Carbonic Anhydrase II
Carbonic Anhydrases
Carbonic Anhydrase Inhibitors
Carbonic Anhydrase III
Ethoxzolamide
Acetazolamide
Carbonic Anhydrase I
Methazolamide
Acidosis, Renal Tubular
Osteopetrosis
Bicarbonates
Benzolamide
Carbon Dioxide
Carbonic Acid
Isoenzymes
Hydrogen-Ion Concentration
Sodium-Bicarbonate Symporters
Zinc
Crystallography, X-Ray
Models, Molecular
Protons
Catalysis
Catalytic Domain
Pancreatitis, Alcoholic
Protein Denaturation
Anion Exchange Protein 1, Erythrocyte
Protein Conformation
Carbonic Anhydrase V
Esterases
Acrolein
Oncogene Proteins v-erbA
Water
Hydrogen Bonding
Erythrocytes
Binding Sites
Cattle
Antiporters
Enzyme Stability
Molecular Sequence Data
Calcium, carbonic anhydrase and gastric acid secretion. (1/207)
Previous data concerning the action of calcium (Ca) on gastric acid secretion (GAS) indicated that calcium ions increase GAS elicited by gastrin released through a vagal mechanism, and also by a direct effect on parietal cells. Our research showed that the stimulating effect of calcium on gastric acid secretion can be antagonized by verapamil administration, which reduces gastric acid secretion . In the present study we followed the effect induced by administration of calcium and Ca-chelating agents (disodium EDTA) on gastric acid secretion and on carbonic anhydrase (CA) activity. We selected two groups of healthy volunteers: Group I (n=21) received a single i.v. dose of CaCl2 (15 mg/kg b.w.), whereas Group II (n=22) received a single i.v. dose of disodium EDTA (5 mg/kg b.w.). We determined blood calcium before and after treatment, gastric acid secretion at 2 hours. erythrocyte CA II activity, and CA IV activity in membrane parietal cells, which were isolated from gastric mucosa obtained by endoscopic biopsy. Assessment of carbonic anhydrase activity was achieved by the stopped-flow method. In Group I calcium administration increased blood calcium, HCl output, CA II and CA IV activity as compared to initial values. In Group II, disodium EDTA reduced blood calcium, HCl output, CA II and CA IV activity as compared to initial values. The results demonstrated that increased blood calcium and GAS values after calcium administration correlated with the increase of erythrocyte CA II and parietal cell CA IV activity, while disodium EDTA induced a reversed process. Our results also show that cytosolic CA II and membrane CA IV values are sensitive to calcium changes and they directly depend on these levels. Our data suggest that intra- and extracellular pH changes induced by carbonic anhydrase might account for the modulation of the physiological and pathological secretory processes in the organism. (+info)A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers. (2/207)
The cytoplasmic carboxyl-terminal domain of AE1, the plasma membrane chloride/bicarbonate exchanger of erythrocytes, contains a binding site for carbonic anhydrase II (CAII). To examine the physiological role of the AE1/CAII interaction, anion exchange activity of transfected HEK293 cells was monitored by following the changes in intracellular pH associated with AE1-mediated bicarbonate transport. AE1-mediated chloride/bicarbonate exchange was reduced 50-60% by inhibition of endogenous carbonic anhydrase with acetazolamide, which indicates that CAII activity is required for full anion transport activity. AE1 mutants, unable to bind CAII, had significantly lower transport activity than wild-type AE1 (10% of wild-type activity), suggesting that a direct interaction was required. To determine the effect of displacement of endogenous wild-type CAII from its binding site on AE1, AE1-transfected HEK293 cells were co-transfected with cDNA for a functionally inactive CAII mutant, V143Y. AE1 activity was maximally inhibited 61 +/- 4% in the presence of V143Y CAII. A similar effect of V143Y CAII was found for AE2 and AE3cardiac anion exchanger isoforms. We conclude that the binding of CAII to the AE1 carboxyl-terminus potentiates anion transport activity and allows for maximal transport. The interaction of CAII with AE1 forms a transport metabolon, a membrane protein complex involved in regulation of bicarbonate metabolism and transport. (+info)Estrogen regulation of ion transporter messenger RNA levels in mouse efferent ductules are mediated differentially through estrogen receptor (ER) alpha and ER beta. (3/207)
Earlier studies have shown that the efferent ductules (ED) of the male mouse are a target for estrogen. The loss of estrogen receptor (ER) function through either knockout technology (alpha ERKO mouse) or chemical interference (pure antagonist, ICI 182 780) results in a failure of a major function of the ED, the reabsorption of testicular fluids. The purpose of this study was to test the hypothesis that estrogen controls fluid (water) reabsorption in the ED by modulating ion transporters important for passive water movement through a leaky epithelium such as the ED. Northern blot analysis was used to detect the mRNA levels for key ion transporters in the following experimental groups: 1) wild-type (WT) control for the 14-day experiment, 2) ER alpha knockout (alpha ERKO) control for the 14-day experiment, 3) WT treated with ICI 182 780 (ICI) for 14 days, 4) alpha ERKO treated with ICI for 14 days, 5) WT control for the 35-day experiment, and 6) WT treated with ICI for 35 days. Estrogen differentially modulated the mRNA levels of key ion transporters. ER alpha mediated carbonic anhydrase II mRNA abundance, and there was a decrease in Na(+)/H(+) exchanger 3 mRNA levels in the alpha ERKO that appeared to be a cellular effect and not a direct estrogen effect. The loss of ER alpha control resulted in an increase in mRNA abundance for the catalytic subunit of Na(+)-K(+) ATPase alpha 1, whereas an increase in the mRNA abundance of the Cl(-)/HCO(3)(-) exchanger and the chloride channel cystic fibrosis transmembrane regulator was significantly ER beta mediated. Our results indicate for the first time that estrogen acting directly and indirectly through both ER alpha and ER beta probably modulates fluid reabsorption in the adult mouse ED by regulating the expression of ion transporters involved in the movement of Na(+) and Cl(-). (+info)Estrogen action and male fertility: roles of the sodium/hydrogen exchanger-3 and fluid reabsorption in reproductive tract function. (4/207)
Estrogen receptor alpha (ER alpha) is essential for male fertility. Its activity is responsible for maintaining epithelial cytoarchitecture in efferent ductules and the reabsorption of fluid for concentrating sperm in the head of the epididymis. These discoveries and others have helped to establish estrogen's bisexual role in reproductive importance. Reported here is the molecular mechanism to explain estrogen's role in fluid reabsorption in the male reproductive tract. It is shown that estrogen regulates expression of the Na(+)/H(+) exchanger-3 (NHE3) and the rate of (22)Na(+) transport, sensitive to an NHE3 inhibitor. Immunohistochemical staining for NHE3, carbonic anhydrase II (CAII), and aquaporin-I (AQP1) was decreased in ER alpha knockout (alpha ERKO) efferent ductules. Targeted gene-deficient mice were compared with alpha ERKO, and the NHE3 knockout and CAII-deficient mice showed alpha ERKO-like fluid accumulation, but only the NHE3 knockout and alpha ERKO mice were infertile. Northern blot analysis showed decreases in mRNA for NHE3 in alpha ERKO and antiestrogen-treated mice. The changes in AQP1 and CAII in alpha ERKO seemed to be secondary because of the disruption of apical cytoarchitecture. Ductal epithelial ultrastructure was abnormal only in alpha ERKO mice. Thus, in the male, estrogen regulates one of the most important epithelial ion transporters and maintains epithelial morphological differentiation in efferent ductules of the male, independent of its regulation of Na(+) transport. Finally, these data raise the possibility of targeting ER alpha in developing a contraceptive for the male. (+info)Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate. (5/207)
