist of a large alpha subunit that forms the ion-conducting pore, as well as one or more beta subunits that modulate the channel's properties. The alpha subunit contains four repeating domains (I-IV), each of which contains six transmembrane segments (S1-S6).

The channel is closed at resting membrane potentials but can be activated by depolarization of the membrane, leading to the opening of the pore and the rapid influx of sodium ions into the cell. This influx of positive charges further depolarizes the membrane, leading to the activation of additional voltage-gated sodium channels and the propagation of the action potential along the cell membrane.

Voltage-gated sodium channels are critical for normal physiological processes such as nerve impulse transmission and muscle contraction. However, mutations in these channels can lead to a variety of channelopathies, including inherited neurological disorders such as epilepsy and peripheral neuropathy. Additionally, certain drugs and toxins can target voltage-gated sodium channels, leading to altered electrical activity in excitable cells and potential toxicity or therapeutic effects.

KCNQ2 potassium channel, also known as Kv7.2 channel, is a type of voltage-gated potassium channel that plays a crucial role in regulating the electrical excitability of neurons. The channel is composed of four KCNQ2 subunits and can form heteromeric complexes with KCNQ3 subunits to form the M-current, which helps to set the resting membrane potential and control the firing frequency of action potentials in neurons.

Mutations in the KCNQ2 gene have been associated with a variety of neurological disorders, including benign familial neonatal seizures (BFNS), epileptic encephalopathy, and intellectual disability. These mutations can alter the function or expression of the KCNQ2 channel, leading to abnormal neuronal excitability and seizure activity.

In summary, KCNQ2 potassium channel is a type of voltage-gated potassium channel that helps regulate the electrical excitability of neurons and has been implicated in several neurological disorders when its function is altered due to genetic mutations.

ATP-sensitive potassium (KATP) channels are a type of ion channel found in the membranes of cells, including those in the heart, muscle, and pancreas. These channels are unique because their opening and closing are regulated by the levels of adenosine triphosphate (ATP) and adenosine diphosphate (ADP) in the cell.

Under normal conditions, when ATP levels are high and ADP levels are low, the KATP channels are closed, which allows the cells to maintain their normal electrical activity. However, during times of metabolic stress or ischemia (a lack of blood flow), the levels of ATP in the cell decrease while the levels of ADP increase. This change in the ATP-to-ADP ratio causes the KATP channels to open, which allows potassium ions to flow out of the cell. The efflux of potassium ions then leads to hyperpolarization of the cell membrane, which helps to protect the cells from damage.

In the pancreas, KATP channels play a crucial role in regulating insulin secretion. In the beta cells of the pancreas, an increase in blood glucose levels leads to an increase in ATP production and a decrease in ADP levels, which causes the KATP channels to close. This closure of the KATP channels leads to depolarization of the cell membrane, which triggers the release of insulin.

Overall, KATP channels are important regulators of cellular electrical activity and play a critical role in protecting cells from damage during times of metabolic stress or ischemia.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

KCNQ3 potassium channel, also known as Kv7.3 or KvLQT3, is a type of voltage-gated potassium channel that plays a crucial role in the regulation of electrical excitability in the brain and other tissues. These channels are composed of four α subunits that form a tetrameric complex, with each subunit containing six transmembrane domains and a pore region.

The KCNQ3 channel is widely expressed in the central nervous system, where it contributes to the regulation of neuronal excitability by mediating the slow component of the delayed rectifier potassium current (IKs). This current helps to set the resting membrane potential and control the firing pattern of action potentials in neurons.

Mutations in the KCNQ3 gene have been associated with a variety of neurological disorders, including benign familial neonatal seizures (BFNS), epileptic encephalopathy, and intellectual disability. These mutations can alter the electrical properties of the channel, leading to changes in neuronal excitability and network activity that underlie these conditions.

Overall, the KCNQ3 potassium channel is an important regulator of neural function and a potential target for therapeutic intervention in neurological disorders associated with altered neuronal excitability.

I'm sorry for any confusion, but "Shal Potassium Channels" is not a widely recognized or established medical term in the field of physiology or pharmacology. It seems like there might be a misunderstanding or a typo in the term you're looking for.

If you're referring to " Shaw Potassium Channels," these are a type of voltage-gated potassium channel named after the scientist who first described them, Robert A. Shaw. These channels play crucial roles in various physiological processes, including the regulation of heart rate and excitability of nerve cells.

If you meant to ask about something else or need further clarification, please provide more context or check the spelling, and I'll be happy to help!

