Aldehyde Dehydrogenase: An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Disulfiram: A carbamate derivative used as an alcohol deterrent. It is a relatively nontoxic substance when administered alone, but markedly alters the intermediary metabolism of alcohol. When alcohol is ingested after administration of disulfiram, blood acetaldehyde concentrations are increased, followed by flushing, systemic vasodilation, respiratory difficulties, nausea, hypotension, and other symptoms (acetaldehyde syndrome). It acts by inhibiting aldehyde dehydrogenase.Acetaldehyde: A colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.Alcohol Dehydrogenase: A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.Betaine-Aldehyde Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.Cyanamide: A cyanide compound which has been used as a fertilizer, defoliant and in many manufacturing processes. It often occurs as the calcium salt, sometimes also referred to as cyanamide. The citrated calcium salt is used in the treatment of alcoholism.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)L-Lactate Dehydrogenase: A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.Alcohol Oxidoreductases: A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).Glyceraldehyde-3-Phosphate Dehydrogenases: Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.Isoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.BenzaldehydesGlutamate Dehydrogenase: An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.Glucosephosphate DehydrogenaseSjogren-Larsson Syndrome: An autosomal recessive neurocutaneous disorder characterized by severe ichthyosis MENTAL RETARDATION; SPASTIC PARAPLEGIA; and congenital ICHTHYOSIS. It is caused by mutation of gene encoding microsomal fatty ALDEHYDE DEHYDROGENASE leading to defect in fatty alcohol metabolism.Malate Dehydrogenase: An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.Isocitrate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.Phosphoramide Mustards: A group of nitrogen mustard compounds which are substituted with a phosphoramide group or its derivatives. They are usually cytotoxic and used as antineoplastic agents.Kinetics: The rate dynamics in chemical or physical systems.NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Chloral Hydrate: A hypnotic and sedative used in the treatment of INSOMNIA.L-Iditol 2-Dehydrogenase: An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14Dihydrolipoamide Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Carbohydrate Dehydrogenases: Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.Succinate Dehydrogenase: A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.Mitochondria, Liver: Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Ethanol: A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Glycerolphosphate DehydrogenaseAldehyde Reductase: An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21.Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Succinate-Semialdehyde Dehydrogenase: An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).Flushing: A transient reddening of the face that may be due to fever, certain drugs, exertion, stress, or a disease process.Hydroxysteroid Dehydrogenases: Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.Glucose 1-Dehydrogenase: A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.Sugar Alcohol Dehydrogenases: Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.Ketoglutarate Dehydrogenase ComplexAcroleinCoenzymes: Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.3-Hydroxysteroid Dehydrogenases: Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.p-Aminoazobenzene: Used in the form of its salts as a dye and as an intermediate in manufacture of Acid Yellow, diazo dyes, and indulines.Xanthine Dehydrogenase: An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.Glucose Dehydrogenases: D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.Phosphogluconate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.Acyl-CoA Dehydrogenases: Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)NADH Dehydrogenase: A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.IMP Dehydrogenase: An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.Lactate Dehydrogenases: Alcohol oxidoreductases with substrate specificity for LACTIC ACID.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Alkadienes: Acyclic branched or unbranched hydrocarbons having two carbon-carbon double bonds.Formate Dehydrogenases: Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.2,2'-Dipyridyl: A reagent used for the determination of iron.Acyl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.17-Hydroxysteroid Dehydrogenases: A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.Neoplastic Stem Cells: Highly proliferative, self-renewing, and colony-forming stem cells which give rise to NEOPLASMS.Alcohols: Alkyl compounds containing a hydroxyl group. They are classified according to relation of the carbon atom: primary alcohols, R-CH2OH; secondary alcohols, R2-CHOH; tertiary alcohols, R3-COH. (From Grant & Hackh's Chemical Dictionary, 5th ed)Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Hydroxybutyrate DehydrogenaseCloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide): A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.Oxidoreductases Acting on CH-NH Group Donors: Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.Nitroglycerin: A volatile vasodilator which relieves ANGINA PECTORIS by stimulating GUANYLATE CYCLASE and lowering cytosolic calcium. It is also sometimes used for TOCOLYSIS and explosives.Ditiocarb: A chelating agent that has been used to mobilize toxic metals from the tissues of humans and experimental animals. It is the main metabolite of DISULFIRAM.Ketone Oxidoreductases: Oxidoreductases that are specific for KETONES.Pyruvate Dehydrogenase (Lipoamide): The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).3-Hydroxyacyl CoA Dehydrogenases: Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.11-beta-Hydroxysteroid Dehydrogenases: Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.Pentaerythritol Tetranitrate: A vasodilator with general properties similar to NITROGLYCERIN but with a more prolonged duration of action. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1025)Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Uridine Diphosphate Glucose Dehydrogenase: An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Molecular Weight: The sum of the weight of all the atoms in a molecule.Retinaldehyde: A carotenoid constituent of visual pigments. It is the oxidized form of retinol which functions as the active component of the visual cycle. It is bound to the protein opsin forming the complex rhodopsin. When stimulated by visible light, the retinal component of the rhodopsin complex undergoes isomerization at the 11-position of the double bond to the cis-form; this is reversed in "dark" reactions to return to the native trans-configuration.Dihydrouracil Dehydrogenase (NADP): An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Betaine: A naturally occurring compound that has been of interest for its role in osmoregulation. As a drug, betaine hydrochloride has been used as a source of hydrochloric acid in the treatment of hypochlorhydria. Betaine has also been used in the treatment of liver disorders, for hyperkalemia, for homocystinuria, and for gastrointestinal disturbances. (From Martindale, The Extra Pharmacopoeia, 30th ed, p1341)Gene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Alcohol Deterrents: Substances interfering with the metabolism of ethyl alcohol, causing unpleasant side effects thought to discourage the drinking of alcoholic beverages. Alcohol deterrents are used in the treatment of alcoholism.3-alpha-Hydroxysteroid Dehydrogenase (B-Specific): A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.Glucosephosphate Dehydrogenase Deficiency: A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.Enzyme Induction: An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.11-beta-Hydroxysteroid Dehydrogenase Type 1: A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Alanine Dehydrogenase: An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.Sheep: Any of the ruminant mammals with curved horns in the genus Ovis, family Bovidae. They possess lachrymal grooves and interdigital glands, which are absent in GOATS.Hydroxyprostaglandin Dehydrogenases: Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Mannitol Dehydrogenases: Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.Fatty Alcohols: Usually high-molecular-weight, straight-chain primary alcohols, but can also range from as few as 4 carbons, derived from natural fats and oils, including lauryl, stearyl, oleyl, and linoleyl alcohols. They are used in pharmaceuticals, cosmetics, detergents, plastics, and lube oils and in textile manufacture. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Benzaldehyde Dehydrogenase (NADP+)Isoelectric Focusing: Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)Butyryl-CoA Dehydrogenase: A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.EsterasesSpectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Glyceraldehyde20-Hydroxysteroid Dehydrogenases: A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).Recombinant Proteins: Proteins prepared by recombinant DNA technology.11-beta-Hydroxysteroid Dehydrogenase Type 2: An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.NitrophenolsChlorpropamide: A sulfonylurea hypoglycemic agent used in the treatment of non-insulin-dependent diabetes mellitus not responding to dietary modification. (From Martindale, The Extra Pharmacopoeia, 30th ed, p277)Mitochondrial Proteins: Proteins encoded by the mitochondrial genome or proteins encoded by the nuclear genome that are imported to and resident in the MITOCHONDRIA.Acyl-CoA Dehydrogenase, Long-Chain: A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.Benzodioxoles: Compounds based on benzene fused to oxole. They can be formed from methylated CATECHOLS such as EUGENOL.KetonesMutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Tretinoin: An important regulator of GENE EXPRESSION during growth and development, and in NEOPLASMS. Tretinoin, also known as retinoic acid and derived from maternal VITAMIN A, is essential for normal GROWTH; and EMBRYONIC DEVELOPMENT. An excess of tretinoin can be teratogenic. It is used in the treatment of PSORIASIS; ACNE VULGARIS; and several other SKIN DISEASES. It has also been approved for use in promyelocytic leukemia (LEUKEMIA, PROMYELOCYTIC, ACUTE).Genes, Bacterial: The functional hereditary units of BACTERIA.Metabolic Detoxication, Drug: Reduction of pharmacologic activity or toxicity of a drug or other foreign substance by a living system, usually by enzymatic action. It includes those metabolic transformations that make the substance more soluble for faster renal excretion.Choline Dehydrogenase: An enzyme bound to the inner mitochondrial membrane that catalyzes the oxidation of CHOLINE to BETAINE.Isovaleryl-CoA Dehydrogenase: A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).3-Isopropylmalate Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Dimethyl Adipimidate: Bifunctional cross-linking agent that links covalently free amino groups of proteins or polypeptides, including those in cell membranes. It is used as reagent or fixative in immunohistochemistry and is a proposed antisickling agent.Malate Dehydrogenase (NADP+)Biotransformation: The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.Horses: Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.Pyruvate Dehydrogenase (Lipoamide)-Phosphatase: (Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.Leucine Dehydrogenase: An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Phosphoglycerate Dehydrogenase: An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Chemistry: A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.Estradiol Dehydrogenases: Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62Alcohol Drinking: Behaviors associated with the ingesting of alcoholic beverages, including social drinking.Chemical Phenomena: The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.Alkanes: The generic name for the group of aliphatic hydrocarbons Cn-H2n+2. They are denoted by the suffix -ane. (Grant & Hackh's Chemical Dictionary, 5th ed)MercaptoethanolEstersAcetates: Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Glutamate Dehydrogenase (NADP+)Vibrio: A genus of VIBRIONACEAE, made up of short, slightly curved, motile, gram-negative rods. Various species produce cholera and other gastrointestinal disorders as well as abortion in sheep and cattle.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (1/1111)

Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction.  (+info)

Xenopus cytosolic thyroid hormone-binding protein (xCTBP) is aldehyde dehydrogenase catalyzing the formation of retinoic acid. (2/1111)

Amino acid sequencing of an internal peptide fragment derived from purified Xenopus cytosolic thyroid hormone-binding protein (xCTBP) demonstrates high similarity to the corresponding sequence of mammalian aldehyde dehydrogenase 1 (ALDH1) (Yamauchi, K., and Tata, J. R. (1994) Eur. J. Biochem. 225, 1105-1112). Here we show that xCTBP was co-purified with ALDH and 3,3',5-triiodo-L-thyronine (T3) binding activities. By photoaffinity labeling with [125I]T3, a T3-binding site in the xCTBP was estimated to reside in amino acid residues 93-114, which is distinct from the active site of the enzyme but present in the NAD+ binding domain. The amino acid sequences deduced from the two isolated xALDH1 cDNAs (xALDH1-I and xALDH1-II) were 94.6% identical to each other and very similar to those of mammalian ALDH1 enzymes. The two recombinant xALDH1 proteins exhibit both T3 binding activity and ALDH activity converting retinal to retinoic acid (RA), which are similar to those of xCTBP. The mRNAs were present abundantly in kidney and intestine of adult female Xenopus. Interestingly, their T3 binding activities were inhibited by NAD+ and NADH but not by NADP+ and NADPH, whereas NAD+ was required for their ALDH activities. Our results demonstrate that xCTBP is identical to ALDH1 and suggest that this protein might modulate RA synthesis and intracellular level of free T3.  (+info)

Stimulation of premature retinoic acid synthesis in Xenopus embryos following premature expression of aldehyde dehydrogenase ALDH1. (3/1111)

In order for nuclear retinoic acid receptors to mediate retinoid signaling, the ligand retinoic acid must first be produced from its vitamin A precursor retinal. Biochemical studies have shown that retinal can be metabolized in vitro to retinoic acid by members of the aldehyde dehydrogenase enzyme family, including ALDH1. Here we describe the first direct evidence that ALDH1 plays a physiological role in retinoic acid synthesis by analysis of retinoid signaling in Xenopus embryos, which have plentiful stores of maternally derived retinal. The Xenopus ALDH1 gene was cloned and shown to be highly conserved with chick and mammalian homologs. Xenopus ALDH1 was not expressed at blastula and gastrula stages, but was expressed at the neurula stage. We used a retinoic acid bioassay to demonstrate that retinoic acid is normally undetectable in embryos from fertilization to the initial gastrula stage, but that a tremendous increase in retinoic acid occurs during neurulation when ALDH1 is first expressed. Overexpression of ALDH1 by injection of Xenopus embryos with mRNAs encoding the mouse, chick or Xenopus ALDH1 homologs induced high levels of retinoic acid detection during the blastula stage. Thus, premature expression of ALDH1 stimulates premature synthesis of retinoic acid. These findings reveal an important conserved role for ALDH1 in retinoic acid synthesis in vivo, and demonstrate that conversion of retinoids from the aldehyde form to the carboxylic acid form is a crucial regulatory step in retinoid signaling.  (+info)

The negative regulation of the rat aldehyde dehydrogenase 3 gene by glucocorticoids: involvement of a single imperfect palindromic glucocorticoid responsive element. (4/1111)

Glucocorticoids repressed the polycyclic aromatic hydrocarbon-dependent induction of Class 3 aldehyde dehydrogenase (ALDH3) enzyme activity and mRNA levels in isolated rat hepatocytes by more than 50 to 80%, with a concentration-dependence consistent with the involvement of the glucocorticoid receptor (GR). No consistent effect on the low basal transcription rate was observed. This effect of glucocorticoids (GC) on polycyclic aromatic hydrocarbon induction was effectively antagonized at the mRNA and protein level by the GR antagonist RU38486. The response was cycloheximide-sensitive, because the protein synthesis inhibitor caused a GC-dependent superinduction of ALDH3 mRNA levels. This suggests that the effects of GC on this gene are complex and both positive and negative gene regulation is possible. The GC-response was recapitulated in HepG2 cells using transient transfection experiments with CAT reporter constructs containing 3.5 kb of 5'-flanking region from ALDH3. This ligand-dependent response was also observed when a chimeric GR (GR DNA-binding domain and peroxisome proliferator-activated receptor ligand-binding domain) was used in place of GR in the presence of the peroxisome proliferator, nafenopin. A putative palindromic glucocorticoid-responsive element exists between -930 and -910 base pairs relative to the transcription start site. If this element was either deleted or mutated, the negative GC-response was completely lost, which suggests that this sequence is responsible, in part, for the negative regulation of the gene. Electrophoretic mobility shift analysis demonstrated that this palindromic glucocorticoid-responsive element is capable of forming a specific DNA-protein complex with human glucocorticoid receptor. In conclusion, the negative regulation of ALDH3 in rat liver is probably mediated through direct GR binding to its canonical responsive element.  (+info)

Molecular analysis of two closely related mouse aldehyde dehydrogenase genes: identification of a role for Aldh1, but not Aldh-pb, in the biosynthesis of retinoic acid. (5/1111)

Mammalian class I aldehyde dehydrogenase (ALDH1) has been implicated as a retinal dehydrogenase in the biosynthesis of retinoic acid, a modulator of gene expression and cell differentiation. As the first step towards studying the regulation of ALDH1 and its physiological role in the biosynthesis of retinoic acid, mouse ALDH1 cDNA and genomic clones have been characterized. During the cloning process, an additional closely related gene was also isolated and named Aldh-pb, owing to its high amino acid sequence identity (92%) with the rat phenobarbitol-inducible ALDH protein (ALDH-PB). Aldh1 spans about 45 kb in length, whereas Aldh-pb spans about 35 kb. Both genes are composed of 13 exons, and the positions of all the exon/intron boundaries are conserved with those of human ALDH1. The promoter regions of Aldh1 and Aldh-pb demonstrate high sequence similarity with those of human ALDH1 and rat ALDH-PB. Expression of Aldh1 and Aldh-pb is tissue-specific, with mRNAs for both genes being found in the liver, lung and testis, but not in the heart, spleen or muscle. Expression of Aldh-pb, but not Aldh1, was also detected at high levels in the kidney. Aldh1 and Aldh-pb encode proteins of 501 amino acids with 90% positional identity. To examine the relative roles of these two enzymes in retinoic acid synthesis in vivo, Xenopus embryos were injected with mRNAs encoding these enzymes to assay the effect on conversion of endogenous retinal into retinoic acid. Injection of ALDH1, but not ALDH-PB, mRNA stimulated retinoic acid synthesis in Xenopus embryos at the blastula stage. Thus our results indicate that Aldh1 can function in retinoic acid synthesis under physiological conditions, but that the closely related Aldh-pb does not share this property.  (+info)

Relationships within the aldehyde dehydrogenase extended family. (6/1111)

One hundred-forty-five full-length aldehyde dehydrogenase-related sequences were aligned to determine relationships within the aldehyde dehydrogenase (ALDH) extended family. The alignment reveals only four invariant residues: two glycines, a phenylalanine involved in NAD binding, and a glutamic acid that coordinates the nicotinamide ribose in certain E-NAD binary complex crystal structures, but which may also serve as a general base for the catalytic reaction. The cysteine that provides the catalytic thiol and its closest neighbor in space, an asparagine residue, are conserved in all ALDHs with demonstrated dehydrogenase activity. Sixteen residues are conserved in at least 95% of the sequences; 12 of these cluster into seven sequence motifs conserved in almost all ALDHs. These motifs cluster around the active site of the enzyme. Phylogenetic analysis of these ALDHs indicates at least 13 ALDH families, most of which have previously been identified but not grouped separately by alignment. ALDHs cluster into two main trunks of the phylogenetic tree. The largest, the "Class 3" trunk, contains mostly substrate-specific ALDH families, as well as the class 3 ALDH family itself. The other trunk, the "Class 1/2" trunk, contains mostly variable substrate ALDH families, including the class 1 and 2 ALDH families. Divergence of the substrate-specific ALDHs occurred earlier than the division between ALDHs with broad substrate specificities. A site on the World Wide Web has also been devoted to this alignment project.  (+info)

The loss in hydrophobic surface area resulting from a Leu to Val mutation at the N-terminus of the aldehyde dehydrogenase presequence prevents import of the protein into mitochondria. (7/1111)