The fructose-based sugar sulphamate RWJ-37497, a potent analogue of the widely used anti-epileptic drug topiramate, possesses anti-convulsant and carbonic anhydrase-inhibitory activities. We have studied the binding interactions of RWJ-37497 in the active site of human carbonic anhydrase II by X-ray crystallography. The atomic positions of the enzyme inhibitor complex were refined at a resolution of 2.1 A (1 A=0.1 nm) to the final crystallographic R and R(free) values of 0.18 and 0.23, respectively. The inhibitor co-ordinates to the active-site zinc ion through its oxygen atom and the ionized nitrogen atom of the sulphamate group by replacing the metal-bound water molecules, although the sulphamoyl oxygen atom provides a rather lengthy co-ordination. The 4,5-cyclic sulphate group is positioned in a hydrophobic pocket of the active site, making contacts with the residues Phe-131, Leu-198, Pro-201 and Pro-202. Since the ligand was found to be intact, concerns about RWJ-37947 irreversibly alkylating the enzyme through its 4,5-cyclic sulphate group were dispelled. (+info)Combinatorial computational method gives new picomolar ligands for a known enzyme. (6/207)
Combinatorial small molecule growth algorithm was used to design inhibitors for human carbonic anhydrase II. Two enantiomeric candidate molecules were predicted to bind with high potency (with R isomer binding stronger than S), but in two distinct conformations. The experiments verified that computational predictions concerning the binding affinities and the binding modes were correct for both isomers. The designed R isomer is the best-known inhibitor (K(d) approximately 30 pM) of human carbonic anhydrase II. (+info)In vivo repression of an erythroid-specific gene by distinct corepressor complexes. (7/207)
To assess the mechanisms of repression of the erythroid-specific carbonic anhydrase II (CAII) locus we used chromatin immunoprecipitation and show that an NCoR-histone deacetylase (HDAC)3 complex is recruited by the nuclear receptor v-ErbA to the intronic HS2 enhancer turning it into a potent silencer. Furthermore we demonstrate that efficient CAII silencing requires binding of a MeCP2-targeted HDAC-containing corepressor complex to the hypermethylated CpG-island at the promoter. Activation of transcription by either AZAdC or thyroid hormone results in loss of one of the two corepressor complexes. Thyroid hormone further replaces the enhancer-bound NCoR-corepressor complex by the TRAP220 coactivator. Treatment with the HDAC inhibitor trichostatin A (TSA) causes activation of CAII transcription and histone H3 and H4 hyperacetylation at the enhancer, apparently without affecting binding of the two corepressor complexes. Unexpectedly, histone H3 and H4 at the fully repressed promoter are already hyperacetylated despite the close apposition of the MeCP2-targeted HDAC complex. Acetylation of histone H4, but not H3, at the promoter is moderately increased following TSA treatment. Our data suggest that the hyperacetylated but repressed CAII promoter is (partially) remodeled and primed for activation in v-ErbA-transformed cells. (+info)Induction of oligodendrocyte-like properties in a primitive hypothalamic cell line by cholesterol, an eye derived growth factor and brain extract. (8/207)
A serum-free medium has been devised which permits proliferation of the mouse primitive nervous cell line F7. When cholesterol, eye-derived growth factor and brain extract are added in this medium for 48 h, 80-90% of oligodendrocyte-like cells are generated. These cells have diminished substrate adhesion. They acquire the capacity to synthesize carbonic anhydrase II and myelin basic protein, two specific proteins of oligodendrocytes. These observations suggest that F7 clonal cell line, which has been previously shown to be a neurophysin cell precursor, is also a precursor for oligodendrocytes, and represents a bipotent stem cell line for both neuronal and glial cell lineages. (+info)Carbonic anhydrase II (CA-II) is a specific isoform of the carbonic anhydrase enzyme, which catalyzes the reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme plays a crucial role in various physiological processes, including pH regulation, electrolyte balance, and biosynthetic reactions.
CA-II is widely distributed in the body, with high concentrations found in erythrocytes (red blood cells), the gastric mucosa, and renal tubules. In erythrocytes, CA-II facilitates the rapid conversion of carbon dioxide generated during cellular respiration to bicarbonate and protons, which can then be transported across the cell membrane for excretion or used in other metabolic processes.
In the gastric mucosa, CA-II helps regulate acid secretion by catalyzing the formation of carbonic acid from water and carbon dioxide, which subsequently dissociates into bicarbonate and a proton. The generated proton can then participate in the production of hydrochloric acid in the stomach.
In renal tubules, CA-II is involved in the reabsorption of bicarbonate ions from the filtrate back into the bloodstream, helping maintain electrolyte balance and pH homeostasis. Additionally, CA-II has been implicated in several pathological conditions, such as neurological disorders, cancer, and osteoporosis, making it a potential therapeutic target for drug development.
Carbonic anhydrases (CAs) are a group of enzymes that catalyze the reversible reaction between carbon dioxide and water to form carbonic acid, which then quickly dissociates into bicarbonate and a proton. This reaction is crucial for maintaining pH balance and regulating various physiological processes in the body, including respiration, secretion of electrolytes, and bone resorption.
There are several isoforms of carbonic anhydrases found in different tissues and organelles, each with distinct functions and properties. For example, CA I and II are primarily found in red blood cells, while CA III is present in various tissues such as the kidney, lung, and eye. CA IV is a membrane-bound enzyme that plays a role in transporting ions across cell membranes.
Carbonic anhydrases have been targeted for therapeutic interventions in several diseases, including glaucoma, epilepsy, and cancer. Inhibitors of carbonic anhydrases can reduce the production of bicarbonate and lower the pH of tumor cells, which may help to slow down their growth and proliferation. However, these inhibitors can also have side effects such as kidney stones and metabolic acidosis, so they must be used with caution.
Carbonic anhydrase inhibitors are a class of medications that work by blocking the action of carbonic anhydrase, an enzyme that is responsible for converting carbon dioxide and water into carbonic acid. This enzyme is found in various tissues throughout the body, including the eyes, kidneys, and nervous system.
By inhibiting the activity of carbonic anhydrase, these medications can reduce the production of bicarbonate ions in the body, which helps to lower the rate of fluid buildup in certain tissues. As a result, carbonic anhydrase inhibitors are often used to treat conditions such as glaucoma, epilepsy, and altitude sickness.