Calcium channel blockers (CCBs) are a class of medications that work by inhibiting the influx of calcium ions into cardiac and smooth muscle cells. This action leads to relaxation of the muscles, particularly in the blood vessels, resulting in decreased peripheral resistance and reduced blood pressure. Calcium channel blockers also have anti-arrhythmic effects and are used in the management of various cardiovascular conditions such as hypertension, angina, and certain types of arrhythmias.

Calcium channel blockers can be further classified into two main categories based on their chemical structure: dihydropyridines (e.g., nifedipine, amlodipine) and non-dihydropyridines (e.g., verapamil, diltiazem). Dihydropyridines are more selective for vascular smooth muscle and have a greater effect on blood pressure than heart rate or conduction. Non-dihydropyridines have a more significant impact on cardiac conduction and contractility, in addition to their vasodilatory effects.

It is important to note that calcium channel blockers may interact with other medications and should be used under the guidance of a healthcare professional. Potential side effects include dizziness, headache, constipation, and peripheral edema.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

G protein-coupled inwardly-rectifying potassium channels (GIRK channels) are a type of potassium channel that are activated by G proteins, which are molecules that help transmit signals within cells. These channels are characterized by their ability to allow potassium ions to flow into the cell more easily than they allow potassium ions to flow out of the cell, hence the term "inwardly-rectifying."

GIRK channels play a role in regulating various physiological processes, including neurotransmission, heart rate, and insulin secretion. They are activated by several different G proteins, including those that are activated by certain neurotransmitters and hormones. When these G proteins bind to the channel, they cause it to open, allowing potassium ions to flow into the cell. This can have various effects on the cell, depending on the type of cell and the specific signals being transmitted.

GIRK channels are composed of four subunits, each of which contains a pore through which potassium ions can pass. These subunits can be made up of different types of proteins, and the specific combination of subunits in a channel can affect its properties and regulation. Mutations in genes that encode GIRK channel subunits have been linked to various diseases, including certain forms of epilepsy and cardiac arrhythmias.

