Barium permanganate (T3D1119)
| Record Information | |||||||||||||||||||||||||||||||||||||||||||||||||
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| Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Creation Date | 2009-06-19 21:58:20 UTC | ||||||||||||||||||||||||||||||||||||||||||||||||
| Update Date | 2014-12-24 20:23:10 UTC | ||||||||||||||||||||||||||||||||||||||||||||||||
| Accession Number | T3D1119 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Identification | |||||||||||||||||||||||||||||||||||||||||||||||||
| Common Name | Barium permanganate | ||||||||||||||||||||||||||||||||||||||||||||||||
| Class | Small Molecule | ||||||||||||||||||||||||||||||||||||||||||||||||
| Description | Barium permanganate is a chemical compound of barium and manganese. Barium is a metallic alkaline earth metal with the symbol Ba, and atomic number 56. It never occurs in nature in its pure form due to its reactivity with air, but combines with other chemicals such as sulfur or carbon and oxygen to form barium compounds that may be found as minerals. Manganese is a naturally occurring metal with the symbol Mn and the atomic number 25. It does not occur naturally in its pure form, but is found in many types of rocks in combination with other substances such as oxygen, sulfur, or chlorine. Manganese occurs naturally in most foods and small amounts are needed to stay healthy, as manganese ions act as cofactors for a number of enzymes. (4, 5, 3) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Compound Type |
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| Chemical Structure |  | ||||||||||||||||||||||||||||||||||||||||||||||||
| Synonyms |
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| Chemical Formula | BaMn2O8 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Average Molecular Mass | 375.198 g/mol | ||||||||||||||||||||||||||||||||||||||||||||||||
| Monoisotopic Mass | 375.741 g/mol | ||||||||||||||||||||||||||||||||||||||||||||||||
| CAS Registry Number | 7787-36-2 | ||||||||||||||||||||||||||||||||||||||||||||||||
| IUPAC Name | hexaoxo-2,4-dioxa-1,5-dimangana-3-barapentane | ||||||||||||||||||||||||||||||||||||||||||||||||
| Traditional Name | hexaoxo-2,4-dioxa-1,5-dimangana-3-barapentane | ||||||||||||||||||||||||||||||||||||||||||||||||
| SMILES | O=[Mn](=O)(=O)O[Ba]O[Mn](=O)(=O)=O | ||||||||||||||||||||||||||||||||||||||||||||||||
| InChI Identifier | InChI=1S/Ba.2Mn.8O | ||||||||||||||||||||||||||||||||||||||||||||||||
| InChI Key | InChIKey=OEXINXUPPPQPLY-UHFFFAOYSA-N | ||||||||||||||||||||||||||||||||||||||||||||||||
| Chemical Taxonomy | |||||||||||||||||||||||||||||||||||||||||||||||||
| Description | belongs to the class of inorganic compounds known as alkaline earth metal permanganates. These are inorganic compounds in which the largest oxoanion is permanganate, and in which the heaviest atom not in an oxoanion is an alkaline earth metal. | ||||||||||||||||||||||||||||||||||||||||||||||||
| Kingdom | Inorganic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
| Super Class | Mixed metal/non-metal compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
| Class | Alkaline earth metal oxoanionic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
| Sub Class | Alkaline earth metal permanganates | ||||||||||||||||||||||||||||||||||||||||||||||||
| Direct Parent | Alkaline earth metal permanganates | ||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative Parents | |||||||||||||||||||||||||||||||||||||||||||||||||
| Substituents |
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| Molecular Framework | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| External Descriptors | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Biological Properties | |||||||||||||||||||||||||||||||||||||||||||||||||
| Status | Detected and Not Quantified | ||||||||||||||||||||||||||||||||||||||||||||||||
| Origin | Exogenous | ||||||||||||||||||||||||||||||||||||||||||||||||
| Cellular Locations |
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| Biofluid Locations | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Tissue Locations | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Pathways | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Applications | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Biological Roles | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Chemical Roles | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||
| State | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||
| Appearance | Purple crystals. | ||||||||||||||||||||||||||||||||||||||||||||||||
| Experimental Properties |
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| Predicted Properties |
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| Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||
| Spectra |
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| Toxicity Profile | |||||||||||||||||||||||||||||||||||||||||||||||||
| Route of Exposure | Oral (3) ; inhalation (3) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Mechanism of Toxicity | Barium is a competitive potassium channel antagonist that blocks the passive efflux of intracellular potassium, resulting in a shift of potassium from extracellular to intracellular compartments. The intracellular translocation of potassium results in a decreased resting membrane potential, making the muscle fibers electrically unexcitable and causing paralysis. Some of these barium's effects may also be due to barium induced neuromuscular blockade and membrane depolarization. Manganese is a cellular toxicant that can impair transport systems, enzyme activities, and receptor functions. It primarily targets the central nervous system, particularily the globus pallidus of the basal ganglia. It is believed that the manganese ion, Mn(II), enhances the autoxidation or turnover of various intracellular catecholamines, leading to increased production of free radicals, reactive oxygen species, and other cytotoxic metabolites, along with a depletion of cellular antioxidant defense mechanisms, leading to oxidative damage and selective destruction of dopaminergic neurons. In addition to dopamine, manganese is thought to perturbations other neurotransmitters, such as GABA and glutamate. In order to produce oxidative damage, manganese must first overwhelm the antioxidant enzyme manganese superoxide dismutase. The neurotoxicity of Mn(II) has also been linked to its ability to substitute for