In glaucoma, for example, these medications can help to reduce pressure within the eye by promoting the drainage of fluid from the eye. In epilepsy, carbonic anhydrase inhibitors can help to reduce the frequency and severity of seizures by reducing the acidity of the blood and brain. And in altitude sickness, these medications can help to alleviate symptoms such as headache, nausea, and shortness of breath by reducing the buildup of fluid in the lungs.
Some common examples of carbonic anhydrase inhibitors include acetazolamide, methazolamide, and dorzolamide. These medications are available in various forms, including tablets, capsules, and eye drops, and are typically prescribed by a healthcare professional.
Carbonic anhydrase III (CAIII) is a member of the carbonic anhydrase enzyme family, which catalyzes the reversible reaction between carbon dioxide and water to form bicarbonate and protons. This enzyme is primarily found in muscle tissues, where it plays a role in regulating pH levels during muscle contraction and relaxation. CAIII has a lower catalytic activity compared to other carbonic anhydrase isoforms, suggesting that it may have additional functions beyond simple CO2 hydration. Additionally, CAIII has been implicated in various physiological processes such as protection against oxidative stress and regulation of muscle metabolism.
Ethoxzolamide is a carbonic anhydrase inhibitor drug that is primarily used to reduce fluid buildup in the eye (ocular pressure) caused by glaucoma or other conditions. It works by decreasing the production of fluid inside the eye, which helps lower the pressure within the eye.
Ethoxzolamide may also be used for other medical purposes, such as treating seizure disorders and preventing altitude sickness. The drug is available in oral tablet form and is typically taken 2-3 times a day.
It's important to note that Ethoxzolamide can have side effects, including frequent urination, tingling sensations in the hands or feet, loss of appetite, and changes in taste perception. It may also interact with other medications, so it's essential to inform your healthcare provider about all the drugs you are taking before starting Ethoxzolamide therapy.
Acetazolamide is a medication that belongs to a class of drugs called carbonic anhydrase inhibitors. It works by decreasing the production of bicarbonate in the body, which helps to reduce the amount of fluid in the eye and brain, making it useful for treating conditions such as glaucoma and epilepsy.
In medical terms, acetazolamide can be defined as: "A carbonic anhydrase inhibitor that is used to treat glaucoma, epilepsy, altitude sickness, and other conditions. It works by decreasing the production of bicarbonate in the body, which helps to reduce the amount of fluid in the eye and brain."
Acetazolamide may also be used for other purposes not listed here, so it is important to consult with a healthcare provider for specific medical advice.
Carbonic anhydrase I is a specific type of carbonic anhydrase, which is an enzyme that catalyzes the reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme is primarily found in red blood cells and plays a crucial role in maintaining pH balance and regulating respiration.
Carbonic anhydrase I, also known as CA I or CA-I, is responsible for hydrating carbon dioxide to form bicarbonate ions and protons, which helps maintain the acid-base balance in the body. It has a relatively slower reaction rate compared to other carbonic anhydrase isoforms.
Defects or mutations in the CA I gene can lead to reduced enzymatic activity and may contribute to certain medical conditions, such as distal renal tubular acidosis (dRTA), a disorder characterized by impaired kidney function and acid-base imbalances. However, other carbonic anhydrase isoforms can compensate for the loss of CA I activity in most cases, so its deficiency rarely causes severe symptoms on its own.
Carbonic anhydrase IV (CA-IV), also known as membrane-associated carbonic anhydrase or CA-IX, is a member of the carbonic anhydrase enzyme family. This enzyme is responsible for catalyzing the reversible reaction that converts carbon dioxide and water into bicarbonate and a proton.
CA-IV is primarily found in the plasma membrane of polarized epithelial cells, where it plays a crucial role in maintaining acid-base balance and ion transport. It is also involved in various physiological processes, including respiration, bone resorption, and pH regulation.
Abnormalities in CA-IV expression or activity have been implicated in several diseases, such as cancer, kidney stones, and osteoporosis. In particular, overexpression of CA-IV has been observed in various types of cancer, where it contributes to tumor acidification, invasion, and metastasis. Therefore, CA-IV is considered a potential therapeutic target for cancer treatment.
Methazolamide is a sulfonamide-derived carbonic anhydrase inhibitor primarily used in the prevention and treatment of glaucoma. It works by decreasing the production of fluid inside the eye, which in turn lowers the pressure within the eye. Additionally, it has been used off-label for conditions such as altitude sickness, epilepsy, intracranial hypertension, and benign prostatic hyperplasia.
The medical definition of Methazolamide is:
A carbonic anhydrase inhibitor that reduces the secretion of aqueous humor, thereby lowering intraocular pressure; used in the treatment of glaucoma. It also has diuretic properties and has been used in the management of altitude sickness, epilepsy, intracranial hypertension, and benign prostatic hyperplasia.
Renal tubular acidosis (RTA) is a medical condition that occurs when the kidneys are unable to properly excrete acid into the urine, leading to an accumulation of acid in the bloodstream. This results in a state of metabolic acidosis.
There are several types of RTA, but renal tubular acidosis type 1 (also known as distal RTA) is characterized by a defect in the ability of the distal tubules to acidify the urine, leading to an inability to lower the pH of the urine below 5.5, even in the face of metabolic acidosis. This results in a persistently alkaline urine, which can lead to calcium phosphate stones and bone demineralization.
Type 1 RTA is often caused by inherited genetic defects, but it can also be acquired due to various kidney diseases, drugs, or autoimmune disorders. Symptoms of type 1 RTA may include fatigue, weakness, muscle cramps, decreased appetite, and vomiting. Treatment typically involves alkali therapy to correct the acidosis and prevent complications.
Osteopetrosis, also known as Albers-Schönberg disease or marble bone disease, is a group of rare genetic disorders characterized by increased bone density due to impaired bone resorption by osteoclasts. This results in brittle bones that are more susceptible to fractures and can also lead to various complications such as anemia, hearing loss, and vision problems. There are several types of osteopetrosis, which vary in severity and age of onset.
The medical definition of osteopetrosis is:
A genetic disorder characterized by defective bone resorption due to impaired osteoclast function, resulting in increased bone density, susceptibility to fractures, and potential complications such as anemia, hearing loss, and vision problems.
Bicarbonates, also known as sodium bicarbonate or baking soda, is a chemical compound with the formula NaHCO3. In the context of medical definitions, bicarbonates refer to the bicarbonate ion (HCO3-), which is an important buffer in the body that helps maintain normal pH levels in blood and other bodily fluids.
The balance of bicarbonate and carbonic acid in the body helps regulate the acidity or alkalinity of the blood, a condition known as pH balance. Bicarbonates are produced by the body and are also found in some foods and drinking water. They work to neutralize excess acid in the body and help maintain the normal pH range of 7.35 to 7.45.