"Local anesthetic inhibition of baseline potassium channels with two pore domains in tandem". Anesthesiology. 90 (4): 1092-102. ... Potassium channel blockers are agents which interfere with conduction through potassium channels. Potassium channel blockers ... Potassium channel Potassium channel opener Amiodarone also blocks CACNA2D2-containing voltage gated calcium channels works by ... Kennard (2005). "Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite ...
"Novel neuroprotectant chiral 3-n-butylphthalide inhibits tandem-pore-domain potassium channel TREK-1". Acta Pharmacologica ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000099337 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... a new weak inward rectifying member of the tandem pore domain potassium channel family". J Biol Chem. 274 (12): 7887-92. doi: ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P6.1, considered ... 1999). "Cloning of a new mouse two-P domain channel subunit and a human homologue with a unique pore structure". J. Biol. Chem ...
This open channel, primarily expressed in the pancreas, is activated at alkaline pH. Tandem pore domain potassium channel ... 2001). "Characterization of TASK-4, a novel member of the pH-sensitive, two-pore domain potassium channel family". FEBS Lett. ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. ... Potassium channel subfamily K member 17 is a protein that in humans is encoded by the KCNK17 gene. This gene encodes K2P17.1, ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000169427 - Ensembl, May 2017 "Human PubMed Reference ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. This open channel is ... a novel tandem pore domain acid-sensitive K+ channel. An extracellular histiding as pH sensor". J. Biol. Chem. 275 (22): 16650- ... two pore domain potassium channel". Brain Res. Mol. Brain Res. 82 (1-2): 74-83. doi:10.1016/S0169-328X(00)00183-2. PMID ...
... to distinguish it from outward potassium currents. Inward rectifiers also differ from tandem pore domain potassium channels, ... IRK channels possess a pore domain, homologous to that of voltage-gated ion channels, and flanking transmembrane segments (TMSs ... Inward-rectifier potassium channels (Kir, IRK) are a specific lipid-gated subset of potassium channels. To date, seven ... such as the delayed rectifier and A-type potassium channels. Those more "typical" potassium channels preferentially carry ...
The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak ... Tandem+Pore+Domain+Potassium+Channel at the U.S. National Library of Medicine Medical Subject Headings (MeSH) "Two-P Potassium ... Below is a list of the 15 known two-pore-domain human potassium channels: Ion channel Potassium channel Goldstein SA, Bayliss ... Enyedi P, Czirják G (Apr 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels". Physiological ...
... is a potassium channel containing two pore-forming P domains. Tandem pore domain potassium channel GRCh38: Ensembl release 89: ... "Regulation of two-pore-domain (K2P) potassium leak channels by the tyrosine kinase inhibitor genistein". British Journal of ... "Expression pattern and functional characteristics of two novel splice variants of the two-pore-domain potassium channel TREK-2 ... Bang H, Kim Y, Kim D (June 2000). "TREK-2, a new member of the mechanosensitive tandem-pore K+ channel family". The Journal of ...
K2P13.1 is a potassium channel containing two pore-forming P domains. Tandem pore domain potassium channel GRCh38: Ensembl ... 2008). "Regulation of two-pore-domain (K2P) potassium leak channels by the tyrosine kinase inhibitor genistein". Br. J. ... a novel subfamily of tandem pore domain K+ channels". J. Biol. Chem. 276 (10): 7302-11. doi:10.1074/jbc.M008985200. PMID ... Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain ...
... is a potassium channel containing two pore-forming P domains. Tandem pore domain potassium channel GRCh38: Ensembl release 89: ... 2008). "Regulation of two-pore-domain (K2P) potassium leak channels by the tyrosine kinase inhibitor genistein". Br. J. ... Han J, Kang D, Kim D (2003). "Functional properties of four splice variants of a human pancreatic tandem-pore K+ channel, TALK- ... Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain ...
... is a potassium channel containing two pore-forming P domains. Tandem pore domain potassium channel GRCh38: Ensembl release 89: ... a novel subfamily of tandem pore domain K+ channels". J. Biol. Chem. 276 (10): 7302-11. doi:10.1074/jbc.M008985200. PMID ... Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain ... Potassium channel, subfamily K, member 12, also known as KCNK12 is a human gene. The protein encoded by this gene, K2P12.1, ...
It may require other non-pore-forming proteins for activity. Tandem pore domain potassium channel GRCh38: Ensembl release 89: ... K2P7.1 is a potassium channel containing two pore-forming P domains. Multiple transcript variants encoding different isoforms ... This gene encodes a member of the superfamily of potassium channel proteins containing two pore-forming P domains. The product ... 2001). "Distribution analysis of human two pore domain potassium channels in tissues of the central nervous system and ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000171303 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P3.1 is an ... Ashmole I, Goodwin PA, Stanfield PR (2002). "TASK-5, a novel member of the tandem pore K+ channel family". Pflügers Arch. 442 ( ... Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000186795 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... K2P18.1 is a potassium channel containing two pore-forming P domains. A flaw in this gene could help trigger migraine headaches ... Potassium channel subfamily K member 18 (KCNK18), also known as TWIK-related spinal cord potassium channel (TRESK) or K2P18.1 ... Kang D, Mariash E, Kim D (2004). "Functional expression of TRESK-2, a new member of the tandem-pore K+ channel family". J. Biol ...