Ca(II) under physiological conditions. It can enter mitochondria via the calcium uniporter and inhibit mitochondrial oxidative phosphorylation. It may also inhibit the efflux of Ca(II), which can result in a loss of mitochondrial membrane integrity. Mn(II) has been shown to inhibit mitochondrial aconitase activity to a significant level, altering amino acid metabolism and cellular iron homeostasis. (4, 3) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Metabolism | Barium compounds are absorbed via ingestion and inhalation, the extent of which depends on the individual compound. In the body, the majority of the barium is found in the bone, while small amounts exists in the muscle, adipose, skin, and connective tissue. Barium is not metabolized in the body, but it may be transported or incorporated into complexes or tissues. Barium is excreted in the urine and faeces. Manganese is absorbed mainly via ingestion, but can also be inhaled. It binds to alpha-2-macroglobulin, albumin, or transferrin in the plasma and is distributed to the brain and all other mammalian tissues, though it tends to accumulate more in the liver, pancreas, and kidney. Manganese is capable of existing in a number of oxidation states and is believed to undergo changes in oxidation state within the body. Manganese oxidation state can influence tissue toxicokinetic behavior, and possibly toxicity. Manganese is excreted primarily in the faeces. (3, 4) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Toxicity Values | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Lethal Dose | 1 to 15 grams for an adult human (barium salts). (1) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Carcinogenicity (IARC Classification) | No indication of carcinogenicity to humans (not listed by IARC). | ||||||||||||||||||||||||||||||||||||||||||||||||
| Uses/Sources | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Minimum Risk Level | Intermediate Oral: 0.2 mg/kg/day (Barium)(2) Chronic Oral: 0.2 mg/kg/day (Barium) (2) Chronic Inhalation: 0.0003 mg/m3 (Manganese) (2) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Health Effects | The health effects of the different barium compounds depend on how well the compound dissolves in water or the stomach contents. At low doses, barium acts as a muscle stimulant, while higher doses affect the nervous system, causing cardiac irregularities, tremors, weakness, anxiety, dyspnea, paralysisand possibly death. Barium may also cause gastrointestinal disturbances, damage the kidneys and cause decreases in body weight. Manganese mainly affects the nervous system and may cause behavioral changes and other nervous system effects, which include movements that may become slow and clumsy. This combination of symptoms when sufficiently severe is referred to as | ||||||||||||||||||||||||||||||||||||||||||||||||
| Symptoms | Ingesting excess barium may cause vomiting, abdominal cramps, diarrhea, difficulties in breathing, increased or decreased blood pressure, numbness around the face, and muscle weakness. High levels may result in changes in heart rhythm or paralysis and possibly death. Manganese mainly affects the nervous system and may cause behavioral changes and other nervous system effects, which include movements that may become slow and clumsy. This combination of symptoms when sufficiently severe is referred to as | ||||||||||||||||||||||||||||||||||||||||||||||||
| Treatment | Intravenous infusion of potassium often relieves many of the symptoms of barium toxicity. (3) | ||||||||||||||||||||||||||||||||||||||||||||||||
| Normal Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||
| Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||
| Abnormal Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||
| Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||
| External Links | |||||||||||||||||||||||||||||||||||||||||||||||||
| DrugBank ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| HMDB ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| PubChem Compound ID | 24587 | ||||||||||||||||||||||||||||||||||||||||||||||||
| ChEMBL ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| ChemSpider ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| KEGG ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| UniProt ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| OMIM ID | |||||||||||||||||||||||||||||||||||||||||||||||||
| ChEBI ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| BioCyc ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| CTD ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Stitch ID | Barium permanganate | ||||||||||||||||||||||||||||||||||||||||||||||||
| PDB ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| ACToR ID | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Wikipedia Link | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| References | |||||||||||||||||||||||||||||||||||||||||||||||||
| Synthesis Reference | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| MSDS | T3D1119.pdf | ||||||||||||||||||||||||||||||||||||||||||||||||
| General References |
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| Gene Regulation | |||||||||||||||||||||||||||||||||||||||||||||||||
| Up-Regulated Genes | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
| Down-Regulated Genes | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
Targets
- General Function:
- Phosphatidylinositol-4,5-bisphosphate binding
- Specific Function:
- In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
- Gene Name:
- KCNJ1
- Uniprot ID:
- P48048
- Molecular Weight:
- 44794.6 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Voltage-gated potassium channel activity
- Specific Function:
- This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
- Gene Name:
- KCNJ11
- Uniprot ID:
- Q14654
- Molecular Weight:
- 43540.375 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Inward rectifier potassium channel activity
- Specific Function:
- Inward rectifying potassium channel that is activated by phosphatidylinositol 4,5-bisphosphate and that probably participates in controlling the resting membrane potential in electrically excitable cells. Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
- Gene Name:
- KCNJ12
- Uniprot ID:
- Q14500
- Molecular Weight:
- 49000.6 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Inward rectifier potassium channel activity
- Specific Function:
- This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity).
