Definitions containing ca(2 ) mg(2 )-atpase

We've found 49 definitions:

adenosinetriphosphatase

adenosinetriphosphatase

ATPase

— Wiktionary

pontin

pontin

An ATPase that is a component of telomerase

— Wiktionary

reptin

reptin

An ATPase that is a component of telomerase

— Wiktionary

Calponin

Calponin

Calponin is a calcium binding protein. Calponin tonically inhibits the ATPase activity of myosin in smooth muscle. Phosphorylation of calponin by a protein kinase, which is dependent upon calcium binding to calmodulin, releases the calponin's inhibition of the smooth muscle ATPase.

— Freebase

4-Chloro-7-nitrobenzofurazan

4-Chloro-7-nitrobenzofurazan

A benzofuran derivative used as a protein reagent since the terminal N-NBD-protein conjugate possesses interesting fluorescence and spectral properties. It has also been used as a covalent inhibitor of both beef heart mitochondrial ATPase and bacterial ATPase.

— U.S. National Library of Medicine

Omeprazole

Omeprazole

A highly effective inhibitor of gastric acid secretion used in the therapy of STOMACH ULCERS and ZOLLINGER-ELLISON SYNDROME. The drug inhibits the H(+)-K(+)-ATPase (H(+)-K(+)-EXCHANGING ATPASE) in the proton pump of GASTRIC PARIETAL CELLS.

— U.S. National Library of Medicine

Katanin

Katanin

Katanin is a microtubule-severing AAA protein. It is named after the Japanese sword, katana. Katanin is a heterodimeric protein first discovered in sea urchins. It contains a 60 kDa ATPase subunit, which functions to sever microtubules. This subunit requires ATP and the presence of microtubules for activation. The second 80 kDA subunit regulates the activity of the ATPase and localizes the protein to the centrosomes. Electron microscopy shows that katanin forms 14–16 nm rings in its active oligomerized state on the walls of microtubules:

— Freebase

Spastin

Spastin

The human gene SPAST codes for the microtubule-severing protein of the same name, commonly known as spastin. This gene encodes a member of the AAA protein family. Members of this protein family share an ATPase domain and have roles in diverse cellular processes including membrane trafficking, intracellular motility, organelle biogenesis, protein folding, and proteolysis. The encoded ATPase may be involved in the assembly or function of nuclear protein complexes. Two transcript variants encoding distinct isoforms have been identified for this gene. Other alternative splice variants have been described but their full length sequences have not been determined. Mutations associated with this gene cause the most frequent form of autosomal dominant spastic paraplegia 4.

— Freebase

ATP-Dependent Endopeptidases

ATP-Dependent Endopeptidases

Endoproteases that contain proteolytic core domains and ATPase-containing regulatory domains.

— U.S. National Library of Medicine

MutS DNA Mismatch-Binding Protein

MutS DNA Mismatch-Binding Protein

A methyl-directed mismatch DNA REPAIR protein that has weak ATPASE activity. MutS was originally described in ESCHERICHIA COLI.

— U.S. National Library of Medicine

Nigericin

Nigericin

A polyether antibiotic which affects ion transport and ATPase activity in mitochondria. It is produced by Streptomyces hygroscopicus. (From Merck Index, 11th ed)

— U.S. National Library of Medicine

Thapsigargin

Thapsigargin

A sesquiterpene lactone found in roots of THAPSIA. It inhibits CA(2+)-TRANSPORTING ATPASE mediated uptake of CALCIUM into SARCOPLASMIC RETICULUM.

— U.S. National Library of Medicine

Proton Pump Inhibitors

Proton Pump Inhibitors

Compounds that inhibit H(+)-K(+)-EXCHANGING ATPASE. They are used as ANTI-ULCER AGENTS and sometimes in place of HISTAMINE H2 ANTAGONISTS for GASTROESOPHAGEAL REFLUX.

— U.S. National Library of Medicine

Aurovertins

Aurovertins

Very toxic and complex pyrone derivatives from the fungus Calcarisporium arbuscula. They bind to and inhibit mitochondrial ATPase, thereby uncoupling oxidative phosphorylation. They are used as biochemical tools.

— U.S. National Library of Medicine

Cyclopiazonic acid

Cyclopiazonic acid

Cyclopiazonic acid is a toxic fungal secondary metabolite. Chemically, it is an indole tetramic acid. CPA was originally isolated from Penicillium cyclopium and subsequently from other P. cyclopium, Penicillium griseofulvum, Penicillium camembertii, Aspergillus flavus and Aspergillus versicolor. Cyclopiazonic acid only appears to be toxic in high concentrations. Biologically, Cyclopiazonic acid is a specific inhibitor of Ca2+-ATPase in the intracellular Ca2+ storage sites.