... suggests it may play an important role in renal potassium transport. Tandem pore domain potassium channel GRCh38: Ensembl ... 2000). "Volatile anesthetics activate the human tandem pore domain baseline K+ channel KCNK5". Anesthesiology. 92 (6): 1722-30 ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. The message for this ... Morton MJ, O'Connell AD, Sivaprasadarao A, Hunter M (2003). "Determinants of pH sensing in the two-pore domain K(+) channels ...
... and it may require other non-pore-forming proteins for activity. Tandem pore domain potassium channel GRCh38: Ensembl release ... Nicolas MT, Barhanin J, Reyes R, Demêmes D (2004). "Cellular localization of TWIK-1, a two-pore-domain potassium channel in the ... This gene encodes K2P1.1, a member of the superfamily of potassium channel proteins containing two pore-forming P domains. The ... Lesage F, Lazdunski M (2000). "Molecular and functional properties of two-pore-domain potassium channels". Am. J. Physiol. ...
... newer evidence suggests that the tandem pore domain potassium channels KCNK3, KCNK9, and KCNK18 are primarily responsible for ... "Pungent agents from Szechuan peppers excite sensory neurons by inhibiting two-pore potassium channels". Nat. Neurosci. 11 (7): ... Although the compound is an agonist at the pain integration channels TRPV1 and TRPA1 like capsaicin, ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000182450 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... February 2001). "The neuroprotective agent sipatrigine (BW619C89) potently inhibits the human tandem pore-domain K(+) channels ... a lipid-gated ion channel that belongs to the superfamily of potassium channel proteins containing two pore-forming P domains ( ... two pore domain potassium channel". Brain Research. Molecular Brain Research. 82 (1-2): 74-83. doi:10.1016/S0169-328X(00)00183- ...
Tandem pore domain potassium channel - are constitutively open or possess high basal activation, such as the "resting potassium ... These domains include the RCK domains of BK channels, and voltage sensor domains of voltage gated K+ channels. These domains ... see potassium channel blocker and potassium channel opener. Potassium channels have a tetrameric structure in which four ... Potassium channel blockers inhibit the flow of potassium ions through the channel. They either compete with potassium binding ...
... it may require other non-pore-forming proteins for activity. Tandem pore domain potassium channel GRCh38: Ensembl release 89: ... 2002). "Expression pattern in brain of TASK-1, TASK-3, and a tandem pore domain K(+) channel subunit, TASK-5, associated with ... one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P15.1 has not been ... Kim D, Gnatenco C (Jun 2001). "TASK-5, a new member of the tandem-pore K(+) channel family". Biochem Biophys Res Commun. 284 (4 ...
"Volatile anesthetics activate the human tandem pore domain baseline K+ channel KCNK5". Anesthesiology. 92 (6): 1722-30. doi: ... Enyedi P, Czirják G (Apr 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels". Physiological ... A potassium channel opener is a type of drug which facilitates ion transmission through potassium channels. Some examples ... an acid-sensitive two-pore domain potassium channel". Neuropharmacology. 40 (4): 551-9. doi:10.1016/S0028-3908(00)00189-1. PMID ...
Tandem pore domain potassium channel GRCh38: Ensembl release 89: ENSG00000082482 - Ensembl, May 2017 GRCm38: Ensembl release 89 ... a lipid-gated ion channel belonging to the two-pore-domain background potassium channel protein family. This type of potassium ... 2005). "Inhibition of the human two-pore domain potassium channel, TREK-1, by fluoxetine and its metabolite norfluoxetine". Br ... Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (2001). "Potassium leak channels and the KCNK family of two-P-domain ...
TREK-1 and TRAAK which are found in mammalian neurons and are classified as potassium channels in the tandem pore domain class ... K2P channels consist of six subfamilies and contain four transmembrane domains, which form two pores each between domains 1-2 ... There is also a large extracellular linker region between domain 1 and the first pore formed between domains 1-2. TRP channels ... In eukaryotes, two of the best known mechanosensitive ion channels are the potassium channels TREK-1 and TRAAK, both of which ...
Tandem pore domain potassium channel: This family of 15 members form what are known as leak channels, and they display Goldman- ... Two-pore-domain potassium channels', these channels have only one pore but two pore domains per subunit. Two-pore channels ... potassium channels are gated by lipids including the inward-rectifier potassium channels and two pore domain potassium channels ... Inward-rectifier potassium channels Two-pore-domain potassium channels: This family of 15 members form what is known as leak ...