- Gene Name:
- KCNJ8
- Uniprot ID:
- Q15842
- Molecular Weight:
- 47967.455 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
5. ATP-sensitive potassium channel (Protein Group)
- General Function:
- Phosphatidylinositol-4,5-bisphosphate binding
- Specific Function:
- In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
- Included Proteins:
- P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
6. ATP-sensitive potassium channel (Protein Group)
- General Function:
- Phosphatidylinositol-4,5-bisphosphate binding
- Specific Function:
- In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
- Included Proteins:
- P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
7. ATP-sensitive potassium channel (Protein Group)
- General Function:
- Phosphatidylinositol-4,5-bisphosphate binding
- Specific Function:
- In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
- Included Proteins:
- P48048 , P78508 , Q14654 , Q14500 , Q9UNX9 , Q99712 , Q15842
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Iron ion binding
- Specific Function:
- Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
- Gene Name:
- ACO2
- Uniprot ID:
- Q99798
- Molecular Weight:
- 85424.745 Da
References
- Crooks DR, Ghosh MC, Braun-Sommargren M, Rouault TA, Smith DR: Manganese targets m-aconitase and activates iron regulatory protein 2 in AF5 GABAergic cells. J Neurosci Res. 2007 Jun;85(8):1797-809. [17469137 ]
- General Function:
- Titin binding
- Specific Function:
- Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis.
- Gene Name:
- CALM1
- Uniprot ID:
- P0DP23
- Molecular Weight:
- 16837.47 Da
References
- Kursula P, Majava V: A structural insight into lead neurotoxicity and calmodulin activation by heavy metals. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt 8):653-6. Epub 2007 Jul 28. [17671360 ]
- General Function:
- Rna binding
- Specific Function:
- Iron sensor. Binds a 4Fe-4S cluster and functions as aconitase when cellular iron levels are high. Functions as mRNA binding protein that regulates uptake, sequestration and utilization of iron when cellular iron levels are low. Binds to iron-responsive elements (IRES) in target mRNA species when iron levels are low. Binding of a 4Fe-4S cluster precludes RNA binding.Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
- Gene Name:
- ACO1
- Uniprot ID:
- P21399
- Molecular Weight:
- 98398.14 Da
References
- Crooks DR, Ghosh MC, Braun-Sommargren M, Rouault TA, Smith DR: Manganese targets m-aconitase and activates iron regulatory protein 2 in AF5 GABAergic cells. J Neurosci Res. 2007 Jun;85(8):1797-809. [17469137 ]
- General Function:
- G-protein activated inward rectifier potassium channel activity
- Specific Function:
- This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
- Gene Name:
- KCNJ3
- Uniprot ID:
- P48549
- Molecular Weight:
- 56602.84 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Inward rectifier potassium channel activity
- Specific Function:
- This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
- Gene Name:
- KCNJ6
- Uniprot ID:
- P48051
- Molecular Weight:
- 48450.96 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- G-protein activated inward rectifier potassium channel activity
- Specific Function:
- This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity).
- Gene Name:
- KCNJ9
- Uniprot ID:
- Q92806
- Molecular Weight:
- 44019.45 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- G-protein activated inward rectifier potassium channel activity
- Specific Function:
- This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium.
- Gene Name:
- KCNJ5
- Uniprot ID:
- P48544
- Molecular Weight:
- 47667.3 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Inward rectifier potassium channel activity
- Specific Function:
- Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
- Gene Name:
- KCNJ13
- Uniprot ID:
- O60928
- Molecular Weight:
- 40529.195 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Inward rectifier potassium channel activity
- Specific Function:
- Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance.
- Gene Name:
- KCNJ16
- Uniprot ID:
- Q9NPI9
- Molecular Weight:
- 47948.585 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization
- Specific Function:
- Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium or cesium.
- Gene Name:
- KCNJ2
- Uniprot ID:
- P63252
- Molecular Weight:
- 48287.82 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Pdz domain binding
- Specific Function:
- Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity).
