Voltage-Dependent Anion Channel 1
Voltage-Dependent Anion Channels
Anions
Ion Channels
Ion Channel Gating
Calcium Channels
Membrane Potentials
Each mammalian mitochondrial outer membrane porin protein is dispensable: effects on cellular respiration. (1/140)
Voltage-dependent anion channels (VDACs, also known as mitochondrial porins) are small pore-forming proteins of the mitochondrial outer membrane found in all eukaryotes. Mammals harbor three distinct VDAC isoforms, with each protein sharing 65-70% sequence identity. Deletion of the yeast VDAC1 gene leads to conditional lethality that can be partially or completely complemented by the mammalian VDAC genes. In vitro, VDACs conduct a variety of small metabolites and in vivo they serve as a binding site for several cytosolic kinases involved in intermediary metabolism, yet the specific physiologic role of each isoform is unknown. Here we show that mouse embryonic stem cells lacking each isoform are viable but exhibit a 30% reduction in oxygen consumption. VDAC1 and VDAC2 deficient cells exhibit reduced cytochrome c oxidase activity, whereas VDAC3 deficient cells have normal activity. These results indicate that VDACs are not essential for cell viability and we speculate that reduced respiration in part reflects decreased outer membrane permeability for small metabolites necessary for oxidative phosphorylation. (+info)Evidence for secretory pathway localization of a voltage-dependent anion channel isoform. (2/140)
Voltage-dependent anion channels (VDACs) are pore-forming proteins (porins) that form the major pathway for movement of adenine nucleotides through the outer mitochondrial membrane. Electrophysiological studies indicate that VDAC-like channel activity is also prevalent in the cell membranes of many mammalian cells. However, the multitopological localization of porins outside the mitochondrion has remained an extremely controversial issue. Herein, we show that usage of two alternative first exons of the murine VDAC-1 gene leads to expression of two porins differing within their N termini. One porin (plasmalemmal VDAC-1) harboring a hydrophobic leader peptide is primarily targeted through the Golgi apparatus to the cell membrane. In contrast, the second isoform lacking the N-terminal leader (mitochondrial VDAC-1) is translocated more efficiently into the outer mitochondrial membrane. Thus, our data provide unique genetic evidence in favor of a multitopological localization of a mitochondrial porin. (+info)Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator. (3/140)
Mitochondria play an essential role in apoptosis by releasing apoptogenic molecules such as cytochrome c and AIF, and some caspases, which are all regulated by Bcl-2 family proteins. Pro-apoptotic Bax and Bak have been shown to induce cytochrome c release and loss of membrane potential (Deltapsi) leading to AIF release in the isolated mitochondria. We have previously shown that Bax and Bak open the voltage-dependent anion channel (VDAC) allowing cytochrome c to pass through the channel, and Bcl-xL closes the channel. However, it has been reported that it is adenine nucleotide translocator (ANT) with which Bax/Bcl-xL interacts that modulate the channel activity. Here, we investigated the role of ANT and VDAC in the changes of isolated mitochondria triggered by Bax and by chemicals that induce permeability transition (PT). In rat and yeast mitochondria, Bax did not affect the ADP/ATP exchange activity of ANT. VDAC-deficient but not ANT-deficient yeast mitochondria showed resistance to cytochrome c release, Deltapsi loss, and swelling caused by Bax and PT inducers. Bcl-xL showed similar inhibition of all these changes in ANT-deficient and wild type yeast mitochondria. Furthermore, Bax induces cytochrome c release in wild type yeast cells but not VDAC1-deficient yeast cells. These data indicate that VDAC, but not ANT, is essential for apoptotic mitochondrial changes. The data also indicate that Bcl-xL and Bax possess an ability to regulate mitochondrial membrane permeability independently of other Bcl-2 family members. (+info)Characterization of porin isoforms expressed in tumor cells. (4/140)
Mitochondria from malignant tumor cell lines show a higher capability for hexokinase binding than those from normal liver. To explore possible differences in hexokinase binding sites of mitochondria between tumor cells and normal liver, we characterized porin isoforms expressed in tumor cells. Cloning experiments on the three porin isoforms, VDAC1, VDAC2 and VDAC3 from malignant tumor cell line AH130 clearly showed that their primary structures were completely identical to those of the corresponding VDACs of normal liver cells. Possible expression of the fourth porin isoform in AH130 cells was excluded by degenerate primer-based RT-PCR. However, the transcript levels of the three VDAC isoforms in AH130 cells were significantly higher than those in normal liver. These results suggest that the high hexokinase-binding capability of malignant tumor cell mitochondria was not due to any structural difference, but due to a quantitative difference in binding sites. (+info)Altered mitochondrial sensitivity for ADP and maintenance of creatine-stimulated respiration in oxidative striated muscles from VDAC1-deficient mice. (5/140)