... potassium channels, tandem pore domain MeSH D12.776.543.550.425.750.900 - potassium channels, voltage-gated MeSH D12.776. ... potassium channels, tandem pore domain MeSH D12.776.543.585.400.750.900 - potassium channels, voltage-gated MeSH D12.776. ... shab potassium channels MeSH D12.776.543.550.425.750.900.249 - ether-a-go-go potassium channels MeSH D12.776.543.550.425.750. ... shab potassium channels MeSH D12.776.543.585.400.750.900.249 - ether-a-go-go potassium channels MeSH D12.776.543.585.400.750. ...
... which each have a pore domain. This contrasts with two-pore-domain potassium channels, which confusingly have only one pore and ... TPCs are formed from two transmembrane non-equivalent tandem Shaker-like, pore-forming subunits, dimerized to form quasi- ... with their two pores, dimerise to form a functional channel. "Two P domain potassium channels". Guide to Pharmacology. ... The first site does not affect the channel. Site 2, composed of residues in VSD2 and the pore domain, inhibits the channel by ...
... potassium channels, tandem pore domain MeSH D12.776.157.530.400.600.900 - potassium channels, voltage-gated MeSH D12.776. ... shab potassium channels MeSH D12.776.157.530.400.600.900.249 - ether-a-go-go potassium channels MeSH D12.776.157.530.400.600. ... kcnq potassium channels MeSH D12.776.157.530.400.600.900.124.249.500 - kcnq1 potassium channel MeSH D12.776.157.530.400.600. ... 900.124.249.750 - kcnq2 potassium channel MeSH D12.776.157.530.400.600.900.124.249.875 - kcnq3 potassium channel MeSH D12.776. ...
"Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2". J. ... "A mechanism for ATP-sensitive potassium channel diversity: Functional coassembly of two pore-forming subunits". Proc. Natl. ... 2001). "The properties of the Kir6.1-6.2 tandem channel co-expressed with SUR2A". Pflügers Arch. 440 (5): 692-698. doi:10.1007/ ... Potassium inwardly-rectifying channel, subfamily J, member 8, also known as KCNJ8, is a human gene encoding the Kir6.1 protein ...
TRPM7 TRPM8 TRPML TRPN TRPP TRPP3 TRPV TRPV1 TRPV2 TRPV3 TRPV4 TRPV5 TRPV6 Talin protein Tandem pore domain potassium channel ... Voltage-gated ion channel Voltage-gated potassium channel Voltage-gated potassium channel database Voltage-gated proton channel ... potassium channel Calcium-activated potassium channel subunit alpha-1 Calcium 2-aminoethylphosphate Calcium channel Canadian ... channel alpha 1 Cyclic nucleotide-gated channel alpha 2 Cyclic nucleotide-gated channel alpha 3 Cyclic nucleotide-gated channel ...
A number of potassium channel structures have been solved including voltage gated, ligand gated, tandem-pore, and inwardly ... Miller AN, Long SB (January 2012). "Crystal structure of the human two-pore domain potassium channel K2P1". Science. 335 (6067 ... The balance between potassium and sodium is maintained by ion transporters in the cell membrane. All potassium ion channels are ... 20 mEq (781 mg) potassium from potassium gluconate (4680 mg), or potassium citrate (2040 mg), mixed a half-cup (1.12 dL) water ...
  • however, it may require other non-pore-forming proteins for activity. (antibodiesinc.com)
  • There is increasing evidence that direct interactions between volatile anesthetics and channel proteins may result in general anesthesia. (silverchair.com)
  • Recent evidence is in favor of direct interactions between volatile anesthetics and channel proteins as the underlying mechanism of general anesthesia. (silverchair.com)
  • These proteins act as channels and allow ions to move across cell membranes. (elifesciences.org)
  • Component of the postsynaptic hippocampal AMPA-type glutamate receptor (AMPAR) complex, at least composed of pore forming AMPAR subunits GRIA1, GRIA2 and GRIA3 and AMPAR auxiliary proteins SHISA6 and SHISA7. (icr.ac.uk)
  • These findings suggest that while channel proteins found in sperm cells from different species look similar and serve similar roles, they are activated in ways that can be very different. (elifesciences.org)
  • Examples of voltage-gated channel blockers include: Linopirdine XE-991 Spooky toxin (SsTx) Potassium channel Potassium channel opener Amiodarone also blocks CACNA2D2-containing voltage gated calcium channels works by selectively blocking the rapid component of the delayed rectifier outward potassium current (IKr) blocks potassium channels of the hERG-type Primarily inhibits outward voltage-gated Kv2.1 potassium channel currents. (wikipedia.org)
  • Although both ketamine and halothane inhibit potassium currents through the Kv2.1 channel, their mechanisms of action at this potential target may be different. (silverchair.com)
  • Apamin-sensitive calcium-activated potassium currents in rabbit ventricles with chronic myocardial infarction. (harvard.edu)
  • Cerebellar ataxia by enhanced Ca(V)2.1 currents is alleviated by Ca2+-dependent K+-channel activators in Cacna1a(S218L) mutant mice. (harvard.edu)
  • In neurons, TASK channels carrying hyperpolarizing K + leak currents, and the pacemaker channel HCN2, carrying depolarizing I h , stabilize the membrane potential by a mutual functional interaction. (biomedcentral.com)
  • May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. (icr.ac.uk)
  • Inwardly rectifying potassium (Kir) channels open at the 'helix bundle crossing' (HBC), formed by the M2 helices at the cytoplasmic end of the transmembrane pore. (nature.com)
  • Potassium two pore domain channel subfamily K member 12 is encoded by the gene KCNK12. (antibodiesinc.com)