An apparent conservative mutation, Leu to Val, at the second residue of the rat liver mitochondrial aldehyde dehydrogenase (ALDH) presequence resulted in a precursor protein that was not imported into mitochondria. Additional mutants were made to substitute various amino acids with nonpolar side chains for Leu2. The Ile, Phe, and Trp mutants were imported to an extent similar to that of the native precursor, but the Ala mutant was imported only about one-fourth as well. It was shown that the N-terminal methionine was removed from the L2V mutant in a reaction catalyzed by methionine aminopeptidase. The N-terminal methionine of native pALDH and the other mutant presequences was blocked, presumably by acetylation. Because of the difference in co-translational modification, the L2V mutant sustained a significant loss in the available hydrophobic surface of the presequence. Import competence was restored to the L2V mutant when it was translated using a system that did not remove Met1. The removal of an Arg-Gly-Pro helix linker segment (residues 11-14) from the L2V mutant, which shifted three leucine residues toward the N-terminus, also restored import competence. These results lead to the conclusion that a minimum amount of hydrophobic surface area near the N-termini of mitochondrial presequences is an essential property to determine their ability to be imported. As a result, both electrostatic and hydrophobic components must be considered when trying to understand the interactions between precursor proteins and proteins of the mitochondrial import apparatus.  (+info)

In vivo mitochondrial import. A comparison of leader sequence charge and structural relationships with the in vitro model resulting in evidence for co-translational import. (8/1111)

The positive charges and structural properties of the mitochondrial leader sequence of aldehyde dehydrogenase have been extensively studied in vitro. The results of these studies showed that increasing the helicity of this leader would compensate for reduced import from positive charge substitutions of arginine with glutamine or the insertion of negative charged residues made in the native leader. In this in vivo study, utilizing the green fluorescent protein (GFP) as a passenger protein, import results showed the opposite effect with respect to helicity, but the results from mutations made within the native leader sequence were consistent between the in vitro and in vivo experiments. Leader mutations that reduced the efficiency of import resulted in a cytosolic accumulation of a truncated GFP chimera that was fluorescent but devoid of a mitochondrial leader. The native leader efficiently imported before GFP could achieve a stable, import-incompetent structure, suggesting that import was coupled with translation. As a test for a co-translational mechanism, a chimera of GFP that contained the native leader of aldehyde dehydrogenase attached at the N terminus and a C-terminal endoplasmic reticulum targeting signal attached to the C terminus of GFP was constructed. This chimera was localized exclusively to mitochondria. The import result with the dual signal chimera provides support for a co-translational mitochondrial import pathway.  (+info)