Voltage-dependent anion channels (VDACs) form the main pathway for metabolites across the mitochondrial outer membrane. The mouse vdac1 gene has been disrupted by gene targeting, and the resulting mutant mice have been examined for defects in muscle physiology. To test the hypothesis that VDAC1 constitutes a pathway for ADP translocation into mitochondria, the apparent mitochondrial sensitivity for ADP (Km(ADP)) and the calculated rate of respiration in the presence of the maximal ADP concentration (Vmax) have been assessed using skinned fibers prepared from two oxidative muscles (ventricle and soleus) and a glycolytic muscle (gastrocnemius) in control and vdac1(-/-) mice. We observed a significant increase in the apparent Km((ADP)) in heart and gastrocnemius, whereas the V(max) remained unchanged in both muscles. In contrast, a significant decrease in both the apparent Km((ADP)) and V(max) was observed in soleus. To test whether VDAC1 is required for creatine stimulation of mitochondrial respiration in oxidative muscles, the apparent Km((ADP)) and Vmax were determined in the presence of 25 mm creatine. The creatine effect on mitochondrial respiration was unchanged in both heart and soleus. These data, together with the significant increase in citrate synthase activity in heart, but not in soleus and gastrocnemius, suggest that distinct metabolic responses to altered mitochondrial outer membrane permeability occur in these different striated muscle types. (+info)VDAC2 (porin-2) expression pattern and localization in the bovine testis. (6/140)
In this study, sequencing of voltage-dependent anion channel 2 (VDAC2, porin-2) cDNA from bovine testis is reported. High identity to the murine, rabbit, and human subtypes at both the nucleotide and amino acid levels is demonstrated. mRNA analysis revealed expression of VDAC2 in bovine testis, whereas high levels of VDAC2 proteins were found in late spermatocytes, spermatids, and spermatozoa. In contrast, VDAC1 (porin-1) is exclusively localized in Sertoli cells. The possible role of testicular VDAC2 in providing energy metabolites and in germ cell apoptosis is discussed. (+info)Immotile sperm and infertility in mice lacking mitochondrial voltage-dependent anion channel type 3. (7/140)
Voltage-dependent anion channels (VDACs), also known as mitochondrial porins, are small channel proteins involved in the translocation of metabolites across the mitochondrial outer membrane. A single channel-forming protein is found in yeast, whereas higher eukaryotes express multiple VDACs, with humans and mice each harboring three distinct channels (VDAC1-3) encoded by separate genes. To begin to assess the functions of each of the three isoforms, the VDAC3 gene was inactivated by targeted disruption in embryonic stem cells. Here we show that mice lacking VDAC3 are healthy, but males are infertile. Although there are normal sperm numbers, the sperm exhibit markedly reduced motility. Structural defects were found in two-thirds of epididymal axonemes, with the most common abnormality being loss of a single microtubule doublet at a conserved position within the axoneme. In testicular sperm, the defect was only rarely observed, suggesting that instability of a normally formed axoneme occurs with sperm maturation. In contrast, tracheal epithelial cilia showed no structural abnormalities. In addition, skeletal muscle mitochondria were abnormally shaped, and activities of the respiratory chain complexes were reduced. These results demonstrate that axonemal defects may be caused by associated nonaxonemal components such as mitochondrial channels and illustrate that normal mitochondrial function is required for stability of the axoneme. (+info)Retinal voltage-dependent anion channel: characterization and cellular localization. (8/140)