  • Different from all other Kvalpha subunits, Kv1.4 harbors two inactivation domains at its N terminus. (uni-regensburg.de)
  • At least eight major groups of K channels exist and they are made up of dozens of different subunits. (ucdenver.edu)
  • brush resides in a cluster of redundant CNGCs encoding subunits which resemble metazoan voltage-gated potassium (Kv1-Kv4) channels in assembly and gating properties. (elifesciences.org)
  • The results reveal a mechanism by which quantitative competition between channel subunits for tetramer assembly can impact the phenotype of the mutation carrier. (elifesciences.org)
  • Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. (icr.ac.uk)
  • Functional analysis suggests that only ID1 may work as a pore-occluding ball domain, whereas ID2 most likely acts as a "docking domain" that attaches ID1 to the cytoplasmic face of the channel. (uni-regensburg.de)
  • Kir channels consist of only two transmembrane helices plus an extensive C-terminal cytoplasmic tail of the channel pore. (nature.com)
  • Our data suggest that pore vestibule structure is an important determinant of NaChBac inactivation, whereas the inactivation mechanism is independent of the number of free cytoplasmic N- and C-termini in the functional channel. (nyu.edu)
  • In interphase they organize the nucleo-cytoplasmic transportation, and during mitosis they get spindle set up in metaphase and nuclear envelope and nuclear pore complicated set up in telophase (Clarke and Zhang, 2008). (researchensemble.com)
  • Effects of calcium-activated potassium channel modulators on afterhyperpolarizing potentials in identified motor and mechanosensory neurons of the medicinal leech. (harvard.edu)
  • Proinflammatory mediators as modulators of decidual calcium channel expression and function. (nottingham.ac.uk)
  • This work is enabled in part through the advent of small molecule modulators of channel function. (stanford.edu)
  • Small molecule toxins serve as lead compounds for the design of isoform-selective channel modulators, affinity reagents, and fluorescence imaging probes. (stanford.edu)
  • Use dependence of ketamine and halothane action was observed in both Kv2.1 and the mutant channel, attributable to augmentation of C-type inactivation. (silverchair.com)
  • Cell membrane glycoproteins that are selectively permeable to potassium ions. (ucdenver.edu)
  • Further experiments found that the channel formed by the mutated CNGC protein is leaky and allows calcium ions to enter the cell in the absence of any cue from the environment. (elifesciences.org)
  • Introduced negative charges at the HBC (G178D) in Kir2.2 channels forces opening, allowing pore wetting and free movement of permeant ions between the cytoplasm and the inner cavity. (nature.com)
  • This channel is activated by signalling molecules inside cells, called 'cyclic nucleotides', and its activity ultimately leads to calcium ions flowing into the sperm cell's tail. (elifesciences.org)
  • In former studies the expression of two different two-pore domain potassium (K 2P ) channels (TASK1, TREK1) were shown to ameliorate neuronal damage due to cerebral ischemia. (biomedcentral.com)
  • Here, we hypothesized that the absence of HCN2, an important functional counter player of TASK channels, affects neuronal survival during stroke-induced tissue damage. (biomedcentral.com)
  • Case Report on: Very Early Afterdepolarizations in HiPSC-Cardiomyocytes-An Artifact by Big Conductance Calcium Activated Potassium Current (Ibk,Ca). Cells. (harvard.edu)
  • Effects of exogenous hydrogen sulphide on calcium signalling, background (TASK) K channel activity and mitochondrial function in chemoreceptor cells. (ox.ac.uk)
  • It is concluded that H(2)S excites type 1 cells through the inhibition of background (TASK) potassium channels leading to membrane depolarisation and voltage-gated Ca(2+) entry. (ox.ac.uk)
  • Potassium channels are present in all types of cells and play critical roles in control of multiple physiological processes. (nature.com)
  • In 2009, researchers identified a potassium ion channel, called CNGK, that starts the electrical signal in the sperm cells of sea urchins. (elifesciences.org)
  • including some of the researchers involved in the 2009 work - now report that the CNGK channel also exists in the sperm cells of a freshwater fish, the zebrafish. (elifesciences.org)
  • Unexpectedly, the CNGK channel is located in the heads of this fish's sperm cells rather than in the tails. (elifesciences.org)
  • Access to toxins and modified forms thereof (including saxitoxin, gonyautoxin, batrachotoxin, and veratridine) through de novo synthesis drives studies to elucidate toxin-receptor interactions and to develop new pharmacologic tools to study ion channel function in primary cells and murine pain models. (stanford.edu)
  • Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, whereas ID2 (residues 40-50) is a 2.5-turn helix made up of small hydrophobic amino acids. (uni-regensburg.de)
  • Molecular dynamics simulations show how protonation of Kir2.2[G178D], or the D173 pore-lining residues, changes solvation, K + ion occupancy, and K + conductance. (nature.com)
  • Activation and inactivation parameters for four different covalently linked tandem dimer or tandem tetramer constructs were indistinguishable from those of the wild-type channel. (nyu.edu)