— Freebase

ATP-Dependent Proteases

ATP-Dependent Proteases

Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.

— U.S. National Library of Medicine

Muscle Fibers, Slow-Twitch

Muscle Fibers, Slow-Twitch

Skeletal muscle fibers characterized by their expression of the Type I MYOSIN HEAVY CHAIN isoforms which have low ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment.

— U.S. National Library of Medicine

Semantides

Semantides

Semantides are macromolecules common to all cells, used in phylogeny because they change slowly over time. The term was coined by Linus Pauling and Emile Zuckerkandl. Examples of these molecules are: ⁕rRNA/rDNA ⁕RNase P RNA ⁕ATPase ⁕RecA protein ⁕Cytochrome C ⁕Heat shock protein genes The above semantides can yield different phylogenetic trees, but if the genetic relatedness is correct for 2 or more, that correlation could mean that the evolutionary tree is correct.

— Freebase

Mi-2 Nucleosome Remodeling and Deacetylase Complex

Mi-2 Nucleosome Remodeling and Deacetylase Complex

A enzyme complex involved in the remodeling of NUCLEOSOMES. The complex is comprised of at least seven subunits and includes both histone deacetylase and ATPase activities.

— U.S. National Library of Medicine

Novobiocin

Novobiocin

An antibiotic compound derived from Streptomyces niveus. It has a chemical structure similar to coumarin. Novobiocin binds to DNA gyrase, and blocks adenosine triphosphatase (ATPase) activity. (From Reynolds, Martindale The Extra Pharmacopoeia, 30th ed, p189)

— U.S. National Library of Medicine

Intracellular

Intracellular

In cell biology, molecular biology and related fields, the word intracellular means "inside the cell". It is used in contrast to extracellular. The cell membrane is the barrier between the two, and chemical composition of intra- and extracellular milieu can be radically different. In most organisms, for example, a Na+/K+ ATPase maintains a high potassium level inside cells while keeping sodium low, leading to chemical excitability. This terms also means existing within the cells.

— Freebase

Proton Pumps

Proton Pumps

Integral membrane proteins that transport protons across a membrane. This transport can be linked to the hydrolysis of ADENOSINE TRIPHOSPHATE. What is referred to as proton pump inhibitors frequently is about POTASSIUM HYDROGEN ATPASE.

— U.S. National Library of Medicine

Secretagogue

Secretagogue

A secretagogue is a substance that causes another substance to be secreted. One example is gastrin, which stimulates the H/K ATPase in the parietal cells. Pentagastrin, a synthetic gastrin, histamine, and acetylcholine are also gastric secretagogues. Sulfonylureas are insulin secretagogues, triggering insulin release by direct action on the KATP channel of the pancreatic beta cells. Blockage of this channel leads to depolarization and secretion of vesicles. Angiotensin II is a secretagogue for aldosterone from the adrenal gland.

— Freebase

Hypoaldosteronism

Hypoaldosteronism

A congenital or acquired condition of insufficient production of ALDOSTERONE by the ADRENAL CORTEX leading to diminished aldosterone-mediated synthesis of Na(+)-K(+)-EXCHANGING ATPASE in renal tubular cells. Clinical symptoms include HYPERKALEMIA, sodium-wasting, HYPOTENSION, and sometimes metabolic ACIDOSIS.

— U.S. National Library of Medicine

Muscle Fibers, Fast-Twitch

Muscle Fibers, Fast-Twitch

Skeletal muscle fibers characterized by their expression of the Type II MYOSIN HEAVY CHAIN isoforms which have high ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment. Several fast types have been identified.

— U.S. National Library of Medicine

N-Ethylmaleimide-Sensitive Proteins

N-Ethylmaleimide-Sensitive Proteins

ATPases that are members of the AAA protein superfamily (ATPase family Associated with various cellular Activities). The NSFs functions, acting in conjunction with SOLUBLE NSF ATTACHMENT PROTEINS (i.e. SNAPs, which have no relation to SNAP 25), are to dissociate SNARE complexes.

— U.S. National Library of Medicine

Ouabain

Ouabain

A cardioactive glycoside consisting of rhamnose and ouabagenin, obtained from the seeds of Strophanthus gratus and other plants of the Apocynaceae; used like DIGITALIS. It is commonly used in cell biological studies as an inhibitor of the NA(+)-K(+)-EXCHANGING ATPASE.