PURPOSE: To characterize and localize retinal voltage-dependent anion channel (VDAC) and to understand its possible contribution to mitochondrial function and dysfunction. METHODS: VDAC was characterized by a method involving purification from isolated mitochondria and reconstitution into a planar lipid bilayer (PLB). The permeability transition pore (PTP) was monitored by Ca(2+) accumulation in isolated mitochondria and swelling of mitochondria. Localization was studied by immunocytochemistry and in situ hybridization. RESULTS: Retinal VDACs exhibited the electrophysiological fingerprint of the VDAC superfamily. It had a maximal chord conductance of 3.7 +/- 0.1 nanosiemens (nS) in 1 M NaCl, and a voltage-dependent conductance that was highest at transmembrane potential close to zero. It was modulated by glutamate, which decreased the channel's open probability, and by La(3+) and ruthenium amine binuclear complex (Ru360), which closed the channel. Energized and freshly prepared retinal mitochondria accumulated Ca(2+) that is inhibited by La(3+) ruthenium red and Ru360. Subsequent to Ca(2+) accumulation, mitochondria released the accumulated Ca(2+), probably through activation of the PTP. Ru360 inhibited Ca(2+) release and mitochondrial swelling. VDAC was present in mitochondria of all retinal cell types: photoreceptor, bipolar, horizontal, amacrine, and ganglion cells. Most cells primarily expressed VDAC-1, but they also expressed VDAC-2 and -3. CONCLUSIONS: These results suggest that VDAC is involved in PTP activity and/or regulation and thus is an important player in retinal degeneration associated with PTP-mediated mitochondrial dysfunction. (+info)Voltage-Dependent Anion Channel 1 (VDAC1) is a protein channel found in the outer mitochondrial membrane. It plays a crucial role in the regulation of metabolite and ion exchange between the cytosol and the mitochondria. VDAC1 is voltage-dependent, meaning that its permeability to anions (negatively charged ions) changes based on the electrical potential across the membrane. This channel is also known as the mitochondrial porin. Its dysfunction has been implicated in various pathological conditions, including neurodegenerative diseases and cancer.
Voltage-Dependent Anion Channels (VDACs) are large protein channels found in the outer mitochondrial membrane. They play a crucial role in the regulation of metabolite and ion exchange between the cytosol and the mitochondria. VDACs are permeable to anions such as chloride, phosphate, and bicarbonate ions, as well as to small molecules and metabolites like ATP, ADP, NADH, and others.
The voltage-dependent property of these channels arises from the fact that their permeability can be modulated by changes in the membrane potential across the outer mitochondrial membrane. At low membrane potentials, VDACs are predominantly open and facilitate the flow of metabolites and ions. However, as the membrane potential becomes more positive, VDACs can transition to a closed or partially closed state, which restricts ion and metabolite movement.
VDACs have been implicated in various cellular processes, including apoptosis, calcium homeostasis, and energy metabolism. Dysregulation of VDAC function has been associated with several pathological conditions, such as neurodegenerative diseases, cancer, and ischemia-reperfusion injury.
An anion is an ion that has a negative electrical charge because it has more electrons than protons. The term "anion" is derived from the Greek word "anion," which means "to go up" or "to move upward." This name reflects the fact that anions are attracted to positively charged electrodes, or anodes, and will move toward them during electrolysis.
Anions can be formed when a neutral atom or molecule gains one or more extra electrons. For example, if a chlorine atom gains an electron, it becomes a chloride anion (Cl-). Anions are important in many chemical reactions and processes, including the conduction of electricity through solutions and the formation of salts.
In medicine, anions may be relevant in certain physiological processes, such as acid-base balance. For example, the concentration of anions such as bicarbonate (HCO3-) and chloride (Cl-) in the blood can affect the pH of the body fluids and help maintain normal acid-base balance. Abnormal levels of anions may indicate the presence of certain medical conditions, such as metabolic acidosis or alkalosis.
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.
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.
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.
Chloride channels are membrane proteins that form hydrophilic pores or gaps, allowing the selective passage of chloride ions (Cl-) across the lipid bilayer of cell membranes. They play crucial roles in various physiological processes, including regulation of neuronal excitability, maintenance of resting membrane potential, fluid and electrolyte transport, and pH and volume regulation of cells.
Chloride channels can be categorized into several groups based on their structure, function, and mechanism of activation. Some of the major classes include:
1. Voltage-gated chloride channels (ClC): These channels are activated by changes in membrane potential and have a variety of functions, such as regulating neuronal excitability and transepithelial transport.