  • Potassium channel blockers used in the treatment of cardiac arrhythmia are classified as class III antiarrhythmic agents. (wikipedia.org)
  • Sodium leak through K2P potassium channels and cardiac arrhythmia, an emerging theme. (uchicago.edu)
  • The syndrome is caused by changes in the structure and function of certain cardiac ion channels and reduced expression of Connexin 43 (Cx43) in the Right Ventricle (RV), predominantly in the Right Ventricular Outflow Tract (VSVD), causing electromechanical abnormalities. (bvsalud.org)
  • Potassium channels whose activation is dependent on intracellular calcium concentrations. (harvard.edu)
  • Direct and indirect activation of the adenosine triphosphate-sensitive potassium channel to induce spinal cord ischemic metabolic tolerance. (ucdenver.edu)
  • A picture is emerging of sperm channel orthologues that employ different activation mechanisms and serve different functions. (elifesciences.org)
  • It is assumed that this ionic interplay between TASK and HCN2 channels enhances the resistance of neurons to insults accompanied by extracellular pH shifts. (biomedcentral.com)
  • For thalamocortical relay neurons, it could be demonstrated that two ion channels, which are predominantly active at rest, strongly influence the resting membrane potential. (biomedcentral.com)
  • Kotler O, Khrapunsky Y, Shvartsman A, Dai H, Plant LD, Goldstein SAN , Fleidervish I. SUMOylation of NaV1.2 channels regulates the velocity of backpropagating action potentials in cortical pyramidal neurons. (uchicago.edu)
  • Reverse use dependence is relevant for potassium channel blockers used as class III antiarrhythmics. (wikipedia.org)
  • Kinetics and voltage dependence of inactivation of a prokaryotic voltage-gated sodium channel (NaChBac) were investigated in an effort to understand its molecular mechanism. (nyu.edu)
  • Thereby, the acidified milieu after arterial occlusion most probably influences the activity of acid-sensing ion channels as well as the cell membrane potential. (biomedcentral.com)
  • Class III agents predominantly block the potassium channels, thereby prolonging repolarization. (wikipedia.org)
  • Potassium channel blockers exhibit reverse use-dependent prolongation of the action potential duration. (wikipedia.org)
  • Rapid State-Dependent Alteration in Kv3 Channel Availability Drives Flexible Synaptic Signaling Dependent on Somatic Subthreshold Depolarization. (ucdenver.edu)
  • Single-channel recordings reveal striking, pH-dependent, subconductance behaviors in G178D (or G178E and equivalent Kir2.1[G177E]) mutant channels, with well-resolved non-cooperative subconductance levels. (nature.com)
  • Cumulative inactivation of voltage-gated (Kv) K(+) channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. (uni-regensburg.de)
  • Kv1.4 channels exhibit rapid "ball-and-chain"-type inactivation gating. (uni-regensburg.de)
  • Here we report the solution structure and function of this "tandem inactivation domain" using NMR spectroscopy and patch clamp recordings. (uni-regensburg.de)
  • Together, the concerted action of ID1 and ID2 may promote rapid inactivation of Kv1.4 that is crucial for the channel function in short term plasticity. (uni-regensburg.de)
  • Halothane accelerated the time constant of current inactivation, whereas ketamine affected this parameter minimally in both channel types. (silverchair.com)
  • Point mutations in the outer part of the pore revealed an important influence of the S195 residue on the process of inactivation. (nyu.edu)
  • For two mutants (S195D and S195E), the maximal and minimal rates of inactivation observed were increased by ∼2.5-fold, and the midpoint of the steady-state inactivation curve was shifted ∼20 mV in the hyperpolarizing direction, compared to the wild-type channel. (nyu.edu)
  • In these respects, NaChBac inactivation resembles C-type or slow inactivation modes observed in other voltage-gated K and Na channels. (nyu.edu)
  • Effects of a potassium channel opener on brain injury and neurologic outcomes in an animal model of neonatal hypoxic-ischemic injury. (ucdenver.edu)
  • Dalfampridine, A potassium channel blocker has also been approved for use in the treatment of multiple sclerosis. (wikipedia.org)
  • Ca(2+)-activated K(+) channel-3.1 blocker TRAM-34 attenuates airway remodeling and eosinophilia in a murine asthma model. (harvard.edu)
  • Screen Quest™ assay kits, a set of HTS-ready tools for high throughput screening of biochemical and cellular targets such as protein kinases, proteases, HDAC, cell apoptosis and cytoxicity, GPCR, ion channels, ADME/metabolism and transporters. (stratech.co.uk)
  • Cyclic nucleotide-gated channel (CNGC) family members mediate Ca 2+ influx from cellular stores in plants (Charpentier et al. (elifesciences.org)
  • In sea urchin sperm, a cyclic nucleotide-gated K + channel (CNGK) mediates a cGMP-induced hyperpolarization that evokes Ca 2+ influx. (elifesciences.org)
  • Since these agents do not affect the sodium channel, conduction velocity is not decreased. (wikipedia.org)
  • This graph shows the total number of publications written about "Potassium Channels, Calcium-Activated" by people in Harvard Catalyst Profiles by year, and whether "Potassium Channels, Calcium-Activated" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Potassium Channels, Calcium-Activated" by people in Profiles. (harvard.edu)
  • Below are the most recent publications written about "Potassium Channels" by people in Profiles. (ucdenver.edu)