In medical testing, bicarbonate levels may be measured as part of an electrolyte panel or as a component of arterial blood gas (ABG) analysis. Low bicarbonate levels can indicate metabolic acidosis, while high levels can indicate metabolic alkalosis. Both conditions can have serious consequences if not treated promptly and appropriately.
Benzolamide is not a recognized medication or pharmaceutical agent in modern medical practice. It is possible that you may have misspelled the name, and there are no direct synonyms for any known medications. If you meant to search for a different term or have more information about the context where this term was used, please let me know so I can provide a more accurate response.
Carbon dioxide (CO2) is a colorless, odorless gas that is naturally present in the Earth's atmosphere. It is a normal byproduct of cellular respiration in humans, animals, and plants, and is also produced through the combustion of fossil fuels such as coal, oil, and natural gas.
In medical terms, carbon dioxide is often used as a respiratory stimulant and to maintain the pH balance of blood. It is also used during certain medical procedures, such as laparoscopic surgery, to insufflate (inflate) the abdominal cavity and create a working space for the surgeon.
Elevated levels of carbon dioxide in the body can lead to respiratory acidosis, a condition characterized by an increased concentration of carbon dioxide in the blood and a decrease in pH. This can occur in conditions such as chronic obstructive pulmonary disease (COPD), asthma, or other lung diseases that impair breathing and gas exchange. Symptoms of respiratory acidosis may include shortness of breath, confusion, headache, and in severe cases, coma or death.
Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.
Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.
In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.
Dansyl compounds are fluorescent compounds that contain a dansyl group, which is a chemical group made up of a sulfonated derivative of dimethylaminonaphthalene. These compounds are often used as tracers in biochemical and medical research because they emit bright fluorescence when excited by ultraviolet or visible light. This property makes them useful for detecting and quantifying various biological molecules, such as amino acids, peptides, and proteins, in a variety of assays and techniques, including high-performance liquid chromatography (HPLC), thin-layer chromatography (TLC), and fluorescence microscopy.
The dansyl group can be attached to biological molecules through chemical reactions that involve the formation of covalent bonds between the sulfonate group in the dansyl compound and amino, thiol, or hydroxyl groups in the target molecule. The resulting dansylated molecules can then be detected and analyzed using various techniques.
Dansyl compounds are known for their high sensitivity, stability, and versatility, making them valuable tools in a wide range of research applications. However, it is important to note that the use of dansyl compounds requires careful handling and appropriate safety precautions, as they can be hazardous if mishandled or ingested.
Sodium-bicarbonate symporters, also known as sodium bicarbonate co-transporters, are membrane transport proteins that facilitate the movement of both sodium ions (Na+) and bicarbonate ions (HCO3-) across the cell membrane in the same direction. These transporters play a crucial role in maintaining acid-base balance in the body by regulating the concentration of bicarbonate ions, which is an important buffer in the blood and other bodily fluids.
The term "symporter" refers to the fact that these proteins transport two or more different molecules or ions in the same direction across a membrane. In this case, sodium-bicarbonate symporters co-transport one sodium ion and one bicarbonate ion together, usually using a concentration gradient of sodium to drive the uptake of bicarbonate.
These transporters are widely expressed in various tissues, including the kidneys, where they help reabsorb bicarbonate ions from the urine back into the bloodstream, and the gastrointestinal tract, where they contribute to the absorption of sodium and bicarbonate from food and drink. Dysfunction of sodium-bicarbonate symporters has been implicated in several diseases, including renal tubular acidosis and hypertension.
Zinc is an essential mineral that is vital for the functioning of over 300 enzymes and involved in various biological processes in the human body, including protein synthesis, DNA synthesis, immune function, wound healing, and cell division. It is a component of many proteins and participates in the maintenance of structural integrity and functionality of proteins. Zinc also plays a crucial role in maintaining the sense of taste and smell.
The recommended daily intake of zinc varies depending on age, sex, and life stage. Good dietary sources of zinc include red meat, poultry, seafood, beans, nuts, dairy products, and fortified cereals. Zinc deficiency can lead to various health problems, including impaired immune function, growth retardation, and developmental delays in children. On the other hand, excessive intake of zinc can also have adverse effects on health, such as nausea, vomiting, and impaired immune function.
X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.
Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.
Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.
Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.
Histidine is an essential amino acid, meaning it cannot be synthesized by the human body and must be obtained through dietary sources. Its chemical formula is C6H9N3O2. Histidine plays a crucial role in several physiological processes, including:
1. Protein synthesis: As an essential amino acid, histidine is required for the production of proteins, which are vital components of various tissues and organs in the body.
2. Hemoglobin synthesis: Histidine is a key component of hemoglobin, the protein in red blood cells responsible for carrying oxygen throughout the body. The imidazole side chain of histidine acts as a proton acceptor/donor, facilitating the release and uptake of oxygen by hemoglobin.
3. Acid-base balance: Histidine is involved in maintaining acid-base homeostasis through its role in the biosynthesis of histamine, which is a critical mediator of inflammatory responses and allergies. The decarboxylation of histidine results in the formation of histamine, which can increase vascular permeability and modulate immune responses.
4. Metal ion binding: Histidine has a high affinity for metal ions such as zinc, copper, and iron. This property allows histidine to participate in various enzymatic reactions and maintain the structural integrity of proteins.
5. Antioxidant defense: Histidine-containing dipeptides, like carnosine and anserine, have been shown to exhibit antioxidant properties by scavenging reactive oxygen species (ROS) and chelating metal ions. These compounds may contribute to the protection of proteins and DNA from oxidative damage.
Dietary sources of histidine include meat, poultry, fish, dairy products, and wheat germ. Histidine deficiency is rare but can lead to growth retardation, anemia, and impaired immune function.
In the context of medicine, particularly in relation to cancer treatment, protons refer to positively charged subatomic particles found in the nucleus of an atom. Proton therapy, a type of radiation therapy, uses a beam of protons to target and destroy cancer cells with high precision, minimizing damage to surrounding healthy tissue. The concentrated dose of radiation is delivered directly to the tumor site, reducing side effects and improving quality of life during treatment.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.
A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.
In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.
Alcoholic pancreatitis is a specific type of pancreatitis, which is inflammation of the pancreas. This condition is caused by excessive and prolonged consumption of alcohol. The exact mechanism by which alcohol induces pancreatitis is not fully understood, but it is believed that alcohol causes damage to the cells of the pancreas, leading to inflammation. This can result in abdominal pain, nausea, vomiting, fever, and increased heart rate. Chronic alcoholic pancreatitis can also lead to serious complications such as diabetes, malnutrition, and pancreatic cancer. Treatment typically involves supportive care, such as hydration, pain management, and nutritional support, along with abstinence from alcohol. In severe cases, surgery may be necessary to remove damaged tissue or to relieve blockages in the pancreas.