2. Ligand-gated chloride channels: These channels are activated by the binding of specific ligands or messenger molecules, like GABA (gamma-aminobutyric acid) or glycine, and are involved in neurotransmission and neuromodulation.
3. Cystic fibrosis transmembrane conductance regulator (CFTR): This is a chloride channel primarily located in the apical membrane of epithelial cells, responsible for secreting chloride ions and water to maintain proper hydration and mucociliary clearance in various organs, including the lungs and pancreas.
4. Calcium-activated chloride channels (CaCCs): These channels are activated by increased intracellular calcium concentrations and participate in various physiological processes, such as smooth muscle contraction, neurotransmitter release, and cell volume regulation.
5. Swelling-activated chloride channels (ClSwells): Also known as volume-regulated anion channels (VRACs), these channels are activated by cell swelling or osmotic stress and help regulate cell volume and ionic homeostasis.
Dysfunction of chloride channels has been implicated in various human diseases, such as cystic fibrosis, myotonia congenita, epilepsy, and certain forms of cancer.
VDAC1
VDAC2
Voltage-dependent anion channel
Bcl-2 family
HK2
Biochemical cascade
List of MeSH codes (D12.776.157)
Avibirnavirus
Bcl-2-like protein 1
List of MeSH codes (D12.776.543)
Synthetic ion channels
VDAC3
Pyruvate dehydrogenase complex
Bestrophin 1
Mitochondrion
Mitochondrial membrane transport protein
BCL2L11
Index of biophysics articles
HK1
DYNLT1
DYNLT3
Mitochondrial permeability transition pore
PRKCE
Apoptosis regulator BAX
Tryptophan-rich sensory protein
Non-selective cation channel-2 family
Mitochondria associated membranes
Channel blocker
Bcl-2 homologous antagonist killer
PPIF
VDAC1 - Wikipedia
SCR 6q22.31-6q24.3 Genes
Citations - OJVM - Scientific Research Publishing
Endostatin Prevents Dietary-Induced Obesity by Inhibiting Adipogenesis and Angiogenesis | Diabetes | American Diabetes...
JCI - Citations to Blocking mitochondrial calcium release in Schwann cells prevents demyelinating neuropathies
Novel Molecular Targets Participating in Myocardial Ischemia-Reperfusion Injury and Cardioprotection
Lifeboat Foundation News Blog - Page 7629
PTEN-induced putative kinase 1
Frontiers | Unraveling the Link Between Mitochondrial Dynamics and Neuroinflammation
Search BioNumbers - The Database of Useful Biological Numbers
MTX1 metaxin 1 [Homo sapiens (human)] - Gene - NCBI
Publications of Rainer Höfgen | Max Planck Institute of Molecular Plant Physiology
Publications of the Group | Max Planck Institute of Molecular Plant Physiology
In Long COVID, Blood Markers Are Linked to Neuropsychiatric Symptoms - Neuroscience News
Autophagy and mitophagy in the context of doxorubicin-induced cardiotoxicity | Oncotarget
Ben-Gurion University of the Negev - Research output - Ben-Gurion University Research Portal
People - School of Health Sciences - The University of Nottingham
Faculty of Medicine - Research output - Lund University
Danielle M Robertson - Research output - University of Texas Southwestern Medical Center
Baoan D Ji - Research output - Mayo Clinic
GSE17974 0H VS 6H IN VITRO ACT CD4 TCELL DN
Antidepressant drug sertraline modulates AMPK-MTOR signaling-mediated autophagy via targeting mitochondrial VDAC1 protein<...
The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins | Journal of Cell...
3EMN | Genus
Rabbit VDAC1 ELISA Kit (ABIN775898)
The Role of Pyruvate Metabolism in Mitochondrial Quality Control and Inflammation
Cerebrospinal Fluid Levels of Kininogen-1 Indicate Early Cognitive Impairment in Parkinson's Disease - PDBWiki annotation of...