— U.S. National Library of Medicine

2-Pyridinylmethylsulfinylbenzimidazoles

2-Pyridinylmethylsulfinylbenzimidazoles

Compounds that contain benzimidazole joined to a 2-methylpyridine via a sulfoxide linkage. Several of the compounds in this class are ANTI-ULCER AGENTS that act by inhibiting the POTASSIUM HYDROGEN ATPASE found in the PROTON PUMP of GASTRIC PARIETAL CELLS.

— U.S. National Library of Medicine

Esomeprazole

Esomeprazole

Esomeprazole is a proton pump inhibitor which reduces acid secretion through inhibition of the H+ / K+ ATPase in gastric parietal cells. By inhibiting the functioning of this transporter, the drug prevents formation of gastric acid. It is used in the treatment of dyspepsia, peptic ulcer disease, gastroesophageal reflux disease and Zollinger-Ellison syndrome. Esomeprazole is the S-enantiomer of omeprazole. Generic versions of Esomeprazole are available in several countries of Europe and in emerging markets like India, Peru, Ecuador, Caribbean Islands, Nigeria, Africa, Sri Lanka, Cambodia and Myanmar under the brand name Raciper.

— Freebase

Gastrin

Gastrin

In humans, gastrin is a peptide hormone that stimulates secretion of gastric acid by the parietal cells of the stomach and aids in gastric motility. It is released by G cells in the antrum of the stomach, duodenum, and the pancreas. It binds to cholecystokinin B receptors to stimulate the release of histamines in enterochromaffin-like cells, and it induces the insertion of K+/H+ ATPase pumps into the apical membrane of parietal cells. Its release is stimulated by peptides in the lumen of the stomach.

— Freebase

Vanadates

Vanadates

Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.

— U.S. National Library of Medicine

Calcimycin

Calcimycin

An ionophorous, polyether antibiotic from Streptomyces chartreusensis. It binds and transports cations across membranes and uncouples oxidative phosphorylation while inhibiting ATPase of rat liver mitochondria. The substance is used mostly as a biochemical tool to study the role of divalent cations in various biological systems.

— U.S. National Library of Medicine

STCH

STCH

Heat shock 70 kDa protein 13 is a protein that in humans is encoded by the HSPA13 gene. The protein encoded by this gene is a member of the heat shock protein 70 family and is found associated with microsomes. Members of this protein family play a role in the processing of cytosolic and secretory proteins, as well as in the removal of denatured or incorrectly folded proteins. The encoded protein contains an ATPase domain and has been shown to associate with a ubiquitin-like protein.

— Freebase

Membrane potential

Membrane potential

Membrane potential is the difference in electrical potential between the interior and the exterior of a biological cell. Typical values of membrane potential range from –40 mV to –80 mV. All animal cells are surrounded by a plasma membrane composed of a lipid bilayer with a variety of types of proteins embedded in it. The membrane potential arises primarily from the interaction between the membrane and the actions of two types of transmembrane proteins embedded in the plasma membrane. The membrane serves as both an insulator and a diffusion barrier to the movement of ions. Ion transporter/pump proteins actively push ions across the membrane to establish concentration gradients across the membrane, and ion channels allow ions to move across the membrane down those concentration gradients, a process known as facilitated diffusion. In the most fundamental example of this, the ion transporter Na+/K+-ATPase pumps sodium cations from the inside to the outside, and potassium cations from the outside to the inside of the cell. This establishes two concentration gradients: a gradient for sodium where its concentration is much higher outside than inside the cell, and a gradient for potassium where its concentration is much higher inside the cell than outside. Transmembrane potassium-selective leak channels allow potassium ions to diffuse across the membrane, down the concentration gradient that was established by the ATPase, creating a charge separation, and thus a voltage, across the membrane. In almost all cases, the ion that determines the so-called "resting" membrane potential of a cell is K+, although other ions do contribute in more minor ways. By convention, the sign of the membrane potential is the voltage inside relative to ground outside the cell. In the case of K+, its diffusion down its concentration gradient creates transmembrane voltage that is negative relative to the outside of the cell, and typically –60 to –80 millivolts in amplitude.

— Freebase

Sodium-Potassium-Exchanging ATPase

Sodium-Potassium-Exchanging ATPase

An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.

— U.S. National Library of Medicine

Bafilomycin

Bafilomycin

The bafilomycins are a family of toxic macrolide antibiotic derived from Streptomyces griseus. These compounds all appear in the same fermentation and have quite similar biological activity. Bafilomycins are specific inhibitors of vacuolar-type H+-ATPase. The most used bafilomycin is bafilomycin A1. This is a useful tool as it can prevent the re-acidification of synaptic vesicles once they have undergone exocytosis. Bafilomycin has antibacterial, antifungal, antineoplastic, immunosuppressive activities.In addition, bafilomycin A1 has antimalarial activity It has been shown to decrease multi-drug resistance. Bafilomycin B1 has been mentioned as a potential antiosteoporotic agent in treating bone lytic diseases.