Title:Mitochondrial Aldehyde Dehydrogenase, A Potential Drug Target for Protection of Heart and Brain from Ischemia/Reperfusion Injury. VOLUME: 15 ISSUE: 10. Author(s):Xiu-Ju Luo, Bin Liu, Qi-Lin Ma and Jun Peng. Affiliation:Department of Pharmacology, School of Pharmaceutical Sciences, Central South University. No.110 Xiang-Ya Road, Changsha, 410078, China.. Keywords:4-hydroxy-2-nonenal (4-HNE), Alda-1, aldehyde, ischemia/reperfusion injury, mitochondrial aldehyde dehydrogenase (ALDH2), oxidative stress.. Abstract:Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes that are responsible for clearance of aldehydes in the body. In animal myocardial or cerebral ischemia/ reperfusion (I/R) models, accumulation of toxic aldehydes, such as 4-hydroxy-2-nonenal and malondialdehyde, is thought to be an important mechanism for myocardial and cerebral I/R injury. Among the isoenzymes of ALDH, ALDH2 is believed to play a major role in clearance ...
TY - JOUR. T1 - The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol-induced flushing increases turnover of the enzyme tetramers in a dominant fashion. AU - Xiao, Qing. AU - Weiner, Henry. AU - Crabb, David W.. PY - 1996/11/1. Y1 - 1996/11/1. N2 - Deficiency in mitochondrial aldehyde dehydrogenase (ALDH2), a tetrameric enzyme, results from inheriting one or two ALDH2*2 alleles. This allele encodes a protein subunit with a lysine for glutamate substitution at position 487 and is dominant over the wild-type allele, ALDH2*1. The ALDH2*2-encoded subunit (ALDH2K) reduces the activity of ALDH2 enzyme in cell lines expressing the wild-type subunit (ALDH2E). In addition to this effect on the enzyme activity, we now report that ALDH2*2 heterozygotes had lower levels of ALDH2 immunoreactive protein in autopsy liver samples. The half-lives of ALDH2 protein in HeLa cell lines expressing ALDH2*1, ALDH2*2, or both were determined by the rate of loss of immunoreactive ...
TY - JOUR. T1 - Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase activity. AU - Hess, David A.. AU - Craft, Timothy P.. AU - Wirthlin, Louisa. AU - Hohm, Sarah. AU - Zhou, Ping. AU - Eades, William C.. AU - Creer, Michael H.. AU - Sands, Mark S.. AU - Nolta, Jan A.. PY - 2008/3/1. Y1 - 2008/3/1. N2 - Transplanted adult progenitor cells distribute to peripheral organs and can promote endogenous cellular repair in damaged tissues. However, development of cell-based regenerative therapies has been hindered by the lack of preclinical models to efficiently assess multiple organ distribution and difficulty defining human cells with regenerative function. After transplantation into β-glucuronidase (GUSB)-deficient NOD/SCID/mucopolysaccharidosis type VII mice, we characterized the distribution of lineage-depleted human umbilical cord blood-derived cells purified by selection using high aldehyde dehydrogenase (ALDH) activity with ...
Preparations of sheep liver cytoplasmic aldehyde dehydrogenase obtained by published methods were found by analytical isoelectric focusing in the pH range 5-8 to contain 5-10% by weight of the mitochondrial aldehyde dehydrogenase. Under the conditions used the pI of the cytoplasmic enzyme is 6.2 and that of the mitochondrial enzyme 6.6. The mitochondrial enzyme can be removed from the preparation by selective precipitation of the cytoplasmic enzyme with (NH4)2SO4. Kinetic experiments and inhibition experiments with disulfiram show that the properties of the two sheep liver enzymes are so different that the presence of 10% mitochondrial enzyme in preparations of the cytoplasmic enzyme can introduce serious errors into results. Our results suggest that the presence of 10 microM-disulfiram in assays may completely inactivate the pure cytoplasmic enzyme. This result is in contrast with a previous report [kitson (1978) Biochem. U. 175, 83-90]. ...
TY - JOUR. T1 - Order and disorder in mitochondrial aldehyde dehydrogenase. AU - Hurley, Thomas. AU - Perez-Miller, Samantha. AU - Breen, Heather. PY - 2001/1/30. Y1 - 2001/1/30. N2 - One of the most notable and currently unexplained features of the mitochondrial form of aldehyde dehydrogenase is its property of half-of-the-sites reactivity. An appropriate description of this phenomenon can be to consider this as the extreme example of negative cooperativity. This implies, therefore, that a pathway of communication must exist between active sites in order to convey the structural consequences of ligand binding. Data from four different structures of human ALDH2 collected during the past 2 years may shed some light on one possible pathway for the propagation of structural information. We recently published a 2.6 Å structure of a binary complex between ALDH2 and NAD+ in which the predominant conformation of the cofactor differed between different subunits in the structure. We now have three ...
TY - CONF. T1 - Expression and characterisation of human aldehyde dehydrogenase 10. T2 - implications for Sjögren-Larsson syndrome. AU - Lloyd, M. D.. AU - Boardman, K. D. E.. AU - Threadgill, M. D.. PY - 2006/9. Y1 - 2006/9. M3 - Other. ER - ...
TY - JOUR. T1 - The effects of cephem antibiotics and related compounds on the aldehyde dehydrogenase in rat liver mitochondria. AU - Chiaki, Kamei. AU - Yukio, Sugimoto. AU - Kenji, Tasaka. PY - 1987/6/15. Y1 - 1987/6/15. N2 - The effects of cephem antibiotics and their related compounds on aldehyde dehydrogenase obtained from rat liver mitochondria were studied. A pH of 8.8 and reaction temperature 24° were the conditions for measurement of enzyme activity. The apparent Michaelis constant Km values for NAD, acetaldehyde and propionaldehyde were 3.8 × 10-5 M, 4.0 × 10-5 M and 2.5 × 10-5 M, respectively. Cefamandole, cefoperazone and cefmetazole, having a 1-methyl-5-thiotetrazol group at position 3 of the cephem ring, caused a relatively potent inhibition of aldehyde dehydrogenase. Cefmetazole and cefoperazone also showed a significant inhibition on highly purified yeast aldehyde dehydrogenase; the extent of inhibition on yeast enzyme was almost the same as that on rat mitochondrial aldehyde ...
Aldehyde dehydrogenases (ALDHs) play a major role in detoxification of aldehydes. High expression of ALDHs is a marker for stem cells of many organs including the lungs. A common polymorphism in ALDH2 gene (ALDH2*2) results in inactivation of the enzyme and is associated with alcohol flushing syndrome and increased risk for cardiovascular and Alzheimers diseases and some cancers. The effect of this ALDH2 polymorphism on the lung and its stem cells has not been thoroughly examined. We examined the association between the ALDH2*2 allele and lung function parameters in a population of healthy individuals. We also examined its association with the incidence of asthma and COPD in patient cohorts. We used the in vitro colony forming assay to detect the effect of the polymorphism on lung epithelial stem cells from both primary human surgical samples and Aldh2*2 transgenic (Tg) and Aldh2 −/− mice. Response to acute and chronic lung injuries was compared between wild type (WT),
Aldehyde dehydrogenases (ALDHs) represent a group of enzymes that detoxify aldehydes by facilitating their oxidation to carboxylic acids, and have been shown to play roles in plant response to abiotic stresses. However, the comprehensive analysis of ALDH superfamily in soybean (Glycine max) has been limited. In present study, a total of 53 GmALDHs were identified in soybean, and grouped into 10 ALDH families according to the ALDH Gene Nomenclature Committee and phylogenetic analysis. These groupings were supported by their gene structures and conserved motifs. Soybean ALDH superfamily expanded mainly by whole genome duplication/segmental duplications. Gene network analysis identified 1146 putative co-functional genes of 51 GmALDHs. Gene Ontology (GO) enrichment analysis suggested the co-functional genes of these 51 GmALDHs were enriched (FDR < 1e-3) in the process of lipid metabolism, photosynthesis, proline catabolism, and small molecule catabolism. In addition, 22 co-functional genes of GmALDHs are
The precise phenotype and biology of acute myeloid leukemia stem cells remain controversial, in part because the "gold standard" immunodeficient mouse engraftment assay fails in a significant fraction of patients and identifies multiple cell-types in others. We sought to analyze the clinical utility of a novel assay for putative leukemia stem cells in a large prospective cohort. The leukemic clones most primitive hematopoietic cellular phenotype was prospectively identified in 109 newly-diagnosed acute myeloid leukemia patients, and correlated with clinical risk groups and outcomes. Most (80/109) patients harbored CD34+CD38- leukemia cells. The CD34+CD38- leukemia cells in 47 of the 80 patients displayed intermediate aldehyde dehydrogenase expression, while normal CD34+CD38- hematopoietic stem cells expressed high levels of aldehyde dehydrogenase. In the other 33/80 patients, the CD34+CD38- leukemia cells exhibited high aldehyde dehydrogenase activity, and most (28/33, 85%) harbored poor-risk ...
Creative Proteomics offer Aldehyde Dehydrogenase Activity Fluorometric Assay Kit. We are specialized in manufacturing Assay Kits.
The purpose of this comprehensive meta-analysis was to assess the association of aldehyde dehydrogenase (ALDH) expression with overall survival (OS) and disease-free survival (DFS)/progression-free survival (PFS) in ovarian cancer patients. Systematic searches of Pubmed databases was performed to identify relevant literature published before February 28, 2018. A total of 14 studies (13 articles) with 2210 ovarian cancer patients were pooled. All included studies were performed by using Immunohistochemistry (IHC) for detection of ALDH expression. Hazard ratio (HR) and 95% confidence interval (CI) were extracted from included studies to evaluate the correlation of ALDH expression with OS and DFS/PFS. High expression of ALDH was associated with worse OS (HR: 1.43; 95% CI: 1.18-1.73) and poor DFS/PFS (HR: 1.55, 95% CI: 1.12-2.14). No evidence of publication bias was observed in OS (Beggs test, P = 0.113; Eggers test, P = 0.355) and DFS/PFS (Beggs test, P = 0.655; Eggers test, P = 0.189) in ovarian