Department of Developmental Biology - Research output - Research Profiles at Washington University School of Medicine
VDAC111
- Voltage-dependent anion-selective channel 1 (VDAC-1) is a beta barrel protein that in humans is encoded by the VDAC1 gene located on chromosome 5. (wikipedia.org)
- In particular, since VDAC1 is the major calcium ion transport channel, its dysfunction is implicated in cancer, Parkinson's (PD), and Alzheimer's disease. (wikipedia.org)
- Of the three isoforms, VDAC1 is the main calcium ion transport channel and the most abundantly transcribed. (wikipedia.org)
- We demonstrated that mitochondrial calcium released by voltage-dependent anion channel 1 (VDAC1) after sciatic nerve injury triggers Schwann cell demyelination via ERK1/2, p38, JNK, and c-JUN activation. (jci.org)
- We report that the ATP conducting mitochondrial outer membrane voltage dependent anion channel-1 (VDAC1) is upregulated in islets from T2D and non-diabetic organ donors under glucotoxic conditions. (lifeboat.com)
- Mechanistically, Sert potentially binds to and antagonizes the mitochondrial VDAC1 (voltage dependent anion channel 1), resulting in reduced cellular ATP (adenosine triphosphate) level, activation of AMP-activated protein kinase (AMPK) and inhibition of its downstream, MTOR (mechanistic target of rapamycin kinase)-RPS6KB1 (ribosomal protein S6 kinase B1) signaling pathway. (elsevierpure.com)
- The voltage-dependent anion channel 1 (VDAC1), localized at the outer mitochondrial membrane (OMM) is a central protein in controlling energy production, cell growth, Ca 2+ homeostasis, and apoptosis. (pdbwiki.org)
- The Voltage-dependent anion channel 1 (VDAC1) is a mitochondrial porin of the outer membrane that mediates the flux of small ions, metabolites and ATP in and out from mitochondria and plays a major role in the regulation of cellular metabolism and apoptosis. (keystonesymposia.org)
- Our previous findings pointed out a new post-translational modification of VDAC1, which was linked to an higher metabolic capacity and a greater resistance to cell death of cancer cells exposed to a long-term hypoxia (1% O 2 ), a feature of locally advanced solid tumors (Brahimi-Horn et al. (keystonesymposia.org)
- The impact of the overexpression of VDAC1 on resistance to chemotherapy has been assessed on different clones obtained from MEF-RAS- Vdac 1 -/- , overexpressing the WT form of VDAC1 or the mutated form of the protein. (keystonesymposia.org)
- We have recently shown that it is possible to restore the normal function of beta-cells by blocking the protein VDAC1 (Voltage-Dependent Anion Channel 1), which is dramatically increased in beta cells of people with T2D. (lu.se)
Protein4
- This protein is a voltage-dependent anion channel and shares high structural homology with the other VDAC isoforms (VDAC2 and VDAC3), which are involved in the regulation of cell metabolism, mitochondrial apoptosis, and spermatogenesis. (wikipedia.org)
- Proliferation is upregulated through two mechanisms: (1) ATP binding to the G-protein-coupled receptor P2Y2, commencing a kinase signaling cascade that activates the serine-threonine kinase Akt, and (2) the transactivation of the epidermal growth factor receptor (EGFR), leading to a series of protein signals that activate the extracellular signal-regulated kinases (ERK) 1/2. (encyclopedia.pub)
- Alterations in Activity-Dependent Neuroprotective Protein in Sporadic and Experimental Parkinson's Disease. (rush.edu)
- Voltage-dependent anion channel 1 is the major pore-forming protein of the mitochondrial outer membrane. (bvsalud.org)
Mitochondria2
- [1] pl. mitochondria ) is an organelle found in the cells of most eukaryotes , such as animals , plants and fungi . (wikipedia.org)
- In the PARK2-dependent pathway, PINK1 activates PARK2 to target many mitochondrial proteins, including NDP52, OPTN and p62, and it combines with LC3 to deliver damaged mitochondria to autophagosomes [ 15 ]. (ijbs.com)
Calcium4
- Disturbances in mitochondrial dynamics may influence many cellular and molecular pathways, as calcium-dependent immune activation, transcription factors phosphorylation, cytokine secretion, organelle transference and even cell death. (frontiersin.org)