— Freebase

Ca(2+) Mg(2+)-ATPase

Ca(2+) Mg(2+)-ATPase

An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3.

— U.S. National Library of Medicine

Adenylyl Imidodiphosphate

Adenylyl Imidodiphosphate

5'-Adenylic acid, monoanhydride with imidodiphosphoric acid. An analog of ATP, in which the oxygen atom bridging the beta to the gamma phosphate is replaced by a nitrogen atom. It is a potent competitive inhibitor of soluble and membrane-bound mitochondrial ATPase and also inhibits ATP-dependent reactions of oxidative phosphorylation.

— U.S. National Library of Medicine

Ryanodine

Ryanodine

A methylpyrrole-carboxylate from RYANIA that disrupts the RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL to modify CALCIUM release from SARCOPLASMIC RETICULUM resulting in alteration of MUSCLE CONTRACTION. It was previously used in INSECTICIDES. It is used experimentally in conjunction with THAPSIGARGIN and other inhibitors of CALCIUM ATPASE uptake of calcium into SARCOPLASMIC RETICULUM.

— U.S. National Library of Medicine

Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

SNARE binding proteins that facilitate the ATP hydrolysis-driven dissociation of the SNARE complex. They are required for the binding of N-ETHYLMALEIMIDE-SENSITIVE PROTEIN (NSF) to the SNARE complex which also stimulates the ATPASE activity of NSF. They are unrelated structurally to SNAP-25 PROTEIN.

— U.S. National Library of Medicine

Caldesmon

Caldesmon

Caldesmon is a protein that in humans is encoded by the CALD1 gene. Caldesmon is a calmodulin binding protein. Like calponin or troponin, caldesmon tonically inhibits the ATPase activity of myosin in smooth muscle. This gene encodes a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca++-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca++-dependent inhibition of smooth muscle contraction. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms.

— Freebase

Pemphigus, Benign Familial

Pemphigus, Benign Familial

An autosomal dominantly inherited skin disorder characterized by recurrent eruptions of vesicles and BULLAE mainly on the neck, axillae, and groin. Mutations in the ATP2C1 gene (encoding the secretory pathway Ca2++/Mn2++ ATPase 1 (SPCA1)) cause this disease. It is clinically and histologically similar to DARIER DISEASE - both have abnormal, unstable DESMOSOMES between KERATINOCYTES and defective CALCIUM-TRANSPORTING ATPASES. It is unrelated to PEMPHIGUS VULGARIS though it closely resembles that disease.

— U.S. National Library of Medicine

Hepatolenticular Degeneration

Hepatolenticular Degeneration

A rare autosomal recessive disease characterized by the deposition of copper in the BRAIN; LIVER; CORNEA; and other organs. It is caused by defects in the ATP7B gene encoding copper-transporting ATPase 2 (EC 3.6.3.4), also known as the Wilson disease protein. The overload of copper inevitably leads to progressive liver and neurological dysfunction such as LIVER CIRRHOSIS; TREMOR; ATAXIA and intellectual deterioration. Hepatic dysfunction may precede neurologic dysfunction by several years.

— U.S. National Library of Medicine

Cardiac Glycosides

Cardiac Glycosides

Cyclopentanophenanthrenes with a 5- or 6-membered lactone ring attached at the 17-position and SUGARS attached at the 3-position. Plants they come from have long been used in congestive heart failure. They increase the force of cardiac contraction without significantly affecting other parameters, but are very toxic at larger doses. Their mechanism of action usually involves inhibition of the NA(+)-K(+)-EXCHANGING ATPASE and they are often used in cell biological studies for that purpose.

— U.S. National Library of Medicine

Proton-Motive Force

Proton-Motive Force

Energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work. Proton-motive force can be generated by a variety of phenomena including the operation of an electron transport chain, illumination of a PURPLE MEMBRANE, and the hydrolysis of ATP by a proton ATPase. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p171)

— U.S. National Library of Medicine

Ruthenium red

Ruthenium red

The inorganic dye ammoniated ruthenium oxychloride, also known as Ruthenium Red, is used in histology to stain aldehyde fixed mucopolysaccharides. Ruthenium Red has also been used as a pharmacological tool to study specific cellular mechanisms. Selectivity is a significant issue in such studies as RR is known to interact with a large number of proteins. These include mammalian ion channels, a plant ion channel, Ca2+-ATPase, mitochondrial Ca2+ uniporter, tubulin, myosin light-chain phosphatase, and Ca2+ binding proteins such as calmodulin. It should be further noted that Ruthenium Red displays nanomolar potency against several of its binding partners. For example, it is a potent inhibitor of intracellular calcium release by Ryanodine receptors. RR has been used on plant material since 1890 for staining pectins, mucilages, and gums. RR is a stereoselective stain for pectic acid, insofar as the staining site occurs between each monomer unit and the next adjacent neighbor.