Protein denaturation is a process in which the native structure of a protein is altered, leading to loss of its biological activity. This can be caused by various factors such as changes in temperature, pH, or exposure to chemicals or radiation. The three-dimensional shape of a protein is crucial for its function, and denaturation causes the protein to lose this shape, resulting in impaired or complete loss of function. Denaturation is often irreversible and can lead to the aggregation of proteins, which can have negative effects on cellular function and can contribute to diseases such as Alzheimer's and Parkinson's.
Anion Exchange Protein 1, Erythrocyte (AE1), also known as Band 3 protein or SLC4A1, is a transmembrane protein found in the membranes of red blood cells (erythrocytes). It plays a crucial role in maintaining the pH and bicarbonate levels of the blood by facilitating the exchange of chloride ions (Cl-) with bicarbonate ions (HCO3-) between the red blood cells and the plasma.
The anion exchange protein 1 is composed of three major domains: a cytoplasmic domain, a transmembrane domain, and an extracellular domain. The cytoplasmic domain interacts with various proteins involved in regulating the cytoskeleton of the red blood cell, while the transmembrane domain contains the ion exchange site. The extracellular domain is responsible for the interaction between red blood cells and contributes to their aggregation.
Mutations in the AE1 gene can lead to various inherited disorders, such as hereditary spherocytosis, Southeast Asian ovalocytosis, and distal renal tubular acidosis type 1. These conditions are characterized by abnormal red blood cell shapes, impaired kidney function, or both.
Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.
Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.
Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.
I apologize, but there seems to be no medical definition for "Carbonic Anhydrase V." Carbonic anhydrases are a family of enzymes that catalyze the reversible hydration of carbon dioxide to form bicarbonate and protons. There are several isoforms of carbonic anhydrase (CA I-IV, CA VI-VIII, etc.), but as far as current scientific knowledge and literature go, there isn't a recognized or well-established isoform called Carbonic Anhydrase V.
It is possible that you may have encountered a mistake or typographical error in your source material. If you have more context or information about where you found this term, I would be happy to help you further research the topic.
Sulfonamides are a group of synthetic antibacterial drugs that contain the sulfonamide group (SO2NH2) in their chemical structure. They are bacteriostatic agents, meaning they inhibit bacterial growth rather than killing them outright. Sulfonamides work by preventing the bacteria from synthesizing folic acid, which is essential for their survival.
The first sulfonamide drug was introduced in the 1930s and since then, many different sulfonamides have been developed with varying chemical structures and pharmacological properties. They are used to treat a wide range of bacterial infections, including urinary tract infections, respiratory tract infections, skin and soft tissue infections, and ear infections.
Some common sulfonamide drugs include sulfisoxazole, sulfamethoxazole, and trimethoprim-sulfamethoxazole (a combination of a sulfonamide and another antibiotic called trimethoprim). While sulfonamides are generally safe and effective when used as directed, they can cause side effects such as rash, nausea, and allergic reactions. It is important to follow the prescribing physician's instructions carefully and to report any unusual symptoms or side effects promptly.
Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds in esters, producing alcohols and carboxylic acids. They are widely distributed in plants, animals, and microorganisms and play important roles in various biological processes, such as metabolism, digestion, and detoxification.
Esterases can be classified into several types based on their substrate specificity, including carboxylesterases, cholinesterases, lipases, and phosphatases. These enzymes have different structures and mechanisms of action but all share the ability to hydrolyze esters.
Carboxylesterases are the most abundant and diverse group of esterases, with a wide range of substrate specificity. They play important roles in the metabolism of drugs, xenobiotics, and lipids. Cholinesterases, on the other hand, specifically hydrolyze choline esters, such as acetylcholine, which is an important neurotransmitter in the nervous system. Lipases are a type of esterase that preferentially hydrolyzes triglycerides and plays a crucial role in fat digestion and metabolism. Phosphatases are enzymes that remove phosphate groups from various molecules, including esters, and have important functions in signal transduction and other cellular processes.
Esterases can also be used in industrial applications, such as in the production of biodiesel, detergents, and food additives. They are often produced by microbial fermentation or extracted from plants and animals. The use of esterases in biotechnology is an active area of research, with potential applications in biofuel production, bioremediation, and medical diagnostics.
Acrolein is an unsaturated aldehyde with the chemical formula CH2CHCHO. It is a colorless liquid that has a distinct unpleasant odor and is highly reactive. Acrolein is produced by the partial oxidation of certain organic compounds, such as glycerol and fatty acids, and it is also found in small amounts in some foods, such as coffee and bread.
Acrolein is a potent irritant to the eyes, nose, and throat, and exposure to high levels can cause coughing, wheezing, and shortness of breath. It has been shown to have toxic effects on the lungs, heart, and nervous system, and prolonged exposure has been linked to an increased risk of cancer.
In the medical field, acrolein is sometimes used as a laboratory reagent or as a preservative for biological specimens. However, due to its potential health hazards, it must be handled with care and appropriate safety precautions should be taken when working with this compound.
The oncogene proteins v-erbA are a subset of oncogenes that were initially discovered in retroviruses, specifically the avian erythroblastosis virus (AEV). These oncogenes are derived from normal cellular genes called proto-oncogenes, which play crucial roles in various cellular processes such as growth, differentiation, and survival.
The v-erbA oncogene protein is a truncated and mutated version of the thyroid hormone receptor alpha (THRA) gene, which is a nuclear receptor that regulates gene expression in response to thyroid hormones. The v-erbA protein can bind to DNA but cannot interact with thyroid hormones, leading to aberrant regulation of gene expression and uncontrolled cell growth, ultimately resulting in cancer.
In particular, the v-erbA oncogene has been implicated in the development of erythroblastosis, a disease characterized by the proliferation of immature red blood cells, leading to anemia and other symptoms. The activation of the v-erbA oncogene can also contribute to the development of other types of cancer, such as leukemia and lymphoma.
Medical definitions of water generally describe it as a colorless, odorless, tasteless liquid that is essential for all forms of life. It is a universal solvent, making it an excellent medium for transporting nutrients and waste products within the body. Water constitutes about 50-70% of an individual's body weight, depending on factors such as age, sex, and muscle mass.
In medical terms, water has several important functions in the human body:
1. Regulation of body temperature through perspiration and respiration.
2. Acting as a lubricant for joints and tissues.
3. Facilitating digestion by helping to break down food particles.
4. Transporting nutrients, oxygen, and waste products throughout the body.
5. Helping to maintain healthy skin and mucous membranes.
6. Assisting in the regulation of various bodily functions, such as blood pressure and heart rate.
Dehydration can occur when an individual does not consume enough water or loses too much fluid due to illness, exercise, or other factors. This can lead to a variety of symptoms, including dry mouth, fatigue, dizziness, and confusion. Severe dehydration can be life-threatening if left untreated.
Hydrogen bonding is not a medical term per se, but it is a fundamental concept in chemistry and biology that is relevant to the field of medicine. Here's a general definition:
Hydrogen bonding is a type of attractive force between molecules or within a molecule, which occurs when a hydrogen atom is bonded to a highly electronegative atom (like nitrogen, oxygen, or fluorine) and is then attracted to another electronegative atom. This attraction results in the formation of a partially covalent bond known as a "hydrogen bond."