  • TASK-1 channels are sensitive to a wide array of physiological and pharmacological mediators that affect their activity such as unsaturated fatty acids, extracellular pH, hypoxia, anaesthetics and intracellular signalling pathways. (ersjournals.com)
  • TWIK-related acid-sensitive potassium channel 1 (TASK-1 encoded by KCNK3) belongs to the family of two-pore domain potassium channels. (ersjournals.com)
  • Recent studies show that modulation of TASK-1 channels, either directly or indirectly by targeting their regulatory mechanisms, has the potential to control pulmonary arterial tone in humans. (ersjournals.com)
  • This review summarises our current state of knowledge of the functional role of TASK-1 channels in the pulmonary circulation in health and disease, with special emphasis on current advancements in the field. (ersjournals.com)
  • The Du Bois lab is interested in understanding the biochemical mechanisms that underlie channel subtype regulation and how such processes may be altered following nerve injury. (stanford.edu)
  • H(2)S inhibited background K(+) current in whole cell perforated patch and reduced background K(+) channel activity in cell-attached patch recordings. (ox.ac.uk)
  • this means that at higher heart rates, when there is increased involvement of the slow K channels, dofetilide has less of an action potential-prolonging effect. (wikipedia.org)
  • A second area of interest focuses on the role of ion channels in electrical conduction and the specific involvement of channel subtypes in the sensation of pain. (stanford.edu)
  • Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression. (icr.ac.uk)
  • We reported the crystal structure of a chicken Kir2.2[G178D] mutant channel 12 , in which the introduced G178D mutations at the HBC functionally stabilize the open conformation, a strategy used previously to obtain an open crystal structure of a bacterial homolog KirBac3.1 13 . (nature.com)
  • Pathway analysis of genes with PFisher's-combined ≤ 1 × 10-3 suggested several pathways, foremost neural-related pathways of signalling and ion channel regulation, to be involved in migraine and MDD aetiology. (ox.ac.uk)
  • Using voltage-clamp techniques, the authors examined the effect of two general anesthetics (ketamine and halothane) on a rat brain potassium channel of known amino acid sequence, and further assessed whether the inhibition of the channel is altered by a partial deletion of the C-terminal sequence of this channel. (silverchair.com)
  • These data indicate that the effects of H(2)S on background K channels are a consequence of inhibition of oxidative phosphorylation. (ox.ac.uk)
  • Potassium Channels, Calcium-Activated" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • Potassium Channels" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (ucdenver.edu)
  • 2007). Here, we report the unusual genetic behavior of a quantitative gain-of-function CNGC mutation ( brush ) in Lotus japonicus resulting in a leaky tetrameric channel. (elifesciences.org)
  • In the present study, we carry out detailed single-channel analyses of cKir2.2[G178D] and hKir2.1[G177E] channels that reveal striking sub-state gating behavior. (nature.com)
  • Mutations in K + channel sequences can lead to a variety of clinical disorders exemplifying their physiological importance [ 3 ]. (ersjournals.com)
  • This implicates expansion of the HBC as a critical step in Kir channel opening, as seen in a recent Kir6.2 structure 11 . (nature.com)
  • In the G178D structure, the HBC gate is slightly wider than in previous structures, and molecular dynamics (MD) simulations demonstrate rapid wetting of the G178D pore at the HBC region, followed by further expansion and K + conductance through the channel. (nature.com)
  • In a second program area, the Du Bois group is exploring voltage-gated ion channel structure and function using the tools of chemistry in combination with those of molecular biology, electrophysiology, microscopy and mass spectrometry. (stanford.edu)
  • In recent years, we have begun exploring the role ion channels play in the aetiology of ovarian cancer. (nottingham.ac.uk)
  • These findings provide important insights into the function of CNGCs and reveal how a small change in a channel protein can have far reaching effects on an organism. (elifesciences.org)
  • Ion Channels as Therapeutic Targets in High Grade Gliomas Cancers. (nottingham.ac.uk)
  • A role for two-pore potassium (K2P) channels in endometrial epithelial function Journal of Cellular and Molecular Medicine. (nottingham.ac.uk)
  • KCNK12 is a member of the two pore domain potassium channel (TC 1.A.1.8) family. (antibodiesinc.com)
  • External K+ modulates the activity of the Arabidopsis potassium channel SKOR via an unusual mechanism. (mpg.de)
  • Cyanide inhibited background K channels to a similar extent to H(2)S and prevented H(2)S exerting any further influence over channel activity. (ox.ac.uk)
  • Distinct roles of the last transmembrane domain in controlling Arabidopsis K+ channel activity. (mpg.de)
  • Assembly of plant Shaker-like K-out channels requires two distinct sites of the channel alpha-subunit. (mpg.de)
  • Ischemia-induced cell depolarization: does the hyperpolarization-activated cation channel HCN2 affect the outcome after stroke in mice? (biomedcentral.com)

No images available that match "potassium channels tandem pore domain"