Melanoma is one of the most aggressive types of human cancer, characterized by enhanced heterogeneity and resistance to conventional therapy at advanced stages. We and others have previously shown that HEDGEHOG-GLI (HH-GLI) signaling is required for melanoma growth and for survival and expansion of melanoma-initiating cells (MICs). Recent reports indicate that HH-GLI signaling regulates a set of genes typically expressed in embryonic stem cells, including SOX2 (sex-determining region Y (SRY)-Box2). Here we address the function of SOX2 in human melanomas and MICs and its interaction with HH-GLI signaling. We find that SOX2 is highly expressed in melanoma stem cells. Knockdown of SOX2 sharply decreases self-renewal in melanoma spheres and in putative melanoma stem cells with high aldehyde dehydrogenase activity (ALDH(high)). Conversely, ectopic expression of SOX2 in melanoma cells enhances their self-renewal in vitro. SOX2 silencing also inhibits cell growth and induces apoptosis in melanoma ...
Aldehyde dehydrogenase (ALDH) activity is commonly used as a marker to identify cancer stem-like cells. The three ALDH1A isoforms have all been individually implicated in cancer stem-like cells and in chemoresistance; however, which isoform is preferentially expressed varies between cell lines. We sought to explore the structural determinants of ALDH1A isoform selectivity in a series of small-molecule inhibitors in support of research into the role of ALDH1A in cancer stem cells. An SAR campaign guided by a cocrystal structure of the HTS hit CM39 (7) with ALDH1A1 afforded first-in-class inhibitors of the ALDH1A subfamily with excellent selectivity over the homologous ALDH2 isoform. We also discovered the first reported modestly selective single isoform 1A2 and 1A3 inhibitors. Two compounds, 13g and 13h, depleted the CD133+ putative cancer stem cell pool, synergized with cisplatin, and achieved efficacious concentrations in vivo following IP administration. Compound 13h additionally synergized ...
2VLE: The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase
Sci. Rep. Aldehyde dehydrogenase enzymes (ALDHs) are very common proteins involved in the oxidation of aliphatic and aromatic aldehydes to their corresponding…
Background: Inherited human aldehyde dehydrogenase 2 (ALDH-2) deficiency reduces the risk for alcoholism. Kudzu plants and extracts have been used for 1,000 years in traditional Chinese medicine to treat alcoholism. Kudzu contains daidzin, which inhibits ALDH-2 and suppresses heavy drinking in rodents. Decreased drinking due to ALDH-2 inhibition is attributed to aversive properties of acetaldehyde accumulated during alcohol consumption. However, daidzin can reduce drinking in some rodents without necessarily increasing acetaldehyde. Therefore, a selective ALDH-2 inhibitor might affect other metabolic factors involved in regulating drinking.. Methods: Aldehyde dehydrogenase 2 inhibitors were synthesized based on the co-crystal structure of ALDH-2 and daidzin. We tested the efficacy of a highly selective reversible ALDH-2 inhibitor, CVT-10216, in models of moderate and high alcohol drinking rats. We studied 2-bottle choice and deprivation-induced drinking paradigms in Fawn Hooded (FH) rats, ...
Aldehyde dehydrogenases (ALDH, EC 1.2.1.3) are a group of enzymes that catalyze the oxidation (dehydrogenation) of aldehydes to carboxylic acids, an action also performed by xanthine oxidase (XO) and aldehyde oxidase (AO).. The aldehyde cinnamaldehyde commonly used as a food flavoring is rapidly oxidized by aldehyde dehydrogenases into the carboxylic acid cinnamic acid.. ...
Oxidizes medium and long chain saturated and unsaturated aldehydes (PubMed:17382292, PubMed:23721920). Metabolizes also benzaldehyde (PubMed:17382292). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (PubMed:17382292). May have a protective role against the cytotoxicity induced by lipid peroxidation (PubMed:17382292).
ALDH activity measured fluorimetrically using a high concentration of aliphatic aldehyde as substrate was studied in human glioblastomas grafted in nude mice. Compared with normal brain, ALDH...
TY - JOUR. T1 - Characterization of the molecular mechanisms underlying increased ischemic damage in the aldehyde dehydrogenase 2 genetic polymorphism using a human induced pluripotent stem cell model system. AU - Ebert, Antje D.. AU - Kodo, Kazuki. AU - Liang, Ping. AU - Wu, Haodi. AU - Huber, Bruno C.. AU - Riegler, Johannes. AU - Churko, Jared. AU - Lee, Jaecheol. AU - De Almeida, Patricia. AU - Lan, Feng. AU - Diecke, Sebastian. AU - Burridge, Paul W.. AU - Gold, Joseph D.. AU - Mochly-Rosen, Daria. AU - Wu, Joseph C.. PY - 2014/9/24. Y1 - 2014/9/24. N2 - Nearly 8% of the human population carries an inactivating point mutation in the gene that encodes the cardioprotective enzyme aldehyde dehydrogenase 2 (ALDH2). This genetic polymorphism (ALDH2∗2) is linked to more severe outcomes from ischemic heart damage and an increased risk of coronary artery disease (CAD), but the underlying molecular bases are unknown. We investigated the ALDH2∗2 mechanisms in a human model system of induced ...
15 min with 200 ml of 50 mM NH4HCO3 at RT. A volume of 200 ml of 100 acetonitrile was added to this solution and incubated for 15 min at room temperature. Solvent was removed and gel plugs were allowed to dry for 30 min at RT under a flow hood. Plugs were rehydrated with 20 ng/ml of modified trypsin (Promega, Madison, WI, USA) in 50 mM NH4HCO3 in a shaking incubator overnight at 37uC. Enough trypsin solution was added in order to completely submerge the gel plugs.sample was acquired for a total of ,2.5 min. MS/MS spectra were searched against the International Protein Index (IPI) database using SEQUEST with the following parameters: two trypsin miscleavages, fixed carbamidomethyl modification, variable methionine oxidation, parent tolerance 10 ppm, and fragment tolerance of 25 mmu or 0.01 Da. Results were filtered with the following criteria: Xcorr1.5, 2.0, 2.5, 3.0 for 1, 2, 3, and 4 charge states, respectively, Delta CN0.1, and P-value (protein and peptide) 0.01. IPI accession numbers were ...
Conditioned medium (CM) from clonal sub-populations of the pancreatic cancer cell line, MiaPaCa-2 with differing invasive abilities, were examined for their effect on in vitro invasion. Conditioned medium from Clone #3 (CM#3) strongly promoted invasion, while CM from Clone #8 (CM#8) inhibited invasion in vitro. 2D DIGE followed by MALDI-TOF MS analysis of CM#3 and CM#8 identified 41 proteins which were differentially regulated; 27 proteins were down-regulated and 14 proteins up-regulated in the invasion-promoting CM#3 when compared to CM#8. Western blotting analysis confirmed the down-regulated expression of gelsolin and the up-regulation of aldehyde dehydrogenase 1A1 in CM#3. Down-regulation of aldehyde dehydrogenase 1A1 in Clone #3 CM and gelsolin levels in Clone #8 CM by siRNA transfection revealed an important involvement of these proteins in promoting and inhibiting invasion in these pancreatic cancer cell lines. ...
NCT 501 (CAS: 1802088-50-1)is a potent and selective theophylline-based inhibitor of aldehyde dehydrogenase 1A1 (ALDH1A1), inhibits hALDH1A1 with IC50 of 40 nM, typically shows better selectivity over other ALDH isozymes and other dehydrogenases (hALDH1B1
TY - JOUR. T1 - Metabolic remodeling induced by mitochondrial aldehyde stress stimulates tolerance to oxidative stress in the heart. AU - Endo, Jin. AU - Sano, Motoaki. AU - Katayama, Takaharu. AU - Hishiki, Takako. AU - Shinmura, Ken. AU - Morizane, Shintaro. AU - Matsuhashi, Tomohiro. AU - Katsumata, Yoshinori. AU - Zhang, Yan. AU - Ito, Hideyuki. AU - Nagahata, Yoshiko. AU - Marchitti, Satori. AU - Nishimaki, Kiyomi. AU - Wolf, Alexander Martin. AU - Nakanishi, Hiroki. AU - Hattori, Fumiyuki. AU - Vasiliou, Vasilis. AU - Adachi, Takeshi. AU - Ohsawa, Ikuroh. AU - Taguchi, Ryo. AU - Hirabayashi, Yoshio. AU - Ohta, Shigeo. AU - Suematsu, Makoto. AU - Ogawa, Satoshi. AU - Fukuda, Keiichi. PY - 2009/11. Y1 - 2009/11. N2 - RATIONALE:: Aldehyde accumulation is regarded as a pathognomonic feature of oxidative stress-associated cardiovascular disease. OBJECTIVE:: We investigated how the heart compensates for the accelerated accumulation of aldehydes. METHODS AND RESULTS:: Aldehyde dehydrogenase 2 ...
Semantic Scholar extracted view of Aldehyde dehydrogenase activity and level of dopamine in certain sections of the brain of rats preferring and refusing ethanol by Kharchenko Nk
Application of stem cell biology to breast cancer research has been limited by the lack of simple methods for identification and isolation of normal and malignant stem cells. Utilizing in vitro and in vivo experimental systems, we show that normal and cancer human mammary epithelial cells with increased aldehyde dehydrogenase activity (ALDH) have stem/progenitor properties. These cells contain the subpopulation of normal breast epithelium with the broadest lineage differentiation potential and greatest growth capacity in a xenotransplant model. In breast carcinomas, high ALDH activity identifies the tumorigenic cell fraction, capable of self-renewal and of generating tumors that recapitulate the heterogeneity of the parental tumor. In a series of 577 breast carcinomas, expression of ALDH1 detected by immunostaining correlated with poor prognosis. These findings offer an important new tool for the study of normal and malignant breast stem cells and facilitate the clinical application of stem cell ...
Hematopoiesis is sustained throughout adult life by balanced self-renewal and differentiation divisions of multipotent cells. The restriction of these cells to specific lineages takes place in an orderly sequence that spans several cell generations, thus creating hierarchies of daughter cells with distinct properties. Hematopoietic stem cells (HSC) represent the cells that head up this hierarchy and are thus able to regenerate and sustain the long term production of all blood cell types when transplanted at low numbers into suitable hosts. Quantification of HSC is achieved by coupling the end-points of donor-derived lymphoid and myeloid cell output to long term limiting dilution transplantation assays.1 In mice, phenotypically distinct cells with different repopulating activities in vivo have been described.2-7 Some short-term repopulating cells (STRC) lack the extensive self-renewal ability of HSC but retain a broad lympho-myeloid differentiation repertoire. Others also show partial restriction ...