In biological systems, hydrogen bonding plays a crucial role in the structure and function of many biomolecules, such as DNA, proteins, and carbohydrates. For example, the double helix structure of DNA is stabilized by hydrogen bonds between complementary base pairs (adenine-thymine and guanine-cytosine). Similarly, the three-dimensional structure of proteins is maintained by a network of hydrogen bonds that help to determine their function.
In medical contexts, hydrogen bonding can be relevant in understanding drug-receptor interactions, where hydrogen bonds between a drug molecule and its target protein can enhance the binding affinity and specificity of the interaction, leading to more effective therapeutic outcomes.
Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.
Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.
In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.
Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Protein folding is the process by which a protein molecule naturally folds into its three-dimensional structure, following the synthesis of its amino acid chain. This complex process is determined by the sequence and properties of the amino acids, as well as various environmental factors such as temperature, pH, and the presence of molecular chaperones. The final folded conformation of a protein is crucial for its proper function, as it enables the formation of specific interactions between different parts of the molecule, which in turn define its biological activity. Protein misfolding can lead to various diseases, including neurodegenerative disorders such as Alzheimer's and Parkinson's disease.
"Cattle" is a term used in the agricultural and veterinary fields to refer to domesticated animals of the genus *Bos*, primarily *Bos taurus* (European cattle) and *Bos indicus* (Zebu). These animals are often raised for meat, milk, leather, and labor. They are also known as bovines or cows (for females), bulls (intact males), and steers/bullocks (castrated males). However, in a strict medical definition, "cattle" does not apply to humans or other animals.
Antiporters, also known as exchange transporters, are a type of membrane transport protein that facilitate the exchange of two or more ions or molecules across a biological membrane in opposite directions. They allow for the movement of one type of ion or molecule into a cell while simultaneously moving another type out of the cell. This process is driven by the concentration gradient of one or both of the substances being transported. Antiporters play important roles in various physiological processes, including maintaining electrochemical balance and regulating pH levels within cells.
Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.
Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Carbonic anhydrase II
Carbonic anhydrase inhibitor
Carbonic anhydrase
Carbonic anhydrase VI
Carbonic anhydrase 5B, mitochondrial
Progestogen ester
Progesterone 3-acetyl enol ether
William S. Sly
Polmacoxib
Band 3 anion transport protein
Anion exchange protein 3
Brinzolamide
Anion exchanger family
Renal tubular acidosis
Sodium-hydrogen antiporter 1
Thalassiosira weissflogii
Electrogenic sodium bicarbonate cotransporter 1
Chloride anion exchanger
Sodium bicarbonate cotransporter 3
Electroneutral sodium bicarbonate exchanger 1
Topiramate
Carbonic anhydrase 4
Estradiol sulfamate
Anion exchange protein 2
Carbonic anhydrase 9
Acetazolamide
Carbonic anhydrase 12
Dynamic combinatorial chemistry
Carbonic anhydrase 14
CA11
Carbonic anhydrase II - Wikipedia
CA2 carbonic anhydrase 2 [Homo sapiens (human)] - Gene - NCBI
Chain A, Carbonic anhydrase 2 (human) | Protein Target - PubChem
Chain A, CARBONIC ANHYDRASE II (human) | Protein Target - PubChem
Carbonic Anhydrase II Recombinant Monoclonal Antibody (ARC1451) (MA5-38188) ...
RCSB PDB - 3M98: Crystal structure of human carbonic anhydrase isozyme II with 5-(1H-benzimidazol-1-ylacetyl)-2...
PRIME PubMed | Thyroxine affects expression of KSPG-related genes, the carbonic anhydrase II gene, and KS sulfation in the...
References: Thermodynamic, Kinetic and Crystallographic Investigations of Benzenesulfonamides as Ligands of Human Carbonic...
Screening Derivatized Peptide Libraries for Tight Binding Inhibitors to Carbonic Anhydrase II by Electrospray Ionization-Mass...
17b -estradiol suppresses gene expression of tartrate resistant acid phosphatase and carbonic anhydrase II in ovariectomized...
4Q08: Crystal structure of chimeric carbonic anhydrase XII with inhibitor
RCSB PDB - 2VVA: Human carbonic anhydrase in complex with CO2
Carbonic Anhydrase I Isoelectric focusing marker, pI 6.6 9001-03-0
Dual carbonic anhydrase and cyclooxygenase-2 inhibition<...
Carbonic Anhydrase II/CA2 Recombinant Protein (RPES2820)
Etiology
PDB 5NY1 | Chain CARBONIC ANHYDRASE II INHIBITOR RA10 | 5NY1 A | 3D Structure | canSARS
Zinc in PDB 1yo2: Proton Transfer From HIS200 in Human Carbonic Anhydrase II
Carbonic anhydrase II deficiency syndrome with amelogenesis imperfecta linked to a homozygous |i|CA2...
1okm.1 | SWISS-MODEL Template Library
Inhibition of carbonic anhydrase II by steroidal and non-steroidal sulphamates. - Department of Pharmacology
1if8.1 | SWISS-MODEL Template Library
Unilateral Glaucoma Medication: Beta-adrenergic blockers, Alpha 2-adrenergic agonists, Carbonic anhydrase inhibitors,...
Identification and Measurement of Carbonic Anhydrase-II Molecule Numbers in the Rat Carotid Body [Abstract]
Inhibition properties of some flavonoids on carbonic anhydrase I, and II isoenzymes purified human erythrocytes | AVESİS
Primary Duodenal Adenocarcinoma Expressing Carbonic Anhydrase IX. | Case Rep Gastroenterol;16(2): 308-312, 2022. | MEDLINE
Copper(II) sulfonamide complexes having enzyme inhibition activities on carbonic anhydrase I: synthesis, characterization and...
CAH14-2-E - Carbonic Anhydrase XIV (cluster #2 Of 8), Eukaryotic | ZINC Is Not Commercial - A database of commercially...
Discovery of 4-sulfamoyl-phenyl-β-lactams as a new class of potent carbonic anhydrase isoforms I, II, IV and VII inhibitors:...
Salts of 5-amino-2-sulfonamide-1,3,4-thiadiazole, a structural and analog of acetazolamide, show interesting carbonic anhydrase...