— Freebase

Thapsigargin

Thapsigargin

Thapsigargin is non-competitive inhibitor of a class of enzymes known by the acronym SERCA, which stands for sarco / endoplasmic reticulum Ca2+ ATPase. Structurally, thapsigargin is classified as a sesquiterpene lactone, and is extracted from a plant, Thapsia garganica. It is a tumor promoter in mammalian cells. The anti-malarial drug artemisinin is also a sesquiterpene lactone, leading to a proposal that this class of drugs works by inhibiting the SERCA of malaria parasites such as Plasmodium falciparum; this hypothesis awaits confirmation. Thapsigargin raises cytosolic calcium concentration by blocking the ability of the cell to pump calcium into the sarcoplasmic and endoplasmic reticula which causes these stores to become depleted. Store-depletion can secondarily activate plasma membrane calcium channels, allowing an influx of calcium into the cytosol. Thapsigargin specifically inhibits the fusion of autophagosomes with lysosomes; the last step in the autophagic process. The inhibition of the autophagic process in turn induces stress on the endoplasmic reticulum which ultimately leads to cellular death. Thapsigargin is useful in experimentation examining the impacts of increasing cytosolic calcium concentrations.

— Freebase

Reabsorption

Reabsorption

In physiology, reabsorption or tubular reabsorption is the flow of glomerular filtrate from the proximal tubule of the nephron into the peritubular capillaries, or from the urine into the blood. It is termed "reabsorption" because this is technically the second time that the nutrients in question are being absorbed into the blood, the first time being from the small intestine into the villi. This happens as a result of sodium transport from the lumen into the blood by the Na+/K+ ATPase in the basolateral membrane of the epithelial cells. Thus, the glomerular filtrate becomes more concentrated, which is one of the steps in forming urine. In this way, many useful solutes, salts and water that have passed in the proximal convoluted tubule through the Bowman's capsule, return in the circulation. These solutes are reabsorbed isotonically, in that the osmotic potential of the fluid leaving the proximal convoluted tubule is the same as that of the initial glomerular filtrate. However, glucose, amino acids, inorganic phosphate, and some other solutes are reabsorbed via secondary active transport through cotransport channels driven by the sodium gradient out of the nephron.

— Freebase

Rho factor

Rho factor

A ρ factor is a prokaryotic protein involved in the termination of transcription. Rho factor binds to the transcription terminator pause site, an exposed region of single stranded RNA after the open reading frame at GC-rich sequences that lack obvious secondary structure. Rho factor is an essential transcription protein in prokaryotes. In Escherichia coli, it is a ~275 kD hexamer of identical subunits. Each subunit has an RNA-binding domain and an ATP-hydrolysis domain. Rho is a member of the family of ATP-dependent hexameric helicases that function by wrapping nucleic acids around a single cleft extending around the entire hexamer. Rho functions as an ancillary factor for RNA polymerase. There are two types of transcriptional termination in prokaryotes, factor-dependent termination and Intrinsic termination. Rho-dependent terminators account for about half of the E. coli factor-dependent terminators. Other termination factors discovered in E. coli include Tau and nusA. Rho-dependent terminators were first discovered in bacteriophage genomes. A Rho factor acts on an RNA substrate. Rho's key function is its helicase activity, for which energy is provided by an RNA-dependent ATP hydrolysis. The initial binding site for Rho is an extended single-stranded region, rich in cytosine and poor in guanine, called the rho utilization site or rut, in the RNA being synthesised, upstream of the actual terminator sequence. Several rho binding sequences have been discovered. No consensus is found among these, but the different sequences each seem specific, as small mutations in the sequence disrupts its function. Rho binds to RNA and then uses its ATPase activity to provide the energy to translocate along the RNA until it reaches the RNA-DNA helical region, where it unwinds the hybrid duplex structure. RNA polymerase pauses at the termination sequence, which is because there is a specific site around 100nt away from the Rho binding site called the Rho-sensitive pause site. So, even though the RNA polymerase is about 40nt per second faster than Rho, it does not pose a problem for the Rho termination mechanism as the RNA polymerase allows Rho factor to catch up.

— Freebase


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