The root cause is a genetic predisposition to acetaldehyde build-up that is most commonly observed in people of Asian decent, hence it being colloquially termed "Asian flush" despite it not being exclusive to Asians.. Acetaldehyde is a toxic by-product of alcohol metabolism that is usually broken down by enzymes in our body in order to stop it from accumulating and causing a toxic reaction - i.e. the various symptoms of Asian flush. All that is required is one of more specific gene variants to be present for acetaldehyde build-up to occur.. One gene variant, observable in approximately 50% of Asian people, is called the mitochondrial ALDH2 allele, which results in a deficient aldehyde dehydrogenase enzyme that works at about 10% of its usual capacity. This enzyme is normally responsible for preventing acetaldehyde build up by catalyzing its conversion into non-toxic acetic acid.. In addition to this, and contrary to common belief, a study confirmed that 80% of Asians and nearly all Japanese, ...
specificalPrinciple of the assay: This assay employs the quantitative sandwich enzyme immunoassay technique. Antibody specific for ALDH5A1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any ALDH5A1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for ALDH5A1 is added to the wells. After washing, avidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of ALDH5A1 bound in the initial step. The color development is stopped and the intensity of the color is measured. ...
Rabbit monoclonal antibody raised against recombinant human ALDH1A1. Recombinant protein corresponding to human ALDH1A1. (MAB21821) - Products - Abnova
Aldehyde dehydrogenases in rat brain: subcellular distribution, properties and involvement in acetaldehyde and dopamine metabolism ...
ALDH1A2 - ALDH1A2 (untagged)-Human aldehyde dehydrogenase 1 family, member A2 (ALDH1A2), transcript variant 2 available for purchase from OriGene - Your Gene Company.
The IUPHAR/BPS Guide to Pharmacology. aldehyde dehydrogenase 5 family member A1 - GABA turnover. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Top performende anti-Maus Aldehyde Dehydrogenase 1 Family, Member A2 Antikörper für Immunofluorescence (Paraffin-embedded Sections) (IF (p)) vergleichen & kaufen.
In this review, we summarize recent advances in understanding vitamin A-dependent regulation of sex-specific differences in metabolic diseases, inflammation, and certain cancers. We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze conversion of retinaldehyde to retinoic acid. Additionally, we propose a
J:63682 Vaz FM, et al., Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4 ...
Some flower cytoplasms express novel mitochondrial genes that cause male sterility. encodes a soluble protein that accumulates in the mitochondrial matrix. Three independent lines of evidence establish that the RF2 protein is an aldehyde dehydrogenase (ALDH). The finding that T cytoplasm plants that are homozygous for the allele are male sterile but accumulate normal amounts of RF2 protein that lacks normal mitochondrial (mt) ALDH activity provides strong evidence that gene also is required for anther development in normal cytoplasm maize. Hence it appears that the gene was recruited recently to function as a nuclear restorer. ALDHs typically have very broad substrate specificities. Indeed the RF2 protein is capable of oxidizing at least three aldehydes. Hence the specific metabolic pathway(s) within which the and gene in restoration relates to its ability to modify the expression of gene was cloned via transposon tagging (Cui et al. 1996 The gene is equivalent to ALDH2B1. Only a few studies of ...
Purpose: Lung cancer stem cells (CSC) with elevated aldehyde dehydrogenase (ALDH) activity are self-renewing, clonogenic, and tumorigenic. The purpose of our study is to elucidate the mechanisms by which lung CSCs are regulated.. Experimental Design: A genome-wide gene expression analysis was performed to identify genes differentially expressed in the ALDH+ versus ALDH− cells. RT-PCR, Western blot analysis, and Aldefluor assay were used to validate identified genes. To explore the function in CSCs, we manipulated their expression followed by colony and tumor formation assays.. Results: We identified a subset of genes that were differentially expressed in common in ALDH+ cells, among which ALDH1A3 was the most upregulated gene in ALDH+ versus ALDH− cells. shRNA-mediated knockdown of ALDH1A3 in non-small cell lung cancer (NSCLC) resulted in a dramatic reduction in ALDH activity, clonogenicity, and tumorigenicity, indicating that ALDH1A3 is required for tumorigenic properties. In contrast, ...
Caused by the lack or reduction of an enzyme called Aldehyde dehydrogenase (ALDH) produced in the liver that breaks down alcohol. Symptoms include flushing, increased heart rate and reduced blood pressure.
Marc Weiner is Associate Research Professor at the Edward J. Bloustein School of Planning and Public Policy at Rutgers University. His research interests include quantitative and qualitative research methodologies; survey research planning, design, operations, data analysis; quantitative data modeling; his teaching interests include demography and population studies; and social movements and power relations. Weiner currently serves as the Bloustein Schools Director of Program Assessment and Conflict of Interest Monitor; previously, he served as Associate Director of the Bloustein Center for Survey Research, as well as Project Director for the Office of Population Research, and Assistant Director for the Survey Research Center, both at Princeton University. Weiner was the founding President of the New Jersey-Pennsylvania Chapter of the American Association for Public Opinion Research and served on the Executive Council of the Association of Academic Survey Research Organizations.. Weiner ...
Our results suggest that the recombinant strain E. coli 029A functionally express our biobrick BBa_K398029. From the statistical analysis that we performed we concluded that the expression of the biobrick BBa_K398006 under the promoter-rbs combination BBa_J23100-BBa_J61117 increases the dodecanal dehydrogenase activity in E. coli cell extracts 2-fold. Moreover, the enzymatic activities measured for the construct BBa_K398029 were equivalent to 33.98% of the Pseudomonas putida aldehyde dehydrogenase activity. Read more about it in our results page View BBa_K398029 in the parts registry Specified Components ...
Mouse monoclonal antibody raised against recombinant ALDH1A1. Recombinant protein corresponding to human ALDH1A1. (MAB10443) - Products - Abnova
BACKGROUND: Aldehyde dehydrogenase 1A1 (ALDH1A1), a member of aldehyde dehydrogenase family, is a marker of stemness in breast cancer. During tumor progression cancer stem cells (CSCs) have been reported to secrete angiogenic factors to orchestrate the formation of pathological angiogenesis. This vasculature can represent the source of self-renewal of CSCs and the route for further tumor spreading. The aim of the present study has been to assess whether ALDH1A1 controls the output of angiogenic factors in breast cancer cells and regulates tumor angiogenesis in a panel of in vitro and in vivo models. METHODS: Stemness status of breast cancer cells was evaluated by the ability to form turmorspheres in vitro. A transwell system was used to assess the angiogenic features of human umbilical vein endothelial cells (HUVEC) when co-cultured with breast cancer cells MCF-7 harboring different levels of ALDH1A1. Under these conditions, we survey endothelial proliferation, migration, tube formation and ...
摘要 旨在研究氨基酸平衡低蛋白质日粮对育肥猪肠道抗菌肽与微生物区系的影响。将20头(60±2.5)kg的育肥猪(杜×长×大)随机分为4个处理:14.0% CP日粮(14.0% CP),添加Glu、Lys、Met、Thr和Trp的12.5% CP日粮(12.5% CP),添加Glu、Lys、Met、Thr和Trp的11.0% CP日粮(11.0% CP),添加Glu、Lys、Met、Thr、Trp和BCAA(Val、Ile、Leu)的11.0% CP日粮(11.0% CP+BCAA)。每个处理5个重复,每个重复1头猪。试验分为5 d预试期和30 d正试期。结果表明:(1)尿液尿素氮和尿酸含量随日粮蛋白质水平降低而显著降低(P,0.05);(2)低蛋白质水平日粮显著降低空肠黏膜、回肠黏膜β-defensin-2水平和ANG1、ANG4 mRNA表达水平(P,0.05);(3)不同蛋白质水平日粮对部分回肠、直肠食糜微生物氨基酸组成有显著影响(P,0.05);(4)与14.0% CP组相比,12.5% CP组Observed species显著提高(P,0.05),11.0% ...
Or ALDH, this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ethanal the breakdown prod...
View mouse Aldh7a1 Chr18:56509687-56572951 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Réactivité: Boeuf (Vache), Chien, Cobaye and more. Comparez ALDH1A2 Anticorps. Commandez directement chez anticorps-enligne.fr.
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Here, we show that SOX11, an embryonic mammary marker that is normally silent in postnatal breast cells, is expressed in many oestrogen receptor-negative preinvasive ductal carcinoma in situ (DCIS) lesions. Mature mammary epithelial cells engineered to express SOX11 showed alterations in progenitor cell populations, including an expanded basal-like population with increased aldehyde dehydrogenase (ALDH) activity, and increased mammosphere-forming capacity. DCIS.com cells engineered to express SOX11 showed increased ALDH activity, which is a feature of cancer stem cells. The CD44+/CD24-/ALDH+ cell population was increased in DCIS.com cells that expressed SOX11. Upregulating SOX11 expression in DCIS.com cells led to increased invasive growth both in vitro and when they were injected intraductally in a mouse model of DCIS that recapitulates human disease. Invasive lesions formed sooner and tumour growth was augmented in vivo, suggesting that SOX11 contributes to the progression of DCIS to invasive ...
"aldehyde dehydrogenase - Homo sapiens". BRENDA. Technische Universität Braunschweig. January 2015. Retrieved 13 April 2015. ... and then aldehyde dehydrogenase (ALDH), which convert it to phenylacetic acid. This means that for significant concentrations ... product which is produced by monoamine oxidase and then further metabolized into β-phenylacetic acid by aldehyde dehydrogenase ... urinary metabolite of phenethylamine and is produced via monoamine oxidase metabolism and subsequent aldehyde dehydrogenase ...
3-hydroxyacyl-CoA dehydrogenase activity. • RNA binding. • acetyl-CoA C-acyltransferase activity. • long-chain-enoyl-CoA ... long-chain-3-hydroxyacyl-CoA dehydrogenase activity. • GO:0001948 protein binding. • catalytic activity. • transferase activity ... HADHB, ECHB, MSTP029, MTPB, TP-BETA, hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase (trifunctional ... "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional ...
acyl-CoA dehydrogenase activity. • identical protein binding. • oxidoreductase activity. • medium-chain-acyl-CoA dehydrogenase ... ACADM, acyl-CoA dehydrogenase, C-4 to C-12 straight chain, ACAD1, MCAD, MCADH, acyl-CoA dehydrogenase medium chain. ... "Mitochondrially encoded NADH dehydrogenase 1". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).. *^ Matsubara Y, Kraus ... ACADM (acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain) is a gene that provides instructions for making an enzyme ...
2cg5: STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL ... "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1-3): 94- ...