Inhibitors6
- This paper describes the use of electrospray ionization-mass spectrometry (ESI-MS) to screen two libraries of soluble compounds to search for tight binding inhibitors for carbonic anhydrase II (EC 4.2.1.1). (figshare.com)
- Medications used to decrease aqueous production include beta-blockers (topical), carbonic anhydrase inhibitors (topical and/or oral), and alpha 2-agonists. (medscape.com)
- Hydroxamate Represents A Versatile Zinc Binding Group For the Development of New Carbonic Anhydrase Inhibitors. (atomistry.com)
- The p-toluensulfonate, the methylsulfonate, and the chlorhydrate monohydrate salts of Hats were evaluated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs) and as anticonvulsants and diuretics, since many CAIs are clinically used as pharmacological agents. (conicet.gov.ar)
- Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV. (proteopedia.org)
- Comment: Carbonic anhydrase inhibitors (CAIs) and salicylates inhibit each other's renal tubular secretion, resulting in increased plasma levels. (medscape.com)
Hydration of carbon dioxide4
- Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. (wikipedia.org)
- The protein encoded by this gene is one of several isozymes of carbonic anhydrase, which catalyzes reversible hydration of carbon dioxide. (nih.gov)
- Carbonic anhydrase, a zinc metalloenzyme, catalyzes the reversible hydration of carbon dioxide to bicarbonate. (rcsb.org)
- Catalyzes reversible reaction involving hydration of carbon dioxide and dehydration of carbonic acid. (medscape.com)
Isoforms3
- Two transcript variants encoding different isoforms have been found for this gene. (nih.gov)
- The human (h) isoforms hCA I, II, IV, VII, IX, and XII were inhibited in their micromolar range by these salts, whereas pathogenic beta and gamma CAs showed similar, weak inhibitory profiles. (conicet.gov.ar)
- Inhibition of various human carbonic anhydrase isoforms (I, II, IX and XII) was tested with the 'cold', non-radiolabelled complexes, and compared with an acetazolamide standard (AZA). (bath.ac.uk)
Isozymes1
- CA2 is one of several (at least 7) isozymes of carbonic anhydrase. (thermofisher.com)
Inhibition studies2
- Characterization, bioinformatic analysis and dithiocarbamate inhibition studies of two new α-carbonic anhydrases, CAH1 and CAH2, from the fruit fly Drosophila melanogaster. (unifi.it)
- Characterization, bioinformatic analysis and dithiocarbamate inhibition studies of two new α-carbonic anhydrases, CAH1 and CAH2, from the fruit fly Drosophila melanogaster / L. Syrjänen;M. E. E;M. Hilvo;D. Vullo;F. Carta;C. T. Supuran;S. Parkkila. (unifi.it)
Isoenzymes1
- In general, sulfonamides and their derivatives are researched for their inhibitory effects on carbonic anhydrase isoenzymes (CAs). (gazi.edu.tr)
Synthesis1
- Thyroxine modifies expressions of KSPG synthesis and carbonic anhydrase genes. (unboundmedicine.com)
Inhibitory1
- Study of glycation process of human carbonic anhydrase II as well as investigation concerning inhibitory influence of 3-beta-hydroxybutyrate on it. (nih.gov)
CAII1
- Carbonic anhydrase 2 (CAII) supports tumor blood endothelial cell survival under lactic acidosis in the tumor microenvironment. (nih.gov)
Carbonate1
- The carbonic anhydrases (or carbonate dehydratases) are classified as metalloenzyme for its zinc ion prosthetic group and form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons, a reversible reaction that takes part in maintaining acid-base balance in blood and other tissues. (assaygenie.com)
Renal tubular3
- A distinct form of osteopetrosis occurs in association with renal tubular acidosis and cerebral calcification due to carbonic anhydrase isoenzyme II deficiency. (medscape.com)
- also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. (proteopedia.org)
- Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation. (proteopedia.org)
Enzyme4
- Among tested compounds, bis-(5-nitro-2 furaldehydemethanesulfonylhydrazone) copper(II) chloride was found to be the most active complex on CA I isoenzyme with IC50 value of 7.03 x 10(-5) M. The enzyme inhibition trends of copper(II) sulfonamides on CA I isoenzyme were also investigated by CV and differential pulse voltammetry (DPV) techniques, qualitatively. (gazi.edu.tr)
- Here, a systematic approach to investigate the effect of an active-site-residue mutation on a model enzyme, human carbonic anhydrase II (CA II), is described. (iucr.org)
- In this study, we describe the effect of a single amino-acid variation on a prototypical enzyme, human carbonic anhydrase II (CA II), by correlating its high-resolution reaction-intermediate structures with the measured kinetic parameters. (iucr.org)
- This radiolabeled monoclonal antibody from Telix Pharmaceuticals targets carbonic anhydrase IX (CAIX), an enzyme that regulates cell proliferation and is highly expressed in many tumor types. (medscape.com)
Reversible1
- Catalyzes a reversible reaction where carbon dioxide becomes hydrated and carbonic acid dehydrated. (medscape.com)
Intracellular2
Abstract1
- abstract = "Carbonic anhydrase IX (CA IX) is currently generating great interest as a marker of tumour hypoxia and a potential chemotherapeutic target. (bath.ac.uk)
Deficiency syndrome2
- A, p.W123X) linked to carbonic anhydrase II deficiency syndrome in a Chinese family. (nih.gov)
- Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis. (proteopedia.org)
Osteopetrosis2
- Loss of carbonic anhydrase activity in bones impairs the ability of osteoclasts to promote bone resorption, leading to osteopetrosis. (wikipedia.org)
- The classification of osteopetrosis shown above is purely clinical and must be supplemented by the molecular insights gained from animal models (see Table 2, in Etiology). (medscape.com)
Gene2
- Carbonic anhydrase II (gene name CA2), is one of sixteen forms of human α carbonic anhydrases. (wikipedia.org)
- Molecular characterization and gene expression of lhcb5 gene encoding CP26 in the light-harvesting complex II of Chlamydomonas reinhardtii. (bio.net)
Monoclonal2
- The following product was used in this experiment: Carbonic Anhydrase II Recombinant Rabbit Monoclonal Antibody (ARC1451) from Thermo Fisher Scientific, catalog # MA5-38188, RRID AB_2898105. (thermofisher.com)
- Samples were incubated with Carbonic Anhydrase II Monoclonal antibody (Product # MA5-38188) using a dilution of 1:1,000, followed by HRP Goat Anti-Rabbit IgG (H+L) at a dilution of 1:10,000. (thermofisher.com)
Protein7
- Carbonic Anhydrase I from human erythrocytes is a protein which is used as a standard pI (isoelectric point) marker for isoelectric focussing experiments. (sigmaaldrich.com)
- Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. (assaygenie.com)
- a 31 kDa protein band was determined which reacted with a rabbit polyclonal antibody specific for rat CA-II in Western blot analysis. (openrespiratorymedicinejournal.com)
- The immunoreactive 31 kDa CA-II protein was detected and quantified by laser scanner densitometry using 125 I-rProtein A as a tracer. (openrespiratorymedicinejournal.com)
- Background Carbonic anhydrase (CA) IX is normally a surface-expressed protein that's upregulated from the hypoxia inducible factor (HIF) and represents a prototypic tumor-associated antigen that's overexpressed about renal cell carcinoma (RCC). (monossabios.com)