- Calcium entry through transient receptor potential vanilloid 1 (TRPV1) ion channels modulates the delicate balance between proliferation and apoptosis. (encyclopedia.pub)
- The noted discrepancy of membrane proteins included calcium binding proteins (annexin A1, annexin A2), and voltage-dependent anion channels proteins (VDAC 1, VDAC 2), suggesting that these molecules may affect JEV attachment to and/or entry into BHK-21 cells and worthy of further investigation. (biomedcentral.com)
- Hypermagnesemia causes blockage of neuromuscular transmission by preventing presynaptic acetylcholine release and by competitively inhibiting calcium influx into the presynaptic nerve channels via the voltage-dependent calcium channel. (medscape.com)
Porins1
- Molecular and cell biology of a family of voltage-dependent anion channel porins in Lotus japonicus. (mpg.de)
Phosphorylation2
- PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control. (sdbonline.org)
- The phosphorylation of Metaxin 1 controls Bak activation during TNFα induced cell death. (nih.gov)
Receptors2
- Inhibitory ryanodine or NAC did not affect insulin secretion induced by glucose plus carbachol, which engages inositol 1,4,5-trisphosphate receptors. (omicsdi.org)
- Signalling in this technique is principally mediated through both centrally and peripherally portrayed cannabinoid-1 receptors (CB1R)5,6. (crispr-reagents.com)
Proteins1
- To discover the molecular programs controlling microglial and macrophage polarization by blood proteins, we developed an unbiased blood-innate immunity multiomic and genetic loss-of-function pipeline consisting of deep sequencing of blood-induced transcriptomes, functional single-cell and oxidative stress transcriptomics, global phosphoproteomics and integration with innate immune signatures from AD and MS models (Extended Data Fig. 1 ). (nature.com)
Outer1
- It forms an ion channel in the outer mitochondrial membrane (OMM) and also the outer cell membrane. (wikipedia.org)
20221
- As of January 1, 2022, Oncotarget has shifted to a continuous publishing model. (oncotarget.com)
Pathway2
- This consequently decreases the expression of mTOR, results in decreased activities of the mTOR complex 1 pathway, and leads to defects in adipogenesis. (diabetesjournals.org)
- Sulindac sulfone inhibits the mTORC1 pathway in colon cancer cells by directly targeting voltage-dependent anion channel 1 and 2. (kwansei.ac.jp)
Molecule1
- This ELISA kit is a solid phase ELISA designed for quantitative determination of vascuolar cell adhesion molecule 1. (anticorps-enligne.fr)
Pathways3
- The opening of transient receptor potential vanilloid 1 (TRPV1) ligand-gated ion channels facilitates transmembrane Ca 2+ and Na + entry, which modifies the delicate balance between apoptotic and proliferative signaling pathways. (encyclopedia.pub)
- Carcinogenesis results from imbalances in the described pathways, which favor proliferation and reduce apoptosis [ 1 ] [ 2 ] . (encyclopedia.pub)
- There are two major mitophagy pathways, namely, PARK2-dependent and PARK2-independent signaling [ 14 ]. (ijbs.com)
Subunit3
- Conformational changes within the subunit b-dimer of the E. coli ATP synthase occur upon binding to the F(1) sector. (shengsci.com)
- Between b-residues 33 and 64 inter-subunit distances in the F(1)-bound b-dimer were found to be too large to accommodate tightly coiled coil packing and therefore suggest a dissociation and disengagement of the dimer upon F(1)-binding. (shengsci.com)
- Finally, it seems appropriate to consider the "sodium channel syndrome" (mutations in the gene of the α subunit of the sodium channel, SCN5A gene) as a single clinical entity that may manifest in a wide range of phenotypes, to thus have a better insight on these cardiac syndromes and potential outcomes for their clinical treatment. (bvsalud.org)
Parkinson's1
- Abnormal alpha-synuclein reduces nigral voltage-dependent anion channel 1 in sporadic and experimental Parkinson's disease. (rush.edu)
Biochemical1
- Arabidopsis ammonium transporters, AtAMT1;1 and AtAMT1;2, have different biochemical properties and functional roles. (mpg.de)
Sodium channel3
- From a physiological and pathophysiological point of view, the conformational states of the sodium channel during heart function constitute a significant aspect for the diagnosis and treatment of heart diseases. (bvsalud.org)