The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by ... Aldehyde dehydrogenase 3 family, member B1 also known as ALDH3B1 is an enzyme that in humans is encoded by the ALDH3B1 gene. ... Hsu LC, Chang WC, Yoshida A (Dec 1994). "Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase ... Hsu LC, Chang WC, Yoshida A (Apr 1997). "Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene ...
Aldehyde dehydrogenase 1 family, member A3, also known as ALDH1A3 or retinaldehyde dehydrogenase 3 (RALDH3), is an enzyme that ... Aldehyde dehydrogenase isozymes are thought to play a major role in the detoxification of aldehydes generated by alcohol ... Rexer BN, Zheng WL, Ong DE (2001). "Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase ... Yoshida A, Rzhetsky A, Hsu LC, Chang C (1998). "Human aldehyde dehydrogenase gene family". Eur. J. Biochem. 251 (3): 549-57. ...
DOPAL is detoxified mainly by aldehyde dehydrogenase. "3,4-dihydroxyphenylacetaldehyde - Compound Summary". PubChem Compound. ... Li, W., Spaziano, V.T., Burke, WJ., "Synthesis of a biochemicallly important aldehyde - 3,4-dihydroxyphenylacetaldehyde", Bio- ...
Gama-Castro S.; Núñez C.; Segura D.; Moreno S.; Guzmán J. & Espín G. (2001). "Azotobacter vinelandii Aldehyde Dehydrogenase ... it is also affected by aldehyde dehydrogenase[13] and the response regulator AlgR.[14] ...
NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ ... alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD- ... Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; ...
Human ALDH1A1 aldehyde dehydrogenase is capable of oxidizing malondialdehyde. Malondialdehyde and other thiobarbituric reactive ... This compound is a reactive aldehyde and is one of the many reactive electrophile species that cause toxic stress in cells and ... The production of this aldehyde is used as a biomarker to measure the level of oxidative stress in an organism. Malondialdehyde ...
Betaine aldehyde is further oxidised in the mitochondria in mice to betaine by the enzyme betaine aldehyde dehydrogenase (EC ... In humans betaine aldehyde activity is performed by a nonspecific cystosolic aldehyde dehydrogenase enzyme (EC 1.2.1.3) TMG is ... "BRENDA - Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase". Brenda-enzymes.org. Retrieved 2016-07-07. Chern, M. K.; ... Pietruszko, R. (1999). "Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver: purification, ...
Other studies have suggested that reduced activity by the enzyme aldehyde dehydrogenase may be responsible for a build-up of ... March 1993). "Analysis of corneal aldehyde dehydrogenase patterns in pathologic corneas". Cornea. 12 (2): 146-54. doi:10.1097/ ...
The encoded protein belongs to the aldehyde dehydrogenase family and is responsible for formate oxidation in vivo. Deficiencies ... ALDH1L1 aldehyde dehydrogenase 1 family, member L1". Human ALDH1L1 genome location and ALDH1L1 gene details page in the UCSC ... 10-formyltetrahydrofolate dehydrogenase is an enzyme that in humans is encoded by the ALDH1L1 gene. The protein encoded by this ... Krupenko SA, Oleinik NV (2002). "10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in ...
Aldehyde dehydrogenase family 3 member B2 is an enzyme that in humans is encoded by the ALDH3B2 gene. This gene encodes a ... "Entrez Gene: ALDH3B2 aldehyde dehydrogenase 3 family, member B2". Human ALDH3B2 genome location and ALDH3B2 gene details page ... member of the aldehyde dehydrogenase family, a group of isozymes that may play a major role in the detoxification of aldehydes ... Hsu LC, Chang WC, Yoshida A (Jun 1997). "Human aldehyde dehydrogenase genes, ALDH7 and ALDH8: genomic organization and gene ...
Aldehyde dehydrogenase 1 family, member A2, also known as ALDH1A2 or retinaldehyde dehydrogenase 2 (RALDH2), is an enzyme that ... "Entrez Gene: ALDH1A2 aldehyde dehydrogenase 1 family, member A2". Duester G (September 2008). "Retinoic Acid Synthesis and ... This protein belongs to the aldehyde dehydrogenase family of proteins. The product of this gene is an enzyme that catalyzes the ... Wang X, Penzes P, Napoli JL (1996). "Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia ...
Aldehyde dehydrogenase-mediated cellular relative insensitivity to the oxazaphosphorines. Curr Pharm Des. 1999 Aug;5(8):607-25 ...
Dyck, Lillian E.. "Polymorphism of a class 3 aldehyde dehydrogenase present in human saliva and in hair roots."Alcoholism, ... Dyck, Lillian E."Absence of the atypical mitochondrial aldehyde dehydrogenase (ALDH2) isozyme in Saskatchewan Cree Indians." ... "Isoenzymes of aldehyde dehydrogenase in human lymphocytes." Alcoholism, Clinical and Experimental Research. 14:4 (August 1990 ...
... is then oxidized to lactic acid by aldehyde dehydrogenase. Lactaldehyde exists in several forms: in open-chain ... Methylglyoxal is converted to D-lactaldehyde by glycerol dehydrogenase (gldA). ...
This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... Aldehyde dehydrogenase 1 family, member A1, also known as ALDH1A1 or retinaldehyde dehydrogenase 1 (RALDH1), is an enzyme that ... 2009). "Aldehyde dehydrogenase 1 is a putative marker for cancer stem cells in head and neck squamous cancer". Biochem. Biophys ... 2009). "Aldehyde dehydrogenase-expressing colon stem cells contribute to tumorigenesis in the transition from colitis to cancer ...
Aldehyde dehydrogenase 8 family, member A1 also known as ALDH8A1 is an enzyme that in humans is encoded by the ALDH8A1 gene. ... This protein belongs to the aldehyde dehydrogenase family of proteins. It plays a role in a pathway of 9-cis-retinoic acid ... Therefore, it is the first known aldehyde dehydrogenase to show a preference for 9-cis-retinal relative to all-trans-retinal. ... "cDNA cloning and expression of a human aldehyde dehydrogenase (ALDH) active with 9-cis-retinal and identification of a rat ...
Algar EM, Abedinia M, VandeBerg JL, Holmes RS (1991). "Purification and properties of baboon corneal aldehyde dehydrogenase: ... King G, Holmes RS (Sep 1993). "Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic ... PDB: 1K87​; Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ (Feb 2003). "Structure of the proline dehydrogenase domain of the ... In the case of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), in addition to the large number of ...
"This protein belongs to the aldehyde dehydrogenase family of proteins. Aldehyde dehydrogenase is the second enzyme of the major ... The enzyme associated with the chemical transformation from acetaldehyde to acetic acid is aldehyde dehydrogenase 2 family ( ... Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic ... The enzyme encoded by this gene is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a ...
Mitochondrial aldehyde dehydrogenase belongs to the aldehyde dehydrogenase family of enzymes that catalyze the chemical ... This protein belongs to the aldehyde dehydrogenase family of enzymes. Aldehyde dehydrogenase is the second enzyme of the major ... Aldehyde dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH2 gene located on chromosome 12. ... "Entrez Gene: ALDH2 aldehyde dehydrogenase 2 family (mitochondrial)". Seitz HK, Meier P (2007). "The role of acetaldehyde in ...
Cheung C, Smith CK, Hoog JO, Hotchkiss SA (Jul 1999). "Expression and localization of human alcohol and aldehyde dehydrogenase ... This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members ... "Genetics of human alcohol and aldehyde dehydrogenases". Advances in Human Genetics. 15: 249-90. doi:10.1007/978-1-4615-8356-1_5 ... Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high ...
Alcohol dehydrogenase Aldehyde dehydrogenase GRCh38: Ensembl release 89: ENSG00000196616 - Ensembl, May 2017 "Human PubMed ... There are more genes in the family of alcohol and aldehyde dehydrogenase genes. These genes are now referred to as ADH1A, ADH1C ... "Alcohol and aldehyde dehydrogenase genotypes and drinking behavior of Chinese living in Shanghai". Human Genetics. 96 (2): 151- ... "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet. 15: 249-90. doi:10.1007/978-1-4615-8356-1_5. PMID ...
... detoxication of the lipid peroxide-derived reactive aldehydes". Plant Cell Physiol. 43 (12): 1445-55. doi:10.1093/pcp/pcf187. ... Glutaryl-CoA dehydrogenase. *Isovaleryl coenzyme A dehydrogenase. *3-oxo-5beta-steroid 4-dehydrogenase ...
Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought. E A ... In plants, the last step in betaine synthesis is catalyzed by betaine-aldehyde dehydrogenase (BADH, EC 1.2.1.8), a nuclear- ... Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought ... Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought ...
Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes that are ... Abstract:Mitochondrial aldehyde dehydrogenase (ALDH2) is an isoenzyme of aldehyde dehydrogenases (ALDH), a group of enzymes ... Keywords: 4-hydroxy-2-nonenal (4-HNE), Alda-1, aldehyde, ischemia/reperfusion injury, mitochondrial aldehyde dehydrogenase ( ... Keywords:4-hydroxy-2-nonenal (4-HNE), Alda-1, aldehyde, ischemia/reperfusion injury, mitochondrial aldehyde dehydrogenase ( ...
Treatment Fatty aldehyde dehydrogenase deficiency. Symptoms and causes Fatty aldehyde dehydrogenase deficiency Prophylaxis ... Fatty aldehyde dehydrogenase deficiency». *. Fatty aldehyde dehydrogenase deficiency - WrongDiagnosis.com. Fatty aldehyde ... Fatty aldehyde dehydrogenase deficiency definition - Medical .... Fatty aldehyde dehydrogenase deficiency: Also known as the ... Fatty aldehyde dehydrogenase deficiency: Also known as the Sjogren-Larsson syndrome, this is a genetic (inherited) disease ...
T1 - Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ... Widespread nonhematopoietic tissue distribution by transplanted human progenitor cells with high aldehyde dehydrogenase ...
title = "Betaine aldehyde dehydrogenase in plants",. abstract = "Plant betaine aldehyde dehydrogenases (BADHs) have been the ... Betaine aldehyde dehydrogenase in plants. Together they form a unique fingerprint. * betaine-aldehyde dehydrogenase ... Fitzgerald, T. L., Waters, D. L. E., & Henry, R. J. (2009). Betaine aldehyde dehydrogenase in plants. Plant Biology, 11(2), 119 ... Fitzgerald, T. L. ; Waters, D. L E ; Henry, R. J. / Betaine aldehyde dehydrogenase in plants. In: Plant Biology. 2009 ; Vol. 11 ...
Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa ... The binding sites of Potassium atom in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From ... Potassium in the structure of Crystallographic Structure of Betaine Aldehyde Dehydrogenase From Pseudomonas Aeruginosa (pdb ...