- Gene Name:
- KCNJ4
- Uniprot ID:
- P48050
- Molecular Weight:
- 49499.61 Da
References
- Alagem N, Dvir M, Reuveny E: Mechanism of Ba(2+) block of a mouse inwardly rectifying K+ channel: differential contribution by two discrete residues. J Physiol. 2001 Jul 15;534(Pt. 2):381-93. [11454958 ]
- General Function:
- Translation repressor activity
- Specific Function:
- RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
- Gene Name:
- IREB2
- Uniprot ID:
- P48200
- Molecular Weight:
- 105043.65 Da
References
- Crooks DR, Ghosh MC, Braun-Sommargren M, Rouault TA, Smith DR: Manganese targets m-aconitase and activates iron regulatory protein 2 in AF5 GABAergic cells. J Neurosci Res. 2007 Jun;85(8):1797-809. [17469137 ]
- General Function:
- Tubulin binding
- Specific Function:
- Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (PubMed:12732622, PubMed:19936054, PubMed:20564047). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
- Gene Name:
- PRNP
- Uniprot ID:
- P04156
- Molecular Weight:
- 27661.21 Da
References
- Brazier MW, Davies P, Player E, Marken F, Viles JH, Brown DR: Manganese binding to the prion protein. J Biol Chem. 2008 May 9;283(19):12831-9. doi: 10.1074/jbc.M709820200. Epub 2008 Mar 10. [18332141 ]
- General Function:
- Voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization
- Specific Function:
- Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity) (PubMed:10646604). Associates with KCNE beta subunits that modulates current kinetics (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505, PubMed:19687231). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity) (PubMed:9312006, PubMed:9108097, PubMed:8900283, PubMed:10646604, PubMed:11101505). Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (PubMed:10713961). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (PubMed:10646604). This interaction with KCNE3 is reduced by 17beta-estradiol, resulting in the reduction of currents (By similarity). During conditions of increased substrate load, maintains the driving force for proximal tubular and intestinal sodium ions absorption, gastric acid secretion, and cAMP-induced jejunal chloride ions secretion (By similarity). Allows the provision of potassium ions to the luminal membrane of the secretory canaliculus in the resting state as well as during stimulated acid secretion (By similarity). When associated with KCNE2, forms an heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (PubMed:11101505). When associated with KCNE4, inhibits voltage-gated potassium channel activity (PubMed:19687231). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (PubMed:12324418). Also forms an heterotetramer with KCNQ5; has a voltage-gated potassium channel activity (PubMed:24855057). Binds with phosphatidylinositol 4,5-bisphosphate (PubMed:25037568).Isoform 2: Non-functional alone but modulatory when coexpressed with the full-length isoform 1.
- Gene Name:
- KCNQ1
- Uniprot ID:
- P51787
- Molecular Weight:
- 74697.925 Da
References
- Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
- General Function:
- Voltage-gated potassium channel activity
- Specific Function:
- Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine. Muscarinic agonist oxotremorine-M strongly suppress KCNQ2/KCNQ3 current in cells in which cloned KCNQ2/KCNQ3 channels were coexpressed with M1 muscarinic receptors.
- Gene Name:
- KCNQ2
- Uniprot ID:
- O43526
- Molecular Weight:
- 95846.575 Da
References
- Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
- General Function:
- Voltage-gated potassium channel activity
- Specific Function:
- Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs.
- Gene Name:
- KCNQ3
- Uniprot ID:
- O43525
- Molecular Weight:
- 96741.515 Da
References
- Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
- General Function:
- Potassium channel activity
- Specific Function:
- Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors.
- Gene Name:
- KCNQ4
- Uniprot ID:
- P56696
- Molecular Weight:
- 77099.99 Da
References
- Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
- General Function:
- Voltage-gated potassium channel activity
- Specific Function:
- Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. Muscarine suppresses KCNQ5 current in Xenopus oocytes in which cloned KCNQ5 channels were coexpressed with M(1) muscarinic receptors.
- Gene Name:
- KCNQ5
- Uniprot ID:
- Q9NR82
- Molecular Weight:
- 102178.015 Da
References
- Gibor G, Yakubovich D, Peretz A, Attali B: External barium affects the gating of KCNQ1 potassium channels and produces a pore block via two discrete sites. J Gen Physiol. 2004 Jul;124(1):83-102. [15226366 ]
- General Function:
- Not Available
- Specific Function:
- Not Available
- Gene Name:
- PRNT
- Uniprot ID:
- Q86SH4
- Molecular Weight:
- 10755.655 Da
References
- Brazier MW, Davies P, Player E, Marken F, Viles JH, Brown DR: Manganese binding to the prion protein. J Biol Chem. 2008 May 9;283(19):12831-9. doi: 10.1074/jbc.M709820200. Epub 2008 Mar 10. [18332141 ]