- Functionalization of the foldamers by a nanomolar ligand of human carbonic anhydrase II (HCA) ensured that they would be held in close proximity to the protein surface. (proteopedia.org)
- ER protein determinations were performed using two-thirds of all breast cancers are ER at the time of diagnosis, the standard methods in the routine clinical laboratory (9). (lu.se)
Cyanamide1
- Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction? (proteopedia.org)
Zinc3
- Structure-based design of a sulfonamide probe for fluorescence anisotropy detection of zinc with a carbonic anhydrase-based biosensor. (expasy.org)
- In the CO 2 -hydration direction, the first step of catalysis is the conversion of CO 2 into HCO 3 − via the nucleophilic attack of a zinc-bound hydroxide. (iucr.org)
- The second step involves the transfer of a proton from the zinc-bound water to bulk solvent, regenerating the zinc-bound hydroxide (equation 2, where B stands for a general base: either a water or a proton-shuttling residue). (iucr.org)
Proximal tubule2
- Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. (wikipedia.org)
- A distinctive feature of type II pRTA is that it is nonprogressing, and when the serum bicarbonate is reduced to approximately 15 mEq/L, a new transport maximum for bicarbonate is established and the proximal tubule is able to reabsorb all of the filtered bicarbonate. (medscape.com)
Acetazolamide2
- Synthesized copper(II) complexes have also sulfonamide group which is the most important pharmacophore for CA inhibition efficiency like acetazolamide (AAZ) as positive control. (gazi.edu.tr)
- Both are highly active enzymes for the CO(2) hydration reaction, being efficiently inhibited by acetazolamide. (unifi.it)
Homo1
- 4lp6 is a 2 chain structure with sequence from Homo sapiens . (proteopedia.org)
Sodium-bicarbonate1
- and sodium-potassium ATPase transporter (ATP1A1), sodium-bicarbonate transporter (NBC), and carbonic anhydrase II (CA2) increased 5- to 10-fold. (unboundmedicine.com)
Mechanism1
- As it relies only on the well-founded assumption that catalysis with CO 2 and O 2 substrates are mutually exclusive, this mechanism should function for any rubisco. (elifesciences.org)
19911
- Furthermore, the CO 2 concentration inside the leaf is typically measured to be lower than ambient due to a balance of stomatal conductance and CO 2 fixation by rubisco itself ( Caemmerer and Evans, 1991 ). (elifesciences.org)
Complexes4
- Here, we report previously undescribed structures of HCAII:CO(2) and HCAII:HCO(3)(-) complexes, together with a 3D molecular film of the enzymatic reaction observed successively in the same crystal after extended exposure to X-ray. (rcsb.org)
- In our present study, copper(II) sulfonamide complexes titled as bis-(2 acetylfuranmethanesulfonylhydrazone) copper(II) chloride, bis-(2-furaldehydemethanesulfonylhydrazone)copper(II) chloride and bis-(5-nitro-2 furaldehydemethanesulfonylhydrazone)copper(II) chloride were synthesized using aromatic sulfonylhydrazones derived from methane sulfonic acid hydrazide. (gazi.edu.tr)
- In order to gain insight into the structure of the copper(II) complexes, computational studies were performed by using DFT/B3LYP/6-311G(d,p) basis set with the Gaussian 09 program package. (gazi.edu.tr)
- The carbonic anhydrase I (CA I) inhibition of copper(II) complexes which goes on competitively was determined by using UV-Vis spectrophotometer technique, and their inhibition parameters such as K-m, IC50 and K-i were calculated. (gazi.edu.tr)
Carbon3
- Figure 1-figure supplement 2 demonstrates that the operon beginning with acRAF indeed encodes a functional inorganic carbon transporter. (elifesciences.org)
- As HCO 3 − can diffuse through the proteinaceous carboxysome shell but CO 2 cannot 5 , carbonic anhydrase generates high concentrations of CO 2 for carbon fixation by Rubisco 6 . (nature.com)
- The reference range of the partial pressure of carbon dioxide (pCO 2 ) of arterial blood is 35-45 mm Hg. (medscape.com)
Mutation1
- A single missense mutation allows AE1 to mediate both electrogenic SO 4 2- -Cl - exchange or electroneutral, H + -independent SO 4 2- -SO 4 2- exchange ( Alper 2006 ). (tcdb.org)
Sulfonamide1
- Three salts of 5-amino-2-sulfonamide-1,3,4-thiadiazole (Hats) were prepared and characterized by physico-chemical methods. (conicet.gov.ar)
Genes1
- Total RNA from tumors the expression of thousands of genes (3) to address complex questions was isolated using two successive rounds of Trizol. (lu.se)
Primary5
- Primary structure of human carbonic anhydrase C." J. Biol. (wikipedia.org)
- Primary Duodenal Adenocarcinoma Expressing Carbonic Anhydrase IX. (bvsalud.org)
- Primary duodenal adenocarcinoma is a rare malignancy whose carbonic anhydrase IX (CA9) expression remains poorly understood. (bvsalud.org)
- The primary outcomes in the phase 2 part of the study include circulating-tumor DNA (ctDNA) clearance or ctDNA recurrence-free survival 6 months after randomization among patients with detectable ctDNA status at randomization. (medscape.com)
- A 3-step approach is used to assess the acid-base disorder: (1) establishment of a primary disturbance, (2) determination of the serum anion gap, and (3) evaluation of compensation. (medscape.com)
Biol1
- 1972) Nat New Biol 235:131-137], but a structure of an HCAII in complex with CO(2) or HCO(3)(-) has remained elusive. (rcsb.org)
Concentration1
- KCl activates phospholipase D at two different concentration ranges: Distinguishing between hyperosmotic stress and membrane depolarization. (bio.net)
Chem1
- Anmäl er till eftersitsen senast måndagen den 20/2 genom e-mail till anita.hoang ´at´ chem.lu.se. (lu.se)
Structures2
- More than 100 distinct human carbonic anhydrase II (HCAII) 3D structures have been generated in last 3 decades [Liljas A, et al. (rcsb.org)
- The structures of copper(II) sulfonamides were determined by using LC-MS, FT-IR and UV-Vis methods, magnetism and conductivity measurements, and also electrochemical studies. (gazi.edu.tr)
Human erythrocytes1
- Carbonic Anhydrase I from human erythrocytes has been used as a pI (isoelectric point) marker in two-dimensional gel electrophoresis. (sigmaaldrich.com)
Structural3
- Firstly, structural analysis is performed on the crystallographic intermediate states of native CA II and its V143I variant. (iucr.org)
- The structural comparison shows that the binding affinities and configurations of the substrate (CO 2 ) and product (HCO 3 − ) are altered in the V143I variant and the water network in the water-replenishment pathway is restructured, while the proton-transfer pathway remains mostly unaffected. (iucr.org)
- This structural information is then used to estimate the modifications of the reaction rate constants and the corresponding free-energy profiles of CA II catalysis. (iucr.org)
Concentrations1
- As such, Form II rubiscos do not perform well in ambient CO 2 and O 2 concentrations. (elifesciences.org)
Tissues1
- Carbonic anhydrases (CAs) are expressed by many solid tumours where they may act to confer a growth advantage on malignant tissues. (ox.ac.uk)