Aldehyde Dehydrogenase 8. Messenger RNA (mRNA) 9. Hydrogen 10. Urea (Carbamide) Related Therapies and Procedures. 1. Oral ...
keywords = "Aldehyde dehydrogenase, Ichthyosis, Mental retardation, Spasticity",. author = "{De Laurenzi}, Vincenzo and Rogers ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ... Patients with SLS have deficient activity of fatty aldehyde dehydrogenase (FALDH), an enzyme involved in long-chain fatty ...
... aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ultimately oxidized to carbon ... Other articles where Aldehyde dehydrogenase is discussed: alcohol consumption: Processing in the liver: …acted upon by another ... acted upon by another enzyme, aldehyde dehydrogenase, and converted to acetate, most of which enters the bloodstream and is ...
... this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ethanal ... Or ALDH, this breaks down various aldehydes into the corresponding carboxylic acids. Its most notable substrate is, of course ...
Aldehyde dehydrogenases (EC 1.2.1.3) are a group of enzymes that catalyse the oxidation of aldehydes. Despite the name " ... Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the ... Marchitti, SA; Brocker, C; Stagos, D; Vasiliou, V (Jun 2008). "Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase ... "Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related ...
Aldehyde dehydrogenaseImported. ,p>Information which has been imported from another database using automatic procedures.,/p> ,p ... tr,Q7M053,Q7M053_RAT Aldehyde dehydrogenase OS=Rattus norvegicus OX=10116 PE=1 SV=1 BSGZPTAVMYILFHKR Align. Format. Add to ...
In enzymology, a betaine-aldehyde dehydrogenase (EC 1.2.1.8) is an enzyme that catalyzes the chemical reaction betaine aldehyde ... Other names in common use include betaine aldehyde oxidase, BADH, betaine aldehyde dehydrogenase, and BetB. This enzyme ... ROTHSCHILD HA, BARRON ES (1954). "The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase". J. Biol. Chem. 209 (2 ... Eklund H; El-Ahmad, M; Ramaswamy, S; Hjelmqvist, L; Jörnvall, H; Eklund, H (1998). "Structure of betaine aldehyde dehydrogenase ...
GO:0008802 betaine-aldehyde dehydrogenase activity GO:0016491 oxidoreductase activity GO:0016620 oxidoreductase activity, ... acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor GO:0046872 metal ion binding ...
Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead (IPR000674). Short name: Ald_Oxase/Xan_DH_a/b ... The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [PMID: ... Aldehyde oxidase (EC:1.2.3.1) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and ... Xanthine dehydrogenase (EC:1.1.1.204) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and ...
NAD-dependent aldehyde dehydrogenase activity, NAD-linked aldehyde dehydrogenase activity, aldehyde dehydrogenase (NAD+), ... aldehyde dehydrogenase (NAD+), aldehyde:NAD+ oxidoreductase activity, CoA-independent aldehyde dehydrogenase activity, m- ... propionaldehyde dehydrogenase activity, CoA-independent aldehyde dehydrogenase activity, NAD-aldehyde dehydrogenase activity, ... NAD-aldehyde dehydrogenase activity, NAD-dependent 4-hydroxynonenal dehydrogenase activity, NAD-dependent aldehyde ...
aldehyde dehydrogenase X, mitochondrial. Names. ALDH class 2. acetaldehyde dehydrogenase 5. aldehyde dehydrogenase 5. ... ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo sapiens] ALDH1B1 aldehyde dehydrogenase 1 family member B1 [Homo ... This protein belongs to the aldehyde dehydrogenases family of proteins. Aldehyde dehydrogenase is the second enzyme of the ... aldehyde dehydrogenase 1 family member B1provided by HGNC. Primary source. HGNC:HGNC:407 See related. Ensembl:ENSG00000137124 ...
Aldehyde dehydrogenase activity promotes survival of human muscle precursor cells.. Jean E1, Laoudj-Chenivesse D, Notarnicola C ... Aldehyde dehydrogenases (ALDH) are a family of enzymes that efficiently detoxify aldehydic products generated by reactive ...
Keywords: Arabidopsis thaliana; Craterostigma plantagineum; abscisic acid; aldehyde dehydrogenase; dehydration; enzyme activity ... Phylogenetically, the Cp- and Ath-ALDH3 and -ALDH4 proteins are closely related to aldehyde dehydrogenases from bacteria and ... Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma ... a gene was isolated with homology to class 3 variable substrate aldehyde dehydrogenases (ALDH). The C. plantagineum gene Cp- ...
Aldehyde dehydrogenase inhibitors. Class Summary. Disulfiram inhibits aldehyde dehydrogenase, and, as a result, acetaldehyde ...
SEARCH RESULTS for: Acetyl Aldehyde Dehydrogenase Inhibitors [Drug Class] (10 results) * Share : JavaScript needed for Sharing ...
Aldehyde dehydrogenase, mitochondrial. A, B, C, D, E, F, G, H. 500. Homo sapiens. Mutation(s): 1 Gene Names: ALDH2, ALDM. EC: ... T244A mutant of human mitochondrial aldehyde dehydrogenase, NAD complex. *DOI: 10.2210/pdb3N83/pdb ...
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids (PubMed:25286108). Responsible for conversion of the ... Fatty aldehyde dehydrogenaseAdd BLAST. 484. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical ... aldehyde dehydrogenase (NAD) activity Source: MGI ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a direct assay for the ... Fatty aldehyde dehydrogenase (EC:1.2.1.31 Publication. ,p>Manually curated information for which there is published ...
2011) Aldehyde dehydrogenase: Its role as a cancer stem cell marker comes down to the specific isoform. Cell Cycle 10(9):1378- ... Aldehyde Dehydrogenase 1A3 Activity Is Markedly Elevated in Mes GSCs Compared with Mes Non-GSCs and PN GSCs.. Based on the ... 2009) Aldehyde dehydrogenase 1 is a marker for normal and malignant human colonic stem cells (SC) and tracks SC overpopulation ... 2011) Aldehyde dehydrogenase activity of breast cancer stem cells is primarily due to isoform ALDH1A3 and its expression is ...
We focus on the characterization of the aldehyde dehydrogenase-1 family of enzymes (ALDH1A1, ALDH1A2, ALDH1A3) that catalyze ... Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?. Jennifer M. Petrosino. ... Petrosino, J.M.; DiSilvestro, D.; Ziouzenkova, O. Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism? Nutrients ... "Aldehyde Dehydrogenase 1A1: Friend or Foe to Female Metabolism?" Nutrients 6, no. 3: 950-973. ...
  • The amino acid sequence deduced from the BADH cDNA sequence showed substantial similarities to those for nonspecific aldehyde dehydrogenases (EC 1.2.1.3 and EC 1.2.1.5) from several sources, including absolute conservation of a decapeptide in the probable active site. (pnas.org)
  • The topic of this work is of major importance since we show that invasion and metastasis in IBC are mediated by a cellular subcomponent with stem cell characteristics expressing the stem cell marker aldehyde dehydrogenase 1 (ALDH1). (aacrjournals.org)
  • In models of triple-negative breast cancer (TNBC), it has recently been shown that the epidermal growth factor receptor (EGFR) pathway is up-regulated in the aldehyde dehydrogenase 1 (ALDH1)-positive cancer stem cell fraction. (uzh.ch)
  • SR-T100 downregulated the expression of stem cell markers, including aldehyde dehydrogenase 1 (ALDH1), Notch1, and FoxM1, and reduced sphere formation in ovarian cancer cells. (jcancer.org)
  • The present study is to determine the expression of aldehyde dehydrogenase 1 (ALDH1) and ATPbinding cassette superfamily G member 2 (ABCG2) in patients with triple-negative breast cancer, and to understand the relationship of ALDH1 and ABCG2 with triple-negative breast cancer. (alliedacademies.org)
  • The purpose of this study was to compare the expression and the prognostic effect of the breast cancer stem cell marker aldehyde dehydrogenase-1 (ALDH1) in young and elderly breast cancer patients. (biomedcentral.com)
  • It is also important in metabolizing other toxic aldehydes such as 4-hydroxy-2-nonenal (4-HNE) and acrolein [ 2 ]. (hindawi.com)
  • In animal myocardial or cerebral ischemia/ reperfusion (I/R) models, accumulation of toxic aldehydes, such as 4-hydroxy-2-nonenal and malondialdehyde, is thought to be an important mechanism for myocardial and cerebral I/R injury. (eurekaselect.com)
  • The results presented last week suggest the potential therapeutic applicability of aldehyde traps as a novel approach to treating SSADH Deficiency by sequestering succinic semialdehyde and other toxic aldehydes. (businessinsider.com)
  • On the other hand, aldehydes are highly reactive compounds, which can form adducts with proteins, DNA, and lipids, affecting the function of these biomolecules and leading to cell toxicity. (hindawi.com)
  • Aldehydes, which are highly reactive molecules, are toxic at high concentrations. (biochemj.org)
  • These results strongly suggest that elevated reactive aldehyde concentration, like that observed in the presence of chronic pain, may render cardiomyocytes more susceptible to I/R injury by SIRT1 carbonylative inactivation and impairment the cardioprotection of LKB1-mediated AMPK activation. (onlinejacc.org)
  • One theory is that a certain type of stem cell, aldehyde dehydrogenase bright stem cells, may stimulate the growth of new vessels. (clinicaltrials.gov)
  • The protein may also be known as SSADH, SSDH, succinate-semialdehyde dehydrogenase, mitochondrial, and NAD(+)-dependent succinic semialdehyde dehydrogenase. (biocompare.com)
  • Aldeyra Therapeutics Presents Evidence for Aldehyde Sequestration as a Potential Therapeutic Approach in Succinic Semialdehyde Dehydrogenase Deficiency at the American Society of Human Genetics. (businessinsider.com)
  • Succinic Semialdehyde Dehydrogenase (SSADH) Deficiency is a neurological disease caused by genetic mutations that result in elevated levels of succinic semialdehyde, which are toxic and ultimately result in severe neurological dysfunction, including motor dysfunction, seizures, speech impairment, intellectual disability, and autistic behavior. (businessinsider.com)
  • and the potential of ADX-102 as an agent for the treatment of Succinic Semialdehyde Dehydrogenase Deficiency (SSADHD). (businessinsider.com)
  • Aldehyde dehydrogenase 1B1: a novel immunohistological marker for colorectal cancer. (nih.gov)
  • Your search returned 21 aldehyde dehydrogenase 1 family member L1 ELISA ELISA Kit across 3 suppliers. (biocompare.com)
  • Aldeyra Therapeutics, Inc. is a biotechnology company devoted to improving lives by inventing, developing and commercializing products that treat diseases thought to be related to endogenous aldehydes, a naturally occurring class of pro-inflammatory and toxic molecules. (businessinsider.com)