- Functional states of the sodium channel (closed, open, and inactivated) and their structure help to understand the cardiac regulation processes. (bvsalud.org)
- Heart relaxation also stands out as an active process, dependent on the energetic output and on specific ion and enzymatic actions, with the role of sodium channel being outstanding in the functional process. (bvsalud.org)
Molecular1
- By off-target modelling we're able to predict both voltage-dependent anion route (VDAC) as well as the adenine nucleotide translocase 1 (ANT1) as the molecular site of ibipinabant inhibition. (crispr-reagents.com)
Flux1
- At low voltage (10mV), the pore is in an "open" state where the channel is weakly anion selective and allows for a greater flux of metabolites. (wikipedia.org)
Concentrations1
- For the quantitative determination of rabbit VCAM-1 concentrations in serum, plasma,cell culture supernates and tissue homogenate. (anticorps-enligne.fr)
Composition1
- However, they show subtle variations in residue composition, secondary structure composition, substrate-binding channel volume, and conformational stability. (bvsalud.org)
Interleukin1
- interleukin 18 receptor 1 [Source:HGNC. (gsea-msigdb.org)
Mitochondrion1
- Structural analysis of mVDAC1's structure showed a barrel-like channel composed of 19 amphipathic β-strands, with the N-terminus and C-terminus both facing towards the inter membrane space of the mitochondrion. (wikipedia.org)
Hypoxia1
- hypoxia up-regulated 1 [Source:HGNC Sy. (gsea-msigdb.org)
Conformational1
- Its permeability is dependent on VDAC1's conformational state which is determined by voltage. (wikipedia.org)
Cancers1
- Doxorubicin (Dox), a non-selective class I anthracycline antibiotic, is a potent chemotherapeutic agent which is used for the treatment of numerous cancers [ 1 ]. (oncotarget.com)
Mice1
- The severity of heart disease is linked to accumulated Dox dosage during the course of the anticancer therapy ranging from 3-5% in patients that received a cumulative dose of 400mg/m 2 to 18-48% in patients receiving 700mg/m 2 (and 100% of mice receiving 71mg/ m 2 ) [ 1 , 6 , 7 ]. (oncotarget.com)
Motif1
- SAYSVFN motif domain containing 1 [Sou. (gsea-msigdb.org)
Neurological1
- The World Health Organization (WHO) have estimated that until 2030, deaths attributed to neurological diseases will increased up to 12.22% ( 1 ). (frontiersin.org)
Clinical1
- Among clinical emergency events, ST-segment elevation (STE) or the non-STE electrocardiogram diagnosis of acute myocardial infarction (AMI) is particularly common worldwide, with a staggering number of annual first episodes as well as recurrent ones [ 1 ]. (hindawi.com)
Induce2
- In other cell types, Ca2+ and ROS jointly induce Ca2+ release mediated by ryanodine receptor (RyR) channels. (omicsdi.org)
- Nephrotoxic drugs, such as antibiotics (gentamicin), diuretics (furosemide), chemotherapeutic drugs (cisplatin) and calcineurin inhibitors (tacrolimus), induce acute kidney injury [ 1 ]. (ijbs.com)
Residue1
- Spectra of frozen b +/- F(1) and calculated interspin distances suggested that where contact between b (2) and F(1) occurs (above about residue 80), the structure of the dimer changes minimally. (shengsci.com)
Inhibitor2
- This inhibitor might be employed in treating this disease in humans [1]. (lifeboat.com)
- Ferrstatin-1, a synthetic antioxidative ferroptosis inhibitor, rescued iron accumulation, lipid peroxidation and ferroptosis caused by inhibition of mitophagy. (ijbs.com)
Transport1
- 1] Relatively little is known about cellular magnesium transport mechanisms. (medscape.com)
Acute1
- Drug-induced acute kidney injury is the second most common cause of acute kidney injury in hospitalized patients, especially in the intensive care unit[ 1 , 2 ]. (ijbs.com)
Pathophysiology1
- However, there yet remain unknown aspects of MIRI and cardioprotection, and in Figure 1 , we present a briefly summarized conceptual diagram of the pathophysiology of MIRI involving the parts mentioned above. (hindawi.com)
Symbol1
- acyl-CoA oxidase 1 [Source:HGNC Symbol. (gsea-msigdb.org)
Beta3
- beta-1,4-galactosyltransferase 5 [Sour. (gsea-msigdb.org)
- hydroxysteroid 17-beta dehydrogenase 1. (gsea-msigdb.org)
- A. Oller 1 , G. Oberdorster 2 teins like beta-actin (ACTB) and keratin (KRT8, KRT2). (cdc.gov)